ID A0A3Q1MDJ9_BOVIN Unreviewed; 630 AA.
AC A0A3Q1MDJ9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=CD44 antigen {ECO:0000256|ARBA:ARBA00020474};
DE AltName: Full=GP90 lymphocyte homing/adhesion receptor {ECO:0000256|ARBA:ARBA00032514};
DE AltName: Full=HUTCH-I {ECO:0000256|ARBA:ARBA00031823};
DE AltName: Full=Hermes antigen {ECO:0000256|ARBA:ARBA00032917};
DE AltName: Full=Hyaluronate receptor {ECO:0000256|ARBA:ARBA00031179};
DE AltName: Full=Phagocytic glycoprotein 1 {ECO:0000256|ARBA:ARBA00029917};
DE AltName: Full=Phagocytic glycoprotein I {ECO:0000256|ARBA:ARBA00029928};
GN Name=CD44 {ECO:0000313|Ensembl:ENSBTAP00000066909.1,
GN ECO:0000313|VGNC:VGNC:54629};
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 {ECO:0000313|Ensembl:ENSBTAP00000066909.1, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000066909.1, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000066909.1,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000066909.1}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000066909.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
CC Cell projection, microvillus {ECO:0000256|ARBA:ARBA00004105}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Secreted
CC {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00323}.
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DR AlphaFoldDB; A0A3Q1MDJ9; -.
DR Ensembl; ENSBTAT00000082456.1; ENSBTAP00000066909.1; ENSBTAG00000011578.6.
DR VEuPathDB; HostDB:ENSBTAG00000011578; -.
DR VGNC; VGNC:54629; CD44.
DR GeneTree; ENSGT00530000063822; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000011578; Expressed in prostate gland and 102 other cell types or tissues.
DR ExpressionAtlas; A0A3Q1MDJ9; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:Ensembl.
DR GO; GO:0035692; C:macrophage migration inhibitory factor receptor complex; IEA:Ensembl.
DR GO; GO:0005902; C:microvillus; IEA:UniProtKB-SubCell.
DR GO; GO:0004896; F:cytokine receptor activity; IEA:Ensembl.
DR GO; GO:0005540; F:hyaluronic acid binding; IEA:Ensembl.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR GO; GO:0030214; P:hyaluronan catabolic process; IEA:Ensembl.
DR GO; GO:0070487; P:monocyte aggregation; IEA:Ensembl.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:1900625; P:positive regulation of monocyte aggregation; IEA:Ensembl.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IEA:Ensembl.
DR GO; GO:2000392; P:regulation of lamellipodium morphogenesis; IEA:Ensembl.
DR GO; GO:0042110; P:T cell activation; IEA:Ensembl.
DR GO; GO:0044319; P:wound healing, spreading of cells; IEA:Ensembl.
DR CDD; cd03516; Link_domain_CD44_like; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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:SF6; CD44 ANTIGEN; 1.
DR PANTHER; PTHR10225; HYALURONAN RECEPTOR; 1.
DR Pfam; PF00193; Xlink; 1.
DR PRINTS; PR00658; CD44.
DR PRINTS; PR01265; LINKMODULE.
DR SMART; SM00445; LINK; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR PROSITE; PS01241; LINK_1; 1.
DR PROSITE; PS50963; LINK_2; 1.
PE 4: Predicted;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000009136};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..630
FT /note="CD44 antigen"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018557056"
FT TRANSMEM 538..559
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..120
FT /note="Link"
FT /evidence="ECO:0000259|PROSITE:PS50963"
FT REGION 156..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..483
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 630 AA; 68643 MW; ABE1D916A1E2401F CRC64;
MDTFWWRAAW GLCLVQLSLA QIDLNITCRY AGVFHVEKNG RYSISKTEAA DLCKAFNSTL
PTMAQMEAAR NIGFETCRYG FIEGHVVIPR IHPNSICAAN NTGVYILTSN TSQYDTYCFN
ASAPPGEDCT SVTDLPNAFE GPITITIVNR DGTRYTKKGE YRTNPEDINP SVVSPSSPPD
DEMSSGSPSE RSTSGGYSIF HTHLPTVHPS PDQDGPWVSS EPENTSDTST DSSIISAGWE
PTEENEDERD RHPSYSGSGI GDDEDFISST ISTTPRVFTH LQENQNWIQR NPDHSNPEAS
LQTTTRMTDV DRSSTSAYGE SWTQEPHSSR SHRGYHDEEE TPHSTSTITT ASTHVSHPHQ
RVTTQSQEDS SWTYVFDPVS HPMGRGHQTK GRMDTSPSTT LQPSADPNMS SVGDLDRTGP
LSMTTHRNDG RRGGNLPEDA TASMEGYTHS PDTNEYTTLT PVTPTKTGSP GVTEVTIVGD
STSKADLTLP GDYGSSHDPS GRSYTTHASE SAGHSSGSEE HGANTTSGPM RKPQIPEWLI
ILASLLALAL ILAVCIAVNS RRRCGQKKKL VINNGNGTME ERKPSGLNGE ASKSQEMVHL
VNKGSSETQD QFMTADETRN LQNVDMKIGV
//
