ID STAB2_HUMAN Reviewed; 2551 AA.
AC Q8WWQ8; Q6ZMK2; Q7Z5N9; Q86UR4; Q8IUG9; Q8TES1; Q9H7H7; Q9NRY3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 10-MAY-2017, entry version 147.
DE RecName: Full=Stabilin-2;
DE AltName: Full=FAS1 EGF-like and X-link domain-containing adhesion molecule 2;
DE AltName: Full=Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 2;
DE Short=FEEL-2;
DE AltName: Full=Hyaluronan receptor for endocytosis;
DE Contains:
DE RecName: Full=190 kDa form stabilin-2;
DE AltName: Full=190 kDa hyaluronan receptor for endocytosis;
DE Flags: Precursor;
GN Name=STAB2 {ECO:0000312|EMBL:CAC82105.1};
GN Synonyms=FEEL2 {ECO:0000303|PubMed:12077138},
GN FELL {ECO:0000303|Ref.7}, FEX2 {ECO:0000303|Ref.3},
GN HARE {ECO:0000312|EMBL:AAO39681.1};
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] {ECO:0000312|EMBL:CAC82105.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT HIS-510.
RX PubMed=11829752; DOI=10.1042/0264-6021:3620155;
RA Politz O., Gratchev A., McCourt P.A.G., Schledzewski K., Guillot P.,
RA Johansson S., Svineng G., Franke P., Kannicht C., Kzhyshkowska J.,
RA Longati P., Velten F.W., Johansson S., Goerdt S.;
RT "Stabilin-1 and -2 constitute a novel family of fasciclin-like
RT hyaluronan receptor homologues.";
RL Biochem. J. 362:155-164(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAC15608.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND VARIANT
RP HIS-510.
RX PubMed=12077138; DOI=10.1074/jbc.M204277200;
RA Adachi H., Tsujimoto M.;
RT "FEEL-1, a novel scavenger receptor with in vitro bacteria-binding and
RT angiogenesis-modulating activities.";
RL J. Biol. Chem. 277:34264-34270(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAP74958.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Park S.-Y., Kim I.-S.;
RT "FEX2, a novel cell adhesion molecule of Fas-1 superfamily mediates
RT cell-cell interaction.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAB15793.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-2551, AND VARIANT
RP THR-2039.
RC TISSUE=Spleen {ECO:0000312|EMBL:BAB15793.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAP74958.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-2551, AND VARIANTS
RP THR-2039 AND VAL-2401.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human
RT spleen.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAO39681.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1136-2551, PROTEIN SEQUENCE OF
RP 1136-1144; 1257-1269; 1597-1605; 1623-1645; 1652-1660; 1813-1817;
RP 1834-1843; 1914-1918; 1953-1957; 2204-2217; 2211-2215 AND 2355-2367,
RP AND TISSUE SPECIFICITY.
RX PubMed=12626425; DOI=10.1093/glycob/cwg029;
RA Zhou B., McGary C.T., Weigel J.A., Saxena A., Weigel P.H.;
RT "Purification and molecular identification of the human hyaluronan
RT receptor for endocytosis.";
RL Glycobiology 13:339-349(2003).
RN [7] {ECO:0000305, ECO:0000312|EMBL:AAP74958.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1599-2551, AND VARIANT VAL-2401.
RA Tao Q., Zhang W., Cao X.;
RT "Molecular cloning and characterization of human FELL sharing homology
RT with CD44.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PROTEIN SEQUENCE OF 1136-1144, GLYCOSYLATION, SUBCELLULAR LOCATION,
RP AND FUNCTION.
RX PubMed=17145755; DOI=10.1074/jbc.M607787200;
RA Harris E.N., Kyosseva S.V., Weigel J.A., Weigel P.H.;
RT "Expression, processing, and glycosaminoglycan binding activity of the
RT recombinant human 315-kDa hyaluronic acid receptor for endocytosis
RT (HARE).";
RL J. Biol. Chem. 282:2785-2797(2007).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=12473645; DOI=10.1074/jbc.M210211200;
RA Tamura Y., Adachi H., Osuga J., Ohashi K., Yahagi N., Sekiya M.,
RA Okazaki H., Tomita S., Iizuka Y., Shimano H., Nagai R., Kimura S.,
RA Tsujimoto M., Ishibashi S.;
RT "FEEL-1 and FEEL-2 are endocytic receptors for advanced glycation end
RT products.";
RL J. Biol. Chem. 278:12613-12617(2003).
RN [10]
RP FUNCTION.
RX PubMed=15208308; DOI=10.1074/jbc.M405322200;
RA Harris E.N., Weigel J.A., Weigel P.H.;
RT "Endocytic function, glycosaminoglycan specificity, and antibody
RT sensitivity of the recombinant human 190-kDa hyaluronan receptor for
RT endocytosis (HARE).";
RL J. Biol. Chem. 279:36201-36209(2004).
RN [11]
RP FUNCTION.
RX PubMed=15572036; DOI=10.1016/j.yexcr.2004.09.017;
RA Hansen B., Longati P., Elvevold K., Nedredal G.-I., Schledzewski K.,
RA Olsen R., Falkowski M., Kzhyshkowska J., Carlsson F., Johansson S.,
RA Smedsroed B., Goerdt S., Johansson S., McCourt P.;
RT "Stabilin-1 and stabilin-2 are both directed into the early endocytic
RT pathway in hepatic sinusoidal endothelium via interactions with
RT clathrin/AP-2, independent of ligand binding.";
RL Exp. Cell Res. 303:160-173(2005).
RN [12]
RP SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH ALPHA-M/BETA-2 [ITGAM/ITGB2] INTEGRIN.
RX PubMed=17675564; DOI=10.1189/jlb.0107052;
RA Jung M.Y., Park S.Y., Kim I.S.;
RT "Stabilin-2 is involved in lymphocyte adhesion to the hepatic
RT sinusoidal endothelium via the interaction with alphaMbeta2
RT integrin.";
RL J. Leukoc. Biol. 82:1156-1165(2007).
RN [13]
RP ERRATUM.
RA Jung M.Y., Park S.Y., Kim I.S.;
RL J. Leukoc. Biol. 83:438-438(2008).
RN [14]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17962816; DOI=10.1038/sj.cdd.4402242;
RA Park S.Y., Jung M.Y., Kim H.J., Lee S.J., Kim S.Y., Lee B.H.,
RA Kwon T.H., Park R.W., Kim I.S.;
RT "Rapid cell corpse clearance by stabilin-2, a membrane
RT phosphatidylserine receptor.";
RL Cell Death Differ. 15:192-201(2008).
RN [15]
RP INTERACTION WITH TMSB4X.
RX PubMed=18519035; DOI=10.1016/j.febslet.2008.03.058;
RA Lee S.J., So I.S., Park S.Y., Kim I.S.;
RT "Thymosin beta4 is involved in stabilin-2-mediated apoptotic cell
RT engulfment.";
RL FEBS Lett. 582:2161-2166(2008).
RN [16]
RP FUNCTION, AND INTERACTION WITH GULP1.
RX PubMed=18230608; DOI=10.1074/jbc.M709105200;
RA Park S.Y., Kang K.B., Thapa N., Kim S.Y., Lee S.J., Kim I.S.;
RT "Requirement of adaptor protein GULP during stabilin-2-mediated cell
RT corpse engulfment.";
RL J. Biol. Chem. 283:10593-10600(2008).
RN [17]
RP FUNCTION.
RX PubMed=18434317; DOI=10.1074/jbc.M710360200;
RA Harris E.N., Weigel J.A., Weigel P.H.;
RT "The human hyaluronan receptor for endocytosis (HARE/Stabilin-2) is a
RT systemic clearance receptor for heparin.";
RL J. Biol. Chem. 283:17341-17350(2008).
RN [18]
RP FUNCTION.
RX PubMed=18573870; DOI=10.1128/MCB.01993-07;
RA Park S.-Y., Kim S.-Y., Jung M.-Y., Bae D.-J., Kim I.-S.;
RT "Epidermal growth factor-like domain repeat of stabilin-2 recognizes
RT phosphatidylserine during cell corpse clearance.";
RL Mol. Cell. Biol. 28:5288-5298(2008).
RN [19]
RP FUNCTION.
RX PubMed=19359419; DOI=10.1152/ajpgi.90717.2008;
RA Harris E.N., Baggenstoss B.A., Weigel P.H.;
RT "Rat and human HARE/stabilin-2 are clearance receptors for high- and
RT low-molecular-weight heparins.";
RL Am. J. Physiol. 296:G1191-G1199(2009).
RN [20]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1743.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2497, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA Wang L., Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT liver phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Phosphatidylserine receptor that enhances the engulfment
CC of apoptotic cells. Hyaluronan receptor that binds to and mediates
CC endocytosis of hyaluronic acid (HA). Acts also, in different
CC species, as a primary systemic scavenger receptor for heparin
CC (Hep), chondroitin sulfate (CS), dermatan sulfate (DS),
CC nonglycosaminoglycan (GAG), acetylated low-density lipoprotein
CC (AcLDL), pro-collagen propeptides and advanced glycation end
CC products (AGE). May serve to maintain tissue integrity by
CC supporting extracellular matrix turnover or it may contribute to
CC maintaining fluidity of bodily liquids by resorption of
CC hyaluronan. Counter receptor which plays an important role in
CC lymphocyte recruitment in the hepatic vasculature. Binds to both
CC Gram-positive and Gram-negative bacteria and may play a role in
CC defense against bacterial infection. The proteolytically processed
CC 190 kDa form also functions as an endocytosis receptor for heparin
CC internalisation as well as HA and CS.
CC {ECO:0000269|PubMed:12077138, ECO:0000269|PubMed:12473645,
CC ECO:0000269|PubMed:15208308, ECO:0000269|PubMed:15572036,
CC ECO:0000269|PubMed:17145755, ECO:0000269|PubMed:17675564,
CC ECO:0000269|PubMed:17962816, ECO:0000269|PubMed:18230608,
CC ECO:0000269|PubMed:18434317, ECO:0000269|PubMed:18573870,
CC ECO:0000269|PubMed:19359419}.
CC -!- SUBUNIT: Interacts with GULP1 and heparin. Also interacts with
CC alpha-M/beta-2 integrin (ITGAM and ITGB2) and thymosin beta 4
CC (TMSB4X and/or TMSB4Y). {ECO:0000269|PubMed:17675564,
CC ECO:0000269|PubMed:18230608, ECO:0000269|PubMed:18519035}.
CC -!- INTERACTION:
CC P20065:Tmsb4x (xeno); NbExp=3; IntAct=EBI-7945957, EBI-7946048;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17675564};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:17675564}.
CC Cytoplasm {ECO:0000269|PubMed:17145755}. Note=Only a small amount
CC appears to be present at the cell surface (PubMed:17145755).
CC -!- TISSUE SPECIFICITY: Highly expressed in sinusoidal endothelial
CC cells of liver, spleen and lymph nodes. Also expressed in non SEC-
CC cells such as HMDMs (monocyte-derivedmacrophages), HAMs (T-cell
CC leukemia virus type 1-associated myelopathy), and several
CC macrophage cell line. {ECO:0000269|PubMed:11829752,
CC ECO:0000269|PubMed:12077138, ECO:0000269|PubMed:12473645,
CC ECO:0000269|PubMed:12626425, ECO:0000269|PubMed:17675564,
CC ECO:0000269|PubMed:17962816}.
CC -!- DOMAIN: Recognizes phosphatidyl serine via its epidermal growth
CC factor-like domains.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:17145755,
CC ECO:0000269|PubMed:19159218}.
CC -!- PTM: Proteolytically processed to yield a 190 kDa protein.
CC {ECO:0000269|PubMed:12626425}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF82398.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC Sequence=BAD18723.1; Type=Frameshift; Positions=240, 253, 588, 1586; Evidence={ECO:0000305};
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DR EMBL; AJ295695; CAC82105.1; -; mRNA.
DR EMBL; AB052958; BAC15608.1; -; mRNA.
DR EMBL; AY311388; AAP74958.1; -; mRNA.
DR EMBL; AK024503; BAB15793.1; -; mRNA.
DR EMBL; AK074051; BAB84877.1; -; mRNA.
DR EMBL; AK160380; BAD18723.1; ALT_FRAME; mRNA.
DR EMBL; AY227444; AAO39681.1; -; mRNA.
DR EMBL; AF160476; AAF82398.1; ALT_INIT; mRNA.
DR CCDS; CCDS31888.1; -.
DR RefSeq; NP_060034.9; NM_017564.9.
DR UniGene; Hs.408249; -.
DR ProteinModelPortal; Q8WWQ8; -.
DR SMR; Q8WWQ8; -.
DR BioGrid; 120727; 5.
DR IntAct; Q8WWQ8; 2.
DR MINT; MINT-6542238; -.
DR STRING; 9606.ENSP00000373539; -.
DR DrugBank; DB08818; Hyaluronic acid.
DR iPTMnet; Q8WWQ8; -.
DR PhosphoSitePlus; Q8WWQ8; -.
DR BioMuta; STAB2; -.
DR DMDM; 145559531; -.
DR PaxDb; Q8WWQ8; -.
DR PeptideAtlas; Q8WWQ8; -.
DR PRIDE; Q8WWQ8; -.
DR Ensembl; ENST00000388887; ENSP00000373539; ENSG00000136011.
DR GeneID; 55576; -.
DR KEGG; hsa:55576; -.
DR UCSC; uc001tjw.4; human.
DR CTD; 55576; -.
DR DisGeNET; 55576; -.
DR GeneCards; STAB2; -.
DR HGNC; HGNC:18629; STAB2.
DR HPA; HPA026871; -.
DR MIM; 608561; gene.
DR neXtProt; NX_Q8WWQ8; -.
DR OpenTargets; ENSG00000136011; -.
DR PharmGKB; PA38611; -.
DR eggNOG; ENOG410IRWM; Eukaryota.
DR eggNOG; ENOG4110T5S; LUCA.
DR GeneTree; ENSGT00870000136421; -.
DR HOVERGEN; HBG079218; -.
DR InParanoid; Q8WWQ8; -.
DR KO; K19013; -.
DR OMA; KCCKGFY; -.
DR OrthoDB; EOG091G002T; -.
DR PhylomeDB; Q8WWQ8; -.
DR TreeFam; TF331489; -.
DR Reactome; R-HSA-2160916; Hyaluronan uptake and degradation.
DR Reactome; R-HSA-3000497; Scavenging by Class H Receptors.
DR ChiTaRS; STAB2; human.
DR GeneWiki; STAB2; -.
DR GenomeRNAi; 55576; -.
DR PRO; PR:Q8WWQ8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR Bgee; ENSG00000136011; -.
DR CleanEx; HS_STAB2; -.
DR ExpressionAtlas; Q8WWQ8; baseline and differential.
DR Genevisible; Q8WWQ8; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:UniProtKB.
DR GO; GO:0005041; F:low-density lipoprotein receptor activity; IDA:UniProtKB.
DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; NAS:UniProtKB.
DR GO; GO:0005044; F:scavenger receptor activity; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; NAS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0030214; P:hyaluronan catabolic process; TAS:Reactome.
DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:UniProtKB.
DR GO; GO:0030193; P:regulation of blood coagulation; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR Gene3D; 2.30.180.10; -; 7.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR000782; FAS1_domain.
DR InterPro; IPR002049; Laminin_EGF.
DR InterPro; IPR000538; Link_dom.
DR Pfam; PF12947; EGF_3; 7.
DR Pfam; PF02469; Fasciclin; 7.
DR Pfam; PF00193; Xlink; 1.
DR SMART; SM00181; EGF; 22.
DR SMART; SM00179; EGF_CA; 8.
DR SMART; SM00180; EGF_Lam; 5.
DR SMART; SM00554; FAS1; 7.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF82153; SSF82153; 7.
DR PROSITE; PS00022; EGF_1; 7.
DR PROSITE; PS01186; EGF_2; 16.
DR PROSITE; PS50026; EGF_3; 21.
DR PROSITE; PS01248; EGF_LAM_1; 2.
DR PROSITE; PS50213; FAS1; 7.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Endocytosis; Glycoprotein; Hyaluronic acid; Laminin EGF-like domain;
KW Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1 19 {ECO:0000255}.
FT CHAIN 20 2551 Stabilin-2.
FT /FTId=PRO_0000007712.
FT CHAIN 1136 2551 190 kDa form stabilin-2.
FT /FTId=PRO_0000007713.
FT TOPO_DOM 20 2458 Extracellular. {ECO:0000255}.
FT TRANSMEM 2459 2479 Helical. {ECO:0000255}.
FT TOPO_DOM 2480 2551 Cytoplasmic. {ECO:0000255}.
FT DOMAIN 108 148 EGF-like 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 156 193 EGF-like 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 195 236 EGF-like 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 237 276 EGF-like 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 322 362 EGF-like 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 371 505 FAS1 1. {ECO:0000255|PROSITE-
FT ProRule:PRU00082}.
FT DOMAIN 515 652 FAS1 2. {ECO:0000255|PROSITE-
FT ProRule:PRU00082}.
FT DOMAIN 736 776 EGF-like 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 826 866 EGF-like 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 867 909 EGF-like 8. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 910 952 EGF-like 9. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 953 992 EGF-like 10. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 994 1127 FAS1 3. {ECO:0000255|PROSITE-
FT ProRule:PRU00082}.
FT DOMAIN 1137 1265 FAS1 4. {ECO:0000255|PROSITE-
FT ProRule:PRU00082}.
FT DOMAIN 1343 1408 Laminin EGF-like 1. {ECO:0000255}.
FT DOMAIN 1432 1470 EGF-like 11. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 1471 1512 EGF-like 12. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 1513 1554 EGF-like 13. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 1555 1594 EGF-like 14. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 1596 1724 FAS1 5. {ECO:0000255|PROSITE-
FT ProRule:PRU00082}.
FT DOMAIN 1740 1881 FAS1 6. {ECO:0000255|PROSITE-
FT ProRule:PRU00082}.
FT DOMAIN 1957 2022 Laminin EGF-like 2. {ECO:0000255}.
FT DOMAIN 2047 2081 EGF-like 15. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 2082 2122 EGF-like 16. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 2123 2165 EGF-like 17. {ECO:0000255|PROSITE-
FT ProRule:PRU00076}.
FT DOMAIN 2198 2291 Link. {ECO:0000255|PROSITE-
FT ProRule:PRU00323}.
FT DOMAIN 2311 2446 FAS1 7. {ECO:0000255|PROSITE-
FT ProRule:PRU00082}.
FT REGION 2504 2514 Interaction with TMSB4X.
FT {ECO:0000269|PubMed:18519035}.
FT MOD_RES 2497 2497 Phosphoserine.
FT {ECO:0000244|PubMed:24275569}.
FT CARBOHYD 133 133 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 337 337 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 449 449 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 619 619 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 720 720 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 761 761 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 847 847 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 925 925 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1016 1016 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1028 1028 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1100 1100 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1247 1247 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1275 1275 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1367 1367 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1429 1429 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1437 1437 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1465 1465 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1573 1573 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1679 1679 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 1743 1743 N-linked (GlcNAc...) asparagine.
FT {ECO:0000269|PubMed:19159218}.
FT CARBOHYD 1993 1993 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 2064 2064 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 2280 2280 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 2296 2296 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 2336 2336 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 2368 2368 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 2382 2382 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT CARBOHYD 2393 2393 N-linked (GlcNAc...) asparagine.
FT {ECO:0000255}.
FT DISULFID 112 126 {ECO:0000250}.
FT DISULFID 120 136 {ECO:0000250}.
FT DISULFID 138 147 {ECO:0000250}.
FT DISULFID 160 171 {ECO:0000250}.
FT DISULFID 164 181 {ECO:0000250}.
FT DISULFID 183 192 {ECO:0000250}.
FT DISULFID 199 210 {ECO:0000250}.
FT DISULFID 204 222 {ECO:0000250}.
FT DISULFID 224 235 {ECO:0000250}.
FT DISULFID 241 252 {ECO:0000250}.
FT DISULFID 246 262 {ECO:0000250}.
FT DISULFID 264 275 {ECO:0000250}.
FT DISULFID 326 338 {ECO:0000250}.
FT DISULFID 332 348 {ECO:0000250}.
FT DISULFID 350 361 {ECO:0000250}.
FT DISULFID 740 754 {ECO:0000250}.
FT DISULFID 748 764 {ECO:0000250}.
FT DISULFID 766 775 {ECO:0000250}.
FT DISULFID 830 843 {ECO:0000250}.
FT DISULFID 837 852 {ECO:0000250}.
FT DISULFID 854 865 {ECO:0000250}.
FT DISULFID 871 885 {ECO:0000250}.
FT DISULFID 879 895 {ECO:0000250}.
FT DISULFID 897 908 {ECO:0000250}.
FT DISULFID 914 928 {ECO:0000250}.
FT DISULFID 922 938 {ECO:0000250}.
FT DISULFID 940 951 {ECO:0000250}.
FT DISULFID 957 970 {ECO:0000250}.
FT DISULFID 964 980 {ECO:0000250}.
FT DISULFID 1348 1362 {ECO:0000250}.
FT DISULFID 1356 1372 {ECO:0000250}.
FT DISULFID 1374 1383 {ECO:0000250}.
FT DISULFID 1395 1406 {ECO:0000250}.
FT DISULFID 1399 1416 {ECO:0000250}.
FT DISULFID 1418 1427 {ECO:0000250}.
FT DISULFID 1436 1446 {ECO:0000250}.
FT DISULFID 1440 1456 {ECO:0000250}.
FT DISULFID 1458 1469 {ECO:0000250}.
FT DISULFID 1475 1488 {ECO:0000250}.
FT DISULFID 1482 1498 {ECO:0000250}.
FT DISULFID 1500 1511 {ECO:0000250}.
FT DISULFID 1517 1530 {ECO:0000250}.
FT DISULFID 1524 1540 {ECO:0000250}.
FT DISULFID 1542 1553 {ECO:0000250}.
FT DISULFID 1559 1572 {ECO:0000250}.
FT DISULFID 1566 1582 {ECO:0000250}.
FT DISULFID 1962 1976 {ECO:0000250}.
FT DISULFID 1970 1986 {ECO:0000250}.
FT DISULFID 1988 1997 {ECO:0000250}.
FT DISULFID 2009 2020 {ECO:0000250}.
FT DISULFID 2014 2030 {ECO:0000250}.
FT DISULFID 2032 2041 {ECO:0000250}.
FT DISULFID 2051 2061 {ECO:0000250}.
FT DISULFID 2055 2067 {ECO:0000250}.
FT DISULFID 2069 2080 {ECO:0000250}.
FT DISULFID 2086 2099 {ECO:0000250}.
FT DISULFID 2093 2108 {ECO:0000250}.
FT DISULFID 2110 2121 {ECO:0000250}.
FT DISULFID 2127 2141 {ECO:0000250}.
FT DISULFID 2135 2151 {ECO:0000250}.
FT DISULFID 2153 2164 {ECO:0000250}.
FT DISULFID 2220 2289 {ECO:0000250}.
FT DISULFID 2244 2265 {ECO:0000250}.
FT VARIANT 110 110 I -> V (in dbSNP:rs17034186).
FT /FTId=VAR_048995.
FT VARIANT 306 306 E -> K (in dbSNP:rs12319476).
FT /FTId=VAR_048996.
FT VARIANT 510 510 P -> H (in dbSNP:rs1609860).
FT {ECO:0000269|PubMed:11829752,
FT ECO:0000269|PubMed:12077138}.
FT /FTId=VAR_019541.
FT VARIANT 787 787 R -> Q (in dbSNP:rs17034336).
FT /FTId=VAR_048997.
FT VARIANT 881 881 R -> H (in dbSNP:rs7973658).
FT /FTId=VAR_048998.
FT VARIANT 1736 1736 N -> T (in dbSNP:rs17034433).
FT /FTId=VAR_048999.
FT VARIANT 2039 2039 P -> T (in dbSNP:rs7306642).
FT {ECO:0000269|PubMed:14702039,
FT ECO:0000269|Ref.5}.
FT /FTId=VAR_049000.
FT VARIANT 2401 2401 L -> V (in dbSNP:rs2271637).
FT {ECO:0000269|Ref.5, ECO:0000269|Ref.7}.
FT /FTId=VAR_049001.
FT VARIANT 2519 2519 Y -> S (in dbSNP:rs3751197).
FT /FTId=VAR_049002.
FT CONFLICT 67 67 G -> R (in Ref. 5; BAD18723).
FT {ECO:0000305}.
FT CONFLICT 152 152 D -> A (in Ref. 5; BAD18723).
FT {ECO:0000305}.
FT CONFLICT 887 887 K -> N (in Ref. 5; BAD18723).
FT {ECO:0000305}.
FT CONFLICT 1136 1136 S -> L (in Ref. 8; AA sequence).
FT {ECO:0000305}.
FT CONFLICT 1151 1151 S -> P (in Ref. 1; CAC82105).
FT {ECO:0000305}.
FT CONFLICT 1276 1276 D -> A (in Ref. 1; CAC82105).
FT {ECO:0000305}.
FT CONFLICT 1522 1522 G -> C (in Ref. 5; BAD18723).
FT {ECO:0000305}.
FT CONFLICT 1557 1557 N -> Y (in Ref. 6; AAO39681).
FT {ECO:0000305}.
FT CONFLICT 1599 1600 IY -> HE (in Ref. 7; AAF82398).
FT {ECO:0000305}.
FT CONFLICT 1854 1854 F -> S (in Ref. 5; BAD18723).
FT {ECO:0000305}.
FT CONFLICT 2249 2249 L -> V (in Ref. 5; BAD18723).
FT {ECO:0000305}.
FT CONFLICT 2253 2253 R -> G (in Ref. 5; BAD18723).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 787 824 ismart:EGF [T]
FT MYHIT 1559 1595 ipfam:EGF_3 [T]
FT MYHIT 111 148 ismart:EGF [T]
FT MYHIT 1513 1554 ismart:EGF_CA [T]
FT MYHIT 1558 1596 ismart:EGF [T]
FT MYHIT 1516 1554 ismart:EGF [T]
FT MYHIT 910 952 ismart:EGF_CA [T]
FT MYHIT 2199 2290 ipfam:Xlink [T]
FT MYHIT 527 654 ipfam:Fasciclin [T]
FT MYHIT 1372 1383 ipat:EGF_1 [T]
FT MYHIT 383 505 ipfam:Fasciclin [T]
FT MYHIT 119 160 ismart:EGF_Lam [T]
FT MYHIT 322 362 iprf:EGF_3 [T]
FT MYHIT 2082 2122 iprf:EGF_3 [T]
FT MYHIT 195 236 iprf:EGF_3 [T]
FT MYHIT 764 775 ipat:EGF_1 [T]
FT MYHIT 1471 1512 ismart:EGF_CA [T]
FT MYHIT 1416 1427 ipat:EGF_2 [T]
FT MYHIT 2311 2446 iprf:FAS1 [T]
FT MYHIT 1149 1265 ipfam:Fasciclin [T]
FT MYHIT 1555 1594 iprf:EGF_3 [T]
FT MYHIT 1345 1395 ismart:EGF_Lam [T]
FT MYHIT 1391 1428 iprf:EGF_3 [T]
FT MYHIT 736 776 ismart:EGF [T]
FT MYHIT 1958 1998 iprf:EGF_3 [T]
FT MYHIT 1372 1406 ipat:EGF_LAM_1 [T]
FT MYHIT 554 655 ismart:FAS1 [T]
FT MYHIT 2220 2265 ipat:LINK_1 [T]
FT MYHIT 2126 2165 ismart:EGF [T]
FT MYHIT 867 909 iprf:EGF_3 [T]
FT MYHIT 2123 2165 ismart:EGF_CA [T]
FT MYHIT 2030 2041 ipat:EGF_2 [T]
FT MYHIT 2198 2291 iprf:LINK_2 [T]
FT MYHIT 1958 1998 ismart:EGF [T]
FT MYHIT 1347 1384 ismart:EGF [T]
FT MYHIT 1456 1469 ipat:EGF_2 [T]
FT MYHIT 371 505 iprf:FAS1 [T]
FT MYHIT 1754 1882 ipfam:Fasciclin [T]
FT MYHIT 994 1127 iprf:FAS1 [T]
FT MYHIT 1968 2009 ismart:EGF_Lam [T]
FT MYHIT 108 148 iprf:EGF_3 [T]
FT MYHIT 2085 2122 ismart:EGF [T]
FT MYHIT 2030 2041 ipat:EGF_1 [T]
FT MYHIT 870 909 ismart:EGF [T]
FT MYHIT 1986 1997 ipat:EGF_1 [T]
FT MYHIT 159 193 ismart:EGF [T]
FT MYHIT 1346 1384 iprf:EGF_3 [T]
FT MYHIT 136 147 ipat:EGF_1 [T]
FT MYHIT 867 909 ismart:EGF_CA [T]
FT MYHIT 1513 1554 iprf:EGF_3 [T]
FT MYHIT 325 362 ismart:EGF [T]
FT MYHIT 2196 2291 ismart:LINK [T]
FT MYHIT 1432 1470 iprf:EGF_3 [T]
FT MYHIT 156 193 iprf:EGF_3 [T]
FT MYHIT 953 992 iprf:EGF_3 [T]
FT MYHIT 895 908 ipat:EGF_2 [T]
FT MYHIT 1474 1512 ismart:EGF [T]
FT MYHIT 910 952 iprf:EGF_3 [T]
FT MYHIT 1596 1724 iprf:FAS1 [T]
FT MYHIT 1394 1428 ismart:EGF [T]
FT MYHIT 1498 1511 ipat:EGF_2 [T]
FT MYHIT 2005 2042 iprf:EGF_3 [T]
FT MYHIT 736 776 ismart:EGF_CA [T]
FT MYHIT 2132 2164 ipfam:EGF_3 [T]
FT MYHIT 406 508 ismart:FAS1 [T]
FT MYHIT 515 652 iprf:FAS1 [T]
FT MYHIT 1475 1511 ipfam:EGF_3 [T]
FT MYHIT 2123 2165 iprf:EGF_3 [T]
FT MYHIT 348 361 ipat:EGF_2 [T]
FT MYHIT 198 236 ismart:EGF [T]
FT MYHIT 2356 2449 ismart:FAS1 [T]
FT MYHIT 2008 2042 ismart:EGF [T]
FT MYHIT 829 866 ismart:EGF [T]
FT MYHIT 1618 1726 ipfam:Fasciclin [T]
FT MYHIT 245 275 ipfam:EGF_3 [T]
FT MYHIT 1008 1129 ipfam:Fasciclin [T]
FT MYHIT 1173 1268 ismart:FAS1 [T]
FT MYHIT 938 951 ipat:EGF_2 [T]
FT MYHIT 2108 2121 ipat:EGF_2 [T]
FT MYHIT 262 275 ipat:EGF_2 [T]
FT MYHIT 1517 1553 ipfam:EGF_3 [T]
FT MYHIT 2086 2121 ipfam:EGF_3 [T]
FT MYHIT 1631 1727 ismart:FAS1 [T]
FT MYHIT 913 952 ismart:EGF [T]
FT MYHIT 181 192 ipat:EGF_1 [T]
FT MYHIT 2047 2081 iprf:EGF_3 [T]
FT MYHIT 237 276 iprf:EGF_3 [T]
FT MYHIT 1137 1265 iprf:FAS1 [T]
FT MYHIT 956 994 ismart:EGF [T]
FT MYHIT 1030 1130 ismart:FAS1 [T]
FT MYHIT 237 276 ismart:EGF_CA [T]
FT MYHIT 1432 1470 ismart:EGF_CA [T]
FT MYHIT 826 866 iprf:EGF_3 [T]
FT MYHIT 957 993 ipfam:EGF_3 [T]
FT MYHIT 1778 1884 ismart:FAS1 [T]
FT MYHIT 852 865 ipat:EGF_2 [T]
FT MYHIT 2012 2069 ismart:EGF_Lam [T]
FT MYHIT 736 776 iprf:EGF_3 [T]
FT MYHIT 164 222 ismart:EGF_Lam [T]
FT MYHIT 2355 2446 ipfam:Fasciclin [T]
FT MYHIT 1416 1427 ipat:EGF_1 [T]
FT MYHIT 2050 2081 ismart:EGF [T]
FT MYHIT 1471 1512 iprf:EGF_3 [T]
FT MYHIT 240 276 ismart:EGF [T]
FT MYHIT 1435 1470 ismart:EGF [T]
FT MYHIT 1740 1881 iprf:FAS1 [T]
SQ SEQUENCE 2551 AA; 276988 MW; 3ACB6A6C3CB80044 CRC64;
MMLQHLVIFC LGLVVQNFCS PAETTGQARR CDRKSLLTIR TECRSCALNL GVKCPDGYTM
ITSGSVGVRD CRYTFEVRTY SLSLPGCRHI CRKDYLQPRC CPGRWGPDCI ECPGGAGSPC
NGRGSCAEGM EGNGTCSCQE GFGGTACETC ADDNLFGPSC SSVCNCVHGV CNSGLDGDGT
CECYSAYTGP KCDKPIPECA ALLCPENSRC SPSTEDENKL ECKCLPNYRG DGKYCDPINP
CLRKICHPHA HCTYLGPNRH SCTCQEGYRG DGQVCLPVDP CQINFGNCPT KSTVCKYDGP
GQSHCECKEH YQNFVPGVGC SMTDICKSDN PCHRNANCTT VAPGRTECIC QKGYVGDGLT
CYGNIMERLR ELNTEPRGKW QGRLTSFISL LDKAYAWPLS KLGPFTVLLP TDKGLKGFNV
NELLVDNKAA QYFVKLHIIA GQMNIEYMNN TDMFYTLTGK SGEIFNSDKD NQIKLKLHGG
KKKVKIIQGD IIASNGLLHI LDRAMDKLEP TFESNNEQTI MTMLQPRYSK FRSLLEETNL
GHALDEDGVG GPYTIFVPNN EALNNMKDGT LDYLLSPEGS RKLLELVRYH IVPFTQLEVA
TLISTPHIRS MANQLIQFNT TDNGQILAND VAMEEIEITA KNGRIYTLTG VLIPPSIVPI
LPHRCDETKR EMKLGTCVSC SLVYWSRCPA NSEPTALFTH RCVYSGRFGS LKSGCARYCN
ATVKIPKCCK GFYGPDCNQC PGGFSNPCSG NGQCADSLGG NGTCICEEGF QGSQCQFCSD
PNKYGPRCNK KCLCVHGTCN NRIDSDGACL TGTCRDGSAG RLCDKQTSAC GPYVQFCHIH
ATCEYSNGTA SCICKAGYEG DGTLCSEMDP CTGLTPGGCS RNAECIKTGT GTHTCVCQQG
WTGNGRDCSE INNCLLPSAG GCHDNASCLY VGPGQNECEC KKGFRGNGID CEPITSCLEQ
TGKCHPLASC QSTSSGVWSC VCQEGYEGDG FLCYGNAAVE LSFLSEAAIF NRWINNASLQ
PTLSATSNLT VLVPSQQATE DMDQDEKSFW LSQSNIPALI KYHMLLGTYR VADLQTLSSS
DMLATSLQGN FLHLAKVDGN ITIEGASIVD GDNAATNGVI HIINKVLVPQ RRLTGSLPNL
LMRLEQMPDY SIFRGYIIQY NLANAIEAAD AYTVFAPNNN AIENYIREKK VLSLEEDVLR
YHVVLEEKLL KNDLHNGMHR ETMLGFSYFL SFFLHNDQLY VNEAPINYTN VATDKGVIHG
LGKVLEIQKN RCDNNDTTII RGRCRTCSSE LTCPFGTKSL GNEKRRCIYT SYFMGRRTLF
IGCQPKCVRT VITRECCAGF FGPQCQPCPG NAQNVCFGNG ICLDGVNGTG VCECGEGFSG
TACETCTEGK YGIHCDQACS CVHGRCNQGP LGDGSCDCDV GWRGVHCDNA TTEDNCNGTC
HTSANCLTNS DGTASCKCAA GFQGNGTICT AINACEISNG GCSAKADCKR TTPGRRVCTC
KAGYTGDGIV CLEINPCLEN HGGCDKNAEC TQTGPNQAAC NCLPAYTGDG KVCTLINVCL
TKNGGCSEFA ICNHTGQVER TCTCKPNYIG DGFTCRGSIY QELPKNPKTS QYFFQLQEHF
VKDLVGPGPF TVFAPLSAAF DEEARVKDWD KYGLMPQVLR YHVVACHQLL LENLKLISNA
TSLQGEPIVI SVSQSTVYIN NKAKIISSDI ISTNGIVHII DKLLSPKNLL ITPKDNSGRI
LQNLTTLATN NGYIKFSNLI QDSGLLSVIT DPIHTPVTLF WPTDQALHAL PAEQQDFLFN
QDNKDKLKEY LKFHVIRDAK VLAVDLPTST AWKTLQGSEL SVKCGAGRDI GDLFLNGQTC
RIVQRELLFD LGVAYGIDCL LIDPTLGGRC DTFTTFDASG ECGSCVNTPS CPRWSKPKGV
KQKCLYNLPF KRNLEGCRER CSLVIQIPRC CKGYFGRDCQ ACPGGPDAPC NNRGVCLDQY
SATGECKCNT GFNGTACEMC WPGRFGPDCL PCGCSDHGQC DDGITGSGQC LCETGWTGPS
CDTQAVLPAV CTPPCSAHAT CKENNTCECN LDYEGDGITC TVVDFCKQDN GGCAKVARCS
QKGTKVSCSC QKGYKGDGHS CTEIDPCADG LNGGCHEHAT CKMTGPGKHK CECKSHYVGD
GLNCEPEQLP IDRCLQDNGQ CHADAKCVDL HFQDTTVGVF HLRSPLGQYK LTFDKAREAC
ANEAATMATY NQLSYAQKAK YHLCSAGWLE TGRVAYPTAF ASQNCGSGVV GIVDYGPRPN
KSEMWDVFCY RMKDVNCTCK VGYVGDGFSC SGNLLQVLMS FPSLTNFLTE VLAYSNSSAR
GRAFLEHLTD LSIRGTLFVP QNSGLGENET LSGRDIEHHL ANVSMFFYND LVNGTTLQTR
LGSKLLITAS QDPLQPTETR FVDGRAILQW DIFASNGIIH VISRPLKAPP APVTLTHTGL
GAGIFFAIIL VTGAVALAAY SYFRINRRTI GFQHFESEED INVAALGKQQ PENISNPLYE
STTSAPPEPS YDPFTDSEER QLEGNDPLRT L
//
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