CD44_HUMAN
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 03-AUG-2022, entry version 248.
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 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 [52]
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 [53]
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 [54]
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 [55]
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 [56]
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: ipaB; 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}. Note=Colocalizes with actin in membrane
CC protrusions at wounding edges. Co-localizes with RDX, EZR and MSN in
CC microvilli. Localizes to cholesterol-rich membrane-bound lipid raft
CC domains. {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: Isoform 10 (epithelial isoform) is expressed by
CC cells of epithelium and highly expressed by carcinomas. Expression is
CC repressed in neuroblastoma cells.
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. O-glycosylation contains more-or-less-sulfated
CC chondroitin sulfate glycans, whose number may affect the accessibility
CC of specific proteinases to their cleavage site(s). It is uncertain if
CC O-glycosylation occurs on Thr-637 or Thr-638.
CC {ECO:0000269|PubMed:12883358, ECO:0000269|PubMed:22171320}.
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; 211.
DR CORUM; P16070; -.
DR DIP; DIP-1121N; -.
DR ELM; P16070; -.
DR IntAct; P16070; 121.
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 GlyGen; P16070; 25 sites, 41 N-linked glycans (2 sites), 2 O-linked glycans (10 sites).
DR iPTMnet; P16070; -.
DR MetOSite; P16070; -.
DR PhosphoSitePlus; P16070; -.
DR SwissPalm; P16070; -.
DR BioMuta; CD44; -.
DR DMDM; 308153615; -.
DR SWISS-2DPAGE; P16070; -.
DR CPTAC; CPTAC-668; -.
DR CPTAC; CPTAC-692; -.
DR EPD; P16070; -.
DR jPOST; P16070; -.
DR MassIVE; P16070; -.
DR MaxQB; P16070; -.
DR PaxDb; P16070; -.
DR PeptideAtlas; P16070; -.
DR PRIDE; 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 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; 5426 antibodies from 58 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 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; RTPATNM; -.
DR OrthoDB; 1098342at2759; -.
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; 25 hits in 1078 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 199 other tissues.
DR ExpressionAtlas; P16070; baseline and differential.
DR Genevisible; P16070; HS.
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:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
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:UniProtKB.
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 Gene3D; 3.10.100.10; -; 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; PTHR10225; 2.
DR PANTHER; PTHR10225:SF6; PTHR10225:SF6; 2.
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; Cell adhesion;
KW Cell membrane; Cell projection; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Membrane; Phosphoprotein; Proteoglycan; Receptor;
KW Reference proteome; 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 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
