ID CD44_MOUSE Reviewed; 778 AA. AC P15379; Q05732; Q61395; Q62060; Q62061; Q62062; Q62063; Q62408; Q62409; AC Q64296; Q99J14; Q9QYX8; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 30-APR-2003, sequence version 3. DT 27-MAR-2024, entry version 215. DE RecName: Full=CD44 antigen; 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=Hermes antigen; DE AltName: Full=Hyaluronate receptor; DE AltName: Full=Lymphocyte antigen 24; DE Short=Ly-24; 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=Ly-24; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6; 7 AND 12). RC STRAIN=DBA/2J; TISSUE=Lung; RX PubMed=1469058; DOI=10.1083/jcb.119.6.1711; RA He Q., Lesley J., Hyman R., Ishihara K., Kincade P.W.; RT "Molecular isoforms of murine CD44 and evidence that the membrane proximal RT domain is not critical for hyaluronate recognition."; RL J. Cell Biol. 119:1711-1719(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13), AND POLYMORPHISM. RX PubMed=2681416; RA Zhou D.F.H., Ding J.F., Picker L.J., Bargatze R.F., Butcher E.C., RA Goeddel D.V.; RT "Molecular cloning and expression of Pgp-1. The mouse homolog of the human RT H-CAM (Hermes) lymphocyte homing receptor."; RL J. Immunol. 143:3390-3395(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13). RX PubMed=2682651; DOI=10.1073/pnas.86.21.8521; RA Nottenburg C., Rees G., St John T.; RT "Isolation of mouse CD44 cDNA: structural features are distinct from the RT primate cDNA."; RL Proc. Natl. Acad. Sci. U.S.A. 86:8521-8525(1989). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10859330; DOI=10.1084/jem.191.12.2053; RA Wittig B.M., Johansson B., Zoeller M., Schwaerzler C., Guenthert U.; RT "Abrogation of experimental colitis correlates with increased apoptosis in RT mice deficient for CD44 variant exon 7 (CD44v7)."; RL J. Exp. Med. 191:2053-2064(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13). 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13). RC STRAIN=C57BL/6J; TISSUE=Embryo; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-778 (ISOFORM 13). RX PubMed=2403559; DOI=10.1016/s0021-9258(19)40235-4; RA Wolffe E.J., Gause W.C., Pelfrey C.M., Holland S.M., Steinberg A.D., RA August J.T.; RT "The cDNA sequence of mouse Pgp-1 and homology to human CD44 cell surface RT antigen and proteoglycan core/link proteins."; RL J. Biol. Chem. 265:341-347(1990). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-637 (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8). RC STRAIN=GR; RX PubMed=8464707; DOI=10.1093/nar/21.5.1225; RA Toelg C., Hofmann M., Herrlich P., Ponta H.; RT "Splicing choice from ten variant exons establishes CD44 variability."; RL Nucleic Acids Res. 21:1225-1229(1993). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 224-637 (ISOFORM 9). RC STRAIN=BALB/cJ; RX PubMed=8509359; DOI=10.1016/s0021-9258(18)31376-0; RA Screaton G.R., Bell M.V., Bell J.I., Jackson D.G.; RT "The identification of a new alternative exon with highly restricted tissue RT expression in transcripts encoding the mouse Pgp-1 (CD44) homing receptor. RT Comparison of all 10 variable exons between mouse, human, and rat."; RL J. Biol. Chem. 268:12235-12238(1993). RN [10] RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 10 AND 11). RC STRAIN=Swiss Webster; RX PubMed=8702806; DOI=10.1074/jbc.271.34.20603; RA Yu Q., Toole B.P.; RT "A new alternatively spliced exon between v9 and v10 provides a molecular RT basis for synthesis of soluble CD44."; RL J. Biol. Chem. 271:20603-20607(1996). RN [11] RP FUNCTION, AND INTERACTION WITH CD74. RX PubMed=8343954; DOI=10.1016/0092-8674(93)90417-o; RA Naujokas M.F., Morin M., Anderson M.S., Peterson M., Miller J.; RT "The chondroitin sulfate form of invariant chain can enhance stimulation of RT T cell responses through interaction with CD44."; RL Cell 74:257-268(1993). RN [12] RP INTERACTION WITH EZR; MSN AND RDX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP 715-LYS--LYS-717. RX PubMed=9472040; DOI=10.1083/jcb.140.4.885; RA Yonemura S., Hirao M., Doi Y., Takahashi N., Kondo T., Tsukita S., RA Tsukita S.; RT "Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino RT acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and RT ICAM-2."; RL J. Cell Biol. 140:885-895(1998). RN [13] RP INTERACTION WITH PKN2, AND SUBCELLULAR LOCATION. RX PubMed=17403031; DOI=10.1111/j.1471-4159.2007.04485.x; RA Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.; RT "Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma kinase RT activation leading to cytoskeleton function and cell migration in RT astrocytes."; RL J. Neurochem. 101:1002-1017(2007). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-726; SER-733 AND SER-742, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006; RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M., RA Thibault P.; RT "The phagosomal proteome in interferon-gamma-activated macrophages."; RL Immunity 30:143-154(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-726 AND SER-742, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Lung, and Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [16] RP INTERACTION WITH TIAM1 AND TIAM2. RX PubMed=19893486; DOI=10.1038/emboj.2009.323; RA Terawaki S., Kitano K., Mori T., Zhai Y., Higuchi Y., Itoh N., Watanabe T., RA Kaibuchi K., Hakoshima T.; RT "The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding RT module."; RL EMBO J. 29:236-250(2010). RN [17] RP TISSUE SPECIFICITY. RX PubMed=22510880; DOI=10.1038/emboj.2012.91; RA Wilson C.H., Crombie C., van der Weyden L., Poulogiannis G., Rust A.G., RA Pardo M., Gracia T., Yu L., Choudhary J., Poulin G.B., McIntyre R.E., RA Winton D.J., March H.N., Arends M.J., Fraser A.G., Adams D.J.; RT "Nuclear receptor binding protein 1 regulates intestinal progenitor cell RT homeostasis and tumour formation."; RL EMBO J. 31:2486-2497(2012). RN [18] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=25065622; DOI=10.1016/j.immuni.2014.06.011; RA Wu C., Thalhamer T., Franca R.F., Xiao S., Wang C., Hotta C., Zhu C., RA Hirashima M., Anderson A.C., Kuchroo V.K.; RT "Galectin-9-CD44 interaction enhances stability and function of adaptive RT regulatory T cells."; RL Immunity 41:270-282(2014). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 23-174 ALONE AND IN COMPLEX WITH RP HYALURONAN, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=17293874; DOI=10.1038/nsmb1201; RA Banerji S., Wright A.J., Noble M., Mahoney D.J., Campbell I.D., Day A.J., RA Jackson D.G.; RT "Structures of the Cd44-hyaluronan complex provide insight into a RT fundamental carbohydrate-protein interaction."; RL Nat. Struct. Mol. Biol. 14:234-239(2007). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 708-727, INTERACTION WITH RDX, RP AND DISULFIDE BOND. RX PubMed=18753140; DOI=10.1074/jbc.m803606200; RA Mori T., Kitano K., Terawaki S., Maesaki R., Fukami Y., Hakoshima T.; RT "Structural basis for CD44 recognition by ERM proteins."; RL J. Biol. Chem. 283:29602-29612(2008). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.12 ANGSTROMS) OF 23-171, INTERACTION WITH HA, AND RP DISULFIDE BOND. RX PubMed=24606063; DOI=10.1021/jm5000276; RA Liu L.K., Finzel B.C.; RT "Fragment-based identification of an inducible binding site on cell surface RT receptor CD44 for the design of protein-carbohydrate interaction RT inhibitors."; RL J. Med. Chem. 57:2714-2725(2014). 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. Participates thereby CC in a wide variety of cellular functions including the activation, CC recirculation and homing of T-lymphocytes, hematopoiesis, inflammation CC and response to bacterial infection. Engages, through its ectodomain, CC extracellular matrix components such as hyaluronan/HA, collagen, growth CC factors, cytokines or proteases and serves as a platform for signal CC transduction by assembling, via its cytoplasmic domain, protein CC complexes containing receptor kinases and membrane proteases CC (PubMed:8343954, PubMed:25065622). Such effectors include PKN2, the CC RhoGTPases RAC1 and RHOA, Rho-kinases and phospholipase C that CC coordinate signaling pathways promoting calcium mobilization and actin- CC mediated cytoskeleton reorganization essential for cell migration and CC adhesion (By similarity). {ECO:0000250|UniProtKB:P16070, CC ECO:0000269|PubMed:25065622, ECO:0000269|PubMed:8343954}. CC -!- SUBUNIT: Interacts with PKN2 (PubMed:17403031). Interacts with TIAM1 CC and TIAM2 (PubMed:19893486). Interacts with HA, as well as other CC glycosaminoglycans, collagen, laminin, and fibronectin via its N- CC terminal segment (PubMed:24606063). Interacts with UNC119. Interacts CC with PDPN (via extracellular domain); this interaction is required for CC PDPN-mediated directional migration and regulation of lamellipodia CC extension/stabilization during cell spreading and migration (By CC similarity). Interacts with RDX, EZR and MSN (via FERM domain) CC (PubMed:9472040, PubMed:18753140). Interacts with EGFR (By similarity). CC Interacts with CD74; this complex is essential for the MIF-induced CC signaling cascade that results in B cell survival (PubMed:8343954). CC {ECO:0000250|UniProtKB:P16070, ECO:0000269|PubMed:17403031, CC ECO:0000269|PubMed:18753140, ECO:0000269|PubMed:19893486, CC ECO:0000269|PubMed:24606063, ECO:0000269|PubMed:8343954, CC ECO:0000269|PubMed:9472040}. CC -!- INTERACTION: CC P15379; O08573: Lgals9; NbExp=2; IntAct=EBI-7565891, EBI-8377586; CC P15379; Q64729: Tgfbr1; NbExp=4; IntAct=EBI-7565891, EBI-2899393; CC P15379; Q60610: Tiam1; NbExp=8; IntAct=EBI-7565891, EBI-1030321; CC P15379; Q6ZPF3: Tiam2; NbExp=8; IntAct=EBI-7565891, EBI-7565978; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17403031, CC ECO:0000269|PubMed:25065622}; Single-pass type I membrane protein CC {ECO:0000269|PubMed:17403031}. Cell projection, microvillus CC {ECO:0000269|PubMed:9472040}. Secreted {ECO:0000250|UniProtKB:P16070}. CC Note=Colocalizes with actin in membrane protrusionFs at wounding edges. CC Co-localizes with RDX, EZR and MSN in microvilli. CC {ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:9472040}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=13; CC Name=1; CC IsoId=P15379-14; Sequence=Displayed; CC Name=2; CC IsoId=P15379-7; Sequence=VSP_007329; CC Name=3; CC IsoId=P15379-8; Sequence=VSP_007330; CC Name=4; Synonyms=M2; CC IsoId=P15379-4; Sequence=VSP_007331; CC Name=5; CC IsoId=P15379-9; Sequence=VSP_007332; CC Name=6; Synonyms=M3; CC IsoId=P15379-5; Sequence=VSP_005326; CC Name=7; Synonyms=M4; CC IsoId=P15379-6; Sequence=VSP_005327; CC Name=8; CC IsoId=P15379-10; Sequence=VSP_007330, VSP_007334; CC Name=9; CC IsoId=P15379-11; Sequence=VSP_007332, VSP_007335; CC Name=10; CC IsoId=P15379-12; Sequence=VSP_007336, VSP_007337; CC Name=11; CC IsoId=P15379-13; Sequence=VSP_007338, VSP_007339; CC Name=12; Synonyms=M1; CC IsoId=P15379-3; Sequence=VSP_005328; CC Name=13; Synonyms=M0; CC IsoId=P15379-2; Sequence=VSP_005329, VSP_007333; CC -!- TISSUE SPECIFICITY: Expressed in the intestinal epithelium. CC {ECO:0000269|PubMed:22510880}. CC -!- DOMAIN: The lectin-like LINK domain is responsible for hyaluronan CC binding. CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P16070}. CC -!- PTM: O-glycosylated; contains chondroitin sulfate glycans which can be CC more or less sulfated. {ECO:0000250|UniProtKB:P16070}. CC -!- PTM: Phosphorylated; activation of PKC results in the dephosphorylation CC of Ser-742 (constitutive phosphorylation site), and the phosphorylation CC of Ser-708. {ECO:0000250}. CC -!- POLYMORPHISM: Two allelic forms of this glycoprotein, PGP-1.1 and PGP- CC 1.2, have been reported. The expressed product is PGP-1.1 (Ly-24.1). 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; X66084; CAA46883.1; -; mRNA. DR EMBL; X66083; CAA46882.1; -; mRNA. DR EMBL; X66082; CAA46881.1; -; mRNA. DR EMBL; X66081; CAA46880.1; -; mRNA. DR EMBL; M30655; AAA39922.1; -; mRNA. DR EMBL; M27129; AAA37406.1; -; mRNA. DR EMBL; M27130; AAA37407.1; -; mRNA. DR EMBL; AJ251594; CAB61888.1; -; mRNA. DR EMBL; BC005676; AAH05676.1; -; mRNA. DR EMBL; AK045226; BAC32269.1; -; mRNA. DR EMBL; J05163; AAA39923.1; -; mRNA. DR EMBL; X69724; CAA49380.1; -; mRNA. DR EMBL; L13611; AAA37145.1; -; mRNA. DR EMBL; U57610; AAC52804.1; -; mRNA. DR EMBL; U57611; AAB08756.1; -; mRNA. DR EMBL; U57612; AAC52805.1; -; Genomic_DNA. DR EMBL; U57612; AAC52806.1; -; Genomic_DNA. DR PIR; A34424; A34424. DR PIR; A37009; A37009. DR PIR; B44355; B44355. DR PIR; D44355; D44355. DR PIR; S30397; S30397. DR RefSeq; NP_001034240.1; NM_001039151.1. DR RefSeq; NP_001171256.1; NM_001177785.1. DR RefSeq; NP_001171257.1; NM_001177786.1. DR RefSeq; NP_001171258.1; NM_001177787.1. DR RefSeq; NP_033981.2; NM_009851.2. DR PDB; 2JCP; X-ray; 1.30 A; A=23-174. DR PDB; 2JCQ; X-ray; 1.25 A; A=23-174. DR PDB; 2JCR; X-ray; 2.00 A; A=23-174. DR PDB; 2ZPY; X-ray; 2.10 A; B=708-727. DR PDB; 4MRD; X-ray; 2.55 A; A=23-171. DR PDB; 4MRE; X-ray; 1.58 A; A=23-171. DR PDB; 4MRF; X-ray; 1.55 A; A=23-171. DR PDB; 4MRG; X-ray; 1.69 A; A=23-171. DR PDB; 4MRH; X-ray; 1.12 A; A=23-171. DR PDB; 4NP2; X-ray; 1.75 A; A=23-171. DR PDB; 4NP3; X-ray; 1.61 A; A=23-171. DR PDB; 5BZC; X-ray; 1.95 A; A=22-171. DR PDB; 5BZE; X-ray; 1.31 A; A=23-171. DR PDB; 5BZF; X-ray; 2.77 A; A=21-171. DR PDB; 5BZG; X-ray; 2.19 A; A=21-171. DR PDB; 5BZH; X-ray; 1.95 A; A=21-171. DR PDB; 5BZI; X-ray; 1.32 A; A=21-171. DR PDB; 5BZJ; X-ray; 1.40 A; A=21-171. DR PDB; 5BZK; X-ray; 1.40 A; A=21-171. DR PDB; 5BZL; X-ray; 1.23 A; A=21-171. DR PDB; 5BZM; X-ray; 1.25 A; A=21-171. DR PDB; 5BZN; X-ray; 1.23 A; A=21-171. DR PDB; 5BZO; X-ray; 1.22 A; A=21-171. DR PDB; 5BZP; X-ray; 1.23 A; A=21-171. DR PDB; 5BZQ; X-ray; 1.20 A; A=21-171. DR PDB; 5BZR; X-ray; 1.15 A; A=21-171. DR PDB; 5BZS; X-ray; 1.50 A; A=21-171. DR PDB; 5BZT; X-ray; 1.25 A; A=21-171. DR PDB; 5SBK; X-ray; 1.23 A; A=23-172. DR PDB; 5SBL; X-ray; 1.20 A; A=23-172. DR PDB; 5SBM; X-ray; 1.14 A; A=23-172. DR PDB; 5SBN; X-ray; 1.18 A; A=23-172. DR PDB; 5SBO; X-ray; 1.27 A; A=23-172. DR PDB; 5SBP; X-ray; 1.27 A; A=23-172. DR PDB; 5SBQ; X-ray; 0.99 A; A=23-172. DR PDB; 5SBR; X-ray; 1.29 A; A=23-172. DR PDB; 5SBS; X-ray; 1.02 A; A=23-172. DR PDB; 5SBT; X-ray; 1.16 A; A=23-172. DR PDB; 5SBU; X-ray; 1.04 A; A=23-172. DR PDB; 5SBV; X-ray; 1.11 A; A=23-172. DR PDB; 5SBW; X-ray; 1.15 A; A=23-172. DR PDB; 5SBX; X-ray; 1.05 A; A=23-172. DR PDB; 5SBY; X-ray; 1.22 A; A=23-172. DR PDB; 5SBZ; X-ray; 1.17 A; A=23-172. DR PDB; 5SC0; X-ray; 1.19 A; A=23-172. DR PDB; 5SC1; X-ray; 1.17 A; A=23-172. DR PDB; 5SC2; X-ray; 1.21 A; A=23-172. DR PDB; 5SC3; X-ray; 1.24 A; A=23-172. DR PDB; 5SC4; X-ray; 1.17 A; A=23-172. DR PDB; 5SC5; X-ray; 1.17 A; A=23-172. DR PDB; 5SC6; X-ray; 1.33 A; A=23-172. DR PDB; 5SC7; X-ray; 1.20 A; A=23-172. DR PDBsum; 2JCP; -. DR PDBsum; 2JCQ; -. DR PDBsum; 2JCR; -. DR PDBsum; 2ZPY; -. DR PDBsum; 4MRD; -. DR PDBsum; 4MRE; -. DR PDBsum; 4MRF; -. DR PDBsum; 4MRG; -. DR PDBsum; 4MRH; -. DR PDBsum; 4NP2; -. DR PDBsum; 4NP3; -. DR PDBsum; 5BZC; -. DR PDBsum; 5BZE; -. DR PDBsum; 5BZF; -. DR PDBsum; 5BZG; -. DR PDBsum; 5BZH; -. DR PDBsum; 5BZI; -. DR PDBsum; 5BZJ; -. DR PDBsum; 5BZK; -. DR PDBsum; 5BZL; -. DR PDBsum; 5BZM; -. DR PDBsum; 5BZN; -. DR PDBsum; 5BZO; -. DR PDBsum; 5BZP; -. DR PDBsum; 5BZQ; -. DR PDBsum; 5BZR; -. DR PDBsum; 5BZS; -. DR PDBsum; 5BZT; -. DR PDBsum; 5SBK; -. DR PDBsum; 5SBL; -. DR PDBsum; 5SBM; -. DR PDBsum; 5SBN; -. DR PDBsum; 5SBO; -. DR PDBsum; 5SBP; -. DR PDBsum; 5SBQ; -. DR PDBsum; 5SBR; -. DR PDBsum; 5SBS; -. DR PDBsum; 5SBT; -. DR PDBsum; 5SBU; -. DR PDBsum; 5SBV; -. DR PDBsum; 5SBW; -. DR PDBsum; 5SBX; -. DR PDBsum; 5SBY; -. DR PDBsum; 5SBZ; -. DR PDBsum; 5SC0; -. DR PDBsum; 5SC1; -. DR PDBsum; 5SC2; -. DR PDBsum; 5SC3; -. DR PDBsum; 5SC4; -. DR PDBsum; 5SC5; -. DR PDBsum; 5SC6; -. DR PDBsum; 5SC7; -. DR AlphaFoldDB; P15379; -. DR SMR; P15379; -. DR BioGRID; 198600; 4. DR CORUM; P15379; -. DR DIP; DIP-29095N; -. DR IntAct; P15379; 14. DR MINT; P15379; -. DR STRING; 10090.ENSMUSP00000005218; -. DR BindingDB; P15379; -. DR ChEMBL; CHEMBL3232693; -. DR GlyCosmos; P15379; 10 sites, No reported glycans. DR GlyGen; P15379; 12 sites, 1 O-linked glycan (1 site). DR iPTMnet; P15379; -. DR PhosphoSitePlus; P15379; -. DR SwissPalm; P15379; -. DR EPD; P15379; -. DR jPOST; P15379; -. DR MaxQB; P15379; -. DR PaxDb; 10090-ENSMUSP00000005218; -. DR PeptideAtlas; P15379; -. DR ProteomicsDB; 279969; -. [P15379-14] DR ProteomicsDB; 279970; -. [P15379-7] DR ProteomicsDB; 279971; -. [P15379-8] DR ProteomicsDB; 279972; -. [P15379-4] DR ProteomicsDB; 279973; -. [P15379-9] DR ProteomicsDB; 279974; -. [P15379-5] DR ProteomicsDB; 279975; -. [P15379-6] DR ProteomicsDB; 279976; -. [P15379-10] DR ProteomicsDB; 279977; -. [P15379-11] DR ProteomicsDB; 279978; -. [P15379-12] DR ProteomicsDB; 279979; -. [P15379-13] DR ProteomicsDB; 279980; -. [P15379-3] DR ProteomicsDB; 279981; -. [P15379-2] DR Pumba; P15379; -. DR DNASU; 12505; -. DR GeneID; 12505; -. DR KEGG; mmu:12505; -. DR AGR; MGI:88338; -. DR CTD; 960; -. DR MGI; MGI:88338; Cd44. DR eggNOG; ENOG502RX7Q; Eukaryota. DR InParanoid; P15379; -. DR OrthoDB; 5358652at2759; -. DR Reactome; R-MMU-1474228; Degradation of the extracellular matrix. DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall. DR Reactome; R-MMU-216083; Integrin cell surface interactions. DR Reactome; R-MMU-2160916; Hyaluronan uptake and degradation. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR BioGRID-ORCS; 12505; 1 hit in 81 CRISPR screens. DR ChiTaRS; Cd44; mouse. DR EvolutionaryTrace; P15379; -. DR PRO; PR:P15379; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P15379; Protein. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI. DR GO; GO:0042995; C:cell projection; ISS:UniProtKB. DR GO; GO:0009986; C:cell surface; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0031258; C:lamellipodium membrane; ISS:UniProtKB. DR GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IDA:BHF-UCL. DR GO; GO:0045121; C:membrane raft; ISO:MGI. DR GO; GO:0005902; C:microvillus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0038024; F:cargo receptor activity; IDA:MGI. DR GO; GO:0016247; F:channel regulator activity; ISO:MGI. DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI. DR GO; GO:0005540; F:hyaluronic acid binding; IMP:MGI. DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central. DR GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IPI:UniProtKB. DR GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IMP:MGI. DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI. DR GO; GO:0007155; P:cell adhesion; ISO:MGI. DR GO; GO:0016477; P:cell migration; ISO:MGI. DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISO:MGI. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:GOC. DR GO; GO:0030214; P:hyaluronan catabolic process; IDA:MGI. DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central. DR GO; GO:0034238; P:macrophage fusion; ISO:MGI. DR GO; GO:0070487; P:monocyte aggregation; ISO:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; IMP:UniProtKB. DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL. DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB. DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:BHF-UCL. DR GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IDA:BHF-UCL. DR GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; IMP:UniProtKB. DR GO; GO:0031175; P:neuron projection development; ISO:MGI. DR GO; GO:0002821; P:positive regulation of adaptive immune response; NAS:BHF-UCL. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL. DR GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI. DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:MGI. DR GO; GO:1900625; P:positive regulation of monocyte aggregation; ISO:MGI. DR GO; GO:0033031; P:positive regulation of neutrophil apoptotic process; ISO:MGI. DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL. DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL. DR GO; GO:0006898; P:receptor-mediated endocytosis; IDA:MGI. DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI. DR GO; GO:2000392; P:regulation of lamellipodium morphogenesis; ISS:UniProtKB. DR GO; GO:0042110; P:T cell activation; ISO:MGI. DR GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI. DR GO; GO:0002246; P:wound healing involved in inflammatory response; IMP:MGI. DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB. DR CDD; cd03516; Link_domain_CD44_like; 1. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1. DR IDEAL; IID50199; -. DR InterPro; IPR016186; C-type_lectin-like/link_sf. DR InterPro; IPR001231; CD44_antigen. DR InterPro; IPR043210; CD44_antigen-like. DR InterPro; IPR016187; CTDL_fold. DR InterPro; IPR000538; Link_dom. DR PANTHER; PTHR10225:SF6; CD44 ANTIGEN; 1. DR PANTHER; PTHR10225; HYALURONAN RECEPTOR; 1. DR Pfam; PF00193; Xlink; 1. DR PRINTS; PR00658; CD44. DR PRINTS; PR01265; LINKMODULE. DR SMART; SM00445; LINK; 1. DR SUPFAM; SSF56436; C-type lectin-like; 1. DR PROSITE; PS01241; LINK_1; 1. DR PROSITE; PS50963; LINK_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane; KW Cell projection; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; KW Proteoglycan; Receptor; Reference proteome; Secreted; Signal; Sulfation; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..22 FT /evidence="ECO:0000250" FT CHAIN 23..778 FT /note="CD44 antigen" FT /id="PRO_0000026689" FT TOPO_DOM 23..685 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 686..706 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 707..778 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 34..123 FT /note="Link" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323" FT REGION 227..685 FT /note="Stem" FT REGION 251..277 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 293..338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 351..370 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 391..591 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 628..678 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 709..727 FT /note="Required for interaction with EZR, MSN and RDX and FT for the co-localization to microvilli" FT /evidence="ECO:0000269|PubMed:9472040" FT COMPBIAS 293..315 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 391..405 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 417..485 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 496..524 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 531..548 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 560..591 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 649..678 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 43 FT /ligand="hyaluronan" FT /ligand_id="ChEBI:CHEBI:132153" FT /evidence="ECO:0000269|PubMed:17293874" FT BINDING 80 FT /ligand="hyaluronan" FT /ligand_id="ChEBI:CHEBI:132153" FT /evidence="ECO:0000269|PubMed:17293874" FT BINDING 81 FT /ligand="hyaluronan" FT /ligand_id="ChEBI:CHEBI:132153" FT /evidence="ECO:0000269|PubMed:17293874" FT BINDING 107 FT /ligand="hyaluronan" FT /ligand_id="ChEBI:CHEBI:132153" FT /evidence="ECO:0000269|PubMed:17293874" FT MOD_RES 410 FT /note="Sulfotyrosine" FT /evidence="ECO:0000250" FT MOD_RES 708 FT /note="Phosphoserine; by PKC" FT /evidence="ECO:0000250|UniProtKB:P16070" FT MOD_RES 726 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT MOD_RES 733 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319" FT MOD_RES 742 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19144319, FT ECO:0007744|PubMed:21183079" FT CARBOHYD 27 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 59 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 102 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 113 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 123 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 183 FT /note="O-linked (Xyl...) (chondroitin sulfate) serine" FT /evidence="ECO:0000250|UniProtKB:P16070" FT CARBOHYD 368 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 425 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 529 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 545 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 603 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 30..132 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323, FT ECO:0000269|PubMed:17293874, ECO:0000269|PubMed:18753140, FT ECO:0000269|PubMed:24606063" FT DISULFID 55..121 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323, FT ECO:0000269|PubMed:17293874, ECO:0000269|PubMed:18753140, FT ECO:0000269|PubMed:24606063" FT DISULFID 79..99 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323, FT ECO:0000269|PubMed:17293874, ECO:0000269|PubMed:18753140, FT ECO:0000269|PubMed:24606063" FT VAR_SEQ 223..637 FT /note="Missing (in isoform 13)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:2403559, FT ECO:0000303|PubMed:2681416, ECO:0000303|PubMed:2682651" FT /id="VSP_005329" FT VAR_SEQ 223..539 FT /note="Missing (in isoform 12)" FT /evidence="ECO:0000303|PubMed:1469058" FT /id="VSP_005328" FT VAR_SEQ 223..504 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:1469058, FT ECO:0000303|PubMed:8464707" FT /id="VSP_005327" FT VAR_SEQ 223..424 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:1469058, FT ECO:0000303|PubMed:8464707" FT /id="VSP_005326" FT VAR_SEQ 223..383 FT /note="Missing (in isoform 5 and isoform 9)" FT /evidence="ECO:0000303|PubMed:8464707, FT ECO:0000303|PubMed:8509359" FT /id="VSP_007332" FT VAR_SEQ 223..346 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:1469058, FT ECO:0000303|PubMed:8464707" FT /id="VSP_007331" FT VAR_SEQ 223..303 FT /note="Missing (in isoform 3 and isoform 8)" FT /evidence="ECO:0000303|PubMed:8464707" FT /id="VSP_007330" FT VAR_SEQ 223..264 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8464707" FT /id="VSP_007329" FT VAR_SEQ 424..504 FT /note="Missing (in isoform 8)" FT /evidence="ECO:0000303|PubMed:8464707" FT /id="VSP_007334" FT VAR_SEQ 463..504 FT /note="Missing (in isoform 9)" FT /evidence="ECO:0000303|PubMed:8509359" FT /id="VSP_007335" FT VAR_SEQ 569..592 FT /note="TKSSAKDARRGGSLPTDTTTSVEG -> VRIIKSNWLLSRNQDVMGVSGGGC FT (in isoform 11)" FT /evidence="ECO:0000305" FT /id="VSP_007338" FT VAR_SEQ 569..580 FT /note="TKSSAKDARRGG -> VCLVVVADFSAL (in isoform 10)" FT /evidence="ECO:0000305" FT /id="VSP_007336" FT VAR_SEQ 581..778 FT /note="Missing (in isoform 10)" FT /evidence="ECO:0000305" FT /id="VSP_007337" FT VAR_SEQ 593..778 FT /note="Missing (in isoform 11)" FT /evidence="ECO:0000305" FT /id="VSP_007339" FT VAR_SEQ 638 FT /note="G -> R (in isoform 13)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:2403559, FT ECO:0000303|PubMed:2681416, ECO:0000303|PubMed:2682651" FT /id="VSP_007333" FT VARIANT 21 FT /note="H -> HPH (in Ly-24.2)" FT /evidence="ECO:0000269|PubMed:2682651" FT VARIANT 194 FT /note="G -> S (in Ly-24.2)" FT /evidence="ECO:0000269|PubMed:2682651" FT MUTAGEN 715..717 FT /note="KKK->QIN: Loss of interaction with EZR, MSN and RDX FT and co-localization to microvilli with EZR, MSN and RDX." FT /evidence="ECO:0000269|PubMed:9472040" FT CONFLICT 326 FT /note="T -> K (in Ref. 4 and 9)" FT /evidence="ECO:0000305" FT CONFLICT 348 FT /note="T -> S (in Ref. 9)" FT /evidence="ECO:0000305" FT CONFLICT 559 FT /note="Y -> H (in Ref. 4, 8 and 9)" FT /evidence="ECO:0000305" FT CONFLICT 572 FT /note="S -> G (in Ref. 4, 8 and 9)" FT /evidence="ECO:0000305" FT CONFLICT 639 FT /note="D -> RD (in Ref. 7)" FT /evidence="ECO:0000305" FT STRAND 23..28 FT /evidence="ECO:0007829|PDB:5SBQ" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:5SBQ" FT HELIX 48..57 FT /evidence="ECO:0007829|PDB:5SBQ" FT HELIX 65..73 FT /evidence="ECO:0007829|PDB:5SBQ" FT STRAND 85..94 FT /evidence="ECO:0007829|PDB:5SBQ" FT HELIX 100..102 FT /evidence="ECO:0007829|PDB:5SBQ" FT STRAND 105..108 FT /evidence="ECO:0007829|PDB:5SBQ" FT STRAND 117..122 FT /evidence="ECO:0007829|PDB:5SBQ" FT STRAND 128..131 FT /evidence="ECO:0007829|PDB:5SBQ" FT STRAND 142..152 FT /evidence="ECO:0007829|PDB:5SBQ" FT STRAND 157..163 FT /evidence="ECO:0007829|PDB:5SBQ" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:5SBQ" FT STRAND 715..719 FT /evidence="ECO:0007829|PDB:2ZPY" SQ SEQUENCE 778 AA; 85617 MW; BD2C073250F6C956 CRC64; MDKFWWHTAW GLCLLQLSLA HQQIDLNVTC RYAGVFHVEK NGRYSISRTE AADLCQAFNS TLPTMDQMKL ALSKGFETCR YGFIEGNVVI PRIHPNAICA ANHTGVYILV TSNTSHYDTY CFNASAPPEE DCTSVTDLPN SFDGPVTITI VNRDGTRYSK KGEYRTHQED IDASNIIDDD VSSGSTIEKS TPEGYILHTY LPTEQPTGDQ DDSFFIRSTL ATIASTVHSK SHAAAQKQNN WIWSWFGNSQ STTQTQEPTT SATTALMTTP ETPPKRQEAQ NWFSWLFQPS ESKSHLHTTT KMPGTESNTN PTGWEPNEEN EDETDTYPSF SGSGIDDDED FISSTIATTP RVSARTEDNQ DWTQWKPNHS NPEVLLQTTT RMADIDRIST SAHGENWTPE PQPPFNNHEY QDEEETPHAT STTPNSTAEA AATQQETWFQ NGWQGKNPPT PSEDSHVTEG TTASAHNNHP SQRITTQSQE DVSWTDFFDP ISHPMGQGHQ TESKDTDSSH STTLQPTAAP NTHLVEDLNR TGPLSVTTPQ SHSQNFSTLH GEPEEDENYP TTSILPSSTK SSAKDARRGG SLPTDTTTSV EGYTFQYPDT MENGTLFPVT PAKTEVFGET EVTLATDSNV NVDGSLPGDR DSSKDSRGSS RTVTHGSELA GHSSANQDSG VTTTSGPMRR PQIPEWLIIL ASLLALALIL AVCIAVNSRR RCGQKKKLVI NGGNGTVEDR KPSELNGEAS KSQEMVHLVN KEPSETPDQC MTADETRNLQ SVDMKIGV //