CD47_PIG
ID CD47_PIG Reviewed; 303 AA.
AC Q9GKE8;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 93.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH THBS1 AND
RP FIBRINOGEN, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Aorta;
RX PubMed=12153520; DOI=10.1046/j.1365-2567.2002.01465.x;
RA Shahein Y.E.A., de Andres D.F., de la Lastra J.M.P.;
RT "Molecular cloning and functional characterization of the pig homologue of
RT integrin-associated protein (IAP/CD47).";
RL Immunology 106:564-576(2002).
CC -!- FUNCTION: Receptor for SIRPA, binding to which prevents maturation of
CC immature dendritic cells and inhibits cytokine production by mature
CC dendritic cells. Interaction with SIRPG mediates cell-cell adhesion,
CC enhances superantigen-dependent T-cell-mediated proliferation and
CC costimulates T-cell activation. Plays an important role in memory
CC formation and synaptic plasticity in the hippocampus. May play a role
CC in membrane transport and/or integrin dependent signal transduction.
CC May prevent premature elimination of red blood cells. May be involved
CC in membrane permeability changes induced following virus infection. May
CC play a role in memory formation (By similarity). Has a role in both
CC cell adhesion by acting as an adhesion receptor for THBS1 on platelets,
CC and in the modulation of integrins. {ECO:0000250,
CC ECO:0000269|PubMed:12153520}.
CC -!- SUBUNIT: Monomer. Interacts with SIRPA, SIRPG, UBQLN1 and UBQLN2 (By
CC similarity). Interacts with THBS1 and fibrinogen. {ECO:0000250,
CC ECO:0000269|PubMed:12153520}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12153520};
CC Multi-pass membrane protein {ECO:0000269|PubMed:12153520}.
CC -!- TISSUE SPECIFICITY: Widely expressed, detected in kidney, liver,
CC platelets, thymus, spleen, macrophages, bone marrow and peripheral
CC blood mononuclear cells. {ECO:0000269|PubMed:12153520}.
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DR EMBL; AF270494; AAG44764.2; -; mRNA.
DR EMBL; AF332698; AAK15531.1; -; mRNA.
DR RefSeq; NP_999147.1; NM_213982.1.
DR AlphaFoldDB; Q9GKE8; -.
DR SMR; Q9GKE8; -.
DR STRING; 9823.ENSSSCP00000012724; -.
DR PaxDb; Q9GKE8; -.
DR PeptideAtlas; Q9GKE8; -.
DR PRIDE; Q9GKE8; -.
DR Ensembl; ENSSSCT00000089744; ENSSSCP00000060591; ENSSSCG00000011942.
DR Ensembl; ENSSSCT00030011212; ENSSSCP00030004990; ENSSSCG00030008181.
DR Ensembl; ENSSSCT00050044579; ENSSSCP00050018332; ENSSSCG00050033230.
DR Ensembl; ENSSSCT00060026025; ENSSSCP00060011021; ENSSSCG00060019294.
DR Ensembl; ENSSSCT00065063226; ENSSSCP00065027375; ENSSSCG00065046221.
DR GeneID; 397042; -.
DR KEGG; ssc:397042; -.
DR CTD; 961; -.
DR VGNC; VGNC:108637; CD47.
DR eggNOG; ENOG502RYTQ; Eukaryota.
DR GeneTree; ENSGT00390000007697; -.
DR InParanoid; Q9GKE8; -.
DR ChiTaRS; CD47; pig.
DR Proteomes; UP000008227; Chromosome 13.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000011942; Expressed in lung and 44 other tissues.
DR ExpressionAtlas; Q9GKE8; baseline and differential.
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 1: Evidence at protein 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_0000042207"
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..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..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 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97829"
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 109
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; 33253 MW; 97B33A919B016F70 CRC64;
MWPLVVVVLL GSAYCGSAQL IFNITKSVEF TVCNTTVTIP CFVNNMEAKN ISELYVKWKF
KGKDIFIFDG AQHISKPSEA FPSSKISPSE LLHGIASLKM DKRDAVIGNY TCEVTELSRE
GETIIELKRR FVSWFSPNEN ILIVIFPILA ILLFWGQFGI LTLKYKSSYT KEKTIFLLVA
GLMLTIIVIV GAILFIPGEY STKNACGLGL IVIPTAILIL LQYCVFMMAL GMSSFTIAIL
ILQVLGHVLS VVGLSLCVSE CTPVHGPLLI SGLGIIALAE LLGLVYMKCV ASDHKTIQPP
RNN
