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 12-AUG-2020, entry version 163. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANTS RP ALA-263 AND LEU-286. RC TISSUE=Placenta; RX PubMed=11185750; DOI=10.1007/s100380070013; RA Ichigotani Y., Matsuda S., Machida K., Oshima K., Iwamoto T., Yamaki K., RA 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 CD47, RP 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 SIRPbeta2- RT CD47 interaction costimulates T-cell proliferation."; RL Blood 105:2421-2427(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX 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., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., 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., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., 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., 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 [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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243. 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 [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., 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: Probable immunoglobulin-like cell surface receptor. On CC binding with CD47, mediates cell-cell adhesion. Engagement on T-cells CC by CD47 on antigen-presenting cells results in enhanced antigen- CC specific T-cell proliferation and costimulates T-cell activation. CC {ECO:0000269|PubMed:15383453}. CC -!- SUBUNIT: Interacts with CD47. {ECO:0000269|PubMed:15383453}. CC -!- INTERACTION: CC Q9P1W8; Q08722: CD47; NbExp=2; IntAct=EBI-1268284, EBI-1268321; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15383453}; Single- CC pass type I membrane protein {ECO:0000269|PubMed:15383453}. 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 Name=3; CC IsoId=Q9P1W8-3; Sequence=VSP_007028; CC Name=4; CC IsoId=Q9P1W8-4; Sequence=VSP_026960; CC -!- TISSUE SPECIFICITY: Detected in liver, and at very low levels in brain, CC heart, lung, pancreas, kidney, placenta and skeletal muscle. Expressed CC on CD4+ T-cells, CD8+ T-cells, CD56-bright natural killer (NK) cells, CC CD20+ cells, and all activated NK cells. Mainly present in the CC paracortical T-cell area of lymph nodes, with only sparse positive CC cells in the mantle and in the germinal center of B-cell follicles. In CC the thymus, primarily expressed in the medulla on mature T-lymphocytes CC that have undergone thymic selection. {ECO:0000269|PubMed:11185750, CC ECO:0000269|PubMed:15383453}. 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; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL138804; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10616.1; -; Genomic_DNA. DR EMBL; BC020629; AAH20629.2; -; mRNA. DR EMBL; BC064532; AAH64532.1; -; mRNA. DR CCDS; CCDS13020.2; -. [Q9P1W8-1] DR CCDS; CCDS13021.2; -. [Q9P1W8-3] DR CCDS; CCDS33434.1; -. [Q9P1W8-4] DR RefSeq; NP_001034597.1; NM_001039508.1. [Q9P1W8-4] DR RefSeq; NP_061026.2; NM_018556.3. [Q9P1W8-1] DR RefSeq; NP_543006.2; NM_080816.2. [Q9P1W8-3] DR RefSeq; XP_011527588.1; XM_011529286.2. [Q9P1W8-2] DR PDB; 2JJW; X-ray; 1.70 A; A=29-147. DR PDB; 4I2X; X-ray; 2.48 A; E/F=29-347. DR PDBsum; 2JJW; -. DR PDBsum; 4I2X; -. DR SMR; Q9P1W8; -. DR BioGRID; 120664; 3. DR IntAct; Q9P1W8; 3. DR STRING; 9606.ENSP00000305529; -. DR GlyGen; Q9P1W8; 4 sites. DR iPTMnet; Q9P1W8; -. DR PhosphoSitePlus; Q9P1W8; -. DR BioMuta; SIRPG; -. DR DMDM; 124053651; -. DR EPD; Q9P1W8; -. DR jPOST; Q9P1W8; -. DR MassIVE; Q9P1W8; -. DR MaxQB; Q9P1W8; -. DR PaxDb; Q9P1W8; -. DR PeptideAtlas; Q9P1W8; -. DR PRIDE; Q9P1W8; -. DR ProteomicsDB; 83672; -. [Q9P1W8-1] DR ProteomicsDB; 83673; -. [Q9P1W8-2] DR ProteomicsDB; 83674; -. [Q9P1W8-3] DR ProteomicsDB; 83675; -. [Q9P1W8-4] DR ABCD; Q9P1W8; 2 sequenced antibodies. DR Antibodypedia; 6584; 315 antibodies. DR DNASU; 55423; -. DR Ensembl; ENST00000216927; ENSP00000216927; ENSG00000089012. [Q9P1W8-4] DR Ensembl; ENST00000303415; ENSP00000305529; ENSG00000089012. [Q9P1W8-1] DR Ensembl; ENST00000344103; ENSP00000342759; ENSG00000089012. [Q9P1W8-3] DR Ensembl; ENST00000381580; ENSP00000370992; ENSG00000089012. [Q9P1W8-2] DR Ensembl; ENST00000381583; ENSP00000370995; ENSG00000089012. [Q9P1W8-4] DR GeneID; 55423; -. DR KEGG; hsa:55423; -. DR UCSC; uc002wfm.1; human. [Q9P1W8-1] DR CTD; 55423; -. DR DisGeNET; 55423; -. DR EuPathDB; HostDB:ENSG00000089012.14; -. DR GeneCards; SIRPG; -. DR HGNC; HGNC:15757; SIRPG. DR HPA; ENSG00000089012; Group enriched (blood, lymphoid tissue). DR MIM; 605466; gene. DR neXtProt; NX_Q9P1W8; -. DR OpenTargets; ENSG00000089012; -. DR PharmGKB; PA38034; -. DR eggNOG; ENOG502S1XD; Eukaryota. DR GeneTree; ENSGT00960000186656; -. DR HOGENOM; CLU_044430_0_0_1; -. DR InParanoid; Q9P1W8; -. DR KO; K06551; -. DR OMA; WLLVDTP; -. DR OrthoDB; 904196at2759; -. DR PhylomeDB; Q9P1W8; -. DR TreeFam; TF341862; -. DR PathwayCommons; Q9P1W8; -. DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall. DR Reactome; R-HSA-391160; Signal regulatory protein family interactions. DR BioGRID-ORCS; 55423; 2 hits in 863 CRISPR screens. DR EvolutionaryTrace; Q9P1W8; -. DR GeneWiki; SIRPG; -. DR GenomeRNAi; 55423; -. DR Pharos; Q9P1W8; Tbio. DR PRO; PR:Q9P1W8; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q9P1W8; protein. DR Bgee; ENSG00000089012; Expressed in lymph node and 118 other tissues. DR Genevisible; Q9P1W8; HS. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. 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 population proliferation; TAS:ProtInc. 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:0050766; P:positive regulation of phagocytosis; IBA:GO_Central. DR GO; GO:0050870; P:positive regulation of T cell activation; IDA:UniProtKB. DR Gene3D; 2.60.40.10; -; 3. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR003599; Ig_sub. DR InterPro; IPR013106; Ig_V-set. DR Pfam; PF07654; C1-set; 2. DR Pfam; PF07686; V-set; 1. DR SMART; SM00409; IG; 2. DR SMART; SM00407; IGc1; 2. DR SMART; SM00406; IGv; 1. DR SUPFAM; SSF48726; SSF48726; 3. DR PROSITE; PS50835; IG_LIKE; 3. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell adhesion; Disulfide bond; KW Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism; KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. FT SIGNAL 1..28 FT /evidence="ECO:0000255" FT CHAIN 29..387 FT /note="Signal-regulatory protein gamma" FT /id="PRO_0000014957" FT TOPO_DOM 29..360 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 361..383 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 384..387 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 29..137 FT /note="Ig-like V-type" FT DOMAIN 146..245 FT /note="Ig-like C1-type 1" FT DOMAIN 252..340 FT /note="Ig-like C1-type 2" FT CARBOHYD 243 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 268 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 309 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 317 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 53..119 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114, FT ECO:0000269|PubMed:18657508" FT DISULFID 168..226 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT DISULFID 271..329 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114" FT VAR_SEQ 1..33 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11185750" FT /id="VSP_007027" FT VAR_SEQ 144..360 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_007028" FT VAR_SEQ 250..360 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15383453" FT /id="VSP_026960" FT VARIANT 263 FT /note="V -> A (in dbSNP:rs6043409)" FT /evidence="ECO:0000269|PubMed:11185750" FT /id="VAR_049936" FT VARIANT 286 FT /note="S -> L (in dbSNP:rs6034239)" FT /evidence="ECO:0000269|PubMed:11185750" FT /id="VAR_049937" FT STRAND 39..43 FT /evidence="ECO:0000244|PDB:2JJW" FT STRAND 49..51 FT /evidence="ECO:0000244|PDB:2JJW" FT STRAND 54..56 FT /evidence="ECO:0000244|PDB:2JJW" FT STRAND 64..71 FT /evidence="ECO:0000244|PDB:2JJW" FT STRAND 75..82 FT /evidence="ECO:0000244|PDB:2JJW" FT STRAND 88..92 FT /evidence="ECO:0000244|PDB:2JJW" FT STRAND 104..106 FT /evidence="ECO:0000244|PDB:2JJW" FT HELIX 111..113 FT /evidence="ECO:0000244|PDB:2JJW" FT STRAND 115..123 FT /evidence="ECO:0000244|PDB:2JJW" FT STRAND 126..128 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 130..134 FT /evidence="ECO:0000244|PDB:2JJW" FT STRAND 138..142 FT /evidence="ECO:0000244|PDB:2JJW" FT STRAND 150..152 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 163..176 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 179..184 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 192..197 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 205..214 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 223..229 FT /evidence="ECO:0000244|PDB:4I2X" FT TURN 231..235 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 238..243 FT /evidence="ECO:0000244|PDB:4I2X" FT HELIX 244..246 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 253..260 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 262..279 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 281..287 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 297..302 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 308..317 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 326..333 FT /evidence="ECO:0000244|PDB:4I2X" FT STRAND 339..344 FT /evidence="ECO:0000244|PDB:4I2X" 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 //