CD44_BOVIN
ID CD44_BOVIN Reviewed; 366 AA.
AC Q29423;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=CD44 antigen;
DE AltName: Full=Extracellular matrix receptor III;
DE Short=ECMR-III;
DE AltName: Full=GP90 lymphocyte homing/adhesion receptor;
DE AltName: Full=HUTCH-I;
DE AltName: Full=Hermes antigen;
DE AltName: Full=Hyaluronate receptor;
DE AltName: Full=Phagocytic glycoprotein 1;
DE Short=PGP-1;
DE AltName: Full=Phagocytic glycoprotein I;
DE Short=PGP-I;
DE AltName: CD_antigen=CD44;
DE Flags: Precursor;
GN Name=CD44;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1922105; DOI=10.1016/0161-5890(91)90028-i;
RA Bosworth B.T., St John T., Gallatin W.M., Harp J.A.;
RT "Sequence of the bovine CD44 cDNA: comparison with human and mouse
RT sequences.";
RL Mol. Immunol. 28:1131-1135(1991).
CC -!- FUNCTION: Cell-surface receptor that plays a role in cell-cell
CC interactions, cell adhesion and migration, helping them to sense and
CC respond to changes in the tissue microenvironment. Participates thereby
CC in a wide variety of cellular functions including the activation,
CC recirculation and homing of T-lymphocytes, hematopoiesis, inflammation
CC and response to bacterial infection. Engages, through its ectodomain,
CC extracellular matrix components such as hyaluronan/HA, collagen, growth
CC factors, cytokines or proteases and serves as a platform for signal
CC transduction by assembling, via its cytoplasmic domain, protein
CC complexes containing receptor kinases and membrane proteases. Such
CC effectors include PKN2, the RhoGTPases RAC1 and RHOA, Rho-kinases and
CC phospholipase C that coordinate signaling pathways promoting calcium
CC mobilization and actin-mediated cytoskeleton reorganization essential
CC for cell migration and adhesion. {ECO:0000250|UniProtKB:P15379,
CC ECO:0000250|UniProtKB:P16070}.
CC -!- SUBUNIT: Interacts with PKN2 (By similarity). Interacts with TIAM1 and
CC TIAM2 (By similarity). Interacts with HA, as well as other
CC glycosaminoglycans, collagen, laminin, and fibronectin via its N-
CC terminal segment. Interacts with UNC119. Interacts with PDPN (via
CC extracellular domain); this interaction is required for PDPN-mediated
CC directional migration and regulation of lamellipodia
CC extension/stabilization during cell spreading and migration (By
CC similarity). Interacts with RDX, EZR and MSN (By similarity). Interacts
CC with EGFR (By similarity). Interacts with CD74; this complex is
CC essential for the MIF-induced signaling cascade that results in B cell
CC survival (By similarity). {ECO:0000250|UniProtKB:P15379,
CC ECO:0000250|UniProtKB:P16070}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15379};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P15379}.
CC Cell projection, microvillus {ECO:0000250|UniProtKB:P15379}.
CC Note=Colocalizes with actin in membrane protrusions at wounding edges.
CC Co-localizes with RDX, EZR and MSN in microvilli.
CC {ECO:0000250|UniProtKB:P15379}.
CC -!- TISSUE SPECIFICITY: Mesenteric lymph node and liver, not in heart.
CC -!- DOMAIN: The lectin-like LINK domain is responsible for hyaluronan
CC binding. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P16070}.
CC -!- PTM: O-glycosylated; contains glycosaminoglycan chondroitin sulfate.
CC {ECO:0000250|UniProtKB:P16070}.
CC -!- PTM: Phosphorylated; activation of PKC results in the dephosphorylation
CC of Ser-330 (constitutive phosphorylation site), and the phosphorylation
CC of Ser-296. {ECO:0000250|UniProtKB:P16070}.
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DR EMBL; X62881; CAA44675.1; -; mRNA.
DR EMBL; S63418; AAB20016.1; -; mRNA.
DR PIR; A53286; A53286.
DR AlphaFoldDB; Q29423; -.
DR SMR; Q29423; -.
DR PaxDb; Q29423; -.
DR PeptideAtlas; Q29423; -.
DR PRIDE; Q29423; -.
DR eggNOG; ENOG502RX7Q; Eukaryota.
DR InParanoid; Q29423; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031258; C:lamellipodium membrane; ISS:UniProtKB.
DR GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005540; F:hyaluronic acid binding; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IEA:GOC.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:2000392; P:regulation of lamellipodium morphogenesis; ISS:UniProtKB.
DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:UniProtKB.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR001231; CD44_antigen.
DR InterPro; IPR043210; CD44_antigen-like.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000538; Link_dom.
DR PANTHER; PTHR10225; PTHR10225; 2.
DR PANTHER; PTHR10225:SF6; PTHR10225:SF6; 2.
DR Pfam; PF00193; Xlink; 1.
DR PRINTS; PR00658; CD44.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Cell projection; Disulfide bond;
KW Glycoprotein; Membrane; Phosphoprotein; Proteoglycan; Receptor;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..366
FT /note="CD44 antigen"
FT /id="PRO_0000026683"
FT TOPO_DOM 21..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 295..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..120
FT /note="Link"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT REGION 156..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..273
FT /note="Stem"
FT REGION 297..315
FT /note="Required for interaction with EZR, MSN and RDX and
FT for co-localization to microvilli"
FT /evidence="ECO:0000250|UniProtKB:P15379"
FT COMPBIAS 167..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="hyaluronan"
FT /ligand_id="ChEBI:CHEBI:132153"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="hyaluronan"
FT /ligand_id="ChEBI:CHEBI:132153"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="hyaluronan"
FT /ligand_id="ChEBI:CHEBI:132153"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="hyaluronan"
FT /ligand_id="ChEBI:CHEBI:132153"
FT /evidence="ECO:0000250"
FT MOD_RES 296
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P16070"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P15379"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15379"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P16070"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DISULFID 53..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT DISULFID 77..97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
SQ 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
