ID SIRPG_HUMAN Reviewed; 387 AA. AC Q9P1W8; B1AKP6; Q5D051; Q5JV25; Q5MKL4; Q8WWA5; Q9NQK8; DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 19-OCT-2011, entry version 95. DE RecName: Full=Signal-regulatory protein gamma; DE Short=SIRP-gamma; DE AltName: Full=CD172 antigen-like family member B; DE AltName: Full=Signal-regulatory protein beta-2; DE Short=SIRP-b2; DE Short=SIRP-beta-2; DE AltName: CD_antigen=CD172g; DE Flags: Precursor; GN Name=SIRPG; Synonyms=SIRPB2; 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 2), TISSUE SPECIFICITY, AND RP VARIANTS ALA-263 AND LEU-286. RC TISSUE=Placenta; RX MEDLINE=21036165; PubMed=11185750; DOI=10.1007/s100380070013; RA Ichigotani Y., Matsuda S., Machida K., Oshima K., Iwamoto T., RA Yamaki K., Hayakawa T., Hamaguchi M.; RT "Molecular cloning of a novel human gene (SIRP-B2) which encodes a new RT member of the SIRP/SHPS-1 protein family."; RL J. Hum. Genet. 45:378-382(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH RP CD47, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Lung, and Ovary; 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 [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243, AND MASS RP SPECTROMETRY. 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 [7] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 29-147, AND DISULFIDE BOND. 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: Probable immunoglobulin-like cell surface receptor. On CC binding with CD47, mediates cell-cell adhesion. Engagement on T- CC cells by CD47 on antigen-presenting cells results in enhanced CC antigen-specific T-cell proliferation and costimulates T-cell CC activation. CC -!- SUBUNIT: Interacts with CD47. CC -!- INTERACTION: CC Q08722:CD47; NbExp=2; IntAct=EBI-1268284, EBI-1268321; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9P1W8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9P1W8-2; Sequence=VSP_007027; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q9P1W8-3; Sequence=VSP_007028; CC Note=No experimental confirmation available; CC Name=4; CC IsoId=Q9P1W8-4; Sequence=VSP_026960; CC -!- TISSUE SPECIFICITY: Detected in liver, and at very low levels in CC brain, heart, lung, pancreas, kidney, placenta and skeletal CC muscle. Expressed on CD4+ T-cells, CD8+ T-cells, CD56-bright CC natural killer (NK) cells, CD20+ cells, and all activated NK CC cells. Mainly present in the paracortical T-cell area of lymph CC nodes, with only sparse positive cells in the mantle and in the CC germinal center of B-cell follicles. In the thymus, primarily CC expressed in the medulla on mature T lymphocytes that have CC undergone thymic selection. CC -!- SIMILARITY: Contains 2 Ig-like C1-type (immunoglobulin-like) CC domains. CC -!- SIMILARITY: Contains 1 Ig-like V-type (immunoglobulin-like) CC domain. 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; AB042624; BAA95692.1; -; mRNA. DR EMBL; AY748247; AAV88530.1; -; mRNA. DR EMBL; AY748248; AAV88531.1; -; mRNA. DR EMBL; AL109809; CAM28283.1; -; Genomic_DNA. DR EMBL; AL138804; CAM28283.1; JOINED; Genomic_DNA. DR EMBL; AL109809; CAM28284.1; -; Genomic_DNA. DR EMBL; AL138804; CAM28284.1; JOINED; Genomic_DNA. DR EMBL; AL109809; CAM28285.1; -; Genomic_DNA. DR EMBL; AL138804; CAM28285.1; JOINED; Genomic_DNA. DR EMBL; CH471133; EAX10616.1; -; Genomic_DNA. DR EMBL; BC020629; AAH20629.2; -; mRNA. DR EMBL; BC064532; AAH64532.1; -; mRNA. DR IPI; IPI00032061; -. DR IPI; IPI00218601; -. DR IPI; IPI00550753; -. DR IPI; IPI00783247; -. DR RefSeq; NP_001034597.1; NM_001039508.1. DR RefSeq; NP_061026.2; NM_018556.3. DR RefSeq; NP_543006.2; NM_080816.2. DR UniGene; Hs.590883; -. DR PDB; 2JJW; X-ray; 1.70 A; A=29-147. DR PDBsum; 2JJW; -. DR ProteinModelPortal; Q9P1W8; -. DR SMR; Q9P1W8; 29-341. DR IntAct; Q9P1W8; 1. DR STRING; Q9P1W8; -. DR PRIDE; Q9P1W8; -. DR Ensembl; ENST00000303415; ENSP00000305529; ENSG00000089012. DR GeneID; 55423; -. DR KEGG; hsa:55423; -. DR UCSC; uc002wfm.1; human. DR UCSC; uc002wfn.1; human. DR UCSC; uc002wfo.1; human. DR CTD; 55423; -. DR GeneCards; GC20M001558; -. DR H-InvDB; HIX0027656; -. DR HGNC; HGNC:15757; SIRPG. DR MIM; 605466; gene. DR neXtProt; NX_Q9P1W8; -. DR PharmGKB; PA38034; -. DR eggNOG; prNOG18752; -. DR GeneTree; ENSGT00440000033339; -. DR HOGENOM; HBG282953; -. DR HOVERGEN; HBG056632; -. DR InParanoid; Q9P1W8; -. DR OMA; CQRETAS; -. DR PhylomeDB; Q9P1W8; -. DR Reactome; REACT_20676; Cell junction organization. DR Reactome; REACT_23853; Interactions of the immunoglobulin superfamily (IgSF) member proteins. DR Reactome; REACT_604; Hemostasis. DR NextBio; 59818; -. DR ArrayExpress; Q9P1W8; -. DR Bgee; Q9P1W8; -. DR CleanEx; HS_SIRPG; -. DR Genevestigator; Q9P1W8; -. DR GermOnline; ENSG00000089012; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; TAS:GOC. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0007596; P:blood coagulation; TAS:Reactome. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0034329; P:cell junction assembly; TAS:Reactome. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc. 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:0050870; P:positive regulation of T cell activation; IDA:UniProtKB. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 3. DR Pfam; PF07654; C1-set; 2. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 1. DR SMART; SM00407; IGc1; 2. DR PROSITE; PS50835; IG_LIKE; 3. DR PROSITE; PS00290; IG_MHC; FALSE_NEG. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Complete proteome; KW Disulfide bond; Glycoprotein; Immunoglobulin domain; Membrane; KW Polymorphism; Reference proteome; Repeat; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1 28 Potential. FT CHAIN 29 387 Signal-regulatory protein gamma. FT /FTId=PRO_0000014957. FT TOPO_DOM 29 360 Extracellular (Potential). FT TRANSMEM 361 383 Helical; (Potential). FT TOPO_DOM 384 387 Cytoplasmic (Potential). FT DOMAIN 29 137 Ig-like V-type. FT DOMAIN 146 245 Ig-like C1-type 1. FT DOMAIN 252 340 Ig-like C1-type 2. FT CARBOHYD 243 243 N-linked (GlcNAc...). FT CARBOHYD 268 268 N-linked (GlcNAc...) (Potential). FT CARBOHYD 309 309 N-linked (GlcNAc...) (Potential). FT CARBOHYD 317 317 N-linked (GlcNAc...) (Potential). FT DISULFID 53 119 FT DISULFID 168 226 Potential. FT DISULFID 271 329 Potential. FT VAR_SEQ 1 33 Missing (in isoform 2). FT /FTId=VSP_007027. FT VAR_SEQ 144 360 Missing (in isoform 3). FT /FTId=VSP_007028. FT VAR_SEQ 250 360 Missing (in isoform 4). FT /FTId=VSP_026960. FT VARIANT 263 263 V -> A (in dbSNP:rs6043409). FT /FTId=VAR_049936. FT VARIANT 286 286 S -> L (in dbSNP:rs6034239). FT /FTId=VAR_049937. FT STRAND 39 42 FT STRAND 49 51 FT STRAND 54 56 FT STRAND 64 68 FT STRAND 75 80 FT STRAND 88 92 FT STRAND 104 106 FT HELIX 111 113 FT STRAND 118 123 FT STRAND 130 133 FT STRAND 139 141 SQ SEQUENCE 387 AA; 42498 MW; 0F5099BE1DE35AC8 CRC64; MPVPASWPHP PGPFLLLTLL LGLTEVAGEE ELQMIQPEKL LLVTVGKTAT LHCTVTSLLP VGPVLWFRGV GPGRELIYNQ KEGHFPRVTT VSDLTKRNNM DFSIRISSIT PADVGTYYCV KFRKGSPENV EFKSGPGTEM ALGAKPSAPV VLGPAARTTP EHTVSFTCES HGFSPRDITL KWFKNGNELS DFQTNVDPTG QSVAYSIRST ARVVLDPWDV RSQVICEVAH VTLQGDPLRG TANLSEAIRV PPTLEVTQQP MRVGNQVNVT CQVRKFYPQS LQLTWSENGN VCQRETASTL TENKDGTYNW TSWFLVNISD QRDDVVLTCQ VKHDGQLAVS KRLALEVTVH QKDQSSDATP GPASSLTALL LIAVLLGPIY VPWKQKT //