CD47_PONAB
ID CD47_PONAB Reviewed; 323 AA.
AC Q5REL0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR857514; CAH89797.1; -; mRNA.
DR RefSeq; NP_001124828.1; NM_001131356.1.
DR AlphaFoldDB; Q5REL0; -.
DR SMR; Q5REL0; -.
DR STRING; 9601.ENSPPYP00000015180; -.
DR GeneID; 100171686; -.
DR KEGG; pon:100171686; -.
DR CTD; 961; -.
DR eggNOG; ENOG502RYTQ; Eukaryota.
DR InParanoid; Q5REL0; -.
DR OrthoDB; 1287706at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0070053; F:thrombospondin receptor activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IEA:InterPro.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:InterPro.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:InterPro.
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; IPR036179; Ig-like_dom_sf.
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 SUPFAM; SSF48726; SSF48726; 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..323
FT /note="Leukocyte surface antigen CD47"
FT /id="PRO_0000042208"
FT TOPO_DOM 19..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..268
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 19..127
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 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 41..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 323 AA; 35241 MW; 50F6B664548A6F50 CRC64;
MWPLVAALLL GSACCGSAQL LFNKTKSVEF TFCNDTVVIP CFVTNMEAQN TTEVYVKWKF
KGRDIYTFDG ALNKSTVPTD FSSAKIEVSQ LLKGDASLKM DKSDAVSHTG NYTCEVTELT
REGETIIELK YRVVSWFSPN ENILIVIFPI FAILLFWGQF GIKTLKYRSG GMDEKTIALL
VAGLIITVIV IVGAILFVPG EYSLKNATGL GLIVTSTGIL ILLHYYVFST AIGLNSFVIA
ILVIQVIAYI LAVVGLSLCI AACIPMHGPL LISGLSILAL AQLLGLVYMK FVASNQKTIQ
PPRKAVEEPL NAFKESKGMM NDE
