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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) (Fragment)

 CD44_CANLF              Reviewed;         351 AA.
Q28284;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
22-NOV-2017, entry version 104.
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; Fragment;
Name=CD44;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Beagle; TISSUE=Thymus;
PubMed=7514890; DOI=10.1016/0167-4781(94)90111-2;
Milde K.F., Alejandro R., Mintz D.H., Pastori R.L.;
"Molecular cloning of the canine CD44 antigen cDNA.";
Biochim. Biophys. Acta 1218:112-114(1994).
-!- 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}.
-!- TISSUE SPECIFICITY: Lymph nodes.
-!- 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. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; Z27115; CAA81630.1; -; mRNA.
PIR; S45305; S45305.
UniGene; Cfa.3800; -.
ProteinModelPortal; Q28284; -.
SMR; Q28284; -.
STRING; 9615.ENSCAFP00000010256; -.
PaxDb; Q28284; -.
PRIDE; Q28284; -.
eggNOG; ENOG410IZCP; Eukaryota.
eggNOG; ENOG4111S6T; LUCA.
HOVERGEN; HBG003850; -.
InParanoid; Q28284; -.
Proteomes; UP000002254; 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 13 {ECO:0000255}.
CHAIN 14 >351 CD44 antigen.
/FTId=PRO_0000026684.
TOPO_DOM 14 263 Extracellular. {ECO:0000255}.
TRANSMEM 264 284 Helical. {ECO:0000255}.
TOPO_DOM 285 >351 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 113 Link. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
REGION 218 263 Stem.
COMPBIAS 143 151 Arg/Lys-rich (basic).
BINDING 34 34 Hyaluronan. {ECO:0000250}.
BINDING 71 71 Hyaluronan. {ECO:0000250}.
BINDING 72 72 Hyaluronan. {ECO:0000250}.
BINDING 98 98 Hyaluronan. {ECO:0000250}.
MOD_RES 286 286 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:P16070}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000250|UniProtKB:P15379}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000250|UniProtKB:P16070}.
CARBOHYD 18 18 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 103 103 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 113 113 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 21 122 {ECO:0000255|PROSITE-ProRule:PRU00323}.
DISULFID 46 111 {ECO:0000255|PROSITE-ProRule:PRU00323}.
DISULFID 70 90 {ECO:0000255|PROSITE-ProRule:PRU00323}.
NON_TER 1 1
NON_TER 351 351
SEQUENCE 351 AA; 38066 MW; E73387E70E20C0E0 CRC64;
LAWGLCLLRL SLAQIDLNIT CRYAGVFHVE KNGRYSISRT AAADLCKAFN STLPTMAQME
RALSVGFETC RYGFIEGHVV IPRIQPNAIC AANHTGVYIL ISNTSQYDTY CFNASAPPEE
DCTSVTHLPN AFDGPITITI VNRDGTRYSQ KGEYRTNPED INPSNPTDDD VSSGSSSERS
TSAGYNIFHT HLPTAYPTED QDSSRVSSNS DHTPITKDHD SSVHPSERSH TTHGSESAGH
SSGSQEGGAN TTSGPMRKPQ IPEWLIILAS LLALALILAV CIAVNSRRRC GQKKKLVINN
GNGAVGDRKP SGINGEASKS QEMVHLVNKE PSETPDQYTT ADETRNLQNV D


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