SIRPG_HUMAN
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 03-AUG-2022, entry version 171.
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 Q9P1W8; P01100: FOS; NbExp=3; IntAct=EBI-1268284, EBI-852851;
CC Q9P1W8; P50440: GATM; NbExp=3; IntAct=EBI-1268284, EBI-2552594;
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}.
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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 AlphaFoldDB; Q9P1W8; -.
DR SMR; Q9P1W8; -.
DR BioGRID; 120664; 3.
DR IntAct; Q9P1W8; 5.
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; 321 antibodies from 33 providers.
DR DNASU; 55423; -.
DR Ensembl; ENST00000216927.4; ENSP00000216927.4; ENSG00000089012.14. [Q9P1W8-4]
DR Ensembl; ENST00000303415.7; ENSP00000305529.3; ENSG00000089012.14. [Q9P1W8-1]
DR Ensembl; ENST00000344103.8; ENSP00000342759.4; ENSG00000089012.14. [Q9P1W8-3]
DR Ensembl; ENST00000381580.5; ENSP00000370992.1; ENSG00000089012.14. [Q9P1W8-2]
DR Ensembl; ENST00000381583.6; ENSP00000370995.2; ENSG00000089012.14. [Q9P1W8-4]
DR GeneID; 55423; -.
DR KEGG; hsa:55423; -.
DR MANE-Select; ENST00000303415.7; ENSP00000305529.3; NM_018556.4; NP_061026.2.
DR UCSC; uc002wfm.1; human. [Q9P1W8-1]
DR CTD; 55423; -.
DR DisGeNET; 55423; -.
DR GeneCards; SIRPG; -.
DR HGNC; HGNC:15757; SIRPG.
DR HPA; ENSG00000089012; Tissue enriched (lymphoid).
DR MIM; 605466; gene.
DR neXtProt; NX_Q9P1W8; -.
DR OpenTargets; ENSG00000089012; -.
DR PharmGKB; PA38034; -.
DR VEuPathDB; HostDB:ENSG00000089012; -.
DR eggNOG; ENOG502S1XD; Eukaryota.
DR GeneTree; ENSGT00960000186656; -.
DR HOGENOM; CLU_044430_0_0_1; -.
DR InParanoid; Q9P1W8; -.
DR OMA; SCESHAF; -.
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 SignaLink; Q9P1W8; -.
DR BioGRID-ORCS; 55423; 14 hits in 1063 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 109 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: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; Reference proteome; Repeat;
KW 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:0007829|PDB:2JJW"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2JJW"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:2JJW"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:2JJW"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:2JJW"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:2JJW"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2JJW"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:2JJW"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:2JJW"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:2JJW"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:2JJW"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 163..176
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 205..214
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 223..229
FT /evidence="ECO:0007829|PDB:4I2X"
FT TURN 231..235
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:4I2X"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 253..260
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 262..279
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 281..287
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 308..317
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:4I2X"
FT STRAND 339..344
FT /evidence="ECO:0007829|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
