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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_HORSE              Reviewed;         359 AA.
Q05078;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
22-NOV-2017, entry version 108.
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;
Equus caballus (Horse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
NCBI_TaxID=9796;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8436424; DOI=10.1007/BF00222474;
Tavernor A.S., Deverson E.V., Coadwell W.J., Lunn D.P., Zhang C.,
Davis W., Butcher G.W.;
"Molecular cloning of equine CD44 cDNA by a COS cell expression
system.";
Immunogenetics 37:474-477(1993).
-!- 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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EMBL; X66862; CAA47331.1; -; mRNA.
PIR; I46245; S24240.
UniGene; Eca.12636; -.
ProteinModelPortal; Q05078; -.
SMR; Q05078; -.
STRING; 9796.ENSECAP00000008636; -.
PaxDb; Q05078; -.
PeptideAtlas; Q05078; -.
PRIDE; Q05078; -.
eggNOG; ENOG410IZCP; Eukaryota.
eggNOG; ENOG4111S6T; LUCA.
HOVERGEN; HBG003850; -.
InParanoid; Q05078; -.
Proteomes; UP000002281; 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_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.
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:0000250}.
CHAIN 21 359 CD44 antigen.
/FTId=PRO_0000026686.
TOPO_DOM 21 266 Extracellular. {ECO:0000255}.
TRANSMEM 267 287 Helical. {ECO:0000255}.
TOPO_DOM 288 359 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 120 Link. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
REGION 225 266 Stem.
COMPBIAS 150 158 Arg/Lys-rich (basic).
BINDING 41 41 Hyaluronan. {ECO:0000250}.
BINDING 78 78 Hyaluronan. {ECO:0000250}.
BINDING 105 105 Hyaluronan. {ECO:0000250}.
MOD_RES 289 289 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P16070}.
MOD_RES 314 314 Phosphoserine.
{ECO:0000250|UniProtKB:P15379}.
MOD_RES 323 323 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}.
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 359 AA; 38990 MW; BE20461C587AA34B CRC64;
MDKFWWRAAW GLCLVPLSLA QIDLNITCRY AGVFHVEKNG RYSISRTEAA DLCKAFNSTL
PTMAQMQKAL NIGFETCRIG FIEGHVVIPP IHPNSICAAN NTGVYILTSN TSQYDTYCFN
ASAPPEEDCT SVTDLPNAFE GPITITIVNR DGTRYTKKGE YRTNPEDINP STPADDDVSS
GSSSERSTSG GYSIFHTHLP TTRPTQDQSS PWVSDSPEKT PTTKDRASGG RAQTTHGSET
SGHSTGSQEG GASTTSGPIR RPQIPEWLII LASLLALALI LAVCIAVNSR RRCGQKKKLV
INNGNGAVDD RKASGLNGEA SRSQEMVHLV NKESSETQDQ FMTADETRNL QNVDMKIGV


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