CD47_BOVIN
ID CD47_BOVIN Reviewed; 303 AA.
AC Q9N0K1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Leukocyte surface antigen CD47;
DE AltName: Full=Integrin-associated protein;
DE Short=IAP;
DE AltName: CD_antigen=CD47;
DE Flags: Precursor;
GN Name=CD47;
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].
RC TISSUE=Monocyte;
RA Brooke G.P., Howard C.J.;
RT "Cloning and distribution of cattle CD47.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has a role in both cell adhesion by acting as an adhesion
CC receptor for THBS1 on platelets, and in the modulation of integrins.
CC Plays an important role in memory formation and synaptic plasticity in
CC the hippocampus. Receptor for SIRPA, binding to which prevents
CC maturation of immature dendritic cells and inhibits cytokine production
CC by mature dendritic cells. Interaction with SIRPG mediates cell-cell
CC adhesion, enhances superantigen-dependent T-cell-mediated proliferation
CC and costimulates T-cell activation. May play a role in membrane
CC transport and/or integrin dependent signal transduction. May prevent
CC premature elimination of red blood cells. May be involved in membrane
CC permeability changes induced following virus infection (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Monomer. Interacts with fibrinogen, PTPNS1, SIRPG, THBS1,
CC UBQLN1 and UBQLN2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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DR EMBL; AJ245943; CAB76905.1; -; mRNA.
DR EMBL; AJ291474; CAC13139.1; -; mRNA.
DR AlphaFoldDB; Q9N0K1; -.
DR SMR; Q9N0K1; -.
DR STRING; 9913.ENSBTAP00000048646; -.
DR PaxDb; Q9N0K1; -.
DR PRIDE; Q9N0K1; -.
DR eggNOG; ENOG502RYTQ; Eukaryota.
DR InParanoid; Q9N0K1; -.
DR OrthoDB; 1287706at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0070062; C:extracellular exosome; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0070053; F:thrombospondin receptor activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central.
DR CDD; cd16090; IgV_CD47; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR006704; CD47.
DR InterPro; IPR013147; CD47-like_TM.
DR InterPro; IPR013270; CD47_Vset.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR037805; IgV_CD47.
DR PANTHER; PTHR10613; PTHR10613; 1.
DR Pfam; PF04549; CD47; 1.
DR Pfam; PF08204; V-set_CD47; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Membrane; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..303
FT /note="Leukocyte surface antigen CD47"
FT /id="PRO_0000042205"
FT TOPO_DOM 19..140
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 237..257
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..303
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..125
FT /note="Ig-like V-type"
FT MOD_RES 19
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:Q08722, ECO:0000305"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97829"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..261
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 41..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 303 AA; 33294 MW; DA1A2AEB50E25D57 CRC64;
MWPLVVVLLL GSVRCGSAQL IFNAIKSVEY TLCNQTVVIP CFVNNVETKN ITELYVRWKF
KGENIFIFDG SQRMSKPSSN FSSAEIAPSE LLRGIASLKM AKSDAVLGNY TCEVTELSRE
GETIIELKYR VVSWFSPNEN ILIVIFPVLA ILLFWGQFGI VTLKYKSNYT KEKAIFLLVA
GLLLTVLVIV GAFLFIPGGY STKNASGLGL IVLPTIILIL LHYCVFMIAM GMSSFTISIL
ILQLLGYVLS VVGFSLCVSE CIPVHGPLLI SGLGIIALAE LLGLVYMKCV ASNHRTIQPP
RNN
