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CD44 antigen (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Hermes antigen) (Hyaluronate receptor) (Lymphocyte antigen 24) (Ly-24) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)

 CD44_MOUSE              Reviewed;         778 AA.
P15379; Q05732; Q61395; Q62060; Q62061; Q62062; Q62063; Q62408;
Q62409; Q64296; Q99J14; Q9QYX8;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
30-APR-2003, sequence version 3.
27-SEP-2017, entry version 182.
RecName: Full=CD44 antigen;
AltName: Full=Extracellular matrix receptor III;
Short=ECMR-III;
AltName: Full=GP90 lymphocyte homing/adhesion receptor;
AltName: Full=HUTCH-I;
AltName: Full=Hermes antigen;
AltName: Full=Hyaluronate receptor;
AltName: Full=Lymphocyte antigen 24;
Short=Ly-24;
AltName: Full=Phagocytic glycoprotein 1;
Short=PGP-1;
AltName: Full=Phagocytic glycoprotein I;
Short=PGP-I;
AltName: CD_antigen=CD44;
Flags: Precursor;
Name=Cd44; Synonyms=Ly-24;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 6; 7 AND 12).
STRAIN=DBA/2J; TISSUE=Lung;
PubMed=1469058; DOI=10.1083/jcb.119.6.1711;
He Q., Lesley J., Hyman R., Ishihara K., Kincade P.W.;
"Molecular isoforms of murine CD44 and evidence that the membrane
proximal domain is not critical for hyaluronate recognition.";
J. Cell Biol. 119:1711-1719(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13), AND POLYMORPHISM.
PubMed=2681416;
Zhou D.F.H., Ding J.F., Picker L.J., Bargatze R.F., Butcher E.C.,
Goeddel D.V.;
"Molecular cloning and expression of Pgp-1. The mouse homolog of the
human H-CAM (Hermes) lymphocyte homing receptor.";
J. Immunol. 143:3390-3395(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 13).
PubMed=2682651; DOI=10.1073/pnas.86.21.8521;
Nottenburg C., Rees G., St John T.;
"Isolation of mouse CD44 cDNA: structural features are distinct from
the primate cDNA.";
Proc. Natl. Acad. Sci. U.S.A. 86:8521-8525(1989).
[4]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
PubMed=10859330; DOI=10.1084/jem.191.12.2053;
Wittig B.M., Johansson B., Zoeller M., Schwaerzler C., Guenthert U.;
"Abrogation of experimental colitis correlates with increased
apoptosis in mice deficient for CD44 variant exon 7 (CD44v7).";
J. Exp. Med. 191:2053-2064(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-778 (ISOFORM 13).
PubMed=2403559;
Wolffe E.J., Gause W.C., Pelfrey C.M., Holland S.M., Steinberg A.D.,
August J.T.;
"The cDNA sequence of mouse Pgp-1 and homology to human CD44 cell
surface antigen and proteoglycan core/link proteins.";
J. Biol. Chem. 265:341-347(1990).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 224-637 (ISOFORMS 1; 2; 3; 4; 5; 6; 7
AND 8).
STRAIN=GR;
PubMed=8464707; DOI=10.1093/nar/21.5.1225;
Toelg C., Hofmann M., Herrlich P., Ponta H.;
"Splicing choice from ten variant exons establishes CD44
variability.";
Nucleic Acids Res. 21:1225-1229(1993).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 224-637 (ISOFORM 9).
STRAIN=BALB/cJ;
PubMed=8509359;
Screaton G.R., Bell M.V., Bell J.I., Jackson D.G.;
"The identification of a new alternative exon with highly restricted
tissue expression in transcripts encoding the mouse Pgp-1 (CD44)
homing receptor. Comparison of all 10 variable exons between mouse,
human, and rat.";
J. Biol. Chem. 268:12235-12238(1993).
[10]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 10 AND 11).
STRAIN=Swiss Webster;
PubMed=8702806; DOI=10.1074/jbc.271.34.20603;
Yu Q., Toole B.P.;
"A new alternatively spliced exon between v9 and v10 provides a
molecular basis for synthesis of soluble CD44.";
J. Biol. Chem. 271:20603-20607(1996).
[11]
INTERACTION WITH PKN2, AND SUBCELLULAR LOCATION.
PubMed=17403031; DOI=10.1111/j.1471-4159.2007.04485.x;
Bourguignon L.Y., Gilad E., Peyrollier K., Brightman A., Swanson R.A.;
"Hyaluronan-CD44 interaction stimulates Rac1 signaling and PKN gamma
kinase activation leading to cytoskeleton function and cell migration
in astrocytes.";
J. Neurochem. 101:1002-1017(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-726; SER-733 AND
SER-742, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-726 AND SER-742, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
INTERACTION WITH TIAM1 AND TIAM2.
PubMed=19893486; DOI=10.1038/emboj.2009.323;
Terawaki S., Kitano K., Mori T., Zhai Y., Higuchi Y., Itoh N.,
Watanabe T., Kaibuchi K., Hakoshima T.;
"The PHCCEx domain of Tiam1/2 is a novel protein- and membrane-binding
module.";
EMBO J. 29:236-250(2010).
[15]
FUNCTION AS RECEPTOR FOR LGALS9, AND SUBCELLULAR LOCATION.
PubMed=25065622; DOI=10.1016/j.immuni.2014.06.011;
Wu C., Thalhamer T., Franca R.F., Xiao S., Wang C., Hotta C., Zhu C.,
Hirashima M., Anderson A.C., Kuchroo V.K.;
"Galectin-9-CD44 interaction enhances stability and function of
adaptive regulatory T cells.";
Immunity 41:270-282(2014).
[16]
X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 23-174 ALONE AND IN COMPLEX
WITH HYALURONAN, SUBUNIT, AND DISULFIDE BONDS.
PubMed=17293874; DOI=10.1038/nsmb1201;
Banerji S., Wright A.J., Noble M., Mahoney D.J., Campbell I.D.,
Day A.J., Jackson D.G.;
"Structures of the Cd44-hyaluronan complex provide insight into a
fundamental carbohydrate-protein interaction.";
Nat. Struct. Mol. Biol. 14:234-239(2007).
-!- FUNCTION: Receptor for hyaluronic acid (HA). Mediates cell-cell
and cell-matrix interactions through its affinity for HA, and
possibly also through its affinity for other ligands such as
osteopontin, collagens, and matrix metalloproteinases (MMPs).
Adhesion with HA plays an important role in cell migration, tumor
growth and progression. In cancer cells, may play an important
role in invadopodia formation. Also involved in lymphocyte
activation, recirculation and homing, and in hematopoiesis (By
similarity). Receptor for LGALS9; the interaction enhances binding
of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3
expression and increased induced regulatory T (iTreg) cell
stability and suppressive function (PubMed:25065622).
{ECO:0000250|UniProtKB:P16070, ECO:0000269|PubMed:25065622}.
-!- SUBUNIT: Interacts with HA, as well as other glycosaminoglycans,
collagen, laminin, and fibronectin via its N-terminal segment (By
similarity). Interacts with ANK, the ERM proteins (VIL2, RDX and
MSN), and NF2 via its C-terminal segment. Interacts with PKN2
(PubMed:17403031). Interacts with TIAM1 and TIAM2
(PubMed:19893486). Interacts with UNC119 (By similarity).
{ECO:0000250|UniProtKB:P16070, ECO:0000269|PubMed:17403031,
ECO:0000269|PubMed:19893486}.
-!- INTERACTION:
O08573:Lgals9; NbExp=2; IntAct=EBI-7565891, EBI-8377586;
Q64729:Tgfbr1; NbExp=4; IntAct=EBI-7565891, EBI-2899393;
Q60610:Tiam1; NbExp=8; IntAct=EBI-7565891, EBI-1030321;
Q6ZPF3:Tiam2; NbExp=8; IntAct=EBI-7565891, EBI-7565978;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17403031,
ECO:0000269|PubMed:25065622}; Single-pass type I membrane protein
{ECO:0000269|PubMed:17403031}. Note=Colocalizes with actin in
membrane protrusions at wounding edges.
{ECO:0000269|PubMed:17403031}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=13;
Name=1;
IsoId=P15379-14; Sequence=Displayed;
Name=2;
IsoId=P15379-7; Sequence=VSP_007329;
Name=3;
IsoId=P15379-8; Sequence=VSP_007330;
Name=4; Synonyms=M2;
IsoId=P15379-4; Sequence=VSP_007331;
Name=5;
IsoId=P15379-9; Sequence=VSP_007332;
Name=6; Synonyms=M3;
IsoId=P15379-5; Sequence=VSP_005326;
Name=7; Synonyms=M4;
IsoId=P15379-6; Sequence=VSP_005327;
Name=8;
IsoId=P15379-10; Sequence=VSP_007330, VSP_007334;
Name=9;
IsoId=P15379-11; Sequence=VSP_007332, VSP_007335;
Name=10;
IsoId=P15379-12; Sequence=VSP_007336, VSP_007337;
Name=11;
IsoId=P15379-13; Sequence=VSP_007338, VSP_007339;
Name=12; Synonyms=M1;
IsoId=P15379-3; Sequence=VSP_005328;
Name=13; Synonyms=M0;
IsoId=P15379-2; Sequence=VSP_005329, VSP_007333;
-!- DOMAIN: The lectin-like LINK domain is responsible for hyaluronan
binding.
-!- PTM: N-glycosylated. {ECO:0000250}.
-!- PTM: O-glycosylated; contains chondroitin sulfate glycans which
can be more or less sulfated. {ECO:0000250}.
-!- PTM: Phosphorylated; activation of PKC results in the
dephosphorylation of Ser-742 (constitutive phosphorylation site),
and the phosphorylation of Ser-708. {ECO:0000250}.
-!- POLYMORPHISM: Two allelic forms of this glycoprotein, PGP-1.1 and
PGP-1.2, have been reported. The expressed product is PGP-1.1 (Ly-
24.1).
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EMBL; X66084; CAA46883.1; -; mRNA.
EMBL; X66083; CAA46882.1; -; mRNA.
EMBL; X66082; CAA46881.1; -; mRNA.
EMBL; X66081; CAA46880.1; -; mRNA.
EMBL; M30655; AAA39922.1; -; mRNA.
EMBL; M27129; AAA37406.1; -; mRNA.
EMBL; M27130; AAA37407.1; -; mRNA.
EMBL; AJ251594; CAB61888.1; -; mRNA.
EMBL; BC005676; AAH05676.1; -; mRNA.
EMBL; AK045226; BAC32269.1; -; mRNA.
EMBL; J05163; AAA39923.1; -; mRNA.
EMBL; X69724; CAA49380.1; -; mRNA.
EMBL; L13611; AAA37145.1; -; mRNA.
EMBL; U57610; AAC52804.1; -; mRNA.
EMBL; U57611; AAB08756.1; -; mRNA.
EMBL; U57612; AAC52805.1; -; Genomic_DNA.
EMBL; U57612; AAC52806.1; -; Genomic_DNA.
PIR; A34424; A34424.
PIR; A37009; A37009.
PIR; B44355; B44355.
PIR; D44355; D44355.
PIR; S30397; S30397.
RefSeq; NP_001034240.1; NM_001039151.1.
RefSeq; NP_001171256.1; NM_001177785.1.
RefSeq; NP_001171257.1; NM_001177786.1.
RefSeq; NP_001171258.1; NM_001177787.1.
RefSeq; NP_033981.2; NM_009851.2.
UniGene; Mm.423621; -.
PDB; 2JCP; X-ray; 1.30 A; A=23-174.
PDB; 2JCQ; X-ray; 1.25 A; A=23-174.
PDB; 2JCR; X-ray; 2.00 A; A=23-174.
PDB; 2ZPY; X-ray; 2.10 A; B=708-727.
PDB; 4MRD; X-ray; 2.55 A; A=23-171.
PDB; 4MRE; X-ray; 1.58 A; A=23-171.
PDB; 4MRF; X-ray; 1.55 A; A=23-171.
PDB; 4MRG; X-ray; 1.69 A; A=23-171.
PDB; 4MRH; X-ray; 1.12 A; A=23-171.
PDB; 4NP2; X-ray; 1.75 A; A=23-171.
PDB; 4NP3; X-ray; 1.61 A; A=23-171.
PDB; 5BZC; X-ray; 1.95 A; A=22-171.
PDB; 5BZE; X-ray; 1.31 A; A=23-171.
PDB; 5BZF; X-ray; 2.77 A; A=21-171.
PDB; 5BZG; X-ray; 2.19 A; A=21-171.
PDB; 5BZH; X-ray; 1.95 A; A=21-171.
PDB; 5BZI; X-ray; 1.32 A; A=21-171.
PDB; 5BZJ; X-ray; 1.40 A; A=21-171.
PDB; 5BZK; X-ray; 1.40 A; A=21-171.
PDB; 5BZL; X-ray; 1.23 A; A=21-171.
PDB; 5BZM; X-ray; 1.25 A; A=21-171.
PDB; 5BZN; X-ray; 1.23 A; A=21-171.
PDB; 5BZO; X-ray; 1.22 A; A=21-171.
PDB; 5BZP; X-ray; 1.23 A; A=21-171.
PDB; 5BZQ; X-ray; 1.20 A; A=21-171.
PDB; 5BZR; X-ray; 1.15 A; A=21-171.
PDB; 5BZS; X-ray; 1.50 A; A=21-171.
PDB; 5BZT; X-ray; 1.25 A; A=21-171.
PDBsum; 2JCP; -.
PDBsum; 2JCQ; -.
PDBsum; 2JCR; -.
PDBsum; 2ZPY; -.
PDBsum; 4MRD; -.
PDBsum; 4MRE; -.
PDBsum; 4MRF; -.
PDBsum; 4MRG; -.
PDBsum; 4MRH; -.
PDBsum; 4NP2; -.
PDBsum; 4NP3; -.
PDBsum; 5BZC; -.
PDBsum; 5BZE; -.
PDBsum; 5BZF; -.
PDBsum; 5BZG; -.
PDBsum; 5BZH; -.
PDBsum; 5BZI; -.
PDBsum; 5BZJ; -.
PDBsum; 5BZK; -.
PDBsum; 5BZL; -.
PDBsum; 5BZM; -.
PDBsum; 5BZN; -.
PDBsum; 5BZO; -.
PDBsum; 5BZP; -.
PDBsum; 5BZQ; -.
PDBsum; 5BZR; -.
PDBsum; 5BZS; -.
PDBsum; 5BZT; -.
ProteinModelPortal; P15379; -.
SMR; P15379; -.
CORUM; P15379; -.
DIP; DIP-29095N; -.
IntAct; P15379; 11.
STRING; 10090.ENSMUSP00000005218; -.
BindingDB; P15379; -.
ChEMBL; CHEMBL3232693; -.
iPTMnet; P15379; -.
PhosphoSitePlus; P15379; -.
SwissPalm; P15379; -.
PaxDb; P15379; -.
PeptideAtlas; P15379; -.
PRIDE; P15379; -.
GeneID; 12505; -.
KEGG; mmu:12505; -.
CTD; 960; -.
MGI; MGI:88338; Cd44.
eggNOG; ENOG410IZCP; Eukaryota.
eggNOG; ENOG4111S6T; LUCA.
HOVERGEN; HBG003850; -.
InParanoid; P15379; -.
KO; K06256; -.
ChiTaRS; Cd44; mouse.
EvolutionaryTrace; P15379; -.
PRO; PR:P15379; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_CD44; -.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
GO; GO:0042995; C:cell projection; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031258; C:lamellipodium membrane; ISS:UniProtKB.
GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005540; F:hyaluronic acid binding; IDA:MGI.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IPI:UniProtKB.
GO; GO:0060442; P:branching involved in prostate gland morphogenesis; IMP:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IDA:MGI.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; ISO:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:GOC.
GO; GO:0030214; P:hyaluronan catabolic process; ISO:MGI.
GO; GO:0070487; P:monocyte aggregation; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; IMP:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
GO; GO:0050728; P:negative regulation of inflammatory response; IMP:UniProtKB.
GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IMP:BHF-UCL.
GO; GO:0002906; P:negative regulation of mature B cell apoptotic process; IDA:BHF-UCL.
GO; GO:0045590; P:negative regulation of regulatory T cell differentiation; IMP:UniProtKB.
GO; GO:0002821; P:positive regulation of adaptive immune response; NAS:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISO:MGI.
GO; GO:0033674; P:positive regulation of kinase activity; ISO:MGI.
GO; GO:1900625; P:positive regulation of monocyte aggregation; ISO:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:BHF-UCL.
GO; GO:2000392; P:regulation of lamellipodium morphogenesis; ISS:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; IDA:MGI.
GO; GO:0002246; P:wound healing involved in inflammatory response; IMP:MGI.
GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR016186; C-type_lectin-like/link.
InterPro; IPR001231; CD44_antigen.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR000538; Link_dom.
PANTHER; PTHR10225:SF8; PTHR10225:SF8; 1.
Pfam; PF00193; Xlink; 1.
PRINTS; PR00658; CD44.
PRINTS; PR01265; LINKMODULE.
SMART; SM00445; LINK; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS01241; LINK_1; 1.
PROSITE; PS50963; LINK_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Disulfide bond; Glycoprotein; Membrane;
Phosphoprotein; Proteoglycan; Receptor; Reference proteome; Signal;
Sulfation; Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 778 CD44 antigen.
/FTId=PRO_0000026689.
TOPO_DOM 23 685 Extracellular. {ECO:0000255}.
TRANSMEM 686 706 Helical. {ECO:0000255}.
TOPO_DOM 707 778 Cytoplasmic. {ECO:0000255}.
DOMAIN 34 123 Link. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
REGION 227 685 Stem.
COMPBIAS 153 161 Arg/Lys-rich (basic).
BINDING 43 43 Hyaluronan.
{ECO:0000269|PubMed:17293874}.
BINDING 80 80 Hyaluronan.
{ECO:0000269|PubMed:17293874}.
BINDING 81 81 Hyaluronan.
{ECO:0000269|PubMed:17293874}.
BINDING 107 107 Hyaluronan.
{ECO:0000269|PubMed:17293874}.
MOD_RES 410 410 Sulfotyrosine. {ECO:0000250}.
MOD_RES 708 708 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P16070}.
MOD_RES 726 726 Phosphothreonine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 733 733 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 742 742 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
CARBOHYD 27 27 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 123 123 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 425 425 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 529 529 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 545 545 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 603 603 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 132 {ECO:0000255|PROSITE-ProRule:PRU00323,
ECO:0000269|PubMed:17293874}.
DISULFID 55 121 {ECO:0000255|PROSITE-ProRule:PRU00323,
ECO:0000269|PubMed:17293874}.
DISULFID 79 99 {ECO:0000255|PROSITE-ProRule:PRU00323,
ECO:0000269|PubMed:17293874}.
VAR_SEQ 223 637 Missing (in isoform 13).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:2403559,
ECO:0000303|PubMed:2681416,
ECO:0000303|PubMed:2682651}.
/FTId=VSP_005329.
VAR_SEQ 223 539 Missing (in isoform 12).
{ECO:0000303|PubMed:1469058}.
/FTId=VSP_005328.
VAR_SEQ 223 504 Missing (in isoform 7).
{ECO:0000303|PubMed:1469058,
ECO:0000303|PubMed:8464707}.
/FTId=VSP_005327.
VAR_SEQ 223 424 Missing (in isoform 6).
{ECO:0000303|PubMed:1469058,
ECO:0000303|PubMed:8464707}.
/FTId=VSP_005326.
VAR_SEQ 223 383 Missing (in isoform 5 and isoform 9).
{ECO:0000303|PubMed:8464707,
ECO:0000303|PubMed:8509359}.
/FTId=VSP_007332.
VAR_SEQ 223 346 Missing (in isoform 4).
{ECO:0000303|PubMed:1469058,
ECO:0000303|PubMed:8464707}.
/FTId=VSP_007331.
VAR_SEQ 223 303 Missing (in isoform 3 and isoform 8).
{ECO:0000303|PubMed:8464707}.
/FTId=VSP_007330.
VAR_SEQ 223 264 Missing (in isoform 2).
{ECO:0000303|PubMed:8464707}.
/FTId=VSP_007329.
VAR_SEQ 424 504 Missing (in isoform 8).
{ECO:0000303|PubMed:8464707}.
/FTId=VSP_007334.
VAR_SEQ 463 504 Missing (in isoform 9).
{ECO:0000303|PubMed:8509359}.
/FTId=VSP_007335.
VAR_SEQ 569 592 TKSSAKDARRGGSLPTDTTTSVEG -> VRIIKSNWLLSRN
QDVMGVSGGGC (in isoform 11).
{ECO:0000305}.
/FTId=VSP_007338.
VAR_SEQ 569 580 TKSSAKDARRGG -> VCLVVVADFSAL (in isoform
10). {ECO:0000305}.
/FTId=VSP_007336.
VAR_SEQ 581 778 Missing (in isoform 10). {ECO:0000305}.
/FTId=VSP_007337.
VAR_SEQ 593 778 Missing (in isoform 11). {ECO:0000305}.
/FTId=VSP_007339.
VAR_SEQ 638 638 G -> R (in isoform 13).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:2403559,
ECO:0000303|PubMed:2681416,
ECO:0000303|PubMed:2682651}.
/FTId=VSP_007333.
VARIANT 21 21 H -> HPH (in Ly-24.2).
{ECO:0000269|PubMed:2682651}.
VARIANT 194 194 G -> S (in Ly-24.2).
{ECO:0000269|PubMed:2682651}.
CONFLICT 326 326 T -> K (in Ref. 4 and 9). {ECO:0000305}.
CONFLICT 348 348 T -> S (in Ref. 9). {ECO:0000305}.
CONFLICT 559 559 Y -> H (in Ref. 4, 8 and 9).
{ECO:0000305}.
CONFLICT 572 572 S -> G (in Ref. 4, 8 and 9).
{ECO:0000305}.
CONFLICT 639 639 D -> RD (in Ref. 7). {ECO:0000305}.
STRAND 23 28 {ECO:0000244|PDB:4MRH}.
STRAND 35 40 {ECO:0000244|PDB:4MRH}.
HELIX 48 57 {ECO:0000244|PDB:4MRH}.
HELIX 65 73 {ECO:0000244|PDB:4MRH}.
STRAND 85 94 {ECO:0000244|PDB:4MRH}.
HELIX 100 102 {ECO:0000244|PDB:4MRH}.
STRAND 105 108 {ECO:0000244|PDB:4MRH}.
STRAND 117 122 {ECO:0000244|PDB:4MRH}.
STRAND 128 131 {ECO:0000244|PDB:4MRH}.
STRAND 142 152 {ECO:0000244|PDB:4MRH}.
STRAND 157 163 {ECO:0000244|PDB:4MRH}.
HELIX 168 170 {ECO:0000244|PDB:4MRH}.
STRAND 715 719 {ECO:0000244|PDB:2ZPY}.
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


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