ID CD47_HUMAN Reviewed; 323 AA. AC Q08722; A8K198; D3DN59; Q53Y71; Q96A60; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 204. DE RecName: Full=Leukocyte surface antigen CD47; DE AltName: Full=Antigenic surface determinant protein OA3; DE AltName: Full=Integrin-associated protein; DE Short=IAP; DE AltName: Full=Protein MER6; DE AltName: CD_antigen=CD47; DE Flags: Precursor; GN Name=CD47; Synonyms=MER6; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM OA3-323). RC TISSUE=Ovary; RX PubMed=1394148; RA Campbell I.G., Freemont P.S., Foulkes W., Trowsdale J.; RT "An ovarian tumor marker with homology to vaccinia virus contains an IgV- RT like region and multiple transmembrane domains."; RL Cancer Res. 52:5416-5420(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM OA3-305), FUNCTION, SUBCELLULAR RP LOCATION, AND TOPOLOGY. RC TISSUE=Myelomonocyte; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM OA3-305). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM OA3-323). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM OA3-305). RC TISSUE=Hippocampus, Leiomyosarcoma, and Ovarian adenocarcinoma; 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 [7] RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION AS CD47. RC TISSUE=Erythrocyte; RX PubMed=7998989; DOI=10.1042/bj3040525; RA Mawby W.J., Holmes C.H., Anstee D.J., Spring F.A., Tanner M.J.A.; RT "Isolation and characterization of CD47 glycoprotein: a multispanning RT membrane protein which is the same as integrin-associated protein (IAP) and RT the ovarian tumour marker OA3."; RL Biochem. J. 304:525-530(1994). RN [8] RP FUNCTION, AND INTERACTION WITH THBS1. RX PubMed=8550562; DOI=10.1074/jbc.271.1.21; RA Gao A.G., Lindberg F.P., Finn M.B., Blystone S.D., Brown E.J., RA Frazier W.A.; RT "Integrin-associated protein is a receptor for the C-terminal domain of RT thrombospondin."; RL J. Biol. Chem. 271:21-24(1996). RN [9] RP INTERACTION WITH UBQLN1 AND UBQLN2. RX PubMed=10549293; DOI=10.1016/s1097-2765(00)80212-9; RA Wu A.-L., Wang J., Zheleznyak A., Brown E.J.; RT "Ubiquitin-related proteins regulate interaction of vimentin intermediate RT filaments with the plasma membrane."; RL Mol. Cell 4:619-625(1999). RN [10] RP DISULFIDE BOND. RX PubMed=11454874; DOI=10.1074/jbc.m106107200; RA Rebres R.A., Vaz L.E., Green J.M., Brown E.J.; RT "Normal ligand binding and signaling by CD47 (integrin-associated protein) RT requires a long range disulfide bond between the extracellular and RT membrane-spanning domains."; RL J. Biol. Chem. 276:34607-34616(2001). RN [11] RP FUNCTION, AND INTERACTION WITH SIRPA. RX PubMed=11509594; DOI=10.4049/jimmunol.167.5.2547; RA Latour S., Tanaka H., Demeure C., Mateo V., Rubio M., Brown E.J., RA Maliszewski C., Lindberg F.P., Oldenborg A., Ullrich A., Delespesse G., RA Sarfati M.; RT "Bidirectional negative regulation of human T and dendritic cells by CD47 RT and its cognate receptor signal-regulator protein-alpha: down-regulation of RT IL-12 responsiveness and inhibition of dendritic cell activation."; RL J. Immunol. 167:2547-2554(2001). RN [12] RP FUNCTION, AND INTERACTION WITH SIRPG. RC TISSUE=T-cell; RX PubMed=15383453; DOI=10.1182/blood-2004-07-2823; RA Piccio L., Vermi W., Boles K.S., Fuchs A., Strader C.A., Facchetti F., RA Cella M., Colonna M.; RT "Adhesion of human T cells to antigen-presenting cells through SIRPbeta2- RT CD47 interaction costimulates T-cell proliferation."; RL Blood 105:2421-2427(2005). RN [13] RP INTERACTION WITH FAS/CD95. RX PubMed=15917238; DOI=10.1074/jbc.m500922200; RA Manna P.P., Dimitry J., Oldenborg P.A., Frazier W.A.; RT "CD47 augments Fas/CD95-mediated apoptosis."; RL J. Biol. Chem. 280:29637-29644(2005). RN [14] RP FUNCTION, AND INTERACTION WITH THBS1. RX PubMed=19004835; DOI=10.1074/jbc.m804860200; RA Isenberg J.S., Annis D.S., Pendrak M.L., Ptaszynska M., Frazier W.A., RA Mosher D.F., Roberts D.D.; RT "Differential interactions of thrombospondin-1, -2, and -4 with CD47 and RT effects on cGMP signaling and ischemic injury responses."; RL J. Biol. Chem. 284:1116-1125(2009). RN [15] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-73 AND ASN-111. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [16] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-50 AND ASN-73. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [17] RP INTERACTION WITH FIBRINOGEN. RX PubMed=22079249; DOI=10.1016/j.bbamem.2011.10.028; RA De Oliveira S., Vitorino de Almeida V., Calado A., Rosario H.S., RA Saldanha C.; RT "Integrin-associated protein (CD47) is a putative mediator for soluble RT fibrinogen interaction with human red blood cells membrane."; RL Biochim. Biophys. Acta 1818:481-490(2012). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [19] RP FUNCTION, AND INDUCTION. RX PubMed=27742621; DOI=10.1093/cvr/cvw218; RA Rogers N.M., Sharifi-Sanjani M., Yao M., Ghimire K., Bienes-Martinez R., RA Mutchler S.M., Knupp H.E., Baust J., Novelli E.M., Ross M., St Croix C., RA Kutten J.C., Czajka C.A., Sembrat J.C., Rojas M., Labrousse-Arias D., RA Bachman T.N., Vanderpool R.R., Zuckerbraun B.S., Champion H.C., Mora A.L., RA Straub A.C., Bilonick R.A., Calzada M.J., Isenberg J.S.; RT "TSP1-CD47 signaling is upregulated in clinical pulmonary hypertension and RT contributes to pulmonary arterial vasculopathy and dysfunction."; RL Cardiovasc. Res. 113:15-29(2017). RN [20] RP FUNCTION, AND INDUCTION. RX PubMed=32679764; DOI=10.3390/cells9071695; RA Ghimire K., Li Y., Chiba T., Julovi S.M., Li J., Ross M.A., Straub A.C., RA O'Connell P.J., Rueegg C., Pagano P.J., Isenberg J.S., Rogers N.M.; RT "CD47 Promotes Age-Associated Deterioration in Angiogenesis, Blood Flow and RT Glucose Homeostasis."; RL Cells 9:0-0(2020). RN [21] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-136 IN COMPLEX WITH SIRPA, RP DISULFIDE BOND, GLYCOSYLATION AT ASN-23; ASN-50; ASN-73 AND ASN-111, AND RP PYROGLUTAMATE FORMATION AT GLN-19. RX PubMed=18657508; DOI=10.1016/j.molcel.2008.05.026; RA Hatherley D., Graham S.C., Turner J., Harlos K., Stuart D.I., Barclay A.N.; RT "Paired receptor specificity explained by structures of signal regulatory RT proteins alone and complexed with CD47."; RL Mol. Cell 31:266-277(2008). CC -!- FUNCTION: Adhesive protein that mediates cell-to-cell interactions CC (PubMed:11509594, PubMed:15383453). Acts as a receptor for CC thrombospondin THBS1 and as modulator of integrin signaling through the CC activation of heterotrimeric G proteins (PubMed:19004835, CC PubMed:8550562, PubMed:7691831). Involved in signal transduction, CC cardiovascular homeostasis, inflammation, apoptosis, angiogenesis, CC cellular self-renewal, and immunoregulation (PubMed:27742621, CC PubMed:19004835, PubMed:8550562, PubMed:11509594, PubMed:7691831, CC PubMed:32679764, PubMed:15383453). Plays a role in modulating pulmonary CC endothelin EDN1 signaling (PubMed:27742621). Modulates nitrous oxide CC (NO) signaling, in response to THBS1, hence playing a role as a pressor CC agent, supporting blood pressure (By similarity). Plays an important CC role in memory formation and synaptic plasticity in the hippocampus (By CC similarity). Receptor for SIRPA, binding to which prevents maturation CC of immature dendritic cells and inhibits cytokine production by mature CC dendritic cells (PubMed:11509594). Interaction with SIRPG mediates CC cell-cell adhesion, enhances superantigen-dependent T-cell-mediated CC proliferation and costimulates T-cell activation (PubMed:15383453). CC Positively modulates FAS-dependent apoptosis in T-cells, perhaps by CC enhancing FAS clustering (By similarity). Plays a role in suppressing CC angiogenesis and may be involved in metabolic dysregulation during CC normal aging (PubMed:32679764). In response to THBS1, negatively CC modulates wound healing (By similarity). Inhibits stem cell self- CC renewal, in response to THBS1, probably by regulation of the stem cell CC transcription factors POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 (By CC similarity). May play a role in membrane transport and/or integrin CC dependent signal transduction (PubMed:7691831). May prevent premature CC elimination of red blood cells (By similarity). CC {ECO:0000250|UniProtKB:P97829, ECO:0000250|UniProtKB:Q61735, CC ECO:0000269|PubMed:11509594, ECO:0000269|PubMed:15383453, CC ECO:0000269|PubMed:19004835, ECO:0000269|PubMed:27742621, CC ECO:0000269|PubMed:32679764, ECO:0000269|PubMed:7691831, CC ECO:0000269|PubMed:8550562}. CC -!- SUBUNIT: Monomer (PubMed:18657508). Interacts with THBS1 (via the C- CC terminal domain) (PubMed:8550562, PubMed:19004835). Interacts with CC SIRPA (PubMed:11509594). Interacts with FAS/CD95; interaction may be CC enhanced by functional activation (PubMed:15917238). Interacts with CC SIRPG, UBQLN1 and UBQLN2 (PubMed:10549293, PubMed:15383453, CC PubMed:18657508). May interact with fibrinogen (PubMed:22079249). CC {ECO:0000269|PubMed:10549293, ECO:0000269|PubMed:11509594, CC ECO:0000269|PubMed:15383453, ECO:0000269|PubMed:15917238, CC ECO:0000269|PubMed:18657508, ECO:0000269|PubMed:19004835, CC ECO:0000269|PubMed:22079249, ECO:0000269|PubMed:8550562}. CC -!- INTERACTION: CC Q08722; Q9P1W8: SIRPG; NbExp=2; IntAct=EBI-1268321, EBI-1268284; CC Q08722; Q8N205: SYNE4; NbExp=3; IntAct=EBI-1268321, EBI-7131783; CC Q08722-3; P05067: APP; NbExp=3; IntAct=EBI-17263290, EBI-77613; CC Q08722-3; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-17263290, EBI-3923617; CC Q08722-3; P15941-11: MUC1; NbExp=3; IntAct=EBI-17263290, EBI-17263240; CC Q08722-3; P15151: PVR; NbExp=3; IntAct=EBI-17263290, EBI-3919694; CC Q08722-3; Q9NRX6: TMEM167B; NbExp=3; IntAct=EBI-17263290, EBI-17684533; 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=4; CC Name=OA3-323; CC IsoId=Q08722-1; Sequence=Displayed; CC Name=OA3-293; CC IsoId=Q08722-2; Sequence=VSP_002535; CC Name=OA3-305; CC IsoId=Q08722-3; Sequence=VSP_002536, VSP_002537; CC Name=OA3-312; CC IsoId=Q08722-4; Sequence=VSP_002538; CC -!- TISSUE SPECIFICITY: Very broadly distributed on normal adult tissues, CC as well as ovarian tumors, being especially abundant in some epithelia CC and the brain. CC -!- INDUCTION: Induced in pulmonary artery and lung parenchyma following CC injury or stress (PubMed:27742621). Expression in arteries increases in CC normal aging (PubMed:32679764). {ECO:0000269|PubMed:27742621, CC ECO:0000269|PubMed:32679764}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X69398; CAA49196.1; -; mRNA. DR EMBL; Z25521; CAA80977.1; -; mRNA. DR EMBL; BT006907; AAP35553.1; -; mRNA. DR EMBL; AK289813; BAF82502.1; -; mRNA. DR EMBL; CH471052; EAW79733.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79734.1; -; Genomic_DNA. DR EMBL; BC010016; AAH10016.1; -; mRNA. DR EMBL; BC012884; AAH12884.1; -; mRNA. DR EMBL; BC037306; AAH37306.1; -; mRNA. DR CCDS; CCDS43125.1; -. [Q08722-3] DR CCDS; CCDS43126.1; -. [Q08722-1] DR PIR; A48997; A48997. DR RefSeq; NP_001768.1; NM_001777.3. [Q08722-1] DR RefSeq; NP_942088.1; NM_198793.2. [Q08722-3] DR PDB; 2JJS; X-ray; 1.85 A; C/D=20-136. DR PDB; 2JJT; X-ray; 2.30 A; C/D=20-136. DR PDB; 2VSC; X-ray; 1.90 A; A/B/C/D=20-136. DR PDB; 4CMM; X-ray; 1.92 A; B=20-136. DR PDB; 4KJY; X-ray; 1.93 A; A/C=19-135. DR PDB; 5IWL; X-ray; 2.80 A; C/D=20-132. DR PDB; 5TZ2; X-ray; 2.30 A; C=19-141. DR PDB; 5TZT; X-ray; 2.89 A; C/D=20-141. DR PDB; 5TZU; X-ray; 2.10 A; C=19-141. DR PDB; 7MYZ; X-ray; 3.40 A; C/D=19-323. DR PDB; 7WN8; X-ray; 2.80 A; A/C=1-323. DR PDB; 7XJF; X-ray; 2.60 A; C=19-134. DR PDB; 7YGG; X-ray; 2.76 A; C/D=19-135. DR PDBsum; 2JJS; -. DR PDBsum; 2JJT; -. DR PDBsum; 2VSC; -. DR PDBsum; 4CMM; -. DR PDBsum; 4KJY; -. DR PDBsum; 5IWL; -. DR PDBsum; 5TZ2; -. DR PDBsum; 5TZT; -. DR PDBsum; 5TZU; -. DR PDBsum; 7MYZ; -. DR PDBsum; 7WN8; -. DR PDBsum; 7XJF; -. DR PDBsum; 7YGG; -. DR AlphaFoldDB; Q08722; -. DR SMR; Q08722; -. DR BioGRID; 107399; 62. DR CORUM; Q08722; -. DR DIP; DIP-39948N; -. DR IntAct; Q08722; 32. DR MINT; Q08722; -. DR STRING; 9606.ENSP00000355361; -. DR BindingDB; Q08722; -. DR ChEMBL; CHEMBL3714583; -. DR GuidetoPHARMACOLOGY; 2943; -. DR TCDB; 1.N.1.1.1; the osteoclast fusion complex (ofc) family. DR GlyConnect; 1456; 18 N-Linked glycans (1 site). DR GlyCosmos; Q08722; 6 sites, 20 glycans. DR GlyGen; Q08722; 7 sites, 23 N-linked glycans (1 site), 1 O-linked glycan (1 site). DR iPTMnet; Q08722; -. DR PhosphoSitePlus; Q08722; -. DR SwissPalm; Q08722; -. DR BioMuta; CD47; -. DR DMDM; 1171879; -. DR CPTAC; CPTAC-5975; -. DR EPD; Q08722; -. DR jPOST; Q08722; -. DR MassIVE; Q08722; -. DR MaxQB; Q08722; -. DR PaxDb; 9606-ENSP00000355361; -. DR PeptideAtlas; Q08722; -. DR ProteomicsDB; 58643; -. [Q08722-1] DR ProteomicsDB; 58644; -. [Q08722-2] DR ProteomicsDB; 58645; -. [Q08722-3] DR ProteomicsDB; 58646; -. [Q08722-4] DR Pumba; Q08722; -. DR ABCD; Q08722; 51 sequenced antibodies. DR Antibodypedia; 4228; 1994 antibodies from 52 providers. DR CPTC; Q08722; 4 antibodies. DR DNASU; 961; -. DR Ensembl; ENST00000355354.13; ENSP00000347512.7; ENSG00000196776.17. [Q08722-3] DR Ensembl; ENST00000361309.6; ENSP00000355361.5; ENSG00000196776.17. [Q08722-1] DR GeneID; 961; -. DR KEGG; hsa:961; -. DR MANE-Select; ENST00000361309.6; ENSP00000355361.5; NM_001777.4; NP_001768.1. DR UCSC; uc003dwt.2; human. [Q08722-1] DR AGR; HGNC:1682; -. DR CTD; 961; -. DR DisGeNET; 961; -. DR GeneCards; CD47; -. DR HGNC; HGNC:1682; CD47. DR HPA; ENSG00000196776; Low tissue specificity. DR MIM; 601028; gene. DR neXtProt; NX_Q08722; -. DR OpenTargets; ENSG00000196776; -. DR PharmGKB; PA26222; -. DR VEuPathDB; HostDB:ENSG00000196776; -. DR eggNOG; ENOG502RYTQ; Eukaryota. DR GeneTree; ENSGT00390000007697; -. DR HOGENOM; CLU_860392_0_0_1; -. DR InParanoid; Q08722; -. DR OMA; CISECTP; -. DR OrthoDB; 4635767at2759; -. DR PhylomeDB; Q08722; -. DR TreeFam; TF336026; -. DR PathwayCommons; Q08722; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-216083; Integrin cell surface interactions. DR Reactome; R-HSA-391160; Signal regulatory protein family interactions. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; Q08722; -. DR SIGNOR; Q08722; -. DR BioGRID-ORCS; 961; 12 hits in 1163 CRISPR screens. DR ChiTaRS; CD47; human. DR EvolutionaryTrace; Q08722; -. DR GeneWiki; CD47; -. DR GenomeRNAi; 961; -. DR Pharos; Q08722; Tchem. DR PRO; PR:Q08722; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q08722; Protein. DR Bgee; ENSG00000196776; Expressed in gingival epithelium and 206 other cell types or tissues. DR ExpressionAtlas; Q08722; baseline and differential. DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL. DR GO; GO:0070062; C:extracellular exosome; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome. DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IPI:ARUK-UCL. DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; ISS:ARUK-UCL. DR GO; GO:0070053; F:thrombospondin receptor activity; IPI:BHF-UCL. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:1904669; P:ATP export; IDA:ARUK-UCL. DR GO; GO:0016477; P:cell migration; ISS:ARUK-UCL. DR GO; GO:0071347; P:cellular response to interleukin-1; ISS:ARUK-UCL. DR GO; GO:0071349; P:cellular response to interleukin-12; IMP:ARUK-UCL. DR GO; GO:0071346; P:cellular response to type II interferon; ISS:ARUK-UCL. DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW. DR GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:ProtInc. DR GO; GO:0050765; P:negative regulation of phagocytosis; ISS:ARUK-UCL. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:UniProtKB. DR GO; GO:0050729; P:positive regulation of inflammatory response; IBA:GO_Central. DR GO; GO:2000439; P:positive regulation of monocyte extravasation; ISS:ARUK-UCL. DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central. DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:ARUK-UCL. DR GO; GO:0050870; P:positive regulation of T cell activation; IDA:UniProtKB. DR GO; GO:0060368; P:regulation of Fc receptor mediated stimulatory signaling pathway; ISS:ARUK-UCL. DR GO; GO:0032653; P:regulation of interleukin-10 production; IMP:ARUK-UCL. DR GO; GO:0032655; P:regulation of interleukin-12 production; IMP:ARUK-UCL. DR GO; GO:0032675; P:regulation of interleukin-6 production; IMP:ARUK-UCL. DR GO; GO:0045428; P:regulation of nitric oxide biosynthetic process; ISS:ARUK-UCL. DR GO; GO:0032680; P:regulation of tumor necrosis factor production; IMP:ARUK-UCL. DR GO; GO:0032649; P:regulation of type II interferon production; IMP:ARUK-UCL. DR CDD; cd16090; IgV_CD47; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 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; LEUKOCYTE SURFACE ANTIGEN CD47; 1. DR PANTHER; PTHR10613:SF0; LEUKOCYTE SURFACE ANTIGEN CD47; 1. DR Pfam; PF04549; CD47; 1. DR Pfam; PF08204; V-set_CD47; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR Genevisible; Q08722; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Angiogenesis; Apoptosis; Cell adhesion; KW Cell membrane; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Immunoglobulin domain; Inflammatory response; 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_0000014880" 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:0000269|PubMed:18657508" 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:0000269|PubMed:18657508" FT CARBOHYD 34 FT /note="N-linked (GlcNAc...) asparagine" FT CARBOHYD 50 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18657508, FT ECO:0000269|PubMed:19349973" FT CARBOHYD 73 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18657508, FT ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:18657508, FT ECO:0000269|PubMed:19159218" FT CARBOHYD 206 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 33..263 FT /evidence="ECO:0000269|PubMed:11454874" FT DISULFID 41..114 FT /evidence="ECO:0000269|PubMed:18657508" FT VAR_SEQ 293..323 FT /note="Missing (in isoform OA3-293)" FT /evidence="ECO:0000305" FT /id="VSP_002535" FT VAR_SEQ 304..305 FT /note="KA -> NN (in isoform OA3-305)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7691831, ECO:0000303|Ref.3" FT /id="VSP_002536" FT VAR_SEQ 306..323 FT /note="Missing (in isoform OA3-305)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7691831, ECO:0000303|Ref.3" FT /id="VSP_002537" FT VAR_SEQ 312..323 FT /note="Missing (in isoform OA3-312)" FT /evidence="ECO:0000305" FT /id="VSP_002538" FT STRAND 26..30 FT /evidence="ECO:0007829|PDB:2JJS" FT STRAND 35..39 FT /evidence="ECO:0007829|PDB:2JJS" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:2JJS" FT HELIX 51..53 FT /evidence="ECO:0007829|PDB:2JJS" FT STRAND 54..60 FT /evidence="ECO:0007829|PDB:2JJS" FT STRAND 63..69 FT /evidence="ECO:0007829|PDB:2JJS" FT HELIX 70..72 FT /evidence="ECO:0007829|PDB:2JJS" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:2JJS" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:2JJS" FT HELIX 88..93 FT /evidence="ECO:0007829|PDB:2JJS" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:2JJS" FT HELIX 102..106 FT /evidence="ECO:0007829|PDB:2JJS" FT STRAND 110..118 FT /evidence="ECO:0007829|PDB:2JJS" FT STRAND 121..131 FT /evidence="ECO:0007829|PDB:2JJS" FT TURN 139..143 FT /evidence="ECO:0007829|PDB:7MYZ" FT HELIX 144..164 FT /evidence="ECO:0007829|PDB:7MYZ" FT HELIX 178..196 FT /evidence="ECO:0007829|PDB:7MYZ" FT STRAND 197..202 FT /evidence="ECO:0007829|PDB:7MYZ" FT HELIX 204..224 FT /evidence="ECO:0007829|PDB:7MYZ" FT HELIX 238..253 FT /evidence="ECO:0007829|PDB:7MYZ" FT TURN 254..260 FT /evidence="ECO:0007829|PDB:7MYZ" FT STRAND 261..264 FT /evidence="ECO:0007829|PDB:7MYZ" FT HELIX 268..292 FT /evidence="ECO:0007829|PDB:7MYZ" SQ SEQUENCE 323 AA; 35214 MW; 5D20730A2632D550 CRC64; MWPLVAALLL GSACCGSAQL LFNKTKSVEF TFCNDTVVIP CFVTNMEAQN TTEVYVKWKF KGRDIYTFDG ALNKSTVPTD FSSAKIEVSQ LLKGDASLKM DKSDAVSHTG NYTCEVTELT REGETIIELK YRVVSWFSPN ENILIVIFPI FAILLFWGQF GIKTLKYRSG GMDEKTIALL VAGLVITVIV IVGAILFVPG EYSLKNATGL GLIVTSTGIL ILLHYYVFST AIGLTSFVIA ILVIQVIAYI LAVVGLSLCI AACIPMHGPL LISGLSILAL AQLLGLVYMK FVASNQKTIQ PPRKAVEEPL NAFKESKGMM NDE //