RASA2_MOUSE
ID RASA2_MOUSE Reviewed; 847 AA.
AC P58069; G3X918;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Ras GTPase-activating protein 2;
DE AltName: Full=GAP1m;
GN Name=Rasa2;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND MUTAGENESIS OF 626-LYS--ARG-628 AND
RP ARG-628.
RC TISSUE=Brain;
RX PubMed=8702543; DOI=10.1074/jbc.271.31.18838;
RA Fukuda M., Mikoshiba K.;
RT "Structure-function relationships of the mouse Gap1m: determination of the
RT inositol 1,3,4,5-tetrakisphosphate-binding domain.";
RL J. Biol. Chem. 271:18838-18842(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-554, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Testis;
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).
CC -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. Binds
CC inositol tetrakisphosphate (IP4) and phospholipids.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}.
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DR EMBL; AB056433; BAB32975.1; -; mRNA.
DR EMBL; AC144935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161257; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466560; EDL20956.1; -; Genomic_DNA.
DR CCDS; CCDS23416.1; -.
DR RefSeq; NP_444498.2; NM_053268.2.
DR AlphaFoldDB; P58069; -.
DR SMR; P58069; -.
DR BioGRID; 227827; 1.
DR STRING; 10090.ENSMUSP00000034984; -.
DR iPTMnet; P58069; -.
DR PhosphoSitePlus; P58069; -.
DR EPD; P58069; -.
DR MaxQB; P58069; -.
DR PaxDb; P58069; -.
DR PeptideAtlas; P58069; -.
DR PRIDE; P58069; -.
DR ProteomicsDB; 300352; -.
DR Antibodypedia; 18019; 54 antibodies from 19 providers.
DR DNASU; 114713; -.
DR Ensembl; ENSMUST00000034984; ENSMUSP00000034984; ENSMUSG00000032413.
DR GeneID; 114713; -.
DR KEGG; mmu:114713; -.
DR UCSC; uc009rcn.1; mouse.
DR CTD; 5922; -.
DR MGI; MGI:2149960; Rasa2.
DR VEuPathDB; HostDB:ENSMUSG00000032413; -.
DR eggNOG; KOG2059; Eukaryota.
DR GeneTree; ENSGT00940000158201; -.
DR HOGENOM; CLU_008096_1_1_1; -.
DR InParanoid; P58069; -.
DR OMA; MFQEERY; -.
DR OrthoDB; 145372at2759; -.
DR PhylomeDB; P58069; -.
DR TreeFam; TF105302; -.
DR Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR BioGRID-ORCS; 114713; 8 hits in 76 CRISPR screens.
DR ChiTaRS; Rasa2; mouse.
DR PRO; PR:P58069; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P58069; protein.
DR Bgee; ENSMUSG00000032413; Expressed in rostral migratory stream and 246 other tissues.
DR ExpressionAtlas; P58069; baseline and differential.
DR Genevisible; P58069; MM.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR CDD; cd13370; PH_GAP1m_mammal-like; 1.
DR Gene3D; 1.10.506.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR037773; RASA2_PH.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001562; Znf_Btk_motif.
DR PANTHER; PTHR10194; PTHR10194; 1.
DR Pfam; PF00779; BTK; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 2.
DR PRINTS; PR00402; TECBTKDOMAIN.
DR SMART; SM00107; BTK; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00509; RAS_GTPASE_ACTIV_1; 1.
DR PROSITE; PS50018; RAS_GTPASE_ACTIV_2; 1.
DR PROSITE; PS51113; ZF_BTK; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; GTPase activation; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15283"
FT CHAIN 2..847
FT /note="Ras GTPase-activating protein 2"
FT /id="PRO_0000056639"
FT DOMAIN 19..137
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 148..288
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 355..549
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT DOMAIN 603..704
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 706..742
FT /note="Btk-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 714
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 725
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 726
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT BINDING 736
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00432"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q15283"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 626..628
FT /note="KKR->QQQ: No binding to IP4, reduced binding to
FT phospholipids."
FT /evidence="ECO:0000269|PubMed:8702543"
FT MUTAGEN 628
FT /note="R->C: Greatly reduced binding to IP4 and to
FT phospholipids."
FT /evidence="ECO:0000269|PubMed:8702543"
FT CONFLICT 11
FT /note="S -> AS (in Ref. 1; BAB32975)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 847 AA; 96401 MW; 54C6C6A3FAACAB2F CRC64;
MAAAAPAAAA SPEAPAVSGS ADPETGDEDS REVRVLQSLR GRIYEAKNLL PYLGPNKMRD
CFCTINLDQE EVYRTQVVEK SLSPYFSEEF YFEIPRTFQY LSFYVYDKNV LQRDLRIGKV
AIKKEDLCSH SGKETWFSLQ PIDSNSEVQG KVHLELRLNE LITENGTVCQ QLVVHIKACH
GLPLINGQSC DPYATVSLVG PSRNDQKKTK VKKKTSNPQF NEVFYFEVTR SSSYSRKSQF
QVEEEDIEKL EIRIDLWNNE NLVQDVFLGE IKVPVNVLRS DSFHQAWYLL QPRDNGNKSS
KTDDLGSLLL TLCYTEDCVL PSEYYGPLKT LLLKSPDVQP VSASAAYILG EICQDQKDAV
LPLVRLLLHH NKLVPFITAV AELDLKDTPD ANAIFRGNSL ATQCLTEMMK IVGGHYLKVT
LKPVLDEICE SSKSCEIDPV KLKEGDNVEN NKENLYYYVD KVFNTIVGSS VSCPTVMCDI
FYSLRQMAAK KFPNHPHVQY SAVSSFVFLR FFAVAILSPH AFHLRPHYPD TQTVRTLTLI
SKTIQIIGNW GCQSRKKSRF KKSVMCEFLK MFQEERYFTD VKKFLDEISS TETKESSGTS
EPVHLKEGEM YKRAQGRTRI GKKNFKKRWF CLTSRELTYH RQQGKDAIYT IPVKNILAVE
KLEEGSFNKK NMFQVIHTEK TLYIQANNCV EANEWIDVLC RVSRCNHNRL SSFHPSAYLN
GNWLCCQETS ESTPGCKPCT AGIPADIQID IDEDRETERI YSIFTLSLLK LQKMEETCGS
IAVYQGPQKE PGYSKFTIED SVATFKTIQQ IKSTIEKLDE PHEKYRKKRS SSAKYGSKEN
PIVGKIS
