MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Sortilin; AltName: Full=100 kDa NT receptor; AltName: Full=Glycoprotein 95; Short=Gp95; AltName: Full=Neurotensin receptor 3; Short=NT3; Short=NTR3; Flags: Precursor; |
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| MyHits synonyms | SORT_HUMAN , Q99523 , B4DWI3 , C0JYZ0 , Q8IZ49 , 91F96A3035A4B43A |
 Legends: 1, Phosphoserine. {ECO:0000244|PubMed:23186163}; 2, Phosphoserine. {ECO:0000244|PubMed:21406692}; 3, Phosphoserine. {ECO:0000244|PubMed:18088087, ECO:0000244|PubMed:21406692, ECO:0000244|PubMed:23186163}; 4, N-linked (GlcNAc...). {ECO:0000305}; 5, N-linked (GlcNAc...). {ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:19349973}; 6, N-linked (GlcNAc...); atypical. {ECO:0000269|PubMed:19349973}; 7, N-linked (GlcNAc...). {ECO:0000255}; 8, N-linked (GlcNAc...). {ECO:0000269|PubMed:19122660}; 9, VARIANT D -> Y (in dbSNP:rs2228605); 10, MUTAGEN Y->A: Reduces endocytosis and Golgi to endosome sorting; when associated with A- 795. {ECO:0000269|PubMed:11331584}; 11, MUTAGEN L->A: Reduces endocytosis and Golgi to endosome sorting; when associated with A- 792. {ECO:0000269|PubMed:11331584}; 12, MUTAGEN S->A: Reduces interaction with GGA1. {ECO:0000269|PubMed:11390366}; 13, CONFLICT V -> M (in Ref. 1; CAA66904). {ECO:0000305}; 14, SIGNAL {ECO:0000250|UniProtKB:O54861}; 15, PROPEP Removed in mature form. {ECO:0000269|PubMed:9756851}; 16, TRANSMEM Helical. {ECO:0000255}; 17, TOPO_DOM Cytoplasmic. {ECO:0000255}; 18, REPEAT BNR 1; 19, REPEAT BNR 2; 20, REPEAT BNR 3; 21, REPEAT BNR 4; 22, REPEAT BNR 5; 23, REPEAT BNR 6; 24, REPEAT BNR 7; 25, REPEAT BNR 8; 26, REPEAT BNR 9; 27, REGION Intrachain binding of the propeptide and the extracellular domain; 28, REGION Interactions with LRPAP1 and NGFB; 29, REGION Golgi to endosome transport and interactions with GGA1 and GGA2; 30, MOTIF Endocytosis signal. {ECO:0000305}; 31, VAR_SEQ Missing (in isoform 2). {ECO:0000303|PubMed:14702039}; 32, VAR_SEQ KA -> T (in isoform 2). {ECO:0000303|PubMed:14702039}; 33, MUTAGEN RWRR->GWRA: Abrogates propeptide cleavage. {ECO:0000269|PubMed:9927419}; 34, MUTAGEN RR->GG: Abrogates propeptide cleavage. {ECO:0000269|PubMed:9927419}; 35, MUTAGEN DD->NN: Reduces interaction with GGA1. {ECO:0000269|PubMed:11390366}; 36, MUTAGEN DED->NQN: Abrogates interaction with GGA1 and impairs localization to the Golgi. {ECO:0000269|PubMed:11390366}; 37, MUTAGEN LL->AA: Abrogates interaction with GGA1 and impairs localization to the Golgi. {ECO:0000269|PubMed:11331584, ECO:0000269|PubMed:11390366}; 38, MUTAGEN Missing: Abrogates interaction with GGA2. Reduces endocytosis and Golgi to endosome sorting; when associated with A-792 and A-795. {ECO:0000269|PubMed:11331584, ECO:0000269|PubMed:11390366}; 39, HELIX {ECO:0000244|PDB:3F6K}; 40, STRAND {ECO:0000244|PDB:3F6K}; 41, STRAND {ECO:0000244|PDB:4PO7}; 42, HELIX {ECO:0000244|PDB:4PO7}; 43, TURN {ECO:0000244|PDB:3F6K}; 44, STRAND {ECO:0000244|PDB:4N7E}; 45, STRAND {ECO:0000244|PDB:4MSL}.
| |
ID SORT_HUMAN Reviewed; 831 AA.
AC Q99523; B4DWI3; C0JYZ0; Q8IZ49;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 3.
DT 18-JAN-2017, entry version 165.
DE RecName: Full=Sortilin;
DE AltName: Full=100 kDa NT receptor;
DE AltName: Full=Glycoprotein 95;
DE Short=Gp95;
DE AltName: Full=Neurotensin receptor 3;
DE Short=NT3;
DE Short=NTR3;
DE Flags: Precursor;
GN Name=SORT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE,
RP INTERACTION WITH LRPAP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP GLYCOSYLATION.
RC TISSUE=T-cell;
RX PubMed=9013611; DOI=10.1074/jbc.272.6.3599;
RA Petersen C.M., Nielsen M.S., Nykjaer A., Jacobsen L., Tommerup N.,
RA Rasmussen H.H., Roeigaard H., Gliemann J., Madsen P., Moestrup S.K.;
RT "Molecular identification of a novel candidate sorting receptor
RT purified from human brain by receptor-associated protein affinity
RT chromatography.";
RL J. Biol. Chem. 272:3599-3605(1997).
RN [2]
RP SEQUENCE REVISION.
RA Madsen P.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 78-100, AND IDENTIFICATION AS A NEUROTENSIN
RP RECEPTOR.
RC TISSUE=Brain;
RX PubMed=9756851; DOI=10.1074/jbc.273.41.26273;
RA Mazella J., Zsurger N., Navarro V., Chabry J., Kaghad M., Caput D.,
RA Ferrara P., Vita M., Gully D., Maffrand J.-P., Vincent J.-P.;
RT "The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-
RT coupled receptor.";
RL J. Biol. Chem. 273:26273-26276(1998).
RN [8]
RP PARTIAL PROTEIN SEQUENCE, INTERACTION WITH LRPAP1, MUTAGENESIS OF
RP 74-ARG--ARG-77 AND 76-ARG-ARG-77, CLEAVAGE BY FURIN, AND
RP GLYCOSYLATION.
RX PubMed=9927419; DOI=10.1093/emboj/18.3.595;
RA Petersen C.M., Nielsen M.S., Jacobsen C., Tauris J., Jacobsen L.,
RA Gliemann J., Moestrup S.K., Madsen P.;
RT "Propeptide cleavage conditions sortilin/neurotensin receptor-3 for
RT ligand binding.";
RL EMBO J. 18:595-604(1999).
RN [9]
RP INTERACTION WITH LRPAP1.
RX PubMed=9657377; DOI=10.1016/S0014-5793(98)00559-6;
RA Tauris J., Ellgaard L., Jacobsen C., Nielsen M.S., Madsen P.,
RA Thoegersen H.C., Gliemann J., Petersen C.M., Moestrup S.K.;
RT "The carboxy-terminal domain of the receptor-associated protein binds
RT to the Vps10p domain of sortilin.";
RL FEBS Lett. 429:27-30(1998).
RN [10]
RP FUNCTION.
RX PubMed=10085125; DOI=10.1074/jbc.274.13.8832;
RA Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M.;
RT "Sortilin/neurotensin receptor-3 binds and mediates degradation of
RT lipoprotein lipase.";
RL J. Biol. Chem. 274:8832-8836(1999).
RN [11]
RP FUNCTION, INTERACTION WITH GGA2, AND MUTAGENESIS OF TYR-792; LEU-795
RP AND 829-LEU-LEU-830.
RX PubMed=11331584; DOI=10.1093/emboj/20.9.2180;
RA Nielsen M.S., Madsen P., Christensen E.I., Nykjaer A., Gliemann J.,
RA Kasper D., Pohlmann R., Petersen C.M.;
RT "The sortilin cytoplasmic tail conveys Golgi-endosome transport and
RT binds the VHS domain of the GGA2 sorting protein.";
RL EMBO J. 20:2180-2190(2001).
RN [12]
RP FUNCTION, INTERACTION WITH GGA1 AND GGA2, AND MUTAGENESIS OF
RP 823-ASP-ASP-824; SER-825; 826-ASP--ASP-828 AND 829-LEU-LEU-830.
RX PubMed=11390366; DOI=10.1074/jbc.C100218200;
RA Takatsu H., Katoh Y., Shiba Y., Nakayama K.;
RT "Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation
RT factor-binding (GGA) proteins interact with acidic dileucine sequences
RT within the cytoplasmic domains of sorting receptors through their
RT Vps27p/Hrs/STAM (VHS) domains.";
RL J. Biol. Chem. 276:28541-28545(2001).
RN [13]
RP CLEAVAGE OF THE EXTRACELLULAR DOMAIN.
RX PubMed=12419319; DOI=10.1016/S0006-291X(02)02564-0;
RA Navarro V., Vincent J.-P., Mazella J.;
RT "Shedding of the luminal domain of the neurotensin receptor-3/sortilin
RT in the HT29 cell line.";
RL Biochem. Biophys. Res. Commun. 298:760-764(2002).
RN [14]
RP FUNCTION, AND INDUCTION.
RX PubMed=12209882; DOI=10.1002/jcp.10151;
RA Maeda S., Nobukuni T., Shimo-Onoda K., Hayashi K., Yone K., Komiya S.,
RA Inoue I.;
RT "Sortilin is upregulated during osteoblastic differentiation of
RT mesenchymal stem cells and promotes extracellular matrix
RT mineralization.";
RL J. Cell. Physiol. 193:73-79(2002).
RN [15]
RP INTERACTION WITH GGA1.
RX PubMed=11859376; DOI=10.1038/415937a;
RA Shiba T., Takatsu H., Nogi T., Matsugaki N., Kawasaki M., Igarashi N.,
RA Suzuki M., Kato R., Earnest T., Nakayama K., Wakatsuki S.;
RT "Structural basis for recognition of acidic-cluster dileucine sequence
RT by GGA1.";
RL Nature 415:937-941(2002).
RN [16]
RP FUNCTION, INTERACTION WITH GM2A AND PSAP, AND SUBCELLULAR LOCATION.
RX PubMed=14657016; DOI=10.1093/emboj/cdg629;
RA Lefrancois S., Zeng J., Hassan A.J., Canuel M., Morales C.R.;
RT "The lysosomal trafficking of sphingolipid activator proteins (SAPs)
RT is mediated by sortilin.";
RL EMBO J. 22:6430-6437(2003).
RN [17]
RP ERRATUM.
RA Lefrancois S., Zeng J., Hassan A.J., Canuel M., Morales C.R.;
RL EMBO J. 23:1680-1680(2004).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12598608;
RA Martin S., Vincent J.-P., Mazella J.;
RT "Involvement of the neurotensin receptor-3 in the neurotensin-induced
RT migration of human microglia.";
RL J. Neurosci. 23:1198-1205(2003).
RN [19]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15313463; DOI=10.1016/j.biocel.2004.04.013;
RA Morinville A., Martin S., Lavallee M., Vincent J.-P., Beaudet A.,
RA Mazella J.;
RT "Internalization and trafficking of neurotensin via NTS3 receptors in
RT HT29 cells.";
RL Int. J. Biochem. Cell Biol. 36:2153-2168(2004).
RN [20]
RP INTERACTION WITH LRPAP1 AND NGFB, SUBCELLULAR LOCATION, DISULFIDE
RP BONDS, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=15364913; DOI=10.1074/jbc.M408873200;
RA Westergaard U.B., Soerensen E.S., Hermey G., Nielsen M.S., Nykjaer A.,
RA Kirkegaard K., Jacobsen C., Gliemann J., Madsen P., Petersen C.M.;
RT "Functional organization of the sortilin Vps10p domain.";
RL J. Biol. Chem. 279:50221-50229(2004).
RN [21]
RP FUNCTION, AND INTERACTION WITH NGFB AND NGFR.
RX PubMed=14985763; DOI=10.1038/nature02319;
RA Nykjaer A., Lee R., Teng K.K., Jansen P., Madsen P., Nielsen M.S.,
RA Jacobsen C., Kliemannel M., Schwarz E., Willnow T.E., Hempstead B.L.,
RA Petersen C.M.;
RT "Sortilin is essential for proNGF-induced neuronal cell death.";
RL Nature 427:843-848(2004).
RN [22]
RP FUNCTION.
RX PubMed=15930396; DOI=10.1523/JNEUROSCI.5123-04.2005;
RA Teng H.K., Teng K.K., Lee R., Wright S., Tevar S., Almeida R.D.,
RA Kermani P., Torkin R., Chen Z.-Y., Lee F.S., Kraemer R.T., Nykjaer A.,
RA Hempstead B.L.;
RT "ProBDNF induces neuronal apoptosis via activation of a receptor
RT complex of p75NTR and sortilin.";
RL J. Neurosci. 25:5455-5463(2005).
RN [23]
RP FUNCTION, AND INTERACTION WITH BDNF.
RX PubMed=15987945; DOI=10.1523/JNEUROSCI.1017-05.2005;
RA Chen Z.-Y., Ieraci A., Teng H., Dall H., Meng C.-X., Herrera D.G.,
RA Nykjaer A., Hempstead B.L., Lee F.S.;
RT "Sortilin controls intracellular sorting of brain-derived neurotrophic
RT factor to the regulated secretory pathway.";
RL J. Neurosci. 25:6156-6166(2005).
RN [24]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [27]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162 AND ASN-163.
RC TISSUE=Leukemic T-cell;
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-
RT linked cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
RN [28]
RP TISSUE SPECIFICITY.
RX PubMed=20048080; DOI=10.1158/0008-5472.CAN-09-1252;
RA Swift S.L., Burns J.E., Maitland N.J.;
RT "Altered expression of neurotensin receptors is associated with the
RT differentiation state of prostate cancer.";
RL Cancer Res. 70:347-356(2010).
RN [29]
RP INVOLVEMENT IN LDLCQ6.
RX PubMed=20686565; DOI=10.1038/nature09270;
RA Teslovich T.M., Musunuru K., Smith A.V., Edmondson A.C.,
RA Stylianou I.M., Koseki M., Pirruccello J.P., Ripatti S., Chasman D.I.,
RA Willer C.J., Johansen C.T., Fouchier S.W., Isaacs A., Peloso G.M.,
RA Barbalic M., Ricketts S.L., Bis J.C., Aulchenko Y.S., Thorleifsson G.,
RA Feitosa M.F., Chambers J., Orho-Melander M., Melander O., Johnson T.,
RA Li X., Guo X., Li M., Shin Cho Y., Jin Go M., Jin Kim Y., Lee J.Y.,
RA Park T., Kim K., Sim X., Twee-Hee Ong R., Croteau-Chonka D.C.,
RA Lange L.A., Smith J.D., Song K., Hua Zhao J., Yuan X., Luan J.,
RA Lamina C., Ziegler A., Zhang W., Zee R.Y., Wright A.F., Witteman J.C.,
RA Wilson J.F., Willemsen G., Wichmann H.E., Whitfield J.B.,
RA Waterworth D.M., Wareham N.J., Waeber G., Vollenweider P.,
RA Voight B.F., Vitart V., Uitterlinden A.G., Uda M., Tuomilehto J.,
RA Thompson J.R., Tanaka T., Surakka I., Stringham H.M., Spector T.D.,
RA Soranzo N., Smit J.H., Sinisalo J., Silander K., Sijbrands E.J.,
RA Scuteri A., Scott J., Schlessinger D., Sanna S., Salomaa V.,
RA Saharinen J., Sabatti C., Ruokonen A., Rudan I., Rose L.M.,
RA Roberts R., Rieder M., Psaty B.M., Pramstaller P.P., Pichler I.,
RA Perola M., Penninx B.W., Pedersen N.L., Pattaro C., Parker A.N.,
RA Pare G., Oostra B.A., O'Donnell C.J., Nieminen M.S., Nickerson D.A.,
RA Montgomery G.W., Meitinger T., McPherson R., McCarthy M.I.,
RA McArdle W., Masson D., Martin N.G., Marroni F., Mangino M.,
RA Magnusson P.K., Lucas G., Luben R., Loos R.J., Lokki M.L., Lettre G.,
RA Langenberg C., Launer L.J., Lakatta E.G., Laaksonen R., Kyvik K.O.,
RA Kronenberg F., Konig I.R., Khaw K.T., Kaprio J., Kaplan L.M.,
RA Johansson A., Jarvelin M.R., Janssens A.C., Ingelsson E., Igl W.,
RA Kees Hovingh G., Hottenga J.J., Hofman A., Hicks A.A.,
RA Hengstenberg C., Heid I.M., Hayward C., Havulinna A.S., Hastie N.D.,
RA Harris T.B., Haritunians T., Hall A.S., Gyllensten U., Guiducci C.,
RA Groop L.C., Gonzalez E., Gieger C., Freimer N.B., Ferrucci L.,
RA Erdmann J., Elliott P., Ejebe K.G., Doring A., Dominiczak A.F.,
RA Demissie S., Deloukas P., de Geus E.J., de Faire U., Crawford G.,
RA Collins F.S., Chen Y.D., Caulfield M.J., Campbell H., Burtt N.P.,
RA Bonnycastle L.L., Boomsma D.I., Boekholdt S.M., Bergman R.N.,
RA Barroso I., Bandinelli S., Ballantyne C.M., Assimes T.L.,
RA Quertermous T., Altshuler D., Seielstad M., Wong T.Y., Tai E.S.,
RA Feranil A.B., Kuzawa C.W., Adair L.S., Taylor H.A. Jr., Borecki I.B.,
RA Gabriel S.B., Wilson J.G., Holm H., Thorsteinsdottir U., Gudnason V.,
RA Krauss R.M., Mohlke K.L., Ordovas J.M., Munroe P.B., Kooner J.S.,
RA Tall A.R., Hegele R.A., Kastelein J.J., Schadt E.E., Rotter J.I.,
RA Boerwinkle E., Strachan D.P., Mooser V., Stefansson K., Reilly M.P.,
RA Samani N.J., Schunkert H., Cupples L.A., Sandhu M.S., Ridker P.M.,
RA Rader D.J., van Duijn C.M., Peltonen L., Abecasis G.R., Boehnke M.,
RA Kathiresan S.;
RT "Biological, clinical and population relevance of 95 loci for blood
RT lipids.";
RL Nature 466:707-713(2010).
RN [30]
RP INVOLVEMENT IN SUSCEPTIBILITY TO MYOCARDIAL INFARCTION.
RX PubMed=20686566; DOI=10.1038/nature09266;
RA Musunuru K., Strong A., Frank-Kamenetsky M., Lee N.E., Ahfeldt T.,
RA Sachs K.V., Li X., Li H., Kuperwasser N., Ruda V.M., Pirruccello J.P.,
RA Muchmore B., Prokunina-Olsson L., Hall J.L., Schadt E.E.,
RA Morales C.R., Lund-Katz S., Phillips M.C., Wong J., Cantley W.,
RA Racie T., Ejebe K.G., Orho-Melander M., Melander O., Koteliansky V.,
RA Fitzgerald K., Krauss R.M., Cowan C.A., Kathiresan S., Rader D.J.;
RT "From noncoding variant to phenotype via SORT1 at the 1p13 cholesterol
RT locus.";
RL Nature 466:714-719(2010).
RN [31]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [32]
RP INTERACTION WITH NTRK1.
RX PubMed=21102451; DOI=10.1038/nn.2689;
RA Vaegter C.B., Jansen P., Fjorback A.W., Glerup S., Skeldal S.,
RA Kjolby M., Richner M., Erdmann B., Nyengaard J.R., Tessarollo L.,
RA Lewin G.R., Willnow T.E., Chao M.V., Nykjaer A.;
RT "Sortilin associates with Trk receptors to enhance anterograde
RT transport and neurotrophin signaling.";
RL Nat. Neurosci. 14:54-61(2011).
RN [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-819 AND SER-825, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [34]
RP INTERACTION WITH CLN5 AND PSAP.
RX PubMed=22431521; DOI=10.1128/MCB.06726-11;
RA Mamo A., Jules F., Dumaresq-Doiron K., Costantino S., Lefrancois S.;
RT "The role of ceroid lipofuscinosis neuronal protein 5 (CLN5) in
RT endosomal sorting.";
RL Mol. Cell. Biol. 32:1855-1866(2012).
RN [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-814 AND SER-825, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [36]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 78-756 IN COMPLEX WITH NTS,
RP SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-406 AND ASN-582.
RX PubMed=19122660; DOI=10.1038/nsmb.1543;
RA Quistgaard E.M., Madsen P., Groftehauge M.K., Nissen P.,
RA Petersen C.M., Thirup S.S.;
RT "Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller
RT domain.";
RL Nat. Struct. Mol. Biol. 16:96-98(2009).
CC -!- FUNCTION: Functions as a sorting receptor in the Golgi compartment
CC and as a clearance receptor on the cell surface. Required for
CC protein transport from the Golgi apparatus to the lysosomes by a
CC pathway that is independent of the mannose-6-phosphate receptor
CC (M6PR). Also required for protein transport from the Golgi
CC apparatus to the endosomes. Promotes neuronal apoptosis by
CC mediating endocytosis of the proapoptotic precursor forms of BDNF
CC (proBDNF) and NGFB (proNGFB). Also acts as a receptor for
CC neurotensin. May promote mineralization of the extracellular
CC matrix during osteogenic differentiation by scavenging
CC extracellular LPL. Probably required in adipocytes for the
CC formation of specialized storage vesicles containing the glucose
CC transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These
CC vesicles provide a stable pool of SLC2A4 and confer increased
CC responsiveness to insulin. May also mediate transport from the
CC endoplasmic reticulum to the Golgi. {ECO:0000269|PubMed:10085125,
CC ECO:0000269|PubMed:11331584, ECO:0000269|PubMed:11390366,
CC ECO:0000269|PubMed:12209882, ECO:0000269|PubMed:12598608,
CC ECO:0000269|PubMed:14657016, ECO:0000269|PubMed:14985763,
CC ECO:0000269|PubMed:15313463, ECO:0000269|PubMed:15930396,
CC ECO:0000269|PubMed:15987945}.
CC -!- SUBUNIT: Interacts with LPL and SLC2A4 (By similarity). Interacts
CC with the cytosolic adapter proteins GGA1 and GGA2. Interacts with
CC numerous ligands including the receptor-associated protein
CC LRPAP1/RAP, GM2A and NTS. Forms a complex with NGFR which binds
CC specifically to the precursor forms of NGFB (proNGFB) and BDNF
CC (proBDNF). Interacts with the Trk receptors NTRK1, NTRK2 and
CC NTRK3; may regulate their anterograde axonal transport and
CC signaling. Interacts with CLN5 (PubMed:22431521). Interacts with
CC PSAP (PubMed:22431521, PubMed:14657016).
CC {ECO:0000250|UniProtKB:Q6PHU5, ECO:0000269|PubMed:11331584,
CC ECO:0000269|PubMed:11390366, ECO:0000269|PubMed:11859376,
CC ECO:0000269|PubMed:14657016, ECO:0000269|PubMed:14985763,
CC ECO:0000269|PubMed:15364913, ECO:0000269|PubMed:15987945,
CC ECO:0000269|PubMed:19122660, ECO:0000269|PubMed:21102451,
CC ECO:0000269|PubMed:22431521, ECO:0000269|PubMed:9013611,
CC ECO:0000269|PubMed:9657377, ECO:0000269|PubMed:9927419}.
CC -!- INTERACTION:
CC Q9UJY5:GGA1; NbExp=2; IntAct=EBI-1057058, EBI-447141;
CC P11151:LPL (xeno); NbExp=6; IntAct=EBI-1057058, EBI-8794090;
CC P01138:NGF; NbExp=4; IntAct=EBI-1057058, EBI-1028250;
CC P04629:NTRK1; NbExp=3; IntAct=EBI-1057058, EBI-1028226;
CC Q16288:NTRK3; NbExp=2; IntAct=EBI-1057058, EBI-3936704;
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC protein. Endoplasmic reticulum membrane {ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000305}. Endosome membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass
CC type I membrane protein {ECO:0000305}. Nucleus membrane
CC {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
CC Cell membrane; Single-pass type I membrane protein; Extracellular
CC side. Lysosome membrane {ECO:0000305}; Single-pass type I membrane
CC protein {ECO:0000305}. Note=Localized to membranes of the
CC endoplasmic reticulum, endosomes, Golgi stack, lysosomes and
CC nucleus. A small fraction of the protein is also localized to the
CC plasma membrane. May also be found in SLC2A4/GLUT4 storage
CC vesicles (GSVs) in adipocytes. Localization to the plasma membrane
CC in adipocytes may be enhanced by insulin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q99523-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q99523-2; Sequence=VSP_046239, VSP_046240;
CC Note=No experimental confirmation available.;
CC -!- TISSUE SPECIFICITY: Expressed in brain and prostate (at protein
CC level). Expressed at high levels in brain, spinal cord, heart,
CC skeletal muscle, thyroid, placenta and testis. Expressed at lower
CC levels in lymphoid organs, kidney, colon and liver.
CC {ECO:0000269|PubMed:20048080, ECO:0000269|PubMed:9013611}.
CC -!- INDUCTION: During osteoblast differentiation.
CC {ECO:0000269|PubMed:12209882}.
CC -!- DOMAIN: The N-terminal propeptide may facilitate precursor
CC transport within the Golgi stack. Intrachain binding of the N-
CC terminal propeptide and the extracellular domain may also inhibit
CC premature ligand binding.
CC -!- DOMAIN: The extracellular domain may be shed following protease
CC cleavage in some cell types.
CC -!- PTM: The N-terminal propeptide is cleaved by furin and possibly
CC other homologous proteases. {ECO:0000269|PubMed:12419319,
CC ECO:0000269|PubMed:9927419}.
CC -!- POLYMORPHISM: Genetic variations in SORT1 influence low density
CC lipoprotein cholesterol (LDL-C) variability and contribute to the
CC low density lipoprotein cholesterol level quantitative trait locus
CC 6 (LDLCQ6) [MIM:613589].
CC -!- DISEASE: Note=A common polymorphism located in a non-coding region
CC between CELSR2 and PSRC1 alters a CEBP transcription factor
CC binding site and is responsible for changes in hepatic expression
CC of SORT1. Altered SORT1 expression in liver affects low density
CC lipoprotein cholesterol levels in plasma and is associated with
CC susceptibility to myocardial infarction.
CC -!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORT1
CC subfamily. {ECO:0000305}.
CC -!- SIMILARITY: Contains 9 BNR repeats. {ECO:0000305}.
DR EMBL; X98248; CAA66904.2; -; mRNA.
DR EMBL; FJ525881; ACN81319.1; -; Genomic_DNA.
DR EMBL; AK301548; BAG63045.1; -; mRNA.
DR EMBL; AL390252; CAI13180.1; -; Genomic_DNA.
DR EMBL; BC023542; AAH23542.1; -; mRNA.
DR CCDS; CCDS55618.1; -. [Q99523-2]
DR CCDS; CCDS798.1; -. [Q99523-1]
DR RefSeq; NP_001192157.1; NM_001205228.1. [Q99523-2]
DR RefSeq; NP_002950.3; NM_002959.6. [Q99523-1]
DR UniGene; Hs.485195; -.
DR UniGene; Hs.703487; -.
DR PDB; 3F6K; X-ray; 2.00 A; A=78-756.
DR PDB; 3G2U; X-ray; 2.30 A; C/D=819-831.
DR PDB; 3G2V; X-ray; 2.10 A; C/D=819-831.
DR PDB; 4MSL; X-ray; 2.70 A; A=78-756.
DR PDB; 4N7E; X-ray; 2.70 A; A=78-756.
DR PDB; 4PO7; X-ray; 2.66 A; A=78-756.
DR PDBsum; 3F6K; -.
DR PDBsum; 3G2U; -.
DR PDBsum; 3G2V; -.
DR PDBsum; 4MSL; -.
DR PDBsum; 4N7E; -.
DR PDBsum; 4PO7; -.
DR ProteinModelPortal; Q99523; -.
DR SMR; Q99523; -.
DR BioGrid; 112180; 128.
DR DIP; DIP-41798N; -.
DR IntAct; Q99523; 136.
DR MINT; MINT-197682; -.
DR STRING; 9606.ENSP00000256637; -.
DR BindingDB; Q99523; -.
DR ChEMBL; CHEMBL3091; -.
DR iPTMnet; Q99523; -.
DR PhosphoSitePlus; Q99523; -.
DR SwissPalm; Q99523; -.
DR BioMuta; SORT1; -.
DR DMDM; 84028263; -.
DR EPD; Q99523; -.
DR MaxQB; Q99523; -.
DR PaxDb; Q99523; -.
DR PeptideAtlas; Q99523; -.
DR PRIDE; Q99523; -.
DR DNASU; 6272; -.
DR Ensembl; ENST00000256637; ENSP00000256637; ENSG00000134243. [Q99523-1]
DR Ensembl; ENST00000538502; ENSP00000438597; ENSG00000134243. [Q99523-2]
DR GeneID; 6272; -.
DR KEGG; hsa:6272; -.
DR UCSC; uc001dxm.3; human. [Q99523-1]
DR CTD; 6272; -.
DR DisGeNET; 6272; -.
DR GeneCards; SORT1; -.
DR HGNC; HGNC:11186; SORT1.
DR HPA; CAB011498; -.
DR HPA; HPA006889; -.
DR MIM; 602458; gene.
DR MIM; 613589; phenotype.
DR neXtProt; NX_Q99523; -.
DR OpenTargets; ENSG00000134243; -.
DR PharmGKB; PA36023; -.
DR eggNOG; ENOG410ISX8; Eukaryota.
DR eggNOG; ENOG410ZJ6Q; LUCA.
DR GeneTree; ENSGT00510000046443; -.
DR HOGENOM; HOG000231347; -.
DR HOVERGEN; HBG080235; -.
DR InParanoid; Q99523; -.
DR KO; K12388; -.
DR OMA; CDSTAKN; -.
DR OrthoDB; EOG091G0ETU; -.
DR PhylomeDB; Q99523; -.
DR TreeFam; TF324918; -.
DR BioCyc; ZFISH:ENSG00000134243-MONOMER; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR ChiTaRS; SORT1; human.
DR EvolutionaryTrace; Q99523; -.
DR GeneWiki; Sortilin_1; -.
DR GenomeRNAi; 6272; -.
DR PRO; PR:Q99523; -.
DR Proteomes; UP000005640; Chromosome 1.
DR Bgee; ENSG00000134243; -.
DR CleanEx; HS_SORT1; -.
DR ExpressionAtlas; Q99523; baseline and differential.
DR Genevisible; Q99523; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005905; C:clathrin-coated pit; IDA:BHF-UCL.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; IDA:BHF-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0030140; C:trans-Golgi network transport vesicle; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0048406; F:nerve growth factor binding; IPI:BHF-UCL.
DR GO; GO:0010465; F:nerve growth factor receptor activity; IDA:BHF-UCL.
DR GO; GO:0030379; F:neurotensin receptor activity, non-G-protein coupled; IDA:BHF-UCL.
DR GO; GO:0006897; P:endocytosis; IDA:BHF-UCL.
DR GO; GO:0008333; P:endosome to lysosome transport; IDA:BHF-UCL.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IDA:BHF-UCL.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IDA:BHF-UCL.
DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0046323; P:glucose import; IMP:BHF-UCL.
DR GO; GO:0006895; P:Golgi to endosome transport; IDA:BHF-UCL.
DR GO; GO:0007275; P:multicellular organism development; IEA:UniProtKB-KW.
DR GO; GO:0014902; P:myotube differentiation; IMP:BHF-UCL.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; IDA:BHF-UCL.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:BHF-UCL.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR GO; GO:0048227; P:plasma membrane to endosome transport; IDA:BHF-UCL.
DR GO; GO:1904037; P:positive regulation of epithelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0032868; P:response to insulin; IMP:BHF-UCL.
DR GO; GO:0016050; P:vesicle organization; IDA:BHF-UCL.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR031777; Sortilin_C.
DR InterPro; IPR031778; Sortilin_N.
DR InterPro; IPR006581; VPS10.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR Pfam; PF15902; Sortilin-Vps10; 1.
DR Pfam; PF15901; Sortilin_C; 1.
DR SMART; SM00602; VPS10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane;
KW Cleavage on pair of basic residues; Complete proteome;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Disulfide bond; Endocytosis; Endoplasmic reticulum; Endosome;
KW Glycoprotein; Golgi apparatus; Lysosome; Membrane; Nucleus;
KW Osteogenesis; Phosphoprotein; Polymorphism; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix; Transport.
FT SIGNAL 1 33 {ECO:0000250|UniProtKB:O54861}.
FT PROPEP 34 77 Removed in mature form.
FT {ECO:0000269|PubMed:9756851}.
FT /FTId=PRO_0000033162.
FT CHAIN 78 831 Sortilin.
FT /FTId=PRO_0000033163.
FT TOPO_DOM 78 755 Extracellular. {ECO:0000255}.
FT TRANSMEM 756 778 Helical. {ECO:0000255}.
FT TOPO_DOM 779 831 Cytoplasmic. {ECO:0000255}.
FT REPEAT 145 156 BNR 1.
FT REPEAT 198 209 BNR 2.
FT REPEAT 240 251 BNR 3.
FT REPEAT 287 298 BNR 4.
FT REPEAT 328 339 BNR 5.
FT REPEAT 377 388 BNR 6.
FT REPEAT 428 439 BNR 7.
FT REPEAT 506 517 BNR 8.
FT REPEAT 548 559 BNR 9.
FT REGION 50 61 Intrachain binding of the propeptide and
FT the extracellular domain.
FT REGION 612 756 Interactions with LRPAP1 and NGFB.
FT REGION 779 831 Golgi to endosome transport and
FT interactions with GGA1 and GGA2.
FT MOTIF 787 792 Endocytosis signal. {ECO:0000305}.
FT MOD_RES 814 814 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 819 819 Phosphoserine.
FT {ECO:0000244|PubMed:21406692}.
FT MOD_RES 825 825 Phosphoserine.
FT {ECO:0000244|PubMed:18088087,
FT ECO:0000244|PubMed:21406692,
FT ECO:0000244|PubMed:23186163}.
FT CARBOHYD 98 98 N-linked (GlcNAc...). {ECO:0000305}.
FT CARBOHYD 162 162 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:19349973}.
FT CARBOHYD 163 163 N-linked (GlcNAc...); atypical.
FT {ECO:0000269|PubMed:19349973}.
FT CARBOHYD 274 274 N-linked (GlcNAc...). {ECO:0000255}.
FT CARBOHYD 406 406 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:19122660}.
FT CARBOHYD 582 582 N-linked (GlcNAc...).
FT {ECO:0000269|PubMed:19122660}.
FT CARBOHYD 684 684 N-linked (GlcNAc...). {ECO:0000255}.
FT DISULFID 86 556
FT DISULFID 257 277
FT DISULFID 448 458
FT DISULFID 612 651
FT DISULFID 634 666
FT DISULFID 668 723
FT DISULFID 675 688
FT DISULFID 702 740
FT VAR_SEQ 1 136 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_046239.
FT VAR_SEQ 278 279 KA -> T (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_046240.
FT VARIANT 358 358 D -> Y (in dbSNP:rs2228605).
FT /FTId=VAR_053681.
FT MUTAGEN 74 77 RWRR->GWRA: Abrogates propeptide
FT cleavage. {ECO:0000269|PubMed:9927419}.
FT MUTAGEN 76 77 RR->GG: Abrogates propeptide cleavage.
FT {ECO:0000269|PubMed:9927419}.
FT MUTAGEN 792 792 Y->A: Reduces endocytosis and Golgi to
FT endosome sorting; when associated with A-
FT 795. {ECO:0000269|PubMed:11331584}.
FT MUTAGEN 795 795 L->A: Reduces endocytosis and Golgi to
FT endosome sorting; when associated with A-
FT 792. {ECO:0000269|PubMed:11331584}.
FT MUTAGEN 823 824 DD->NN: Reduces interaction with GGA1.
FT {ECO:0000269|PubMed:11390366}.
FT MUTAGEN 825 825 S->A: Reduces interaction with GGA1.
FT {ECO:0000269|PubMed:11390366}.
FT MUTAGEN 826 828 DED->NQN: Abrogates interaction with GGA1
FT and impairs localization to the Golgi.
FT {ECO:0000269|PubMed:11390366}.
FT MUTAGEN 829 830 LL->AA: Abrogates interaction with GGA1
FT and impairs localization to the Golgi.
FT {ECO:0000269|PubMed:11331584,
FT ECO:0000269|PubMed:11390366}.
FT MUTAGEN 829 830 Missing: Abrogates interaction with GGA2.
FT Reduces endocytosis and Golgi to endosome
FT sorting; when associated with A-792 and
FT A-795. {ECO:0000269|PubMed:11331584,
FT ECO:0000269|PubMed:11390366}.
FT CONFLICT 650 650 V -> M (in Ref. 1; CAA66904).
FT {ECO:0000305}.
FT HELIX 92 97 {ECO:0000244|PDB:3F6K}.
FT STRAND 100 106 {ECO:0000244|PDB:3F6K}.
FT STRAND 110 116 {ECO:0000244|PDB:3F6K}.
FT STRAND 118 121 {ECO:0000244|PDB:3F6K}.
FT STRAND 124 130 {ECO:0000244|PDB:3F6K}.
FT STRAND 136 138 {ECO:0000244|PDB:4PO7}.
FT STRAND 141 149 {ECO:0000244|PDB:3F6K}.
FT HELIX 158 161 {ECO:0000244|PDB:3F6K}.
FT HELIX 168 170 {ECO:0000244|PDB:3F6K}.
FT STRAND 172 174 {ECO:0000244|PDB:3F6K}.
FT STRAND 182 186 {ECO:0000244|PDB:3F6K}.
FT STRAND 196 202 {ECO:0000244|PDB:3F6K}.
FT STRAND 208 211 {ECO:0000244|PDB:3F6K}.
FT STRAND 216 218 {ECO:0000244|PDB:3F6K}.
FT STRAND 221 223 {ECO:0000244|PDB:3F6K}.
FT STRAND 226 234 {ECO:0000244|PDB:3F6K}.
FT STRAND 239 244 {ECO:0000244|PDB:3F6K}.
FT STRAND 247 261 {ECO:0000244|PDB:3F6K}.
FT HELIX 263 265 {ECO:0000244|PDB:4PO7}.
FT STRAND 267 271 {ECO:0000244|PDB:3F6K}.
FT STRAND 273 275 {ECO:0000244|PDB:3F6K}.
FT TURN 277 282 {ECO:0000244|PDB:3F6K}.
FT STRAND 283 291 {ECO:0000244|PDB:3F6K}.
FT STRAND 297 309 {ECO:0000244|PDB:3F6K}.
FT STRAND 312 318 {ECO:0000244|PDB:3F6K}.
FT STRAND 320 322 {ECO:0000244|PDB:4PO7}.
FT STRAND 325 332 {ECO:0000244|PDB:3F6K}.
FT STRAND 351 356 {ECO:0000244|PDB:3F6K}.
FT STRAND 361 366 {ECO:0000244|PDB:3F6K}.
FT STRAND 368 370 {ECO:0000244|PDB:4PO7}.
FT STRAND 372 379 {ECO:0000244|PDB:3F6K}.
FT STRAND 385 395 {ECO:0000244|PDB:3F6K}.
FT TURN 397 399 {ECO:0000244|PDB:3F6K}.
FT STRAND 414 419 {ECO:0000244|PDB:3F6K}.
FT STRAND 421 423 {ECO:0000244|PDB:4N7E}.
FT STRAND 425 432 {ECO:0000244|PDB:3F6K}.
FT STRAND 438 441 {ECO:0000244|PDB:3F6K}.
FT STRAND 453 456 {ECO:0000244|PDB:4PO7}.
FT STRAND 459 462 {ECO:0000244|PDB:3F6K}.
FT HELIX 465 469 {ECO:0000244|PDB:3F6K}.
FT STRAND 488 497 {ECO:0000244|PDB:3F6K}.
FT STRAND 504 510 {ECO:0000244|PDB:3F6K}.
FT STRAND 516 521 {ECO:0000244|PDB:3F6K}.
FT STRAND 523 528 {ECO:0000244|PDB:3F6K}.
FT HELIX 529 531 {ECO:0000244|PDB:3F6K}.
FT STRAND 533 538 {ECO:0000244|PDB:3F6K}.
FT STRAND 546 552 {ECO:0000244|PDB:3F6K}.
FT STRAND 558 561 {ECO:0000244|PDB:3F6K}.
FT STRAND 567 573 {ECO:0000244|PDB:3F6K}.
FT STRAND 581 590 {ECO:0000244|PDB:3F6K}.
FT STRAND 595 603 {ECO:0000244|PDB:3F6K}.
FT HELIX 604 606 {ECO:0000244|PDB:3F6K}.
FT HELIX 614 616 {ECO:0000244|PDB:3F6K}.
FT STRAND 617 621 {ECO:0000244|PDB:3F6K}.
FT TURN 630 633 {ECO:0000244|PDB:3F6K}.
FT STRAND 638 645 {ECO:0000244|PDB:3F6K}.
FT STRAND 661 665 {ECO:0000244|PDB:3F6K}.
FT HELIX 670 672 {ECO:0000244|PDB:3F6K}.
FT STRAND 673 675 {ECO:0000244|PDB:3F6K}.
FT STRAND 683 685 {ECO:0000244|PDB:3F6K}.
FT HELIX 696 704 {ECO:0000244|PDB:3F6K}.
FT HELIX 707 710 {ECO:0000244|PDB:3F6K}.
FT STRAND 714 717 {ECO:0000244|PDB:3F6K}.
FT STRAND 724 726 {ECO:0000244|PDB:4MSL}.
FT STRAND 734 736 {ECO:0000244|PDB:3F6K}.
FT HELIX 737 740 {ECO:0000244|PDB:3F6K}.
FT HELIX 741 743 {ECO:0000244|PDB:3F6K}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 143 572 ipfam:Sortilin-Vps10 [T]
FT MYHIT 575 740 ipfam:Sortilin_C [T]
FT MYHIT 133 745 ismart:VPS10 [T]
SQ SEQUENCE 831 AA; 92068 MW; 91F96A3035A4B43A CRC64;
MERPWGAADG LSRWPHGLGL LLLLQLLPPS TLSQDRLDAP PPPAAPLPRW SGPIGVSWGL
RAAAAGGAFP RGGRWRRSAP GEDEECGRVR DFVAKLANNT HQHVFDDLRG SVSLSWVGDS
TGVILVLTTF HVPLVIMTFG QSKLYRSEDY GKNFKDITDL INNTFIRTEF GMAIGPENSG
KVVLTAEVSG GSRGGRIFRS SDFAKNFVQT DLPFHPLTQM MYSPQNSDYL LALSTENGLW
VSKNFGGKWE EIHKAVCLAK WGSDNTIFFT TYANGSCKAD LGALELWRTS DLGKSFKTIG
VKIYSFGLGG RFLFASVMAD KDTTRRIHVS TDQGDTWSMA QLPSVGQEQF YSILAANDDM
VFMHVDEPGD TGFGTIFTSD DRGIVYSKSL DRHLYTTTGG ETDFTNVTSL RGVYITSVLS
EDNSIQTMIT FDQGGRWTHL RKPENSECDA TAKNKNECSL HIHASYSISQ KLNVPMAPLS
EPNAVGIVIA HGSVGDAISV MVPDVYISDD GGYSWTKMLE GPHYYTILDS GGIIVAIEHS
SRPINVIKFS TDEGQCWQTY TFTRDPIYFT GLASEPGARS MNISIWGFTE SFLTSQWVSY
TIDFKDILER NCEEKDYTIW LAHSTDPEDY EDGCILGYKE QFLRLRKSSV CQNGRDYVVT
KQPSICLCSL EDFLCDFGYY RPENDSKCVE QPELKGHDLE FCLYGREEHL TTNGYRKIPG
DKCQGGVNPV REVKDLKKKC TSNFLSPEKQ NSKSNSVPII LAIVGLMLVT VVAGVLIVKK
YVCGGRFLVH RYSVLQQHAE ANGVDGVDAL DTASHTNKSG YHDDSDEDLL E
//
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