ID SIRPG_HUMAN Reviewed; 387 AA. AC Q9P1W8; Q5D051; Q5JV25; Q5MKL4; Q8WWA5; Q9NQK8; DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 16-JUN-2009, entry version 74. DE RecName: Full=Signal-regulatory protein gamma; DE AltName: Full=Signal-regulatory protein beta-2; DE Short=SIRP-beta-2; DE Short=SIRP-b2; DE AltName: Full=CD172 antigen-like family member B; 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 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). 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 -!- 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; AL138804; CAC00474.1; -; Genomic_DNA. DR EMBL; AL138804; CAI16692.2; -; Genomic_DNA. DR EMBL; AL109809; CAI16692.2; JOINED; Genomic_DNA. DR EMBL; AL138804; CAM23420.1; -; Genomic_DNA. DR EMBL; AL109809; CAM23420.1; JOINED; Genomic_DNA. DR EMBL; AL109809; CAM28283.1; -; Genomic_DNA. DR EMBL; AL138804; CAM28283.1; JOINED; Genomic_DNA. DR EMBL; AL109809; CAM28285.1; -; Genomic_DNA. DR EMBL; AL138804; CAM28285.1; JOINED; 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; -. DR RefSeq; NP_061026.2; -. DR RefSeq; NP_543006.2; -. DR UniGene; Hs.590883; -. DR PDB; 2JJW; X-ray; 1.70 A; A=29-147. DR PDBsum; 2JJW; -. DR SMR; Q9P1W8; 31-153. DR IntAct; Q9P1W8; 1. DR PRIDE; Q9P1W8; -. DR Ensembl; ENSG00000089012; Homo sapiens. DR GeneID; 55423; -. DR KEGG; hsa:55423; -. DR GeneCards; GC20M001558; -. DR HGNC; HGNC:15757; SIRPG. DR MIM; 605466; gene. DR HOGENOM; Q9P1W8; -. DR HOVERGEN; Q9P1W8; -. DR OMA; Q9P1W8; LLGPIYV. DR Reactome; REACT_604; Hemostasis. DR Reactome; REACT_6900; Signaling in Immune system. DR NextBio; 59818; -. DR ArrayExpress; Q9P1W8; -. DR Bgee; Q9P1W8; -. DR CleanEx; HS_SIRPG; -. DR GermOnline; ENSG00000089012; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; EXP:Reactome. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0007242; P:intracellular signaling cascade; TAS:ProtInc. 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; IPR003006; Ig/MHC_CS. 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; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism; Repeat; KW Signal; Transmembrane. 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 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...) (Potential). 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 Potential. 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. 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 //