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 23-MAY-2018, entry version 167. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT IgV-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 RT family member with multiple membrane spanning domains implicated in RT alpha-v beta-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 RT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT (IAP) and 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 RT intermediate 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 RT protein) requires a long range disulfide bond between the RT extracellular and 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., RA Delespesse G., Sarfati M.; RT "Bidirectional negative regulation of human T and dendritic cells by RT CD47 and its cognate receptor signal-regulator protein-alpha: down- RT regulation of IL-12 responsiveness and inhibition of dendritic cell RT activation."; RL J. Immunol. 167:2547-2554(2001). RN [11] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). 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 RT SIRPbeta2-CD47 interaction costimulates T-cell proliferation."; RL Blood 105:2421-2427(2005). RN [13] 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 RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [14] 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- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [15] 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., RA Ayoub D., 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 [16] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 19-136 IN COMPLEX WITH RP SIRPA, DISULFIDE BOND, GLYCOSYLATION AT ASN-23; ASN-50; ASN-73 AND RP ASN-111, AND 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., RA Barclay A.N.; RT "Paired receptor specificity explained by structures of signal RT regulatory 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 CC adhesion receptor for THBS1 on platelets, and in the modulation of CC integrins. Plays an important role in memory formation and CC synaptic plasticity in the hippocampus (By similarity). Receptor CC for SIRPA, binding to which prevents maturation of immature CC dendritic cells and inhibits cytokine production by mature CC dendritic cells. Interaction with SIRPG mediates cell-cell CC adhesion, enhances superantigen-dependent T-cell-mediated CC proliferation and costimulates T-cell activation. May play a role CC in membrane transport and/or integrin dependent signal CC transduction. May prevent premature elimination of red blood CC cells. May be involved in membrane permeability changes induced CC following virus infection. {ECO:0000250, CC ECO:0000269|PubMed:11509594, ECO:0000269|PubMed:15383453, CC ECO:0000269|PubMed:7691831}. CC -!- SUBUNIT: Interacts with THBS1 and fibrinogen (By similarity). CC Monomer. Interacts with SIRPA, SIRPG, UBQLN1 and UBQLN2. CC {ECO:0000250, ECO:0000269|PubMed:10549293, CC ECO:0000269|PubMed:11509594, ECO:0000269|PubMed:15383453, CC ECO:0000269|PubMed:18657508}. CC -!- INTERACTION: CC Q9P1W8:SIRPG; NbExp=2; IntAct=EBI-1268321, EBI-1268284; CC Q8N205:SYNE4; NbExp=3; IntAct=EBI-1268321, EBI-7131783; 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 Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=OA3-312; CC IsoId=Q08722-4; Sequence=VSP_002538; CC -!- TISSUE SPECIFICITY: Very broadly distributed on normal adult CC tissues, as well as ovarian tumors, being especially abundant in CC some epithelia and the brain. 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 UniGene; Hs.446414; -. 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 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 ProteinModelPortal; Q08722; -. DR SMR; Q08722; -. DR BioGrid; 107399; 26. DR CORUM; Q08722; -. DR DIP; DIP-39948N; -. DR IntAct; Q08722; 5. DR MINT; Q08722; -. DR STRING; 9606.ENSP00000355361; -. DR TCDB; 1.N.1.1.1; the osteoclast fusion complex (ofc) family. DR iPTMnet; Q08722; -. DR PhosphoSitePlus; Q08722; -. DR SwissPalm; Q08722; -. DR BioMuta; CD47; -. DR DMDM; 1171879; -. DR EPD; Q08722; -. DR MaxQB; Q08722; -. DR PaxDb; Q08722; -. DR PeptideAtlas; Q08722; -. DR PRIDE; Q08722; -. DR DNASU; 961; -. DR Ensembl; ENST00000355354; ENSP00000347512; ENSG00000196776. [Q08722-3] DR Ensembl; ENST00000361309; ENSP00000355361; ENSG00000196776. [Q08722-1] DR GeneID; 961; -. DR KEGG; hsa:961; -. DR UCSC; uc003dwt.2; human. [Q08722-1] DR CTD; 961; -. DR DisGeNET; 961; -. DR EuPathDB; HostDB:ENSG00000196776.14; -. DR GeneCards; CD47; -. DR HGNC; HGNC:1682; CD47. DR HPA; CAB016055; -. DR HPA; HPA044659; -. DR MIM; 601028; gene. DR neXtProt; NX_Q08722; -. DR OpenTargets; ENSG00000196776; -. DR PharmGKB; PA26222; -. DR eggNOG; ENOG410IJTS; Eukaryota. DR eggNOG; ENOG41113GI; LUCA. DR GeneTree; ENSGT00390000007697; -. DR HOGENOM; HOG000013020; -. DR HOVERGEN; HBG003808; -. DR InParanoid; Q08722; -. DR KO; K06266; -. DR OMA; VYMKFVA; -. DR OrthoDB; EOG091G0HUR; -. DR PhylomeDB; Q08722; -. DR TreeFam; TF336026; -. 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 SIGNOR; Q08722; -. DR ChiTaRS; CD47; human. DR EvolutionaryTrace; Q08722; -. DR GeneWiki; CD47; -. DR GenomeRNAi; 961; -. DR PRO; PR:Q08722; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000196776; -. DR CleanEx; HS_CD47; -. DR ExpressionAtlas; Q08722; baseline and differential. DR Genevisible; Q08722; HS. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. 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:0070053; F:thrombospondin receptor activity; IPI:BHF-UCL. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome. DR GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:ProtInc. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0008228; P:opsonization; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell 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; IEA:Ensembl. DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl. DR GO; GO:0050870; P:positive regulation of T cell activation; IDA:UniProtKB. DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl. DR CDD; cd16090; IgV_CD47; 1. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR006704; CD47. DR InterPro; IPR013147; CD47_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 Complete proteome; Direct protein sequencing; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein; KW Pyrrolidone carboxylic acid; Reference proteome; Signal; KW Transmembrane; Transmembrane helix. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 323 Leukocyte surface antigen CD47. FT /FTId=PRO_0000014880. FT TOPO_DOM 19 141 Extracellular. {ECO:0000255}. FT TRANSMEM 142 162 Helical. {ECO:0000255}. FT TOPO_DOM 163 176 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 177 197 Helical. {ECO:0000255}. FT TOPO_DOM 198 207 Extracellular. {ECO:0000255}. FT TRANSMEM 208 228 Helical. {ECO:0000255}. FT TOPO_DOM 229 235 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 236 256 Helical. {ECO:0000255}. FT TOPO_DOM 257 268 Extracellular. {ECO:0000255}. FT TRANSMEM 269 289 Helical. {ECO:0000255}. FT TOPO_DOM 290 323 Cytoplasmic. {ECO:0000255}. FT DOMAIN 19 127 Ig-like V-type. FT MOD_RES 19 19 Pyrrolidone carboxylic acid. FT {ECO:0000269|PubMed:18657508}. FT MOD_RES 89 89 Phosphoserine. FT {ECO:0000250|UniProtKB:P97829}. FT CARBOHYD 23 23 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:18657508}. FT CARBOHYD 34 34 N-linked (GlcNAc...) asparagine. FT CARBOHYD 50 50 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:18657508, FT ECO:0000269|PubMed:19349973}. FT CARBOHYD 73 73 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:18657508, FT ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19349973}. FT CARBOHYD 111 111 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:18657508, FT ECO:0000269|PubMed:19159218}. FT CARBOHYD 206 206 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 33 263 {ECO:0000269|PubMed:11454874}. FT DISULFID 41 114 {ECO:0000269|PubMed:18657508}. FT VAR_SEQ 293 323 Missing (in isoform OA3-293). FT {ECO:0000305}. FT /FTId=VSP_002535. FT VAR_SEQ 304 305 KA -> NN (in isoform OA3-305). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7691831, FT ECO:0000303|Ref.3}. FT /FTId=VSP_002536. FT VAR_SEQ 306 323 Missing (in isoform OA3-305). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7691831, FT ECO:0000303|Ref.3}. FT /FTId=VSP_002537. FT VAR_SEQ 312 323 Missing (in isoform OA3-312). FT {ECO:0000305}. FT /FTId=VSP_002538. FT STRAND 26 30 {ECO:0000244|PDB:2JJS}. FT STRAND 35 39 {ECO:0000244|PDB:2JJS}. FT STRAND 42 45 {ECO:0000244|PDB:2JJS}. FT HELIX 51 53 {ECO:0000244|PDB:2JJS}. FT STRAND 54 60 {ECO:0000244|PDB:2JJS}. FT STRAND 63 69 {ECO:0000244|PDB:2JJS}. FT HELIX 70 72 {ECO:0000244|PDB:2JJS}. FT STRAND 74 76 {ECO:0000244|PDB:2JJS}. FT HELIX 79 81 {ECO:0000244|PDB:2JJS}. FT HELIX 88 93 {ECO:0000244|PDB:2JJS}. FT STRAND 98 101 {ECO:0000244|PDB:2JJS}. FT HELIX 102 106 {ECO:0000244|PDB:2JJS}. FT STRAND 110 118 {ECO:0000244|PDB:2JJS}. FT STRAND 121 131 {ECO:0000244|PDB:2JJS}. 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 //