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 27-MAR-2024, entry version 188. 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}, FELL GN {ECO:0000303|Ref.7}, FEX2 {ECO:0000303|Ref.3}, HARE GN {ECO:0000312|EMBL:AAO39681.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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 hyaluronan RT 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 cell- RT 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 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 THR-2039 RP 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 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 1136-1144; RP 1257-1269; 1597-1605; 1623-1645; 1652-1660; 1813-1817; 1834-1843; RP 1914-1918; 1953-1957; 2204-2217; 2211-2215 AND 2355-2367, AND TISSUE RP 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 receptor RT 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 with RT CD44."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [8] RP PROTEIN SEQUENCE OF 1136-1144, GLYCOSYLATION, SUBCELLULAR LOCATION, AND RP 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 WITH RP 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 sinusoidal RT endothelium via the interaction with alphaMbeta2 integrin."; RL J. Leukoc. Biol. 82:1156-1165(2007). RN [13] RP ERRATUM OF PUBMED:17675564. 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., Kwon T.H., RA Park R.W., Kim I.S.; RT "Rapid cell corpse clearance by stabilin-2, a membrane phosphatidylserine RT 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 corpse RT 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 low- RT 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 multiple RT 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 BY RP 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Phosphatidylserine receptor that enhances the engulfment of CC apoptotic cells. Hyaluronan receptor that binds to and mediates CC endocytosis of hyaluronic acid (HA). Acts also, in different species, CC as a primary systemic scavenger receptor for heparin (Hep), chondroitin CC sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), CC acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides CC and advanced glycation end products (AGE). May serve to maintain tissue CC integrity by supporting extracellular matrix turnover or it may CC contribute to 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 Gram- CC positive and Gram-negative bacteria and may play a role in defense CC against bacterial infection. The proteolytically processed 190 kDa form CC also functions as an endocytosis receptor for heparin internalization CC as well as HA and CS. {ECO:0000269|PubMed:12077138, CC ECO:0000269|PubMed:12473645, ECO:0000269|PubMed:15208308, CC ECO:0000269|PubMed:15572036, ECO:0000269|PubMed:17145755, CC ECO:0000269|PubMed:17675564, ECO:0000269|PubMed:17962816, CC ECO:0000269|PubMed:18230608, ECO:0000269|PubMed:18434317, CC ECO:0000269|PubMed:18573870, ECO:0000269|PubMed:19359419}. CC -!- SUBUNIT: Interacts with GULP1 and heparin. Also interacts with alpha- CC M/beta-2 integrin (ITGAM and ITGB2) and thymosin beta 4 (TMSB4X and/or CC TMSB4Y). {ECO:0000269|PubMed:17675564, ECO:0000269|PubMed:18230608, CC ECO:0000269|PubMed:18519035}. CC -!- INTERACTION: CC Q8WWQ8; 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 cells of CC liver, spleen and lymph nodes. Also expressed in non SEC-cells such as CC HMDMs (monocyte-derivedmacrophages), HAMs (T-cell leukemia virus type CC 1-associated myelopathy), and several macrophage cell line. CC {ECO:0000269|PubMed:11829752, ECO:0000269|PubMed:12077138, CC ECO:0000269|PubMed:12473645, ECO:0000269|PubMed:12626425, CC ECO:0000269|PubMed:17675564, ECO:0000269|PubMed:17962816}. CC -!- DOMAIN: Recognizes phosphatidyl serine via its epidermal growth factor- CC 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=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAD18723.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 5N86; X-ray; 1.48 A; A/B=2311-2449. DR PDBsum; 5N86; -. DR AlphaFoldDB; Q8WWQ8; -. DR SMR; Q8WWQ8; -. DR BioGRID; 120727; 7. DR IntAct; Q8WWQ8; 4. DR MINT; Q8WWQ8; -. DR STRING; 9606.ENSP00000373539; -. DR DrugBank; DB08818; Hyaluronic acid. DR CarbonylDB; Q8WWQ8; -. DR GlyCosmos; Q8WWQ8; 28 sites, No reported glycans. DR GlyGen; Q8WWQ8; 30 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q8WWQ8; -. DR PhosphoSitePlus; Q8WWQ8; -. DR BioMuta; STAB2; -. DR DMDM; 145559531; -. DR EPD; Q8WWQ8; -. DR jPOST; Q8WWQ8; -. DR MassIVE; Q8WWQ8; -. DR PaxDb; 9606-ENSP00000373539; -. DR PeptideAtlas; Q8WWQ8; -. DR ProteomicsDB; 74924; -. DR Antibodypedia; 18052; 182 antibodies from 22 providers. DR DNASU; 55576; -. DR Ensembl; ENST00000388887.7; ENSP00000373539.2; ENSG00000136011.15. DR GeneID; 55576; -. DR KEGG; hsa:55576; -. DR MANE-Select; ENST00000388887.7; ENSP00000373539.2; NM_017564.10; NP_060034.9. DR UCSC; uc001tjw.4; human. DR AGR; HGNC:18629; -. DR CTD; 55576; -. DR DisGeNET; 55576; -. DR GeneCards; STAB2; -. DR HGNC; HGNC:18629; STAB2. DR HPA; ENSG00000136011; Tissue enriched (lymphoid). DR MIM; 608561; gene. DR neXtProt; NX_Q8WWQ8; -. DR OpenTargets; ENSG00000136011; -. DR PharmGKB; PA38611; -. DR VEuPathDB; HostDB:ENSG00000136011; -. DR eggNOG; KOG1218; Eukaryota. DR GeneTree; ENSGT00940000156566; -. DR HOGENOM; CLU_001035_0_0_1; -. DR InParanoid; Q8WWQ8; -. DR OMA; RDCVEIN; -. DR OrthoDB; 2970631at2759; -. DR PhylomeDB; Q8WWQ8; -. DR TreeFam; TF331489; -. DR PathwayCommons; Q8WWQ8; -. DR Reactome; R-HSA-2160916; Hyaluronan uptake and degradation. DR Reactome; R-HSA-3000497; Scavenging by Class H Receptors. DR SignaLink; Q8WWQ8; -. DR BioGRID-ORCS; 55576; 6 hits in 1146 CRISPR screens. DR ChiTaRS; STAB2; human. DR GeneWiki; STAB2; -. DR GenomeRNAi; 55576; -. DR Pharos; Q8WWQ8; Tbio. DR PRO; PR:Q8WWQ8; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q8WWQ8; Protein. DR Bgee; ENSG00000136011; Expressed in spleen and 115 other cell types or tissues. DR ExpressionAtlas; Q8WWQ8; baseline and differential. 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:0005886; C:plasma membrane; IDA:UniProtKB. 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 particle receptor activity; IDA:UniProtKB. DR GO; GO:0015035; F:protein-disulfide reductase 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:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB. DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB. DR GO; GO:0030214; P:hyaluronan catabolic process; IEA:Ensembl. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:UniProtKB. DR CDD; cd03515; Link_domain_TSG_6_like; 1. DR Gene3D; 2.30.180.10; FAS1 domain; 7. DR Gene3D; 2.10.25.10; Laminin; 14. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1. DR Gene3D; 2.170.300.10; Tie2 ligand-binding domain superfamily; 1. DR InterPro; IPR016186; C-type_lectin-like/link_sf. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR024731; EGF_dom. DR InterPro; IPR036378; FAS1_dom_sf. DR InterPro; IPR000782; FAS1_domain. DR InterPro; IPR002049; LE_dom. DR InterPro; IPR000538; Link_dom. DR PANTHER; PTHR24038; STABILIN; 1. DR PANTHER; PTHR24038:SF0; STABILIN-2; 1. DR Pfam; PF12947; EGF_3; 11. 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 SMART; SM00286; PTI; 8. DR SUPFAM; SSF56436; C-type lectin-like; 1. DR SUPFAM; SSF57196; EGF/Laminin; 2. DR SUPFAM; SSF82153; FAS1 domain; 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. DR Genevisible; Q8WWQ8; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Cytoplasm; Direct protein sequencing; KW Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; KW Hyaluronic acid; Laminin EGF-like domain; Membrane; Phosphoprotein; KW Receptor; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..2551 FT /note="Stabilin-2" FT /id="PRO_0000007712" FT CHAIN 1136..2551 FT /note="190 kDa form stabilin-2" FT /id="PRO_0000007713" FT TOPO_DOM 20..2458 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 2459..2479 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 2480..2551 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 108..148 FT /note="EGF-like 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 156..193 FT /note="EGF-like 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 195..236 FT /note="EGF-like 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 237..276 FT /note="EGF-like 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 322..362 FT /note="EGF-like 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 371..505 FT /note="FAS1 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 515..652 FT /note="FAS1 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 736..776 FT /note="EGF-like 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 826..866 FT /note="EGF-like 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 867..909 FT /note="EGF-like 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 910..952 FT /note="EGF-like 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 953..992 FT /note="EGF-like 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 994..1127 FT /note="FAS1 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 1137..1265 FT /note="FAS1 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 1343..1408 FT /note="Laminin EGF-like 1" FT /evidence="ECO:0000255" FT DOMAIN 1432..1470 FT /note="EGF-like 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 1471..1512 FT /note="EGF-like 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 1513..1554 FT /note="EGF-like 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 1555..1594 FT /note="EGF-like 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 1596..1724 FT /note="FAS1 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 1740..1881 FT /note="FAS1 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT DOMAIN 1957..2022 FT /note="Laminin EGF-like 2" FT /evidence="ECO:0000255" FT DOMAIN 2047..2081 FT /note="EGF-like 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 2082..2122 FT /note="EGF-like 16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 2123..2165 FT /note="EGF-like 17" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076" FT DOMAIN 2198..2291 FT /note="Link" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323" FT DOMAIN 2311..2446 FT /note="FAS1 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00082" FT REGION 2504..2514 FT /note="Interaction with TMSB4X" FT /evidence="ECO:0000269|PubMed:18519035" FT REGION 2512..2551 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2512..2530 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2533..2551 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2497 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CARBOHYD 133 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 337 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 449 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 619 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 720 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 761 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 847 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 925 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1016 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1028 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1100 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1247 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1275 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1367 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1429 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1437 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1465 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1573 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1679 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1743 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 1993 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2064 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2280 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2296 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2336 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2368 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2382 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 2393 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 112..126 FT /evidence="ECO:0000250" FT DISULFID 120..136 FT /evidence="ECO:0000250" FT DISULFID 138..147 FT /evidence="ECO:0000250" FT DISULFID 160..171 FT /evidence="ECO:0000250" FT DISULFID 164..181 FT /evidence="ECO:0000250" FT DISULFID 183..192 FT /evidence="ECO:0000250" FT DISULFID 199..210 FT /evidence="ECO:0000250" FT DISULFID 204..222 FT /evidence="ECO:0000250" FT DISULFID 224..235 FT /evidence="ECO:0000250" FT DISULFID 241..252 FT /evidence="ECO:0000250" FT DISULFID 246..262 FT /evidence="ECO:0000250" FT DISULFID 264..275 FT /evidence="ECO:0000250" FT DISULFID 326..338 FT /evidence="ECO:0000250" FT DISULFID 332..348 FT /evidence="ECO:0000250" FT DISULFID 350..361 FT /evidence="ECO:0000250" FT DISULFID 740..754 FT /evidence="ECO:0000250" FT DISULFID 748..764 FT /evidence="ECO:0000250" FT DISULFID 766..775 FT /evidence="ECO:0000250" FT DISULFID 830..843 FT /evidence="ECO:0000250" FT DISULFID 837..852 FT /evidence="ECO:0000250" FT DISULFID 854..865 FT /evidence="ECO:0000250" FT DISULFID 871..885 FT /evidence="ECO:0000250" FT DISULFID 879..895 FT /evidence="ECO:0000250" FT DISULFID 897..908 FT /evidence="ECO:0000250" FT DISULFID 914..928 FT /evidence="ECO:0000250" FT DISULFID 922..938 FT /evidence="ECO:0000250" FT DISULFID 940..951 FT /evidence="ECO:0000250" FT DISULFID 957..970 FT /evidence="ECO:0000250" FT DISULFID 964..980 FT /evidence="ECO:0000250" FT DISULFID 1348..1362 FT /evidence="ECO:0000250" FT DISULFID 1356..1372 FT /evidence="ECO:0000250" FT DISULFID 1374..1383 FT /evidence="ECO:0000250" FT DISULFID 1395..1406 FT /evidence="ECO:0000250" FT DISULFID 1399..1416 FT /evidence="ECO:0000250" FT DISULFID 1418..1427 FT /evidence="ECO:0000250" FT DISULFID 1436..1446 FT /evidence="ECO:0000250" FT DISULFID 1440..1456 FT /evidence="ECO:0000250" FT DISULFID 1458..1469 FT /evidence="ECO:0000250" FT DISULFID 1475..1488 FT /evidence="ECO:0000250" FT DISULFID 1482..1498 FT /evidence="ECO:0000250" FT DISULFID 1500..1511 FT /evidence="ECO:0000250" FT DISULFID 1517..1530 FT /evidence="ECO:0000250" FT DISULFID 1524..1540 FT /evidence="ECO:0000250" FT DISULFID 1542..1553 FT /evidence="ECO:0000250" FT DISULFID 1559..1572 FT /evidence="ECO:0000250" FT DISULFID 1566..1582 FT /evidence="ECO:0000250" FT DISULFID 1962..1976 FT /evidence="ECO:0000250" FT DISULFID 1970..1986 FT /evidence="ECO:0000250" FT DISULFID 1988..1997 FT /evidence="ECO:0000250" FT DISULFID 2009..2020 FT /evidence="ECO:0000250" FT DISULFID 2014..2030 FT /evidence="ECO:0000250" FT DISULFID 2032..2041 FT /evidence="ECO:0000250" FT DISULFID 2051..2061 FT /evidence="ECO:0000250" FT DISULFID 2055..2067 FT /evidence="ECO:0000250" FT DISULFID 2069..2080 FT /evidence="ECO:0000250" FT DISULFID 2086..2099 FT /evidence="ECO:0000250" FT DISULFID 2093..2108 FT /evidence="ECO:0000250" FT DISULFID 2110..2121 FT /evidence="ECO:0000250" FT DISULFID 2127..2141 FT /evidence="ECO:0000250" FT DISULFID 2135..2151 FT /evidence="ECO:0000250" FT DISULFID 2153..2164 FT /evidence="ECO:0000250" FT DISULFID 2220..2289 FT /evidence="ECO:0000250" FT DISULFID 2244..2265 FT /evidence="ECO:0000250" FT VARIANT 110 FT /note="I -> V (in dbSNP:rs17034186)" FT /id="VAR_048995" FT VARIANT 306 FT /note="E -> K (in dbSNP:rs12319476)" FT /id="VAR_048996" FT VARIANT 510 FT /note="P -> H (in dbSNP:rs1609860)" FT /evidence="ECO:0000269|PubMed:11829752, FT ECO:0000269|PubMed:12077138" FT /id="VAR_019541" FT VARIANT 787 FT /note="R -> Q (in dbSNP:rs17034336)" FT /id="VAR_048997" FT VARIANT 881 FT /note="R -> H (in dbSNP:rs7973658)" FT /id="VAR_048998" FT VARIANT 1736 FT /note="N -> T (in dbSNP:rs17034433)" FT /id="VAR_048999" FT VARIANT 2039 FT /note="P -> T (in dbSNP:rs7306642)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5" FT /id="VAR_049000" FT VARIANT 2401 FT /note="L -> V (in dbSNP:rs2271637)" FT /evidence="ECO:0000269|Ref.5, ECO:0000269|Ref.7" FT /id="VAR_049001" FT VARIANT 2519 FT /note="Y -> S (in dbSNP:rs3751197)" FT /id="VAR_049002" FT CONFLICT 67 FT /note="G -> R (in Ref. 5; BAD18723)" FT /evidence="ECO:0000305" FT CONFLICT 152 FT /note="D -> A (in Ref. 5; BAD18723)" FT /evidence="ECO:0000305" FT CONFLICT 887 FT /note="K -> N (in Ref. 5; BAD18723)" FT /evidence="ECO:0000305" FT CONFLICT 1136 FT /note="S -> L (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 1151 FT /note="S -> P (in Ref. 1; CAC82105)" FT /evidence="ECO:0000305" FT CONFLICT 1276 FT /note="D -> A (in Ref. 1; CAC82105)" FT /evidence="ECO:0000305" FT CONFLICT 1522 FT /note="G -> C (in Ref. 5; BAD18723)" FT /evidence="ECO:0000305" FT CONFLICT 1557 FT /note="N -> Y (in Ref. 6; AAO39681)" FT /evidence="ECO:0000305" FT CONFLICT 1599..1600 FT /note="IY -> HE (in Ref. 7; AAF82398)" FT /evidence="ECO:0000305" FT CONFLICT 1854 FT /note="F -> S (in Ref. 5; BAD18723)" FT /evidence="ECO:0000305" FT CONFLICT 2249 FT /note="L -> V (in Ref. 5; BAD18723)" FT /evidence="ECO:0000305" FT CONFLICT 2253 FT /note="R -> G (in Ref. 5; BAD18723)" FT /evidence="ECO:0000305" FT HELIX 2314..2318 FT /evidence="ECO:0007829|PDB:5N86" FT HELIX 2322..2324 FT /evidence="ECO:0007829|PDB:5N86" FT HELIX 2325..2335 FT /evidence="ECO:0007829|PDB:5N86" FT HELIX 2339..2348 FT /evidence="ECO:0007829|PDB:5N86" FT STRAND 2355..2360 FT /evidence="ECO:0007829|PDB:5N86" FT TURN 2362..2364 FT /evidence="ECO:0007829|PDB:5N86" FT HELIX 2373..2377 FT /evidence="ECO:0007829|PDB:5N86" FT HELIX 2388..2390 FT /evidence="ECO:0007829|PDB:5N86" FT STRAND 2396..2399 FT /evidence="ECO:0007829|PDB:5N86" FT STRAND 2404..2410 FT /evidence="ECO:0007829|PDB:5N86" FT STRAND 2415..2417 FT /evidence="ECO:0007829|PDB:5N86" FT STRAND 2419..2422 FT /evidence="ECO:0007829|PDB:5N86" FT STRAND 2425..2434 FT /evidence="ECO:0007829|PDB:5N86" FT STRAND 2437..2444 FT /evidence="ECO:0007829|PDB:5N86" 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 //