CD47_HUMAN
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 03-AUG-2022, entry version 195.
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 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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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: 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 (By similarity). Receptor for SIRPA, binding to which
CC prevents maturation of immature dendritic cells and inhibits cytokine
CC production by mature dendritic cells. Interaction with SIRPG mediates
CC cell-cell adhesion, enhances superantigen-dependent T-cell-mediated
CC proliferation and costimulates T-cell activation. May play a role in
CC membrane transport and/or integrin dependent signal transduction. May
CC prevent premature elimination of red blood cells. May be involved in
CC membrane permeability changes induced following virus infection.
CC {ECO:0000250, ECO:0000269|PubMed:11509594, ECO:0000269|PubMed:15383453,
CC ECO:0000269|PubMed:7691831}.
CC -!- SUBUNIT: Interacts with THBS1 and fibrinogen (By similarity). Monomer.
CC Interacts with SIRPA, SIRPG, UBQLN1 and UBQLN2. {ECO:0000250,
CC ECO:0000269|PubMed:10549293, ECO:0000269|PubMed:11509594,
CC ECO:0000269|PubMed:15383453, ECO:0000269|PubMed:18657508}.
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.
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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 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 AlphaFoldDB; Q08722; -.
DR SMR; Q08722; -.
DR BioGRID; 107399; 58.
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 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 EPD; Q08722; -.
DR jPOST; Q08722; -.
DR MassIVE; Q08722; -.
DR MaxQB; Q08722; -.
DR PaxDb; Q08722; -.
DR PeptideAtlas; Q08722; -.
DR PRIDE; Q08722; -.
DR ProteomicsDB; 58643; -. [Q08722-1]
DR ProteomicsDB; 58644; -. [Q08722-2]
DR ProteomicsDB; 58645; -. [Q08722-3]
DR ProteomicsDB; 58646; -. [Q08722-4]
DR ABCD; Q08722; 50 sequenced antibodies.
DR Antibodypedia; 4228; 1332 antibodies from 51 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 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; YKSNRTN; -.
DR OrthoDB; 1287706at2759; -.
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; 10 hits in 1083 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 204 other tissues.
DR ExpressionAtlas; Q08722; baseline and differential.
DR Genevisible; Q08722; HS.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
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: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:1904669; P:ATP export; IDA:ARUK-UCL.
DR GO; GO:0016477; P:cell migration; ISS:ARUK-UCL.
DR GO; GO:0071346; P:cellular response to interferon-gamma; 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:0007229; P:integrin-mediated signaling pathway; TAS:ProtInc.
DR GO; GO:1905450; P:negative regulation of Fc-gamma receptor signaling pathway involved in 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:0032649; P:regulation of interferon-gamma production; IMP: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 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 1: Evidence at protein level;
KW 3D-structure; 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..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
