CD44_HORSE
ID CD44_HORSE Reviewed; 359 AA.
AC Q05078;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 124.
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 Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8436424; DOI=10.1007/bf00222474;
RA Tavernor A.S., Deverson E.V., Coadwell W.J., Lunn D.P., Zhang C., Davis W.,
RA Butcher G.W.;
RT "Molecular cloning of equine CD44 cDNA by a COS cell expression system.";
RL Immunogenetics 37:474-477(1993).
CC -!- FUNCTION: Cell-surface receptor that plays a role in cell-cell
CC interactions, as well as cell adhesion and migration, helping them to
CC sense and respond to changes in the tissue microenvironment.
CC Participates thereby in a wide variety of cellular functions including
CC the activation, recirculation and homing of T-lymphocytes,
CC hematopoiesis, inflammation and response to bacterial infection.
CC Engages, through its ectodomain, extracellular matrix components such
CC as hyaluronan/HA, collagen, growth factors, cytokines or proteases and
CC serves as a platform for signal transduction by assembling, via its
CC cytoplasmic domain, protein complexes containing receptor kinases and
CC membrane proteases. Such effectors include PKN2, the RhoGTPases RAC1
CC and RHOA, Rho-kinases and phospholipase C that coordinate signaling
CC pathways promoting calcium mobilization and actin-mediated cytoskeleton
CC reorganization essential for cell migration and adhesion.
CC {ECO:0000250|UniProtKB:P15379, 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 -!- DOMAIN: The lectin-like LINK domain is responsible for hyaluronan
CC binding. {ECO:0000250}.
CC -!- PTM: Phosphorylated; activation of PKC results in the dephosphorylation
CC of Ser-323 (constitutive phosphorylation site), and the phosphorylation
CC of Ser-289. {ECO:0000250|UniProtKB:P16070}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P16070}.
CC -!- PTM: O-glycosylated; addition of the glycosaminoglycan chondroitin
CC sulfate, of sulfate, of phosphate to cytoplasmic domain serine
CC residues. {ECO:0000250|UniProtKB:P16070}.
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DR EMBL; X66862; CAA47331.1; -; mRNA.
DR PIR; I46245; S24240.
DR AlphaFoldDB; Q05078; -.
DR SMR; Q05078; -.
DR PaxDb; Q05078; -.
DR PeptideAtlas; Q05078; -.
DR InParanoid; Q05078; -.
DR Proteomes; UP000002281; 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:0000250"
FT CHAIN 21..359
FT /note="CD44 antigen"
FT /id="PRO_0000026686"
FT TOPO_DOM 21..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..120
FT /note="Link"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00323"
FT REGION 156..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..266
FT /note="Stem"
FT REGION 290..308
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 165..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..259
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 105
FT /ligand="hyaluronan"
FT /ligand_id="ChEBI:CHEBI:132153"
FT /evidence="ECO:0000250"
FT MOD_RES 289
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P16070"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15379"
FT MOD_RES 323
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 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 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
