ID A0A0A6YVS6_MOUSE Unreviewed; 1281 AA.
AC A0A0A6YVS6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 2.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Synaptic Ras GTPase activating protein 1 homolog (rat) {ECO:0000313|Ensembl:ENSMUSP00000141245.3};
DE Flags: Fragment;
GN Name=Syngap1 {ECO:0000313|Ensembl:ENSMUSP00000141245.3,
GN ECO:0000313|MGI:MGI:3039785};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000141245.3, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0007829|PubMed:16452087}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [2] {ECO:0007829|PubMed:18034455}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000141245.3, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141245.3,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5] {ECO:0000313|Ensembl:ENSMUSP00000141245.3}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000141245.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR ProteomicsDB; 320362; -.
DR Antibodypedia; 29204; 296 antibodies from 35 providers.
DR Ensembl; ENSMUST00000193200.6; ENSMUSP00000141245.3; ENSMUSG00000067629.14.
DR AGR; MGI:3039785; -.
DR MGI; MGI:3039785; Syngap1.
DR VEuPathDB; HostDB:ENSMUSG00000067629; -.
DR GeneTree; ENSGT00940000158438; -.
DR HOGENOM; CLU_001727_1_0_1; -.
DR ChiTaRS; Syngap1; mouse.
DR Proteomes; UP000000589; Chromosome 17.
DR Bgee; ENSMUSG00000067629; Expressed in primary visual cortex and 73 other cell types or tissues.
DR ExpressionAtlas; A0A0A6YVS6; baseline and differential.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR CDD; cd04013; C2_SynGAP_like; 1.
DR CDD; cd13375; PH_SynGAP; 1.
DR CDD; cd05136; RasGAP_DAB2IP; 1.
DR CDD; cd22265; UDM1_RNF168; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR021887; DAB2P_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR037779; SynGAP_PH.
DR PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
DR PANTHER; PTHR10194:SF25; RAS_RAP GTPASE-ACTIVATING PROTEIN SYNGAP; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12004; DAB2P_C; 1.
DR Pfam; PF00616; RasGAP; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Proteomics identification {ECO:0007829|EPD:A0A0A6YVS6,
KW ECO:0007829|MaxQB:A0A0A6YVS6};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 202..236
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 227..348
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 428..620
FT /note="Ras-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50018"
FT REGION 354..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1177..1243
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 710..730
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1021
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1049..1097
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1114..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000141245.3"
SQ SEQUENCE 1281 AA; 141895 MW; 9BF4759F1DC8CA6E CRC64;
XSYAPFRDVR GPPMHRTQYV HSPYDRPGWN PRFCIISGNQ LLMLDEDEIH PLLIRDRRSE
SSRNKLLRRT VSVPVEGRPH GEHEYHLGRS RRKSVPGGKQ YSMEAAPAAP FRPSQGFLSR
RLKSSIKRTK SQPKLDRTSS FRQILPRFRS ADHDRARLMQ SFKESHSHES LLSPSSAAEA
LELNLDEDSI IKPVHSSILG QEFCFEVTTS SGTKCFACRS AAERDKWIEN LQRAVKPNKD
NSRRVDNVLK LWIIEARELP PKKRYYCELC LDDMLYARTT SKPRSASGDT VFWGEHFEFN
NLPAVRALRL HLYRDSDKKR KKDKAGYVGL VTVPVATLAG RHFTEQWYPV TLPTGSGGSG
GMGSGGGGGS GGGSGGKGKG GCPAVRLKAR YQTMSILPME LYKEFAEYVT NHYRMLCAVL
EPALNVKGKE EVASALVHIL QSTGKAKDFL SDMAMSEVDR FMEREHLIFR ENTLATKAIE
EYMRLIGQKY LKDAIGEFIR ALYESEENCE VDPIKCTASS LAEHQANLRM CCELALCKVV
NSHCVFPREL KEVFASWRLR CAERGREDIA DRLISASLFL RFLCPAIMSP SLFGLMQEYP
DEQTSRTLTL IAKVIQNLAN FSKFTSKEDF LGFMNEFLEL EWGSMQQFLY EISNLDTLTN
SSSFEGYIDL GRELSTLHAL LWEVLPQLSK EALLKLGPLP RLLNDISTAL RNPNIQRQPS
RQSERTRSQP MVLRGPSAEM QGYMMRDLNS SIDLQSFMAR GLNSSMDMAR LPSPTKEKPP
PPPPGGGKDL FYVSRPPLAR SSPAYCTSSS DITEPEQKML SVNKSVSMLD LQGDGPGGRL
NSSSVSNLAA VGDLLHSSQA SLTAALGLRP APAGRLSQGS GSSITAAGMR LSQMGVTTDG
VPAQQLRIPL SFQNPLFHMA ADGPGPPAGH GGSSGHGPPS SHHHHHHHHH HRGGEPPGDT
FAPFHGYSKS EDLSSGVPKP PAASILHSHS YSDEFGPSGT DFTRRQLSLQ DSLQHMLSPP
QITIGPQRPA PSGPGGGSGG GSGGGQPPPL QRGKSQQLTV SAAQKPRPSS GNLLQSPEPS
YGPARPRQQS LSKEGSIGGS GGSGGGGGGG LKPSITKQHS QTPSTLNPTM PASERTVAWV
SNMPHLSADI ESAHIEREEY KLKEYSKSMD ESRLDRVKEY EEEIHSLKER LHMSNRKLEE
YERRLLSQEE QTSKILMQYQ ARLEQSEKRL RQQQVEKDSQ IKSIIGRLML VEEELRRDHP
AMAEPLPEPK KRLLDAQLLI R
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