ID CD44_HUMAN Reviewed; 742 AA. AC P16070; A5YRN9; B6EAT9; D3DR12; D3DR13; O95370; P22511; Q04858; AC Q13419; Q13957; Q13958; Q13959; Q13960; Q13961; Q13967; Q13968; AC Q13980; Q15861; Q16064; Q16065; Q16066; Q16208; Q16522; Q86T72; AC Q86Z27; Q8N694; Q92493; Q96J24; Q9H5A5; Q9UC28; Q9UC29; Q9UC30; AC Q9UCB0; Q9UJ36; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 05-OCT-2010, sequence version 3. DT 11-NOV-2015, entry version 195. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT the 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; RA Stamenkovic I., Aruffo A., Amiot M., Seed B.; RT "The hematopoietic and epithelial forms of CD44 are distinct RT polypeptides with different adhesion potentials for hyaluronate- RT 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 RT human CD44 lymphocyte 'homing' receptor expressed by hemopoietic RT 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., RA 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., RA 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 RP AND HIS-494. RX PubMed=7508842; 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 RP 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 RT the CD44 alternative splicing pattern of MCF-7 breast carcinoma cells RT treated 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 RT binding 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 RT mammary 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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., 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., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [17] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 12), AND RP VARIANTS 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 RT project: 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; 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; RA Shepley M.P., Racaniello V.R.; RT "A monoclonal antibody that blocks poliovirus attachment recognizes RT the lymphocyte homing receptor CD44."; RL J. Virol. 68:1301-1308(1994). RN [22] RP NUCLEOTIDE SEQUENCE [MRNA] OF 184-625 (ISOFORM 10), AND VARIANT RP 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 RT heparan-sulfate intrinsic membrane proteoglycan with additional RT 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 RT CD44 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 RP 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 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 [26] RP PHOSPHORYLATION AT SER-706. RX PubMed=9580567; RA Peck D., Isacke C.M.; RT "Hyaluronan-dependent cell migration can be blocked by a CD44 RT cytoplasmic domain peptide containing a phosphoserine at position RT 325."; RL J. Cell Sci. 111:1595-1601(1998). RN [27] 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 [28] RP GLYCOSYLATION, AND PROTEOLYTIC PROCESSING. RX PubMed=12883358; DOI=10.1097/00008390-200308000-00001; RA Bartolazzi A.; RT "CD44s adhesive function spontaneous and PMA-inducible CD44 cleavage RT are regulated at post-translational level in cells of melanocytic RT lineage."; RL Melanoma Res. 13:325-337(2003). RN [29] 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., RA Moore R.J., 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 [30] 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [31] RP FUNCTION. RX PubMed=16541107; DOI=10.1038/sj.emboj.7601039; RA Vikesaa J., Hansen T.V., Joenson L., Borup R., Wewer U.M., RA Christiansen J., Nielsen F.C.; RT "RNA-binding IMPs promote cell adhesion and invadopodia formation."; RL EMBO J. 25:1456-1468(2006). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION RP BY 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 RT sequential IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [33] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION RP BY 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 RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [34] 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 [35] 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 RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [36] 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 [37] 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 [38] 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [39] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [40] RP GLYCOSYLATION AT THR-637 AND THR-638, STRUCTURE OF CARBOHYDRATES, AND RP IDENTIFICATION BY MASS 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 RT N-and O-linked glycosylations by CID and ECD."; RL Mol. Cell. Proteomics 0:0-0(2011). RN [41] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [42] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [43] 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., RA Ayoub D., 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 [44] 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 RT inflammatory leukocyte homing receptor CD44."; RL Mol. Cell 13:483-496(2004). RN [45] 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., RA Sugahara K.N., Hayasaka H., Miyasaka M., Terasawa H., Shimada I.; RT "Ligand-induced structural changes of the CD44 hyaluronan-binding RT domain revealed by NMR."; RL J. Biol. Chem. 281:40089-40095(2006). RN [46] 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., RA Rao N.; RT "A blood group-related polymorphism of CD44 abolishes a hyaluronan- RT binding consensus sequence without preventing hyaluronan binding."; RL J. Biol. Chem. 271:7147-7153(1996). CC -!- FUNCTION: Receptor for hyaluronic acid (HA). Mediates cell-cell CC and cell-matrix interactions through its affinity for HA, and CC possibly also through its affinity for other ligands such as CC osteopontin, collagens, and matrix metalloproteinases (MMPs). CC Adhesion with HA plays an important role in cell migration, tumor CC growth and progression. In cancer cells, may play an important CC role in invadopodia formation. Also involved in lymphocyte CC activation, recirculation and homing, and in hematopoiesis. CC Altered expression or dysfunction causes numerous pathogenic CC phenotypes. Great protein heterogeneity due to numerous CC alternative splicing and post-translational modification events. CC Receptor for LGALS9; the interaction enhances binding of SMAD3 to CC the FOXP3 promoter, leading to up-regulation of FOXP3 expression CC and increased induced regulatory T (iTreg) cell stability and CC suppressive function (By similarity). CC {ECO:0000250|UniProtKB:P15379, ECO:0000269|PubMed:16541107}. CC -!- SUBUNIT: Interacts with PKN2 (By similarity). 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). Interacts CC with ANK, the ERM proteins (VIL2, RDX and MSN), and NF2 via its C- CC terminal segment. Interacts with UNC119 (PubMed:19381274). CC {ECO:0000250|UniProtKB:P15379, ECO:0000269|PubMed:14992719, CC ECO:0000269|PubMed:17085435, ECO:0000269|PubMed:19381274}. CC -!- INTERACTION: CC P18011:ipaB (xeno); NbExp=4; IntAct=EBI-490245, EBI-490239; CC P26038:MSN; NbExp=6; IntAct=EBI-490245, EBI-528768; CC Q9UPY5:SLC7A11; NbExp=4; IntAct=EBI-490245, EBI-3843348; CC P10451:SPP1; NbExp=4; IntAct=EBI-490245, EBI-723648; CC -!- SUBCELLULAR LOCATION: Cell membrane CC {ECO:0000250|UniProtKB:P15379}; Single-pass type I membrane CC protein {ECO:0000250|UniProtKB:P15379}. Note=Colocalizes with CC actin in membrane protrusions at wounding edges. CC {ECO:0000250|UniProtKB:P15379}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=19; CC Comment=Additional isoforms seem to exist. Additional isoforms CC are produced by alternative splicing of 10 out of 19 exons CC within the extracellular domain. Additional diversity is CC generated through the utilization of internal splice donor and CC acceptor sites within 2 of the exons. A variation in the CC cytoplasmic domain was shown to result from the alternative CC splicing of 2 exons. Isoform CD44 is expected to be expressed in CC normal cells. Splice variants have been found in many tumor cell CC lines. Exons 5, 6, 7, 8, 9, 10, 11, 13, 14 and 19 are CC alternatively spliced. Experimental confirmation may be lacking CC for some isoforms. {ECO:0000269|PubMed:1465456}; CC Name=1; Synonyms=CD44; CC IsoId=P16070-1; Sequence=Displayed; CC Note=Corresponds to the largest isoform.; 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 Note=Alternative splice donor/acceptor on exon 5.; CC Name=4; Synonyms=Epidermal; CC IsoId=P16070-4; Sequence=VSP_005307, VSP_005308; CC Note=Lacks exon 6.; CC Name=5; CC IsoId=P16070-5; Sequence=VSP_005313; CC Note=Alternative splice donor/acceptor on exon 7.; CC Name=6; CC IsoId=P16070-6; Sequence=VSP_005314, VSP_005315; CC Note=Lacks exon 10.; CC Name=7; CC IsoId=P16070-7; Sequence=VSP_005316, VSP_005317; CC Note=Lacks exon 13.; CC Name=8; CC IsoId=P16070-8; Sequence=VSP_005318, VSP_005319; CC Note=Lacks exon 14.; CC Name=9; CC IsoId=P16070-9; Sequence=VSP_005320, VSP_005321; CC Note=Lacks exon 19.; CC Name=10; Synonyms=CD44E, CD44R1, Epithelial, Keratinocyte; CC IsoId=P16070-10; Sequence=VSP_005309, VSP_005310; CC Note=Lacks exons 6-11.; CC Name=11; Synonyms=CD44R2; CC IsoId=P16070-11; Sequence=VSP_022797; CC Note=Lacks exons 6-13.; CC Name=12; Synonyms=CDw44, Reticulocyte; CC IsoId=P16070-12; Sequence=VSP_005311, VSP_005312; CC Note=Lacks exons 6-14.; CC Name=13; Synonyms=CD44R4; CC IsoId=P16070-13; Sequence=VSP_005309, VSP_005310, VSP_005318, CC VSP_005319; CC Note=Lacks exons 6-11 and exon 14.; CC Name=14; Synonyms=CD44R5; CC IsoId=P16070-14; Sequence=VSP_005309, VSP_005310, VSP_005316, CC VSP_005317, VSP_005318, VSP_005319; CC Note=Lacks exons 6-11, exon 13 and exon 14.; CC Name=15; Synonyms=Hermes; CC IsoId=P16070-15; Sequence=VSP_005311, VSP_005312, VSP_005320, CC VSP_005321; CC Note=Lacks exons 6-14 and exon 19.; CC Name=16; CC IsoId=P16070-16; Sequence=VSP_005305, VSP_005306, VSP_005314, CC VSP_005315; CC Note=Alternative splice donor/acceptor on exon 5 and lacks exon CC 10.; CC Name=17; CC IsoId=P16070-17; Sequence=VSP_005313, VSP_005314, VSP_005315; CC Note=Alternative splice donor/acceptor on exon 7 and lacks exon CC 10.; CC Name=18; CC IsoId=P16070-18; Sequence=VSP_005311, VSP_005312, VSP_043575; CC Note=No experimental confirmation available.; CC Name=19; Synonyms=CD44RC; CC IsoId=P16070-19; Sequence=VSP_043870, VSP_043871; CC Note=Soluble isoform, has enhanced hyaluronan binding.; CC -!- TISSUE SPECIFICITY: Isoform 10 (epithelial isoform) is expressed CC by cells of epithelium and highly expressed by carcinomas. CC Expression is repressed in neuroblastoma cells. CC -!- DOMAIN: The lectin-like LINK domain is responsible for hyaluronan CC binding. {ECO:0000250}. CC -!- PTM: Proteolytically cleaved in the extracellular matrix by CC specific proteinases (possibly MMPs) in several cell lines and CC tumors. {ECO:0000269|PubMed:12883358}. CC -!- PTM: N- and O-glycosylated. O-glycosylation contains more-or-less- CC sulfated chondroitin sulfate glycans, whose number may affect the CC accessibility of specific proteinases to their cleavage site(s). CC It is uncertain if O-glycosylation occurs on Thr-637 or Thr-638. CC {ECO:0000269|PubMed:12883358, ECO:0000269|PubMed:16335952, CC ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320}. CC -!- PTM: Phosphorylated; activation of PKC results in the CC dephosphorylation of Ser-706 (constitutive phosphorylation site), CC and the phosphorylation of Ser-672. {ECO:0000269|PubMed:12032545, CC ECO:0000269|PubMed:9580567}. CC -!- POLYMORPHISM: CD44 is responsible for the Indian blood group CC system. The molecular basis of the In(A)=In1/In(B)=In2 blood group CC antigens is a single variation in position 46; In(B), the most CC frequent allele, has Arg-46. CC -!- SIMILARITY: Contains 1 Link domain. {ECO:0000255|PROSITE- CC ProRule:PRU00323}. CC -!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene CC mutation database; CC URL="http://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 CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/CD44ID980CH11p13.html"; 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; CAC10347.1; -; 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 UniGene; Hs.502328; -. 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 PDBsum; 1POZ; -. DR PDBsum; 1UUH; -. DR PDBsum; 2I83; -. DR PDBsum; 4PZ3; -. DR PDBsum; 4PZ4; -. DR ProteinModelPortal; P16070; -. DR SMR; P16070; 20-170. DR BioGrid; 107398; 81. DR DIP; DIP-1121N; -. DR IntAct; P16070; 16. DR MINT; MINT-5000740; -. DR STRING; 9606.ENSP00000398632; -. DR BindingDB; P16070; -. DR ChEMBL; CHEMBL3232692; -. DR DrugBank; DB08818; Hyaluronan. DR PhosphoSite; P16070; -. DR BioMuta; CD44; -. DR DMDM; 308153615; -. DR SWISS-2DPAGE; P16070; -. DR MaxQB; P16070; -. DR PaxDb; P16070; -. DR PRIDE; P16070; -. DR DNASU; 960; -. DR Ensembl; ENST00000263398; ENSP00000263398; ENSG00000026508. [P16070-12] DR Ensembl; ENST00000278386; ENSP00000278386; ENSG00000026508. [P16070-19] DR Ensembl; ENST00000352818; ENSP00000309732; ENSG00000026508. [P16070-18] DR Ensembl; ENST00000415148; ENSP00000389830; ENSG00000026508. [P16070-4] DR Ensembl; ENST00000428726; ENSP00000398632; ENSG00000026508. [P16070-1] DR Ensembl; ENST00000433892; ENSP00000392331; ENSG00000026508. [P16070-10] DR Ensembl; ENST00000434472; ENSP00000404447; ENSG00000026508. [P16070-11] DR GeneID; 960; -. DR KEGG; hsa:960; -. DR UCSC; uc001mvu.3; human. [P16070-1] DR UCSC; uc001mvv.3; human. [P16070-4] DR UCSC; uc001mvw.3; human. [P16070-10] DR UCSC; uc001mvx.3; human. [P16070-12] DR UCSC; uc001mvy.3; human. [P16070-19] DR UCSC; uc001mwc.4; human. [P16070-11] DR UCSC; uc010rer.2; human. [P16070-18] DR UCSC; uc021qfw.1; human. [P16070-15] DR CTD; 960; -. DR GeneCards; CD44; -. DR HGNC; HGNC:1681; CD44. DR HPA; CAB000112; -. DR HPA; CAB000316; -. DR HPA; HPA005785; -. DR MIM; 107269; gene. DR MIM; 172290; gene. DR MIM; 609027; phenotype. DR neXtProt; NX_P16070; -. DR PharmGKB; PA26221; -. DR eggNOG; ENOG410IZCP; Eukaryota. DR eggNOG; ENOG4111S6T; LUCA. DR GeneTree; ENSGT00530000063822; -. DR HOGENOM; HOG000115236; -. DR HOVERGEN; HBG003850; -. DR InParanoid; P16070; -. DR KO; K06256; -. DR OMA; SHPMGRG; -. DR OrthoDB; EOG77HDFT; -. DR PhylomeDB; P16070; -. DR TreeFam; TF334173; -. 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-877300; Interferon gamma signaling. DR ChiTaRS; CD44; human. DR EvolutionaryTrace; P16070; -. DR GeneWiki; CD44; -. DR GenomeRNAi; 960; -. DR NextBio; 4000; -. DR PRO; PR:P16070; -. DR Proteomes; UP000005640; Chromosome 11. DR Bgee; P16070; -. DR ExpressionAtlas; P16070; baseline and differential. DR Genevisible; P16070; HS. DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:HPA. DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB. DR GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IDA:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0005518; F:collagen binding; NAS:UniProtKB. DR GO; GO:0005540; F:hyaluronic acid binding; IDA:UniProtKB. DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IDA:UniProtKB. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IEA:Ensembl. DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl. DR GO; GO:0005975; P:carbohydrate metabolic process; TAS:Reactome. DR GO; GO:0051216; P:cartilage development; IEP: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; TAS:Reactome. DR GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0030203; P:glycosaminoglycan metabolic process; TAS:Reactome. DR GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB. DR GO; GO:0030212; P:hyaluronan metabolic process; TAS:Reactome. DR GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. 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:0010628; P:positive regulation of gene expression; IEA:Ensembl. 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:0016337; P:single organismal cell-cell adhesion; NAS:UniProtKB. DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl. DR GO; GO:0002246; P:wound healing involved in inflammatory response; IEA:Ensembl. DR Gene3D; 3.10.100.10; -; 1. DR InterPro; IPR016186; C-type_lectin-like. DR InterPro; IPR016187; C-type_lectin_fold. DR InterPro; IPR001231; CD44_antigen. DR InterPro; IPR000538; Link_dom. DR Pfam; PF00193; Xlink; 1. DR PRINTS; PR00658; CD44. DR PRINTS; PR01265; LINKMODULE. DR SMART; SM00445; LINK; 1. DR SUPFAM; SSF56436; SSF56436; 1. DR PROSITE; PS01241; LINK_1; 1. DR PROSITE; PS50963; LINK_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Blood group antigen; KW Cell adhesion; Cell membrane; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane; KW Phosphoprotein; Polymorphism; Proteoglycan; KW Pyrrolidone carboxylic acid; Receptor; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 20 {ECO:0000250}. FT CHAIN 21 742 CD44 antigen. FT /FTId=PRO_0000026687. FT TOPO_DOM 21 649 Extracellular. {ECO:0000255}. FT TRANSMEM 650 670 Helical. {ECO:0000255}. FT TOPO_DOM 671 742 Cytoplasmic. {ECO:0000255}. FT DOMAIN 32 120 Link. {ECO:0000255|PROSITE- FT ProRule:PRU00323}. FT REGION 224 649 Stem. FT COMPBIAS 150 158 Arg/Lys-rich (basic). FT BINDING 41 41 Hyaluronan. {ECO:0000250}. FT BINDING 78 78 Hyaluronan. {ECO:0000250}. FT BINDING 79 79 Hyaluronan. {ECO:0000250}. FT BINDING 105 105 Hyaluronan. {ECO:0000250}. FT MOD_RES 21 21 Pyrrolidone carboxylic acid. FT {ECO:0000305}. FT MOD_RES 672 672 Phosphoserine; by PKC. FT {ECO:0000269|PubMed:12032545}. FT MOD_RES 686 686 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 697 697 Phosphoserine. FT {ECO:0000250|UniProtKB:P15379}. FT MOD_RES 706 706 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:19367720, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:21406692, FT ECO:0000269|PubMed:9580567}. FT CARBOHYD 25 25 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 57 57 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 100 100 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 110 110 N-linked (GlcNAc...). FT {ECO:0000269|PubMed:19159218}. FT CARBOHYD 120 120 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 350 350 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 548 548 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 599 599 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 636 636 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 637 637 O-linked (GalNAc...); or Thr-638. FT {ECO:0000269|PubMed:22171320}. FT CARBOHYD 638 638 O-linked (GalNAc...); or Thr-637. FT {ECO:0000269|PubMed:22171320}. FT DISULFID 28 129 {ECO:0000255|PROSITE-ProRule:PRU00323}. FT DISULFID 53 118 {ECO:0000255|PROSITE-ProRule:PRU00323}. FT DISULFID 77 97 {ECO:0000255|PROSITE-ProRule:PRU00323}. FT VAR_SEQ 23 29 DLNITCR -> GVGRRKS (in isoform 2). FT {ECO:0000303|PubMed:8352881}. FT /FTId=VSP_005303. FT VAR_SEQ 30 742 Missing (in isoform 2). FT {ECO:0000303|PubMed:8352881}. FT /FTId=VSP_005304. FT VAR_SEQ 78 139 RYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYC FT FNASAPPEEDCTSVTDLPNAF -> SLHCSQQSKKVWAEEK FT ASDQQWQWSCGGQKAKWTQRRGQQVSGNGAFGEQGVVRNSR FT PVYDS (in isoform 19). FT {ECO:0000303|PubMed:10933060}. FT /FTId=VSP_043870. FT VAR_SEQ 140 742 Missing (in isoform 19). FT {ECO:0000303|PubMed:10933060}. FT /FTId=VSP_043871. FT VAR_SEQ 192 192 G -> A (in isoform 3 and isoform 16). FT {ECO:0000305}. FT /FTId=VSP_005305. FT VAR_SEQ 193 223 Missing (in isoform 3 and isoform 16). FT {ECO:0000305}. FT /FTId=VSP_005306. FT VAR_SEQ 223 535 Missing (in isoform 11). FT {ECO:0000303|PubMed:2056274, FT ECO:0000303|Ref.12}. FT /FTId=VSP_022797. FT VAR_SEQ 223 223 T -> N (in isoform 10, isoform 13 and FT isoform 14). {ECO:0000303|PubMed:1991450, FT ECO:0000303|PubMed:2007624, FT ECO:0000303|PubMed:2056274, FT ECO:0000303|PubMed:8352881, FT ECO:0000303|Ref.11}. FT /FTId=VSP_005309. FT VAR_SEQ 223 223 T -> R (in isoform 12, isoform 15 and FT isoform 18). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005, FT ECO:0000303|PubMed:1840487, FT ECO:0000303|PubMed:2466575, FT ECO:0000303|PubMed:2466576, FT ECO:0000303|Ref.10, ECO:0000303|Ref.11, FT ECO:0000303|Ref.13}. FT /FTId=VSP_005311. FT VAR_SEQ 223 223 T -> S (in isoform 4). FT {ECO:0000303|PubMed:1281868, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_005307. FT VAR_SEQ 224 604 Missing (in isoform 12, isoform 15 and FT isoform 18). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17974005, FT ECO:0000303|PubMed:1840487, FT ECO:0000303|PubMed:2466575, FT ECO:0000303|PubMed:2466576, FT ECO:0000303|Ref.10, ECO:0000303|Ref.11, FT ECO:0000303|Ref.13}. FT /FTId=VSP_005312. FT VAR_SEQ 224 472 Missing (in isoform 10, isoform 13 and FT isoform 14). {ECO:0000303|PubMed:1991450, FT ECO:0000303|PubMed:2007624, FT ECO:0000303|PubMed:2056274, FT ECO:0000303|PubMed:8352881, FT ECO:0000303|Ref.11}. FT /FTId=VSP_005310. FT VAR_SEQ 224 266 Missing (in isoform 4). FT {ECO:0000303|PubMed:1281868, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_005308. FT VAR_SEQ 266 273 Missing (in isoform 5 and isoform 17). FT {ECO:0000305}. FT /FTId=VSP_005313. FT VAR_SEQ 385 385 I -> T (in isoform 6, isoform 16 and FT isoform 17). {ECO:0000305}. FT /FTId=VSP_005314. FT VAR_SEQ 386 428 Missing (in isoform 6, isoform 16 and FT isoform 17). {ECO:0000305}. FT /FTId=VSP_005315. FT VAR_SEQ 506 506 Q -> R (in isoform 7 and isoform 14). FT {ECO:0000303|PubMed:8352881}. FT /FTId=VSP_005316. FT VAR_SEQ 507 535 Missing (in isoform 7 and isoform 14). FT {ECO:0000303|PubMed:8352881}. FT /FTId=VSP_005317. FT VAR_SEQ 536 536 N -> R (in isoform 8, isoform 13 and FT isoform 14). FT {ECO:0000303|PubMed:8352881}. FT /FTId=VSP_005318. FT VAR_SEQ 537 604 Missing (in isoform 8, isoform 13 and FT isoform 14). FT {ECO:0000303|PubMed:8352881}. FT /FTId=VSP_005319. FT VAR_SEQ 605 625 Missing (in isoform 18). FT {ECO:0000303|Ref.13}. FT /FTId=VSP_043575. FT VAR_SEQ 675 675 R -> S (in isoform 9 and isoform 15). FT {ECO:0000303|PubMed:2466576}. FT /FTId=VSP_005320. FT VAR_SEQ 676 742 Missing (in isoform 9 and isoform 15). FT {ECO:0000303|PubMed:2466576}. FT /FTId=VSP_005321. FT VARIANT 46 46 R -> P (in In(A) antigen). FT {ECO:0000269|PubMed:8636151}. FT /FTId=VAR_006490. FT VARIANT 393 393 T -> M (in dbSNP:rs11607491). FT /FTId=VAR_030325. FT VARIANT 417 417 K -> R (in dbSNP:rs9666607). FT {ECO:0000269|PubMed:1465456, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:1717145, FT ECO:0000269|PubMed:7508842}. FT /FTId=VAR_021147. FT VARIANT 479 479 I -> T (in dbSNP:rs1467558). FT {ECO:0000269|PubMed:1281868, FT ECO:0000269|PubMed:1465456, FT ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:1991450, FT ECO:0000269|PubMed:2007624, FT ECO:0000269|PubMed:2056274, FT ECO:0000269|PubMed:7508842, FT ECO:0000269|PubMed:8352881, FT ECO:0000269|Ref.11}. FT /FTId=VAR_030326. FT VARIANT 494 494 D -> H (in dbSNP:rs12273397). FT {ECO:0000269|PubMed:7508842}. FT /FTId=VAR_030327. FT CONFLICT 26 26 I -> M (in Ref. 10; AAA82949). FT {ECO:0000305}. FT CONFLICT 109 109 S -> Y (in Ref. 1; AAA35674, 2; AAA51950, FT 3; CAA38951 and 7; CAB61878). FT {ECO:0000305}. FT CONFLICT 221 221 A -> R (in Ref. 3; CAA38951). FT {ECO:0000305}. FT CONFLICT 241 241 T -> A (in Ref. 7; CAB61878). FT {ECO:0000305}. FT CONFLICT 410 410 E -> V (in Ref. 5; CAA47271). FT {ECO:0000305}. FT CONFLICT 494 494 D -> N (in Ref. 7; CAB61878). FT {ECO:0000305}. FT CONFLICT 555 555 T -> H (in Ref. 3; CAA38951). FT {ECO:0000305}. FT CONFLICT 620 620 G -> E (in Ref. 1; AAA35674). FT {ECO:0000305}. FT CONFLICT 697 697 S -> I (in Ref. 11; AAM50041 and 16; FT AAH67348). {ECO:0000305}. FT STRAND 21 26 {ECO:0000244|PDB:4PZ3}. FT STRAND 33 38 {ECO:0000244|PDB:4PZ3}. FT HELIX 46 55 {ECO:0000244|PDB:4PZ3}. FT STRAND 57 59 {ECO:0000244|PDB:1POZ}. FT HELIX 63 71 {ECO:0000244|PDB:4PZ3}. FT STRAND 80 82 {ECO:0000244|PDB:4PZ3}. FT STRAND 85 92 {ECO:0000244|PDB:4PZ3}. FT HELIX 98 100 {ECO:0000244|PDB:4PZ3}. FT STRAND 103 106 {ECO:0000244|PDB:4PZ3}. FT STRAND 109 111 {ECO:0000244|PDB:1POZ}. FT STRAND 114 119 {ECO:0000244|PDB:4PZ3}. FT STRAND 121 123 {ECO:0000244|PDB:2I83}. FT STRAND 125 128 {ECO:0000244|PDB:4PZ3}. FT STRAND 130 132 {ECO:0000244|PDB:2I83}. FT STRAND 139 148 {ECO:0000244|PDB:4PZ3}. FT TURN 150 152 {ECO:0000244|PDB:1POZ}. FT STRAND 154 160 {ECO:0000244|PDB:4PZ3}. FT HELIX 165 168 {ECO:0000244|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 //