ID CD44_HUMAN Reviewed; 742 AA. AC P16070; A5YRN9; B6EAT9; D3DR12; D3DR13; O95370; P22511; Q04858; Q13419; AC Q13957; Q13958; Q13959; Q13960; Q13961; Q13967; Q13968; Q13980; Q15861; AC Q16064; Q16065; Q16066; Q16208; Q16522; Q86T72; Q86Z27; Q8N694; Q92493; AC Q96J24; Q9H5A5; Q9UC28; Q9UC29; Q9UC30; Q9UCB0; Q9UJ36; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 27-MAR-2024, entry version 257. DE RecName: Full=CD44 antigen; DE AltName: Full=CDw44; DE AltName: Full=Epican; DE AltName: Full=Extracellular matrix receptor III; DE Short=ECMR-III; DE AltName: Full=GP90 lymphocyte homing/adhesion receptor; DE AltName: Full=HUTCH-I; DE AltName: Full=Heparan sulfate proteoglycan; DE AltName: Full=Hermes antigen; DE AltName: Full=Hyaluronate receptor; DE AltName: Full=Phagocytic glycoprotein 1; DE Short=PGP-1; DE AltName: Full=Phagocytic glycoprotein I; DE Short=PGP-I; DE AltName: CD_antigen=CD44; DE Flags: Precursor; GN Name=CD44; Synonyms=LHR, MDU2, MDU3, MIC4; 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] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12). RX PubMed=2466575; DOI=10.1016/0092-8674(89)90638-7; RA Stamenkovic I., Amiot M., Pesando J.M., Seed B.; RT "A lymphocyte molecule implicated in lymph node homing is a member of the RT cartilage link protein family."; RL Cell 56:1057-1062(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12). RC TISSUE=Reticulocyte; RX PubMed=1840487; DOI=10.1016/0006-291x(91)91009-2; RA Harn H.-J., Isola N., Cooper D.L.; RT "The multispecific cell adhesion molecule CD44 is represented in RT reticulocyte cDNA."; RL Biochem. Biophys. Res. Commun. 178:1127-1134(1991). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), AND VARIANT THR-479. RX PubMed=1991450; DOI=10.1002/j.1460-2075.1991.tb07955.x; RA Stamenkovic I., Aruffo A., Amiot M., Seed B.; RT "The hematopoietic and epithelial forms of CD44 are distinct polypeptides RT with different adhesion potentials for hyaluronate-bearing cells."; RL EMBO J. 10:343-348(1991). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 11), AND VARIANT THR-479. RC TISSUE=Myeloid leukemia cell; RX PubMed=2056274; DOI=10.1084/jem.174.1.1; RA Dougherty G.J., Lansdorp P.M., Cooper D.L., Humphries R.K.; RT "Molecular cloning of CD44R1 and CD44R2, two novel isoforms of the human RT CD44 lymphocyte 'homing' receptor expressed by hemopoietic cells."; RL J. Exp. Med. 174:1-5(1991). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANT THR-479. RC TISSUE=Keratinocyte; RX PubMed=1281868; DOI=10.1111/1523-1747.ep12614896; RA Kugelman L.C., Ganguly S., Haggerty J.G., Weissman S.M., Milstone L.M.; RT "The core protein of epican, a heparan sulfate proteoglycan on RT keratinocytes, is an alternative form of CD44."; RL J. Invest. Dermatol. 99:886-891(1992). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANTS RP ARG-417 AND THR-479. RC TISSUE=Lymphoblast; RX PubMed=1465456; DOI=10.1073/pnas.89.24.12160; RA Screaton G.R., Bell M.V., Jackson D.G., Cornelis F.B., Gerth U., Bell J.I.; RT "Genomic structure of DNA encoding the lymphocyte homing receptor CD44 RT reveals at least 12 alternatively spliced exons."; RL Proc. Natl. Acad. Sci. U.S.A. 89:12160-12164(1992). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-417; THR-479 AND RP HIS-494. RX PubMed=7508842; DOI=10.1007/978-3-642-78253-4_4; RA Gunthert U.; RT "CD44: a multitude of isoforms with diverse functions."; RL Curr. Top. Microbiol. Immunol. 184:47-63(1993). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 13 AND 14), AND VARIANT THR-479. RC TISSUE=Mammary carcinoma; RX PubMed=8352881; DOI=10.1002/mc.2940070403; RA Tanabe K.K., Nishi T., Saya H.; RT "Novel variants of CD44 arising from alternative splicing: changes in the RT CD44 alternative splicing pattern of MCF-7 breast carcinoma cells treated RT with hyaluronidase."; RL Mol. Carcinog. 7:212-220(1993). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 19). RX PubMed=10933060; DOI=10.1038/sj.neo.7900045; RA Chiu R.K., Carpenito C., Dougherty S.T., Hayes G.M., Dougherty G.J.; RT "Identification and characterization of CD44RC, a novel alternatively RT spliced soluble CD44 isoform that can potentiate the hyaluronan binding RT activity of cell surface CD44."; RL Neoplasia 1:446-452(1999). RN [10] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 12). RC TISSUE=Articular cartilage; RA Bosch P.P., Stevens J.W., Buckwalter J.A., Midura R.J.; RT "CD44 in normal and neoplastic human cartilage."; RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 10 AND 12), AND VARIANT THR-479. RC TISSUE=Colon adenocarcinoma, and Retinal pigment epithelium; RA Wiebe G.J., Freund D., Corbeil D.; RT "Sequence analysis of the human CD44 antigen."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [12] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 11). RA Xiang Q., Wang J., Fan C., He X., Huang L., Zhu H., Qiu X., Luo W.; RT "Sequence analysis of a novel human CD44 variant."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [13] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 18). RA Fang X., Xu W., Zhang X.; RT "Construction of human CD44 eukaryotic vector and its expression in mammary RT carcinoma cells MCF-7."; RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases. RN [14] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 12). RC TISSUE=Spinal cord; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [15] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [16] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [17] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 12), AND VARIANTS RP ARG-417 AND THR-479. RC TISSUE=Pancreas, and Retinal pigment epithelium; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [18] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-22. RC TISSUE=Lymphoblast; RX PubMed=1922057; DOI=10.1128/mcb.11.11.5446-5453.1991; RA Shtivelman E., Bishop J.M.; RT "Expression of CD44 is repressed in neuroblastoma cells."; RL Mol. Cell. Biol. 11:5446-5453(1991). RN [19] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-742 (ISOFORM 15). RX PubMed=2466576; DOI=10.1016/0092-8674(89)90639-9; RA Goldstein L.A., Zhou D.F.H., Picker L.J., Minty C.N., Bargatze R.F., RA Ding J.F., Butcher E.C.; RT "A human lymphocyte homing receptor, the hermes antigen, is related to RT cartilage proteoglycan core and link proteins."; RL Cell 56:1063-1072(1989). RN [20] RP PROTEIN SEQUENCE OF 55-108. RC TISSUE=Glial tumor; RX PubMed=7527301; DOI=10.1007/bf01519984; RA Okada H., Yoshida J., Seo H., Wakabayashi T., Sugita K., Hagiwara M.; RT "Anti-(glioma surface antigen) monoclonal antibody G-22 recognizes RT overexpressed CD44 in glioma cells."; RL Cancer Immunol. Immunother. 39:313-317(1994). RN [21] RP PROTEIN SEQUENCE OF 67-89. RC TISSUE=Peripheral blood; RX PubMed=7508992; DOI=10.1128/jvi.68.3.1301-1308.1994; RA Shepley M.P., Racaniello V.R.; RT "A monoclonal antibody that blocks poliovirus attachment recognizes the RT lymphocyte homing receptor CD44."; RL J. Virol. 68:1301-1308(1994). RN [22] RP NUCLEOTIDE SEQUENCE [MRNA] OF 184-625 (ISOFORM 10), AND VARIANT THR-479. RC TISSUE=Foreskin; RX PubMed=2007624; DOI=10.1083/jcb.113.1.207; RA Brown T.A., Bouchard T., St John T., Wayner E., Carter W.G.; RT "Human keratinocytes express a new CD44 core protein (CD44E) as a heparan- RT sulfate intrinsic membrane proteoglycan with additional exons."; RL J. Cell Biol. 113:207-221(1991). RN [23] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 221-267. RX PubMed=8148709; DOI=10.1136/bmj.308.6929.619; RA Matsumura Y., Hanbury D., Smith J., Tarin D.; RT "Non-invasive detection of malignancy by identification of unusual CD44 RT gene activity in exfoliated cancer cells."; RL BMJ 308:619-624(1994). RN [24] RP NUCLEOTIDE SEQUENCE [MRNA] OF 267-603 (ISOFORM 1), AND VARIANT ARG-417. RC TISSUE=Lung; RX PubMed=1717145; RA Hofmann M., Rudy W., Zoeller M., Toelg C., Ponta H., Herrlich P., RA Guenthert U.; RT "CD44 splice variants confer metastatic behavior in rats: homologous RT sequences are expressed in human tumor cell lines."; RL Cancer Res. 51:5292-5297(1991). RN [25] RP FUNCTION. RX PubMed=7528188; DOI=10.1016/0198-8859(94)90026-4; RA Funaro A., Spagnoli G.C., Momo M., Knapp W., Malavasi F.; RT "Stimulation of T cells via CD44 requires leukocyte-function-associated RT antigen interactions and interleukin-2 production."; RL Hum. Immunol. 40:267-278(1994). RN [26] RP REVIEW ON FUNCTION, AND POST-TRANSLATIONAL MODIFICATIONS. RX PubMed=12511867; DOI=10.1038/nrm1004; RA Ponta H., Sherman L., Herrlich P.A.; RT "CD44: from adhesion molecules to signalling regulators."; RL Nat. Rev. Mol. Cell Biol. 4:33-45(2003). RN [27] RP PHOSPHORYLATION AT SER-706. RX PubMed=9580567; DOI=10.1242/jcs.111.11.1595; RA Peck D., Isacke C.M.; RT "Hyaluronan-dependent cell migration can be blocked by a CD44 cytoplasmic RT domain peptide containing a phosphoserine at position 325."; RL J. Cell Sci. 111:1595-1601(1998). RN [28] RP PHOSPHORYLATION AT SER-672. RX PubMed=12032545; DOI=10.1038/ncb797; RA Legg J.W., Lewis C.A., Parsons M., Ng T., Isacke C.M.; RT "A novel PKC-regulated mechanism controls CD44 ezrin association and RT directional cell motility."; RL Nat. Cell Biol. 4:399-407(2002). RN [29] RP GLYCOSYLATION, AND PROTEOLYTIC PROCESSING. RX PubMed=12883358; DOI=10.1097/01.cmr.0000056256.56735.0f; RA Bartolazzi A.; RT "CD44s adhesive function spontaneous and PMA-inducible CD44 cleavage are RT regulated at post-translational level in cells of melanocytic lineage."; RL Melanoma Res. 13:325-337(2003). RN [30] RP FUNCTION, AND INTERACTION WITH PKN2. RX PubMed=15123640; DOI=10.1074/jbc.m403608200; RA Bourguignon L.Y., Singleton P.A., Diedrich F.; RT "Hyaluronan-CD44 interaction with Rac1-dependent protein kinase N-gamma RT promotes phospholipase Cgamma1 activation, Ca(2+) signaling, and cortactin- RT cytoskeleton function leading to keratinocyte adhesion and RT differentiation."; RL J. Biol. Chem. 279:29654-29669(2004). RN [31] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., RA Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-706, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [33] RP FUNCTION. RX PubMed=16541107; DOI=10.1038/sj.emboj.7601039; RA Vikesaa J., Hansen T.V., Joenson L., Borup R., Wewer U.M., Christiansen J., RA Nielsen F.C.; RT "RNA-binding IMPs promote cell adhesion and invadopodia formation."; RL EMBO J. 25:1456-1468(2006). RN [34] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [35] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [36] 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 [37] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57 AND ASN-110. 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 [38] RP INTERACTION WITH UNC119. RX PubMed=19381274; DOI=10.1371/journal.pone.0005211; RA Vepachedu R., Karim Z., Patel O., Goplen N., Alam R.; RT "Unc119 protects from Shigella infection by inhibiting the Abl family RT kinases."; RL PLoS ONE 4:E5211-E5211(2009). RN [39] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [40] RP FUNCTION. RX PubMed=19703720; DOI=10.1016/j.jhep.2009.06.021; RA Crosby H.A., Lalor P.F., Ross E., Newsome P.N., Adams D.H.; RT "Adhesion of human haematopoietic (CD34+) stem cells to human liver RT compartments is integrin and CD44 dependent and modulated by CXCR3 and RT CXCR4."; RL J. Hepatol. 51:734-749(2009). RN [41] RP FUNCTION, AND INTERACTION WITH EGFR. RX PubMed=18757307; DOI=10.1165/rcmb.2008-0073oc; RA Casalino-Matsuda S.M., Monzon M.E., Day A.J., Forteza R.M.; RT "Hyaluronan fragments/CD44 mediate oxidative stress-induced MUC5B up- RT regulation in airway epithelium."; RL Am. J. Respir. Cell Mol. Biol. 40:277-285(2009). RN [42] RP INTERACTION WITH PDPN. RX PubMed=20962267; DOI=10.1091/mbc.e10-06-0489; RA Martin-Villar E., Fernandez-Munoz B., Parsons M., Yurrita M.M., Megias D., RA Perez-Gomez E., Jones G.E., Quintanilla M.; RT "Podoplanin associates with CD44 to promote directional cell migration."; RL Mol. Biol. Cell 21:4387-4399(2010). RN [43] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-706, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [44] 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., Buerckstuemmer T., RA 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 [45] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [46] RP GLYCOSYLATION, STRUCTURE OF CARBOHYDRATES, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RX PubMed=22171320; DOI=10.1074/mcp.m111.013649; RA Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.; RT "Human urinary glycoproteomics; attachment site specific analysis of N- and RT O-linked glycosylations by CID and ECD."; RL Mol. Cell. Proteomics 11:1-17(2012). RN [47] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=22726066; DOI=10.1111/j.1440-1827.2012.02823.x; RA Yoshida T., Matsuda Y., Naito Z., Ishiwata T.; RT "CD44 in human glioma correlates with histopathological grade and cell RT migration."; RL Pathol. Int. 62:463-470(2012). RN [48] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH EGFR. RX PubMed=23589287; DOI=10.1074/jbc.m113.451336; RA Midgley A.C., Rogers M., Hallett M.B., Clayton A., Bowen T., Phillips A.O., RA Steadman R.; RT "Transforming growth factor-beta1 (TGF-beta1)-stimulated fibroblast to RT myofibroblast differentiation is mediated by hyaluronan (HA)-facilitated RT epidermal growth factor receptor (EGFR) and CD44 co-localization in lipid RT rafts."; RL J. Biol. Chem. 288:14824-14838(2013). RN [49] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 AND SER-706, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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 [50] RP IDENTIFICATION 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., 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). RN [51] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-180. RX PubMed=25326458; DOI=10.1074/mcp.m114.043703; RA Noborn F., Gomez Toledo A., Sihlbom C., Lengqvist J., Fries E., Kjellen L., RA Nilsson J., Larson G.; RT "Identification of chondroitin sulfate linkage region glycopeptides reveals RT prohormones as a novel class of proteoglycans."; RL Mol. Cell. Proteomics 14:41-49(2015). RN [52] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [53] RP DEVELOPMENTAL STAGE. RX PubMed=29777959; DOI=10.1016/j.actbio.2018.05.023; RA Felemban M., Dorgau B., Hunt N.C., Hallam D., Zerti D., Bauer R., Ding Y., RA Collin J., Steel D., Krasnogor N., Al-Aama J., Lindsay S., Mellough C., RA Lako M.; RT "Extracellular matrix component expression in human pluripotent stem cell- RT derived retinal organoids recapitulates retinogenesis in vivo and reveals RT an important role for IMPG1 and CD44 in the development of photoreceptors RT and interphotoreceptor matrix."; RL Acta Biomater. 74:207-221(2018). RN [54] RP TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-180. RX PubMed=32337544; DOI=10.1093/glycob/cwaa039; RA Toledo A.G., Pihl J., Spliid C.B., Persson A., Nilsson J., Pereira M.A., RA Gustavsson T., Choudhary S., Oo H.Z., Black P.C., Daugaard M., Esko J.D., RA Larson G., Salanti A., Clausen T.M.; RT "An affinity chromatography and glycoproteomics workflow to profile the RT chondroitin sulfate proteoglycans that interact with malarial VAR2CSA in RT the placenta and in cancer."; RL Glycobiology 30:989-1002(2020). RN [55] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-180. RX PubMed=36213313; DOI=10.1007/s42485-022-00092-3; RA Ramarajan M.G., Saraswat M., Budhraja R., Garapati K., Raymond K., RA Pandey A.; RT "Mass spectrometric analysis of chondroitin sulfate-linked peptides."; RL J. Proteins Proteom. 13:187-203(2022). RN [56] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION AT SER-180. RX PubMed=37453717; DOI=10.1016/j.mcpro.2023.100617; RA Noborn F., Nilsson J., Sihlbom C., Nikpour M., Kjellen L., Larson G.; RT "Mapping the Human Chondroitin Sulfate Glycoproteome Reveals an Unexpected RT Correlation Between Glycan Sulfation and Attachment Site Characteristics."; RL Mol. Cell. Proteomics 22:100617-100617(2023). RN [57] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-178, STRUCTURE BY NMR OF RP 20-178, AND INTERACTION WITH HA. RX PubMed=14992719; DOI=10.1016/s1097-2765(04)00080-2; RA Teriete P., Banerji S., Noble M., Blundell C.D., Wright A.J., RA Pickford A.R., Lowe E., Mahoney D.J., Tammi M.I., Kahmann J.D., RA Campbell I.D., Day A.J., Jackson D.G.; RT "Structure of the regulatory hyaluronan binding domain in the inflammatory RT leukocyte homing receptor CD44."; RL Mol. Cell 13:483-496(2004). RN [58] RP STRUCTURE BY NMR OF 20-178 IN COMPLEX WITH HA. RX PubMed=17085435; DOI=10.1074/jbc.m608425200; RA Takeda M., Ogino S., Umemoto R., Sakakura M., Kajiwara M., Sugahara K.N., RA Hayasaka H., Miyasaka M., Terasawa H., Shimada I.; RT "Ligand-induced structural changes of the CD44 hyaluronan-binding domain RT revealed by NMR."; RL J. Biol. Chem. 281:40089-40095(2006). RN [59] RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) OF 18-171, INTERACTION WITH HA, AND RP DISULFIDE BOND. RX PubMed=25195884; DOI=10.1107/s2053230x14015532; RA Liu L.K., Finzel B.; RT "High-resolution crystal structures of alternate forms of the human CD44 RT hyaluronan-binding domain reveal a site for protein interaction."; RL Acta Crystallogr. F Struct. Biol. Commun. 70:1155-1161(2014). RN [60] RP VARIANT BLOOD GROUP INDIAN PRO-46. RX PubMed=8636151; DOI=10.1074/jbc.271.12.7147; RA Telen M.J., Udani M., Washington M.K., Levesque M.C., Lloyd E., Rao N.; RT "A blood group-related polymorphism of CD44 abolishes a hyaluronan-binding RT consensus sequence without preventing hyaluronan binding."; RL J. Biol. Chem. 271:7147-7153(1996). CC -!- FUNCTION: Cell-surface receptor that plays a role in cell-cell CC interactions, cell adhesion and migration, helping them to sense and CC respond to changes in the tissue microenvironment (PubMed:16541107, CC PubMed:19703720, PubMed:22726066). Participates thereby in a wide CC variety of cellular functions including the activation, recirculation CC and homing of T-lymphocytes, hematopoiesis, inflammation and response CC to bacterial infection (PubMed:7528188). Engages, through its CC ectodomain, extracellular matrix components such as hyaluronan/HA, CC collagen, growth factors, cytokines or proteases and serves as a CC platform for signal transduction by assembling, via its cytoplasmic CC domain, protein complexes containing receptor kinases and membrane CC proteases (PubMed:18757307, PubMed:23589287). Such effectors include CC PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C CC that coordinate signaling pathways promoting calcium mobilization and CC actin-mediated cytoskeleton reorganization essential for cell migration CC and adhesion (PubMed:15123640). {ECO:0000269|PubMed:15123640, CC ECO:0000269|PubMed:16541107, ECO:0000269|PubMed:18757307, CC ECO:0000269|PubMed:19703720, ECO:0000269|PubMed:22726066, CC ECO:0000269|PubMed:23589287, ECO:0000269|PubMed:7528188}. CC -!- SUBUNIT: Interacts with PKN2 (PubMed:15123640). Interacts with TIAM1 CC and TIAM2 (By similarity). Interacts with HA, as well as other CC glycosaminoglycans, collagen, laminin, and fibronectin via its N- CC terminal segment (PubMed:14992719, PubMed:17085435, PubMed:25195884). CC Interacts with UNC119 (PubMed:19381274). Interacts with PDPN (via CC extracellular domain); this interaction is required for PDPN-mediated CC directional migration and regulation of lamellipodia CC extension/stabilization during cell spreading and migration CC (PubMed:20962267). Interacts with RDX, EZR and MSN (By similarity). CC Interacts with EGFR (PubMed:18757307, PubMed:23589287). Interacts with CC CD74; this complex is essential for the MIF-induced signaling cascade CC that results in B cell survival (By similarity). CC {ECO:0000250|UniProtKB:P15379, ECO:0000269|PubMed:14992719, CC ECO:0000269|PubMed:15123640, ECO:0000269|PubMed:17085435, CC ECO:0000269|PubMed:18757307, ECO:0000269|PubMed:19381274, CC ECO:0000269|PubMed:20962267, ECO:0000269|PubMed:23589287, CC ECO:0000269|PubMed:25195884}. CC -!- INTERACTION: CC P16070; P04233: CD74; NbExp=9; IntAct=EBI-490245, EBI-2622890; CC P16070; P26038: MSN; NbExp=6; IntAct=EBI-490245, EBI-528768; CC P16070; Q9UPY5: SLC7A11; NbExp=4; IntAct=EBI-490245, EBI-3843348; CC P16070; P18011: sctE; Xeno; NbExp=4; IntAct=EBI-490245, EBI-490239; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22726066, CC ECO:0000269|PubMed:23589287}; Single-pass type I membrane protein CC {ECO:0000255}. Cell projection, microvillus CC {ECO:0000250|UniProtKB:P15379}. Secreted {ECO:0000269|PubMed:25326458, CC ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. CC Note=Colocalizes with actin in membrane protrusions at wounding edges. CC Co-localizes with RDX, EZR and MSN in microvilli. Localizes to CC cholesterol-rich membrane-bound lipid raft domains. CC {ECO:0000250|UniProtKB:P15379, ECO:0000269|PubMed:23589287}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=19; CC Comment=Additional isoforms seem to exist. Additional isoforms are CC produced by alternative splicing of 10 out of 19 exons within the CC extracellular domain. Additional diversity is generated through the CC utilization of internal splice donor and acceptor sites within 2 of CC the exons. A variation in the cytoplasmic domain was shown to result CC from the alternative splicing of 2 exons. Isoform CD44 is expected to CC be expressed in normal cells. Splice variants have been found in many CC tumor cell lines. Exons 5, 6, 7, 8, 9, 10, 11, 13, 14 and 19 are CC alternatively spliced. Experimental confirmation may be lacking for CC some isoforms. {ECO:0000269|PubMed:1465456}; CC Name=1; Synonyms=CD44; CC IsoId=P16070-1; Sequence=Displayed; CC Name=2; Synonyms=CD44SP; CC IsoId=P16070-2; Sequence=VSP_005303, VSP_005304; CC Name=3; CC IsoId=P16070-3; Sequence=VSP_005305, VSP_005306; CC Name=4; Synonyms=Epidermal; CC IsoId=P16070-4; Sequence=VSP_005307, VSP_005308; CC Name=5; CC IsoId=P16070-5; Sequence=VSP_005313; CC Name=6; CC IsoId=P16070-6; Sequence=VSP_005314, VSP_005315; CC Name=7; CC IsoId=P16070-7; Sequence=VSP_005316, VSP_005317; CC Name=8; CC IsoId=P16070-8; Sequence=VSP_005318, VSP_005319; CC Name=9; CC IsoId=P16070-9; Sequence=VSP_005320, VSP_005321; CC Name=10; Synonyms=CD44E, CD44R1, Epithelial, Keratinocyte; CC IsoId=P16070-10; Sequence=VSP_005309, VSP_005310; CC Name=11; Synonyms=CD44R2; CC IsoId=P16070-11; Sequence=VSP_022797; CC Name=12; Synonyms=CDw44, Reticulocyte; CC IsoId=P16070-12; Sequence=VSP_005311, VSP_005312; CC Name=13; Synonyms=CD44R4; CC IsoId=P16070-13; Sequence=VSP_005309, VSP_005310, VSP_005318, CC VSP_005319; CC Name=14; Synonyms=CD44R5; CC IsoId=P16070-14; Sequence=VSP_005309, VSP_005310, VSP_005316, CC VSP_005317, VSP_005318, VSP_005319; CC Name=15; Synonyms=Hermes; CC IsoId=P16070-15; Sequence=VSP_005311, VSP_005312, VSP_005320, CC VSP_005321; CC Name=16; CC IsoId=P16070-16; Sequence=VSP_005305, VSP_005306, VSP_005314, CC VSP_005315; CC Name=17; CC IsoId=P16070-17; Sequence=VSP_005313, VSP_005314, VSP_005315; CC Name=18; CC IsoId=P16070-18; Sequence=VSP_005311, VSP_005312, VSP_043575; CC Name=19; Synonyms=CD44RC; CC IsoId=P16070-19; Sequence=VSP_043870, VSP_043871; CC -!- TISSUE SPECIFICITY: Detected in fibroblasts and urine (at protein CC level) (PubMed:25326458, PubMed:36213313, PubMed:37453717). Detected in CC placenta (at protein level) (PubMed:32337544). Isoform 10 (epithelial CC isoform) is expressed by cells of epithelium and highly expressed by CC carcinomas. Expression is repressed in neuroblastoma cells. CC {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:32337544, CC ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. CC -!- DEVELOPMENTAL STAGE: Expressed in the developing retina between 16 and CC 19 weeks post-conception, specifically in the outer neuroblastic zone, CC inner neuroblastic zone, interphotoreceptor zone and the retinal CC pigment epithelium (at protein level). {ECO:0000269|PubMed:29777959}. CC -!- DOMAIN: The lectin-like LINK domain is responsible for hyaluronan CC binding. {ECO:0000250}. CC -!- PTM: Proteolytically cleaved in the extracellular matrix by specific CC proteinases (possibly MMPs) in several cell lines and tumors. CC {ECO:0000269|PubMed:12883358}. CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12883358, CC ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, CC ECO:0000269|PubMed:22171320}. CC -!- PTM: O-glycosylated; contains chondroitin sulfate glycans which can be CC more or less sulfated and whose number may affect the accessibility of CC specific proteinases to their cleavage site(s). It is uncertain if O- CC glycosylation occurs on Thr-637 or Thr-638. CC {ECO:0000269|PubMed:12883358, ECO:0000269|PubMed:22171320, CC ECO:0000269|PubMed:25326458}. CC -!- PTM: Phosphorylated; activation of PKC results in the dephosphorylation CC of Ser-706 (constitutive phosphorylation site), and the phosphorylation CC of Ser-672. {ECO:0000269|PubMed:12032545, ECO:0000269|PubMed:9580567}. CC -!- POLYMORPHISM: CD44 is responsible for the Indian blood group system. CC The molecular basis of the In(A)=In1/In(B)=In2 blood group antigens is CC a single variation in position 46; In(B), the most frequent allele, has CC Arg-46. {ECO:0000269|PubMed:8636151}. CC -!- MISCELLANEOUS: [Isoform 1]: Corresponds to the largest isoform. CC -!- MISCELLANEOUS: [Isoform 3]: Alternative splice donor/acceptor on exon CC 5. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: Lacks exon 6. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 5]: Alternative splice donor/acceptor on exon CC 7. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 6]: Lacks exon 10. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 7]: Lacks exon 13. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 8]: Lacks exon 14. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 9]: Lacks exon 19. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 10]: Lacks exons 6-11. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 11]: Lacks exons 6-13. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 12]: Lacks exons 6-14. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 13]: Lacks exons 6-11 and exon 14. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 14]: Lacks exons 6-11, exon 13 and exon 14. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 15]: Lacks exons 6-14 and exon 19. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 16]: Alternative splice donor/acceptor on exon CC 5 and lacks exon 10. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 17]: Alternative splice donor/acceptor on exon CC 7 and lacks exon 10. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 19]: Soluble isoform, has enhanced hyaluronan CC binding. {ECO:0000305}. CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene mutation CC database; CC URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=indian"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=CD44 entry; CC URL="https://en.wikipedia.org/wiki/CD44"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/980/cd44-(cd44-molecule-(indian-blood-group))"; 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; M24915; AAA35674.1; -; mRNA. DR EMBL; M59040; AAA51950.1; -; mRNA. DR EMBL; X55150; CAA38951.1; -; mRNA. DR EMBL; X56794; CAA40133.1; -; mRNA. DR EMBL; X66733; CAA47271.1; -; mRNA. DR EMBL; L05423; AAB13622.1; -; Genomic_DNA. DR EMBL; L05407; AAB13622.1; JOINED; Genomic_DNA. DR EMBL; L05408; AAB13622.1; JOINED; Genomic_DNA. DR EMBL; L05409; AAB13622.1; JOINED; Genomic_DNA. DR EMBL; L05410; AAB13622.1; JOINED; Genomic_DNA. DR EMBL; L05420; AAB13622.1; JOINED; Genomic_DNA. DR EMBL; L05421; AAB13622.1; JOINED; Genomic_DNA. DR EMBL; L05422; AAB13622.1; JOINED; Genomic_DNA. DR EMBL; M69215; AAB13622.1; JOINED; Genomic_DNA. DR EMBL; L05423; AAB13623.1; -; Genomic_DNA. DR EMBL; L05407; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05408; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05410; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05411; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05412; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05414; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05415; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05416; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05417; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05418; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05419; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05420; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05421; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05422; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; M69215; AAB13623.1; JOINED; Genomic_DNA. DR EMBL; L05424; AAB13624.1; -; Genomic_DNA. DR EMBL; L05407; AAB13624.1; JOINED; Genomic_DNA. DR EMBL; L05408; AAB13624.1; JOINED; Genomic_DNA. DR EMBL; L05410; AAB13624.1; JOINED; Genomic_DNA. DR EMBL; L05420; AAB13624.1; JOINED; Genomic_DNA. DR EMBL; L05421; AAB13624.1; JOINED; Genomic_DNA. DR EMBL; L05422; AAB13624.1; JOINED; Genomic_DNA. DR EMBL; M69215; AAB13624.1; JOINED; Genomic_DNA. DR EMBL; L05424; AAB13625.1; -; Genomic_DNA. DR EMBL; L05407; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05408; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05410; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05411; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05412; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05414; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05416; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05417; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05418; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05419; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05420; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05421; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05422; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; M69215; AAB13625.1; JOINED; Genomic_DNA. DR EMBL; L05424; AAB13626.1; -; Genomic_DNA. DR EMBL; L05407; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05408; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05410; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05411; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05412; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05414; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05416; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05417; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05418; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05419; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05420; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05421; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05422; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; M69215; AAB13626.1; JOINED; Genomic_DNA. DR EMBL; L05424; AAB13627.1; -; Genomic_DNA. DR EMBL; L05407; AAB13627.1; JOINED; Genomic_DNA. DR EMBL; L05408; AAB13627.1; JOINED; Genomic_DNA. DR EMBL; L05410; AAB13627.1; JOINED; Genomic_DNA. DR EMBL; L05417; AAB13627.1; JOINED; Genomic_DNA. DR EMBL; L05418; AAB13627.1; JOINED; Genomic_DNA. DR EMBL; L05420; AAB13627.1; JOINED; Genomic_DNA. DR EMBL; L05421; AAB13627.1; JOINED; Genomic_DNA. DR EMBL; L05422; AAB13627.1; JOINED; Genomic_DNA. DR EMBL; M69215; AAB13627.1; JOINED; Genomic_DNA. DR EMBL; L05424; AAB13628.1; -; Genomic_DNA. DR EMBL; L05407; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05408; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05410; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05411; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05412; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05414; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05415; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05416; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05417; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05418; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05419; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05420; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05421; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; L05422; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; M69215; AAB13628.1; JOINED; Genomic_DNA. DR EMBL; AJ251595; CAB61878.1; -; mRNA. DR EMBL; S66400; AAB27917.1; -; mRNA. DR EMBL; S66400; AAB27918.2; -; mRNA. DR EMBL; S66400; AAB27919.1; -; mRNA. DR EMBL; AF098641; AAC70782.1; -; mRNA. DR EMBL; U40373; AAA82949.1; -; mRNA. DR EMBL; AY101192; AAM50040.1; -; mRNA. DR EMBL; AY101193; AAM50041.1; -; mRNA. DR EMBL; EF581837; ABQ59315.1; -; mRNA. DR EMBL; FJ216964; ACI46596.1; -; mRNA. DR EMBL; AL832642; CAD89965.1; -; mRNA. DR EMBL; AL133330; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL136989; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL356215; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471064; EAW68147.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68148.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68149.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68151.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68152.1; -; Genomic_DNA. DR EMBL; BC004372; AAH04372.1; -; mRNA. DR EMBL; BC067348; AAH67348.1; -; mRNA. DR EMBL; M25078; AAA36138.1; -; mRNA. DR EMBL; X55938; CAA39404.1; -; mRNA. DR EMBL; S72928; AAB30429.1; -; Genomic_DNA. DR EMBL; X62739; CAA44602.1; -; mRNA. DR CCDS; CCDS31455.1; -. [P16070-4] DR CCDS; CCDS31456.1; -. [P16070-10] DR CCDS; CCDS31457.1; -. [P16070-12] DR CCDS; CCDS31458.1; -. [P16070-19] DR CCDS; CCDS55754.1; -. [P16070-11] DR CCDS; CCDS55755.1; -. [P16070-18] DR CCDS; CCDS7897.1; -. [P16070-1] DR PIR; A47195; A47195. DR PIR; I37369; I37369. DR PIR; I77371; I77371. DR PIR; I77372; I77372. DR PIR; JH0417; JH0417. DR PIR; JH0518; JH0518. DR PIR; S13530; S13530. DR PIR; S24222; S24222. DR RefSeq; NP_000601.3; NM_000610.3. [P16070-1] DR RefSeq; NP_001001389.1; NM_001001389.1. [P16070-4] DR RefSeq; NP_001001390.1; NM_001001390.1. [P16070-10] DR RefSeq; NP_001001391.1; NM_001001391.1. [P16070-12] DR RefSeq; NP_001001392.1; NM_001001392.1. [P16070-19] DR RefSeq; NP_001189484.1; NM_001202555.1. [P16070-11] DR RefSeq; NP_001189485.1; NM_001202556.1. [P16070-18] DR RefSeq; NP_001189486.1; NM_001202557.1. [P16070-15] DR RefSeq; XP_011518790.1; XM_011520488.1. [P16070-13] DR PDB; 1POZ; NMR; -; A=20-178. DR PDB; 1UUH; X-ray; 2.20 A; A/B=20-178. DR PDB; 2I83; NMR; -; A=21-178. DR PDB; 4PZ3; X-ray; 1.08 A; A/B=18-170. DR PDB; 4PZ4; X-ray; 1.60 A; A/B=18-171. DR PDB; 6TXS; X-ray; 2.20 A; BBB=678-685. DR PDBsum; 1POZ; -. DR PDBsum; 1UUH; -. DR PDBsum; 2I83; -. DR PDBsum; 4PZ3; -. DR PDBsum; 4PZ4; -. DR PDBsum; 6TXS; -. DR AlphaFoldDB; P16070; -. DR SMR; P16070; -. DR BioGRID; 107398; 232. DR CORUM; P16070; -. DR DIP; DIP-1121N; -. DR ELM; P16070; -. DR IntAct; P16070; 122. DR MINT; P16070; -. DR STRING; 9606.ENSP00000398632; -. DR BindingDB; P16070; -. DR ChEMBL; CHEMBL3232692; -. DR DrugBank; DB06550; Bivatuzumab. DR DrugBank; DB08818; Hyaluronic acid. DR TCDB; 9.B.87.1.31; the selenoprotein p receptor (selp-receptor) family. DR GlyConnect; 736; 42 N-Linked glycans (2 sites). DR GlyCosmos; P16070; 19 sites, 43 glycans. DR GlyGen; P16070; 62 sites, 41 N-linked glycans (2 sites), 4 O-linked glycans (46 sites). DR iPTMnet; P16070; -. DR MetOSite; P16070; -. DR PhosphoSitePlus; P16070; -. DR SwissPalm; P16070; -. DR BioMuta; CD44; -. DR DMDM; 308153615; -. DR CPTAC; CPTAC-668; -. DR CPTAC; CPTAC-692; -. DR EPD; P16070; -. DR jPOST; P16070; -. DR MassIVE; P16070; -. DR MaxQB; P16070; -. DR PaxDb; 9606-ENSP00000398632; -. DR PeptideAtlas; P16070; -. DR ProteomicsDB; 53266; -. [P16070-1] DR ProteomicsDB; 53267; -. [P16070-10] DR ProteomicsDB; 53268; -. [P16070-11] DR ProteomicsDB; 53269; -. [P16070-12] DR ProteomicsDB; 53270; -. [P16070-13] DR ProteomicsDB; 53271; -. [P16070-14] DR ProteomicsDB; 53272; -. [P16070-15] DR ProteomicsDB; 53273; -. [P16070-16] DR ProteomicsDB; 53274; -. [P16070-17] DR ProteomicsDB; 53275; -. [P16070-18] DR ProteomicsDB; 53276; -. [P16070-19] DR ProteomicsDB; 53278; -. [P16070-3] DR ProteomicsDB; 53279; -. [P16070-4] DR ProteomicsDB; 53280; -. [P16070-5] DR ProteomicsDB; 53281; -. [P16070-6] DR ProteomicsDB; 53282; -. [P16070-7] DR ProteomicsDB; 53283; -. [P16070-8] DR ProteomicsDB; 53284; -. [P16070-9] DR Pumba; P16070; -. DR TopDownProteomics; P16070-12; -. [P16070-12] DR TopDownProteomics; P16070-14; -. [P16070-14] DR TopDownProteomics; P16070-18; -. [P16070-18] DR TopDownProteomics; P16070-4; -. [P16070-4] DR TopDownProteomics; P16070-7; -. [P16070-7] DR ABCD; P16070; 22 sequenced antibodies. DR Antibodypedia; 804; 6018 antibodies from 59 providers. DR CPTC; P16070; 2 antibodies. DR DNASU; 960; -. DR Ensembl; ENST00000263398.11; ENSP00000263398.6; ENSG00000026508.21. [P16070-12] DR Ensembl; ENST00000278386.10; ENSP00000278386.6; ENSG00000026508.21. [P16070-19] DR Ensembl; ENST00000352818.8; ENSP00000309732.6; ENSG00000026508.21. [P16070-18] DR Ensembl; ENST00000415148.6; ENSP00000389830.2; ENSG00000026508.21. [P16070-4] DR Ensembl; ENST00000428726.8; ENSP00000398632.2; ENSG00000026508.21. [P16070-1] DR Ensembl; ENST00000433892.6; ENSP00000392331.2; ENSG00000026508.21. [P16070-10] DR Ensembl; ENST00000434472.6; ENSP00000404447.2; ENSG00000026508.21. [P16070-11] DR GeneID; 960; -. DR KEGG; hsa:960; -. DR MANE-Select; ENST00000428726.8; ENSP00000398632.2; NM_000610.4; NP_000601.3. DR UCSC; uc001mvu.4; human. [P16070-1] DR AGR; HGNC:1681; -. DR CTD; 960; -. DR DisGeNET; 960; -. DR GeneCards; CD44; -. DR HGNC; HGNC:1681; CD44. DR HPA; ENSG00000026508; Tissue enhanced (salivary). DR MIM; 107269; gene. DR MIM; 172290; gene. DR MIM; 609027; phenotype. DR neXtProt; NX_P16070; -. DR OpenTargets; ENSG00000026508; -. DR PharmGKB; PA26221; -. DR VEuPathDB; HostDB:ENSG00000026508; -. DR eggNOG; ENOG502RX7Q; Eukaryota. DR GeneTree; ENSGT00530000063822; -. DR HOGENOM; CLU_391256_0_0_1; -. DR InParanoid; P16070; -. DR OMA; SAYGEKW; -. DR OrthoDB; 5358652at2759; -. DR PhylomeDB; P16070; -. DR TreeFam; TF334173; -. DR PathwayCommons; P16070; -. DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-2160916; Hyaluronan uptake and degradation. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR SignaLink; P16070; -. DR SIGNOR; P16070; -. DR BioGRID-ORCS; 960; 34 hits in 1179 CRISPR screens. DR ChiTaRS; CD44; human. DR EvolutionaryTrace; P16070; -. DR GeneWiki; CD44; -. DR GenomeRNAi; 960; -. DR Pharos; P16070; Tbio. DR PRO; PR:P16070; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P16070; Protein. DR Bgee; ENSG00000026508; Expressed in parotid gland and 201 other cell types or tissues. DR ExpressionAtlas; P16070; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central. DR GO; GO:0042995; C:cell projection; IDA:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0031258; C:lamellipodium membrane; IDA:UniProtKB. DR GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IDA:BHF-UCL. DR GO; GO:0005902; C:microvillus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0030667; C:secretory granule membrane; TAS:Reactome. DR GO; GO:0005518; F:collagen binding; NAS:UniProtKB. DR GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central. DR GO; GO:0051216; P:cartilage development; IEP:UniProtKB. DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB. DR GO; GO:0016477; P:cell migration; IDA:UniProtKB. DR GO; GO:0098609; P:cell-cell adhesion; NAS:UniProtKB. DR GO; GO:0007160; P:cell-matrix adhesion; NAS:UniProtKB. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IDA:UniProtKB. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:GOC. DR GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central. DR GO; GO:0070487; P:monocyte aggregation; IMP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB. DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IDA:BHF-UCL. DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:BHF-UCL. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL. DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IMP:UniProtKB. DR GO; GO:1900625; P:positive regulation of monocyte aggregation; IMP:BHF-UCL. DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL. DR GO; GO:2000392; P:regulation of lamellipodium morphogenesis; IMP:UniProtKB. DR GO; GO:0042110; P:T cell activation; IDA:UniProtKB. DR GO; GO:0044319; P:wound healing, spreading of cells; IMP:UniProtKB. DR CDD; cd03516; Link_domain_CD44_like; 1. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1. DR InterPro; IPR016186; C-type_lectin-like/link_sf. DR InterPro; IPR001231; CD44_antigen. DR InterPro; IPR043210; CD44_antigen-like. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR000538; Link_dom. DR PANTHER; PTHR10225:SF6; CD44 ANTIGEN; 1. DR PANTHER; PTHR10225; HYALURONAN RECEPTOR; 1. DR Pfam; PF00193; Xlink; 1. DR PRINTS; PR00658; CD44. DR PRINTS; PR01265; LINKMODULE. DR SMART; SM00445; LINK; 1. DR SUPFAM; SSF56436; C-type lectin-like; 1. DR PROSITE; PS01241; LINK_1; 1. DR PROSITE; PS50963; LINK_2; 1. DR SWISS-2DPAGE; P16070; -. DR Genevisible; P16070; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Blood group antigen; Cell adhesion; KW Cell membrane; Cell projection; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Membrane; Phosphoprotein; Proteoglycan; Receptor; KW Reference proteome; Secreted; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..20 FT /evidence="ECO:0000250" FT CHAIN 21..742 FT /note="CD44 antigen" FT /id="PRO_0000026687" FT TOPO_DOM 21..649 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 650..670 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 671..742 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 32..120 FT /note="Link" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323" FT REGION 160..189 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 224..649 FT /note="Stem" FT REGION 261..285 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 372..558 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 590..642 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 673..691 FT /note="Required for interaction with EZR, MSN and RDX and FT for co-localization to microvilli" FT /evidence="ECO:0000250|UniProtKB:P15379" FT COMPBIAS 167..189 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 261..277 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 381..403 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 418..455 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 473..491 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 499..516 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 529..558 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 590..620 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 627..642 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 41 FT /ligand="hyaluronan" FT /ligand_id="ChEBI:CHEBI:132153" FT /evidence="ECO:0000250" FT BINDING 78 FT /ligand="hyaluronan" FT /ligand_id="ChEBI:CHEBI:132153" FT /evidence="ECO:0000250" FT BINDING 79 FT /ligand="hyaluronan" FT /ligand_id="ChEBI:CHEBI:132153" FT /evidence="ECO:0000250" FT BINDING 105 FT /ligand="hyaluronan" FT /ligand_id="ChEBI:CHEBI:132153" FT /evidence="ECO:0000250" FT MOD_RES 672 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000269|PubMed:12032545" FT MOD_RES 686 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 697 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P15379" FT MOD_RES 706 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:9580567, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT CARBOHYD 25 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 57 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 100 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 110 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218" FT CARBOHYD 120 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 180 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000269|PubMed:25326458, FT ECO:0000269|PubMed:32337544, ECO:0000269|PubMed:36213313, FT ECO:0000269|PubMed:37453717" FT CARBOHYD 350 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 548 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 599 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 636 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 28..129 FT /evidence="ECO:0000269|PubMed:25195884, FT ECO:0007744|PDB:4PZ3, ECO:0007744|PDB:4PZ4" FT DISULFID 53..118 FT /evidence="ECO:0000269|PubMed:25195884, FT ECO:0007744|PDB:4PZ3, ECO:0007744|PDB:4PZ4" FT DISULFID 77..97 FT /evidence="ECO:0000269|PubMed:25195884, FT ECO:0007744|PDB:4PZ3, ECO:0007744|PDB:4PZ4" FT VAR_SEQ 23..29 FT /note="DLNITCR -> GVGRRKS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8352881" FT /id="VSP_005303" FT VAR_SEQ 30..742 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8352881" FT /id="VSP_005304" FT VAR_SEQ 78..139 FT /note="RYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDC FT TSVTDLPNAF -> SLHCSQQSKKVWAEEKASDQQWQWSCGGQKAKWTQRRGQQVSGNG FT AFGEQGVVRNSRPVYDS (in isoform 19)" FT /evidence="ECO:0000303|PubMed:10933060" FT /id="VSP_043870" FT VAR_SEQ 140..742 FT /note="Missing (in isoform 19)" FT /evidence="ECO:0000303|PubMed:10933060" FT /id="VSP_043871" FT VAR_SEQ 192 FT /note="G -> A (in isoform 3 and isoform 16)" FT /evidence="ECO:0000305" FT /id="VSP_005305" FT VAR_SEQ 193..223 FT /note="Missing (in isoform 3 and isoform 16)" FT /evidence="ECO:0000305" FT /id="VSP_005306" FT VAR_SEQ 223..535 FT /note="Missing (in isoform 11)" FT /evidence="ECO:0000303|PubMed:2056274, ECO:0000303|Ref.12" FT /id="VSP_022797" FT VAR_SEQ 223 FT /note="T -> N (in isoform 10, isoform 13 and isoform 14)" FT /evidence="ECO:0000303|PubMed:1991450, FT ECO:0000303|PubMed:2007624, ECO:0000303|PubMed:2056274, FT ECO:0000303|PubMed:8352881, ECO:0000303|Ref.11" FT /id="VSP_005309" FT VAR_SEQ 223 FT /note="T -> R (in isoform 12, isoform 15 and isoform 18)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:1840487, FT ECO:0000303|PubMed:2466575, ECO:0000303|PubMed:2466576, FT ECO:0000303|Ref.10, ECO:0000303|Ref.11, ECO:0000303|Ref.13" FT /id="VSP_005311" FT VAR_SEQ 223 FT /note="T -> S (in isoform 4)" FT /evidence="ECO:0000303|PubMed:1281868, FT ECO:0000303|PubMed:15489334" FT /id="VSP_005307" FT VAR_SEQ 224..604 FT /note="Missing (in isoform 12, isoform 15 and isoform 18)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005, ECO:0000303|PubMed:1840487, FT ECO:0000303|PubMed:2466575, ECO:0000303|PubMed:2466576, FT ECO:0000303|Ref.10, ECO:0000303|Ref.11, ECO:0000303|Ref.13" FT /id="VSP_005312" FT VAR_SEQ 224..472 FT /note="Missing (in isoform 10, isoform 13 and isoform 14)" FT /evidence="ECO:0000303|PubMed:1991450, FT ECO:0000303|PubMed:2007624, ECO:0000303|PubMed:2056274, FT ECO:0000303|PubMed:8352881, ECO:0000303|Ref.11" FT /id="VSP_005310" FT VAR_SEQ 224..266 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:1281868, FT ECO:0000303|PubMed:15489334" FT /id="VSP_005308" FT VAR_SEQ 266..273 FT /note="Missing (in isoform 5 and isoform 17)" FT /evidence="ECO:0000305" FT /id="VSP_005313" FT VAR_SEQ 385 FT /note="I -> T (in isoform 6, isoform 16 and isoform 17)" FT /evidence="ECO:0000305" FT /id="VSP_005314" FT VAR_SEQ 386..428 FT /note="Missing (in isoform 6, isoform 16 and isoform 17)" FT /evidence="ECO:0000305" FT /id="VSP_005315" FT VAR_SEQ 506 FT /note="Q -> R (in isoform 7 and isoform 14)" FT /evidence="ECO:0000303|PubMed:8352881" FT /id="VSP_005316" FT VAR_SEQ 507..535 FT /note="Missing (in isoform 7 and isoform 14)" FT /evidence="ECO:0000303|PubMed:8352881" FT /id="VSP_005317" FT VAR_SEQ 536 FT /note="N -> R (in isoform 8, isoform 13 and isoform 14)" FT /evidence="ECO:0000303|PubMed:8352881" FT /id="VSP_005318" FT VAR_SEQ 537..604 FT /note="Missing (in isoform 8, isoform 13 and isoform 14)" FT /evidence="ECO:0000303|PubMed:8352881" FT /id="VSP_005319" FT VAR_SEQ 605..625 FT /note="Missing (in isoform 18)" FT /evidence="ECO:0000303|Ref.13" FT /id="VSP_043575" FT VAR_SEQ 675 FT /note="R -> S (in isoform 9 and isoform 15)" FT /evidence="ECO:0000303|PubMed:2466576" FT /id="VSP_005320" FT VAR_SEQ 676..742 FT /note="Missing (in isoform 9 and isoform 15)" FT /evidence="ECO:0000303|PubMed:2466576" FT /id="VSP_005321" FT VARIANT 46 FT /note="R -> P (in In(A) antigen; dbSNP:rs369473842)" FT /evidence="ECO:0000269|PubMed:8636151" FT /id="VAR_006490" FT VARIANT 393 FT /note="T -> M (in dbSNP:rs11607491)" FT /id="VAR_030325" FT VARIANT 417 FT /note="K -> R (in dbSNP:rs9666607)" FT /evidence="ECO:0000269|PubMed:1465456, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:1717145, FT ECO:0000269|PubMed:7508842" FT /id="VAR_021147" FT VARIANT 479 FT /note="I -> T (in dbSNP:rs1467558)" FT /evidence="ECO:0000269|PubMed:1281868, FT ECO:0000269|PubMed:1465456, ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:1991450, ECO:0000269|PubMed:2007624, FT ECO:0000269|PubMed:2056274, ECO:0000269|PubMed:7508842, FT ECO:0000269|PubMed:8352881, ECO:0000269|Ref.11" FT /id="VAR_030326" FT VARIANT 494 FT /note="D -> H (in dbSNP:rs12273397)" FT /evidence="ECO:0000269|PubMed:7508842" FT /id="VAR_030327" FT CONFLICT 26 FT /note="I -> M (in Ref. 10; AAA82949)" FT /evidence="ECO:0000305" FT CONFLICT 109 FT /note="S -> Y (in Ref. 1; AAA35674, 2; AAA51950, 3; FT CAA38951 and 7; CAB61878)" FT /evidence="ECO:0000305" FT CONFLICT 221 FT /note="A -> R (in Ref. 3; CAA38951)" FT /evidence="ECO:0000305" FT CONFLICT 241 FT /note="T -> A (in Ref. 7; CAB61878)" FT /evidence="ECO:0000305" FT CONFLICT 410 FT /note="E -> V (in Ref. 5; CAA47271)" FT /evidence="ECO:0000305" FT CONFLICT 494 FT /note="D -> N (in Ref. 7; CAB61878)" FT /evidence="ECO:0000305" FT CONFLICT 555 FT /note="T -> H (in Ref. 3; CAA38951)" FT /evidence="ECO:0000305" FT CONFLICT 620 FT /note="G -> E (in Ref. 1; AAA35674)" FT /evidence="ECO:0000305" FT CONFLICT 697 FT /note="S -> I (in Ref. 11; AAM50041 and 16; AAH67348)" FT /evidence="ECO:0000305" FT STRAND 21..26 FT /evidence="ECO:0007829|PDB:4PZ3" FT STRAND 33..38 FT /evidence="ECO:0007829|PDB:4PZ3" FT HELIX 46..55 FT /evidence="ECO:0007829|PDB:4PZ3" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:1POZ" FT HELIX 63..71 FT /evidence="ECO:0007829|PDB:4PZ3" FT STRAND 80..82 FT /evidence="ECO:0007829|PDB:4PZ3" FT STRAND 85..92 FT /evidence="ECO:0007829|PDB:4PZ3" FT HELIX 98..100 FT /evidence="ECO:0007829|PDB:4PZ3" FT STRAND 103..106 FT /evidence="ECO:0007829|PDB:4PZ3" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:1POZ" FT STRAND 114..119 FT /evidence="ECO:0007829|PDB:4PZ3" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:2I83" FT STRAND 125..128 FT /evidence="ECO:0007829|PDB:4PZ3" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:2I83" FT STRAND 139..148 FT /evidence="ECO:0007829|PDB:4PZ3" FT TURN 150..152 FT /evidence="ECO:0007829|PDB:1POZ" FT STRAND 154..160 FT /evidence="ECO:0007829|PDB:4PZ3" FT HELIX 165..168 FT /evidence="ECO:0007829|PDB:4PZ3" SQ SEQUENCE 742 AA; 81538 MW; BB9B66B19B970349 CRC64; MDKFWWHAAW GLCLVPLSLA QIDLNITCRF AGVFHVEKNG RYSISRTEAA DLCKAFNSTL PTMAQMEKAL SIGFETCRYG FIEGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTYCFN ASAPPEEDCT SVTDLPNAFD GPITITIVNR DGTRYVQKGE YRTNPEDIYP SNPTDDDVSS GSSSERSSTS GGYIFYTFST VHPIPDEDSP WITDSTDRIP ATTLMSTSAT ATETATKRQE TWDWFSWLFL PSESKNHLHT TTQMAGTSSN TISAGWEPNE ENEDERDRHL SFSGSGIDDD EDFISSTIST TPRAFDHTKQ NQDWTQWNPS HSNPEVLLQT TTRMTDVDRN GTTAYEGNWN PEAHPPLIHH EHHEEEETPH STSTIQATPS STTEETATQK EQWFGNRWHE GYRQTPKEDS HSTTGTAAAS AHTSHPMQGR TTPSPEDSSW TDFFNPISHP MGRGHQAGRR MDMDSSHSIT LQPTANPNTG LVEDLDRTGP LSMTTQQSNS QSFSTSHEGL EEDKDHPTTS TLTSSNRNDV TGGRRDPNHS EGSTTLLEGY TSHYPHTKES RTFIPVTSAK TGSFGVTAVT VGDSNSNVNR SLSGDQDTFH PSGGSHTTHG SESDGHSHGS QEGGANTTSG PIRTPQIPEW LIILASLLAL ALILAVCIAV NSRRRCGQKK KLVINSGNGA VEDRKPSGLN GEASKSQEMV HLVNKESSET PDQFMTADET RNLQNVDMKI GV //