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

 CD44_PAPHA              Reviewed;         362 AA.
P14745;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
22-NOV-2017, entry version 107.
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=Phagocytic glycoprotein 1;
Short=PGP-1;
AltName: Full=Phagocytic glycoprotein I;
Short=PGP-I;
AltName: CD_antigen=CD44;
Flags: Precursor;
Name=CD44;
Papio hamadryas (Hamadryas baboon).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Papio.
NCBI_TaxID=9557;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 66-74.
PubMed=2471974; DOI=10.1073/pnas.86.12.4659;
Idzerda R.L., Carter W.G., Nottenburg C., Wayner E.A., Gallatin W.M.,
St John T.;
"Isolation and DNA sequence of a cDNA clone encoding a lymphocyte
adhesion receptor for high endothelium.";
Proc. Natl. Acad. Sci. U.S.A. 86:4659-4663(1989).
-!- 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.
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. {ECO:0000250|UniProtKB:P15379,
ECO:0000250|UniProtKB:P16070}.
-!- SUBUNIT: Interacts with HA, as well as other glycosaminoglycans,
collagen, laminin, and fibronectin via its N-terminal segment.
Interacts with ANK, the ERM proteins (VIL2, RDX and MSN), and NF2
via its C-terminal segment. Interacts with PKN2. Interacts with
TIAM1 and TIAM2. Interacts with UNC119. Interacts with PDPN (via
extracellular domain); this interaction is required for PDPN-
mediated directional migration and regulation of lamellipodia
extension/stabilization during cell spreading and migration (By
similarity). {ECO:0000250|UniProtKB:P15379,
ECO:0000250|UniProtKB:P16070}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P15379}; Single-pass type I membrane
protein {ECO:0000250|UniProtKB:P15379}. Note=Colocalizes with
actin in membrane protrusions at wounding edges.
{ECO:0000250|UniProtKB:P15379}.
-!- DOMAIN: The lectin-like LINK domain is responsible for hyaluronan
binding. {ECO:0000250}.
-!- PTM: Extensively modified including N- and O-linked glycosylation,
addition of the glycosaminoglycan chondroitin sulfate, of sulfate,
of phosphate to cytoplasmic domain serine residues.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M22452; AAA35385.1; -; mRNA.
ProteinModelPortal; P14745; -.
SMR; P14745; -.
PRIDE; P14745; -.
HOVERGEN; HBG003850; -.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0042995; C:cell projection; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031258; C:lamellipodium membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0005540; F:hyaluronic acid binding; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:2000392; P:regulation of lamellipodium morphogenesis; ISS:UniProtKB.
GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR001231; CD44_antigen.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR000538; Link_dom.
PANTHER; PTHR10225:SF6; PTHR10225:SF6; 2.
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;
Cell adhesion; Cell membrane; Direct protein sequencing;
Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; Proteoglycan;
Receptor; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000250}.
CHAIN 21 362 CD44 antigen.
/FTId=PRO_0000026690.
TOPO_DOM 21 269 Extracellular. {ECO:0000255}.
TRANSMEM 270 290 Helical. {ECO:0000255}.
TOPO_DOM 291 362 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 120 Link. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
REGION 225 269 Stem.
COMPBIAS 150 158 Arg/Lys-rich (basic).
BINDING 41 41 Hyaluronan. {ECO:0000250}.
BINDING 78 78 Hyaluronan. {ECO:0000250}.
BINDING 79 79 Hyaluronan. {ECO:0000250}.
BINDING 105 105 Hyaluronan. {ECO:0000250}.
MOD_RES 292 292 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P16070}.
MOD_RES 317 317 Phosphoserine.
{ECO:0000250|UniProtKB:P15379}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000250|UniProtKB:P16070}.
CARBOHYD 25 25 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 100 100 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 120 120 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 129 {ECO:0000255|PROSITE-ProRule:PRU00323}.
DISULFID 53 118 {ECO:0000255|PROSITE-ProRule:PRU00323}.
DISULFID 77 97 {ECO:0000255|PROSITE-ProRule:PRU00323}.
CONFLICT 67 67 E -> V (in Ref. 1; AA sequence).
{ECO:0000305}.
SEQUENCE 362 AA; 39379 MW; 578BFCE7C3D52FFF CRC64;
MDKFWWRAAW GLCLVQLSLA QIDLNITCRF EGIYHVEKNG RYSISRTEAA DLCKAFNSTL
PTMAQMEKAL SIGFETCRYG FIEGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTYCFN
ASAPPGEDCT SVTDLPNAFD GPITITIVNR DGTRYVKKGE YRTNPEDINP SSPTDDDVSS
GSSSERSSTL GGYIFYNHFS TSPPIPDEDG PWITDSTDRT PATRDQGAFD PSGGSHTTHG
SESAGHSHGS REGGANTTSG PLRTPQIPEW LIILASLLAL ALILAVCIAV NSRRRCGQKK
KLVINNGNGA VEDRKSSGLN GEASKSQEMV HLVNKESSET PDQFMTADET RNLQNVDMKI
GV


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