ID MARH3_HUMAN Reviewed; 253 AA.
AC Q86UD3; A8K264; B9EJE7;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 12-APR-2017, entry version 123.
DE RecName: Full=E3 ubiquitin-protein ligase MARCH3;
DE EC=2.3.2.27;
DE AltName: Full=Membrane-associated RING finger protein 3;
DE AltName: Full=Membrane-associated RING-CH protein III;
DE Short=MARCH-III;
DE AltName: Full=RING finger protein 173;
DE AltName: Full=RING-type E3 ubiquitin transferase MARCH3 {ECO:0000305};
GN Name=MARCH3; Synonyms=RNF173;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP GLN-68.
RC TISSUE=Thalamus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16428329; DOI=10.1093/jb/mvj012;
RA Fukuda H., Nakamura N., Hirose S.;
RT "MARCH-III is a novel component of endosomes with properties similar
RT to those of MARCH-II.";
RL J. Biochem. 139:137-145(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237 AND SER-243, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which may be involved in
CC endosomal trafficking. E3 ubiquitin ligases accept ubiquitin from
CC an E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC then directly transfer the ubiquitin to targeted substrates.
CC {ECO:0000250|UniProtKB:Q5XIE5}.
CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
CC enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC protein]-L-lysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with MARCH2 and STX6. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:16428329}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16428329}. Early endosome membrane
CC {ECO:0000269|PubMed:16428329}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16428329}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86UD3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86UD3-2; Sequence=VSP_055451, VSP_055452;
CC Note=No experimental confirmation available.;
CC -!- DOMAIN: The RING-CH-type zinc finger domain is required for E3
CC ligase activity. {ECO:0000255|PROSITE-ProRule:PRU00623}.
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DR EMBL; AK290129; BAF82818.1; -; mRNA.
DR EMBL; AC004507; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005221; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC137794; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62412.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62413.1; -; Genomic_DNA.
DR EMBL; BC047569; AAH47569.1; -; mRNA.
DR EMBL; BC146948; AAI46949.1; -; mRNA.
DR EMBL; BC146964; AAI46965.1; -; mRNA.
DR CCDS; CCDS4141.1; -. [Q86UD3-1]
DR RefSeq; NP_848545.1; NM_178450.4. [Q86UD3-1]
DR UniGene; Hs.132441; -.
DR ProteinModelPortal; Q86UD3; -.
DR SMR; Q86UD3; -.
DR BioGrid; 125416; 8.
DR IntAct; Q86UD3; 10.
DR STRING; 9606.ENSP00000309141; -.
DR iPTMnet; Q86UD3; -.
DR PhosphoSitePlus; Q86UD3; -.
DR DMDM; 59798460; -.
DR PaxDb; Q86UD3; -.
DR PRIDE; Q86UD3; -.
DR Ensembl; ENST00000308660; ENSP00000309141; ENSG00000173926. [Q86UD3-1]
DR Ensembl; ENST00000515241; ENSP00000421979; ENSG00000173926. [Q86UD3-2]
DR GeneID; 115123; -.
DR KEGG; hsa:115123; -.
DR UCSC; uc003kuf.4; human. [Q86UD3-1]
DR CTD; 115123; -.
DR GeneCards; MARCH3; -.
DR HGNC; HGNC:28728; MARCH3.
DR HPA; HPA043406; -.
DR MIM; 613333; gene.
DR neXtProt; NX_Q86UD3; -.
DR OpenTargets; ENSG00000173926; -.
DR PharmGKB; PA134901491; -.
DR eggNOG; KOG1609; Eukaryota.
DR eggNOG; COG5183; LUCA.
DR GeneTree; ENSGT00730000110355; -.
DR HOGENOM; HOG000293394; -.
DR HOVERGEN; HBG052411; -.
DR InParanoid; Q86UD3; -.
DR KO; K10658; -.
DR OMA; TVEDCSS; -.
DR OrthoDB; EOG091G14LW; -.
DR PhylomeDB; Q86UD3; -.
DR TreeFam; TF319557; -.
DR UniPathway; UPA00143; -.
DR GenomeRNAi; 115123; -.
DR PRO; PR:Q86UD3; -.
DR Proteomes; UP000005640; Chromosome 5.
DR Bgee; ENSG00000173926; -.
DR CleanEx; HS_MARCH3; -.
DR Genevisible; Q86UD3; HS.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005764; C:lysosome; IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR033275; MARCH-like.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23012; PTHR23012; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasmic vesicle;
KW Endocytosis; Endosome; Membrane; Metal-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 253 E3 ubiquitin-protein ligase MARCH3.
FT /FTId=PRO_0000055927.
FT TRANSMEM 145 165 Helical. {ECO:0000255}.
FT TRANSMEM 182 202 Helical. {ECO:0000255}.
FT ZN_FING 63 123 RING-CH-type. {ECO:0000255|PROSITE-
FT ProRule:PRU00623}.
FT MOD_RES 237 237 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT MOD_RES 243 243 Phosphoserine.
FT {ECO:0000244|PubMed:23186163}.
FT VAR_SEQ 132 138 WLRNPGP -> VSKWGTS (in isoform 2).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_055451.
FT VAR_SEQ 139 253 Missing (in isoform 2).
FT {ECO:0000303|PubMed:15489334}.
FT /FTId=VSP_055452.
FT VARIANT 68 68 R -> Q (in dbSNP:rs34821177).
FT {ECO:0000269|PubMed:14702039}.
FT /FTId=VAR_053639.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 63 123 iprf:ZF_RING_CH [T]
FT MYHIT 71 116 ipfam:RINGv [T]
FT MYHIT 70 117 ismart:RINGv [T]
SQ SEQUENCE 253 AA; 28504 MW; 6E090675CEBC8A88 CRC64;
MTTSRCSHLP EVLPDCTSSA APVVKTVEDC GSLVNGQPQY VMQVSAKDGQ LLSTVVRTLA
TQSPFNDRPM CRICHEGSSQ EDLLSPCECT GTLGTIHRSC LEHWLSSSNT SYCELCHFRF
AVERKPRPLV EWLRNPGPQH EKRTLFGDMV CFLFITPLAT ISGWLCLRGA VDHLHFSSRL
EAVGLIALTV ALFTIYLFWT LVSFRYHCRL YNEWRRTNQR VILLIPKSVN VPSNQPSLLG
LHSVKRNSKE TVV
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