Signal-regulatory protein gamma (SIRP-gamma) (CD172 antigen-like family member B) (Signal-regulatory protein beta-2) (SIRP-b2) (SIRP-beta-2) (CD antigen CD172g)

 SIRPG_HUMAN             Reviewed;         387 AA.
 Q9P1W8; B1AKP6; Q5D051; Q5JV25; Q5MKL4; Q8WWA5; Q9NQK8;
 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
 23-JAN-2007, sequence version 3.
 07-APR-2021, entry version 166.
 RecName: Full=Signal-regulatory protein gamma;
          Short=SIRP-gamma;
 AltName: Full=CD172 antigen-like family member B;
 AltName: Full=Signal-regulatory protein beta-2;
          Short=SIRP-b2;
          Short=SIRP-beta-2;
 AltName: CD_antigen=CD172g;
 Flags: Precursor;
 Name=SIRPG; Synonyms=SIRPB2;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
 Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
 Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANTS
 ALA-263 AND LEU-286.
 TISSUE=Placenta;
 PubMed=11185750; DOI=10.1007/s100380070013;
 Ichigotani Y., Matsuda S., Machida K., Oshima K., Iwamoto T., Yamaki K.,
 Hayakawa T., Hamaguchi M.;
 "Molecular cloning of a novel human gene (SIRP-B2) which encodes a new
 member of the SIRP/SHPS-1 protein family.";
 J. Hum. Genet. 45:378-382(2000).
 [2]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, INTERACTION WITH CD47,
 SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
 TISSUE=T-cell;
 PubMed=15383453; DOI=10.1182/blood-2004-07-2823;
 Piccio L., Vermi W., Boles K.S., Fuchs A., Strader C.A., Facchetti F.,
 Cella M., Colonna M.;
 "Adhesion of human T cells to antigen-presenting cells through SIRPbeta2-
 CD47 interaction costimulates T-cell proliferation.";
 Blood 105:2421-2427(2005).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=11780052; DOI=10.1038/414865a;
 Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
 Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
 Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
 Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
 Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
 Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
 Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
 Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
 Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
 Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
 Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
 Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
 Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
 Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
 Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
 Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
 Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
 Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
 Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
 Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
 Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
 Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
 Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
 "The DNA sequence and comparative analysis of human chromosome 20.";
 Nature 414:865-871(2001).
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
 Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
 Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
 Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
 Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
 Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
 Hunkapiller M.W., Myers E.W., Venter J.C.;
 Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
 [5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
 TISSUE=Lung, and Ovary;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA project:
 the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [6]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-243.
 TISSUE=Leukemic T-cell;
 PubMed=19349973; DOI=10.1038/nbt.1532;
 Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
 Schiess R., Aebersold R., Watts J.D.;
 "Mass-spectrometric identification and relative quantification of N-linked
 cell surface glycoproteins.";
 Nat. Biotechnol. 27:378-386(2009).
 [7]
 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 29-147, AND DISULFIDE BOND.
 PubMed=18657508; DOI=10.1016/j.molcel.2008.05.026;
 Hatherley D., Graham S.C., Turner J., Harlos K., Stuart D.I., Barclay A.N.;
 "Paired receptor specificity explained by structures of signal regulatory
 proteins alone and complexed with CD47.";
 Mol. Cell 31:266-277(2008).
 -!- FUNCTION: Probable immunoglobulin-like cell surface receptor. On
     binding with CD47, mediates cell-cell adhesion. Engagement on T-cells
     by CD47 on antigen-presenting cells results in enhanced antigen-
     specific T-cell proliferation and costimulates T-cell activation.
     {ECO:0000269|PubMed:15383453}.
 -!- SUBUNIT: Interacts with CD47. {ECO:0000269|PubMed:15383453}.
 -!- INTERACTION:
     Q9P1W8; Q08722: CD47; NbExp=2; IntAct=EBI-1268284, EBI-1268321;
     Q9P1W8; P01100: FOS; NbExp=3; IntAct=EBI-1268284, EBI-852851;
     Q9P1W8; P50440: GATM; NbExp=3; IntAct=EBI-1268284, EBI-2552594;
 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:15383453}; Single-
     pass type I membrane protein {ECO:0000269|PubMed:15383453}.
 -!- ALTERNATIVE PRODUCTS:
     Event=Alternative splicing; Named isoforms=4;
     Name=1;
       IsoId=Q9P1W8-1; Sequence=Displayed;
     Name=2;
       IsoId=Q9P1W8-2; Sequence=VSP_007027;
     Name=3;
       IsoId=Q9P1W8-3; Sequence=VSP_007028;
     Name=4;
       IsoId=Q9P1W8-4; Sequence=VSP_026960;
 -!- TISSUE SPECIFICITY: Detected in liver, and at very low levels in brain,
     heart, lung, pancreas, kidney, placenta and skeletal muscle. Expressed
     on CD4+ T-cells, CD8+ T-cells, CD56-bright natural killer (NK) cells,
     CD20+ cells, and all activated NK cells. Mainly present in the
     paracortical T-cell area of lymph nodes, with only sparse positive
     cells in the mantle and in the germinal center of B-cell follicles. In
     the thymus, primarily expressed in the medulla on mature T-lymphocytes
     that have undergone thymic selection. {ECO:0000269|PubMed:11185750,
     ECO:0000269|PubMed:15383453}.
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 EMBL; AB042624; BAA95692.1; -; mRNA.
 EMBL; AY748247; AAV88530.1; -; mRNA.
 EMBL; AY748248; AAV88531.1; -; mRNA.
 EMBL; AL109809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; AL138804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; CH471133; EAX10616.1; -; Genomic_DNA.
 EMBL; BC020629; AAH20629.2; -; mRNA.
 EMBL; BC064532; AAH64532.1; -; mRNA.
 CCDS; CCDS13020.2; -. [Q9P1W8-1]
 CCDS; CCDS13021.2; -. [Q9P1W8-3]
 CCDS; CCDS33434.1; -. [Q9P1W8-4]
 RefSeq; NP_001034597.1; NM_001039508.1. [Q9P1W8-4]
 RefSeq; NP_061026.2; NM_018556.3. [Q9P1W8-1]
 RefSeq; NP_543006.2; NM_080816.2. [Q9P1W8-3]
 RefSeq; XP_011527588.1; XM_011529286.2. [Q9P1W8-2]
 PDB; 2JJW; X-ray; 1.70 A; A=29-147.
 PDB; 4I2X; X-ray; 2.48 A; E/F=29-347.
 PDBsum; 2JJW; -.
 PDBsum; 4I2X; -.
 SMR; Q9P1W8; -.
 BioGRID; 120664; 3.
 IntAct; Q9P1W8; 5.
 STRING; 9606.ENSP00000305529; -.
 GlyGen; Q9P1W8; 4 sites.
 iPTMnet; Q9P1W8; -.
 PhosphoSitePlus; Q9P1W8; -.
 BioMuta; SIRPG; -.
 DMDM; 124053651; -.
 EPD; Q9P1W8; -.
 jPOST; Q9P1W8; -.
 MassIVE; Q9P1W8; -.
 MaxQB; Q9P1W8; -.
 PaxDb; Q9P1W8; -.
 PeptideAtlas; Q9P1W8; -.
 PRIDE; Q9P1W8; -.
 ProteomicsDB; 83672; -. [Q9P1W8-1]
 ProteomicsDB; 83673; -. [Q9P1W8-2]
 ProteomicsDB; 83674; -. [Q9P1W8-3]
 ProteomicsDB; 83675; -. [Q9P1W8-4]
 ABCD; Q9P1W8; 2 sequenced antibodies.
 Antibodypedia; 6584; 326 antibodies.
 DNASU; 55423; -.
 Ensembl; ENST00000216927; ENSP00000216927; ENSG00000089012. [Q9P1W8-4]
 Ensembl; ENST00000303415; ENSP00000305529; ENSG00000089012. [Q9P1W8-1]
 Ensembl; ENST00000344103; ENSP00000342759; ENSG00000089012. [Q9P1W8-3]
 Ensembl; ENST00000381580; ENSP00000370992; ENSG00000089012. [Q9P1W8-2]
 Ensembl; ENST00000381583; ENSP00000370995; ENSG00000089012. [Q9P1W8-4]
 GeneID; 55423; -.
 KEGG; hsa:55423; -.
 UCSC; uc002wfm.1; human. [Q9P1W8-1]
 CTD; 55423; -.
 DisGeNET; 55423; -.
 GeneCards; SIRPG; -.
 HGNC; HGNC:15757; SIRPG.
 HPA; ENSG00000089012; Group enriched (blood, lymphoid tissue).
 MIM; 605466; gene.
 neXtProt; NX_Q9P1W8; -.
 OpenTargets; ENSG00000089012; -.
 PharmGKB; PA38034; -.
 VEuPathDB; HostDB:ENSG00000089012.14; -.
 eggNOG; ENOG502S1XD; Eukaryota.
 GeneTree; ENSGT00960000186656; -.
 HOGENOM; CLU_044430_0_0_1; -.
 InParanoid; Q9P1W8; -.
 OMA; WLLVDTP; -.
 OrthoDB; 904196at2759; -.
 PhylomeDB; Q9P1W8; -.
 TreeFam; TF341862; -.
 PathwayCommons; Q9P1W8; -.
 Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
 Reactome; R-HSA-391160; Signal regulatory protein family interactions.
 BioGRID-ORCS; 55423; 7 hits in 979 CRISPR screens.
 EvolutionaryTrace; Q9P1W8; -.
 GeneWiki; SIRPG; -.
 GenomeRNAi; 55423; -.
 Pharos; Q9P1W8; Tbio.
 PRO; PR:Q9P1W8; -.
 Proteomes; UP000005640; Chromosome 20.
 RNAct; Q9P1W8; protein.
 Bgee; ENSG00000089012; Expressed in lymph node and 118 other tissues.
 Genevisible; Q9P1W8; HS.
 GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
 GO; GO:0016020; C:membrane; IDA:UniProtKB.
 GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
 GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
 GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
 GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
 GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
 GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
 GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:UniProtKB.
 GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central.
 GO; GO:0050870; P:positive regulation of T cell activation; IDA:UniProtKB.
 Gene3D; 2.60.40.10; -; 3.
 InterPro; IPR007110; Ig-like_dom.
 InterPro; IPR036179; Ig-like_dom_sf.
 InterPro; IPR013783; Ig-like_fold.
 InterPro; IPR003597; Ig_C1-set.
 InterPro; IPR003599; Ig_sub.
 InterPro; IPR013106; Ig_V-set.
 Pfam; PF07654; C1-set; 2.
 Pfam; PF07686; V-set; 1.
 SMART; SM00409; IG; 2.
 SMART; SM00407; IGc1; 2.
 SMART; SM00406; IGv; 1.
 SUPFAM; SSF48726; SSF48726; 3.
 PROSITE; PS50835; IG_LIKE; 3.
 1: Evidence at protein level;
 3D-structure; Alternative splicing; Cell adhesion; Disulfide bond;
 Glycoprotein; Immunoglobulin domain; Membrane; Reference proteome; Repeat;
 Signal; Transmembrane; Transmembrane helix.
 SIGNAL          1..28
                 /evidence="ECO:0000255"
 CHAIN           29..387
                 /note="Signal-regulatory protein gamma"
                 /id="PRO_0000014957"
 TOPO_DOM        29..360
                 /note="Extracellular"
                 /evidence="ECO:0000255"
 TRANSMEM        361..383
                 /note="Helical"
                 /evidence="ECO:0000255"
 TOPO_DOM        384..387
                 /note="Cytoplasmic"
                 /evidence="ECO:0000255"
 DOMAIN          29..137
                 /note="Ig-like V-type"
 DOMAIN          146..245
                 /note="Ig-like C1-type 1"
 DOMAIN          252..340
                 /note="Ig-like C1-type 2"
 CARBOHYD        243
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000269|PubMed:19349973"
 CARBOHYD        268
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        309
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        317
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 DISULFID        53..119
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
                 ECO:0000269|PubMed:18657508"
 DISULFID        168..226
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
 DISULFID        271..329
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
 VAR_SEQ         1..33
                 /note="Missing (in isoform 2)"
                 /evidence="ECO:0000303|PubMed:11185750"
                 /id="VSP_007027"
 VAR_SEQ         144..360
                 /note="Missing (in isoform 3)"
                 /evidence="ECO:0000303|PubMed:15489334"
                 /id="VSP_007028"
 VAR_SEQ         250..360
                 /note="Missing (in isoform 4)"
                 /evidence="ECO:0000303|PubMed:15383453"
                 /id="VSP_026960"
 VARIANT         263
                 /note="V -> A (in dbSNP:rs6043409)"
                 /evidence="ECO:0000269|PubMed:11185750"
                 /id="VAR_049936"
 VARIANT         286
                 /note="S -> L (in dbSNP:rs6034239)"
                 /evidence="ECO:0000269|PubMed:11185750"
                 /id="VAR_049937"
 STRAND          39..43
                 /evidence="ECO:0007744|PDB:2JJW"
 STRAND          49..51
                 /evidence="ECO:0007744|PDB:2JJW"
 STRAND          54..56
                 /evidence="ECO:0007744|PDB:2JJW"
 STRAND          64..71
                 /evidence="ECO:0007744|PDB:2JJW"
 STRAND          75..82
                 /evidence="ECO:0007744|PDB:2JJW"
 STRAND          88..92
                 /evidence="ECO:0007744|PDB:2JJW"
 STRAND          104..106
                 /evidence="ECO:0007744|PDB:2JJW"
 HELIX           111..113
                 /evidence="ECO:0007744|PDB:2JJW"
 STRAND          115..123
                 /evidence="ECO:0007744|PDB:2JJW"
 STRAND          126..128
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          130..134
                 /evidence="ECO:0007744|PDB:2JJW"
 STRAND          138..142
                 /evidence="ECO:0007744|PDB:2JJW"
 STRAND          150..152
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          163..176
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          179..184
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          192..197
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          205..214
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          223..229
                 /evidence="ECO:0007744|PDB:4I2X"
 TURN            231..235
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          238..243
                 /evidence="ECO:0007744|PDB:4I2X"
 HELIX           244..246
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          253..260
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          262..279
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          281..287
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          297..302
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          308..317
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          326..333
                 /evidence="ECO:0007744|PDB:4I2X"
 STRAND          339..344
                 /evidence="ECO:0007744|PDB:4I2X"
 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

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