CD47_MOUSE
ID CD47_MOUSE Reviewed; 303 AA.
AC Q61735; Q921Z2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 161.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND SUBCELLULAR LOCATION.
RC TISSUE=Pre-B cell;
RX PubMed=7691831; DOI=10.1083/jcb.123.2.485;
RA Lindberg F.P., Gresham H.D., Schwarz E., Brown E.J.;
RT "Molecular cloning of integrin-associated protein: an immunoglobulin family
RT member with multiple membrane spanning domains implicated in alpha-v beta-
RT 3-dependent ligand binding.";
RL J. Cell Biol. 123:485-496(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Stromal cell;
RX PubMed=9504415; DOI=10.1093/oxfordjournals.jbchem.a021895;
RA Furusawa T., Yanai N., Hara T., Miyajima A., Obinata M.;
RT "Integrin-associated protein (IAP, also termed CD47) is involved in stroma-
RT supported erythropoiesis.";
RL J. Biochem. 123:101-106(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 83-303 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 86-99, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000269|PubMed:7691831};
CC Multi-pass membrane protein {ECO:0000269|PubMed:7691831}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61735-2; Sequence=VSP_015793;
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DR EMBL; Z25524; CAA80978.1; -; mRNA.
DR EMBL; AB012693; BAA25401.1; -; mRNA.
DR EMBL; BC009094; AAH09094.1; -; mRNA.
DR EMBL; BC012667; AAH12667.1; -; mRNA.
DR CCDS; CCDS28212.1; -. [Q61735-2]
DR PIR; S36646; S36646.
DR RefSeq; NP_034711.1; NM_010581.3. [Q61735-2]
DR RefSeq; XP_006521874.1; XM_006521811.3.
DR AlphaFoldDB; Q61735; -.
DR SMR; Q61735; -.
DR BioGRID; 200835; 13.
DR IntAct; Q61735; 5.
DR STRING; 10090.ENSMUSP00000099853; -.
DR GuidetoPHARMACOLOGY; 2943; -.
DR GlyConnect; 2479; 23 N-Linked glycans (3 sites).
DR GlyGen; Q61735; 7 sites, 23 N-linked glycans (3 sites).
DR PhosphoSitePlus; Q61735; -.
DR SwissPalm; Q61735; -.
DR EPD; Q61735; -.
DR jPOST; Q61735; -.
DR MaxQB; Q61735; -.
DR PeptideAtlas; Q61735; -.
DR PRIDE; Q61735; -.
DR ProteomicsDB; 279982; -. [Q61735-1]
DR ProteomicsDB; 279983; -. [Q61735-2]
DR Antibodypedia; 4228; 1332 antibodies from 51 providers.
DR DNASU; 16423; -.
DR Ensembl; ENSMUST00000084838; ENSMUSP00000099853; ENSMUSG00000055447. [Q61735-2]
DR GeneID; 16423; -.
DR KEGG; mmu:16423; -.
DR UCSC; uc007zkg.1; mouse. [Q61735-2]
DR UCSC; uc007zkh.1; mouse. [Q61735-1]
DR CTD; 961; -.
DR MGI; MGI:96617; Cd47.
DR VEuPathDB; HostDB:ENSMUSG00000055447; -.
DR eggNOG; ENOG502RYTQ; Eukaryota.
DR GeneTree; ENSGT00390000007697; -.
DR HOGENOM; CLU_860392_0_0_1; -.
DR InParanoid; Q61735; -.
DR OrthoDB; 1287706at2759; -.
DR PhylomeDB; Q61735; -.
DR TreeFam; TF336026; -.
DR Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-MMU-216083; Integrin cell surface interactions.
DR Reactome; R-MMU-391160; Signal regulatory protein family interactions.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 16423; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Cd47; mouse.
DR PRO; PR:Q61735; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q61735; protein.
DR Bgee; ENSMUSG00000055447; Expressed in fetal liver hematopoietic progenitor cell and 264 other tissues.
DR ExpressionAtlas; Q61735; baseline and differential.
DR Genevisible; Q61735; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0070062; C:extracellular exosome; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; ISO:MGI.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; ISO:MGI.
DR GO; GO:0070053; F:thrombospondin receptor activity; ISO:MGI.
DR GO; GO:1904669; P:ATP export; ISO:MGI.
DR GO; GO:0016477; P:cell migration; ISO:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR GO; GO:0071349; P:cellular response to interleukin-12; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IDA:MGI.
DR GO; GO:0070487; P:monocyte aggregation; IMP:MGI.
DR GO; GO:1905450; P:negative regulation of Fc-gamma receptor signaling pathway involved in phagocytosis; ISO:MGI.
DR GO; GO:0008228; P:opsonization; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:MGI.
DR GO; GO:2000439; P:positive regulation of monocyte extravasation; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:MGI.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0050870; P:positive regulation of T cell activation; ISO:MGI.
DR GO; GO:0032649; P:regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0032653; P:regulation of interleukin-10 production; ISO:MGI.
DR GO; GO:0032655; P:regulation of interleukin-12 production; ISO:MGI.
DR GO; GO:0032675; P:regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; IDA:ARUK-UCL.
DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0009617; P:response to bacterium; IMP:MGI.
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 Alternative splicing; Cell adhesion; Cell membrane;
KW Direct protein sequencing; 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_0000042206"
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..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..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 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
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 80
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 129
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"
FT VAR_SEQ 131
FT /note="T -> TAFNTDQGSACSYEEEKGGCKL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7691831, ECO:0000303|PubMed:9504415"
FT /id="VSP_015793"
SQ SEQUENCE 303 AA; 33098 MW; 87C0E6EF758FFF58 CRC64;
MWPLAAALLL GSCCCGSAQL LFSNVNSIEF TSCNETVVIP CIVRNVEAQS TEEMFVKWKL
NKSYIFIYDG NKNSTTTDQN FTSAKISVSD LINGIASLKM DKRDAMVGNY TCEVTELSRE
GKTVIELKNR TVSWFSPNEK ILIVIFPILA ILLFWGKFGI LTLKYKSSHT NKRIILLLVA
GLVLTVIVVV GAILLIPGEK PVKNASGLGL IVISTGILIL LQYNVFMTAF GMTSFTIAIL
ITQVLGYVLA LVGLCLCIMA CEPVHGPLLI SGLGIIALAE LLGLVYMKFV ASNQRTIQPP
RNR
