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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_BOVIN              Reviewed;         366 AA.
Q29423;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
30-AUG-2017, entry version 106.
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;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1922105; DOI=10.1016/0161-5890(91)90028-I;
Bosworth B.T., St John T., Gallatin W.M., Harp J.A.;
"Sequence of the bovine CD44 cDNA: comparison with human and mouse
sequences.";
Mol. Immunol. 28:1131-1135(1991).
-!- 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.
{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}.
-!- TISSUE SPECIFICITY: Mesenteric lymph node and liver, not in heart.
-!- DOMAIN: The lectin-like LINK domain is responsible for hyaluronan
binding. {ECO:0000250}.
-!- PTM: N- and O-glycosylated; contains glycosaminoglycan chondroitin
sulfate. {ECO:0000250}.
-!- PTM: Phosphorylated on serine residues. {ECO:0000250}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; X62881; CAA44675.1; -; mRNA.
EMBL; S63418; AAB20016.1; -; mRNA.
PIR; A53286; A53286.
UniGene; Bt.5494; -.
ProteinModelPortal; Q29423; -.
SMR; Q29423; -.
STRING; 9913.ENSBTAP00000048925; -.
PaxDb; Q29423; -.
PeptideAtlas; Q29423; -.
PRIDE; Q29423; -.
eggNOG; ENOG410IZCP; Eukaryota.
eggNOG; ENOG4111S6T; LUCA.
HOGENOM; HOG000231746; -.
HOVERGEN; HBG003850; -.
InParanoid; Q29423; -.
Proteomes; UP000009136; Unplaced.
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.
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.
2: Evidence at transcript level;
Cell adhesion; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Membrane; Phosphoprotein; Proteoglycan; Receptor;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 366 CD44 antigen.
/FTId=PRO_0000026683.
TOPO_DOM 21 273 Extracellular. {ECO:0000255}.
TRANSMEM 274 294 Helical. {ECO:0000255}.
TOPO_DOM 295 366 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 120 Link. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
REGION 229 273 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 296 296 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P16070}.
MOD_RES 314 314 Phosphothreonine.
{ECO:0000250|UniProtKB:P15379}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000250|UniProtKB:P15379}.
MOD_RES 330 330 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 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 260 260 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}.
SEQUENCE 366 AA; 40002 MW; 438A5A1E631E02B4 CRC64;
MDTFWWRAAW GLCLVQLSLA QIDLNITCRY AGVFHVEKNG RYSISKTEAA DLCKAFNSTL
PTMAQMEAAR NIGFETCRYG FIEGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTICFN
ASAPPGEDCT SVTDLPNAFE GPITITIVNR DGTRYTKKGE YRTNPEDINP SVVSPSSPPD
DEMSSGSPSE RSTSGGYSIF HTHLPTVHPS RPRRPWSQRA ENTSDTRDYG SSHDPSGRSY
TTHASESAGH SSGSEEHGAN TTSGPMRKPQ IPEWLIILAS LLALALILAV CIAVNSRRRC
GQKKKLVINN GNGTMEERKP SGLNGEASKS QEMVHLVNKG SSETPDQFMT ADETRNLQNV
DMKIGV


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