ID   RASA2_RAT               Reviewed;         847 AA.
AC   Q63713;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=Ras GTPase-activating protein 2;
DE   AltName: Full=GAP1m;
GN   Name=Rasa2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=7935405; DOI=10.1128/mcb.14.10.6879-6885.1994;
RA   Maekawa M., Li S., Iwamatsu A., Morishita T., Yokota K., Imai Y.,
RA   Kohsaka S., Nakamura S., Hattori S.;
RT   "A novel mammalian Ras GTPase-activating protein which has phospholipid-
RT   binding and Btk homology regions.";
RL   Mol. Cell. Biol. 14:6879-6885(1994).
CC   -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway. May bind
CC       inositol tetrakisphosphate (IP4) and phospholipids.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Higher expression in brain,
CC       placenta, and kidney.
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DR   EMBL; D30734; BAA06398.1; -; mRNA.
DR   PIR; A56039; A56039.
DR   RefSeq; NP_001099194.1; NM_001105724.1.
DR   AlphaFoldDB; Q63713; -.
DR   SMR; Q63713; -.
DR   STRING; 10116.ENSRNOP00000016327; -.
DR   PaxDb; Q63713; -.
DR   Ensembl; ENSRNOT00000016327; ENSRNOP00000016327; ENSRNOG00000011909.
DR   GeneID; 25597; -.
DR   KEGG; rno:25597; -.
DR   UCSC; RGD:3538; rat.
DR   CTD; 5922; -.
DR   RGD; 3538; Rasa2.
DR   eggNOG; KOG2059; Eukaryota.
DR   GeneTree; ENSGT00940000158201; -.
DR   HOGENOM; CLU_008096_1_1_1; -.
DR   InParanoid; Q63713; -.
DR   OMA; MFQEERY; -.
DR   OrthoDB; 145372at2759; -.
DR   PhylomeDB; Q63713; -.
DR   TreeFam; TF105302; -.
DR   Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR   PRO; PR:Q63713; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000011909; Expressed in thymus and 19 other tissues.
DR   Genevisible; Q63713; RN.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
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   2: Evidence at transcript 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_0000056640"
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:0000250|UniProtKB:P58069"
SQ   SEQUENCE   847 AA;  96374 MW;  A7E88AF2DA74516B CRC64;
     MAAAAPAAAA LTEAPAVPGT AEPETGDEDS REVRVLQSLR GRIYEAKNLL PYLGPNKMRD
     CFCTINLDQE EVYRTQVVEK SLSPYFSEEF YFEIPRTFQY LSFYVYDKNV LQRDLRIGKV
     AIKKEDLCSH SGKETWFSLQ PIDSNSEVQG KVHLELKLNE LITENGTVCQ QLVVHIKACH
     GLPLINGQSC DPYATVSLVG PSRNDQKKTK VKKKTSNPQF NEVFYFEVTR SSSYTRKSQF
     QVEEEDIEKL EIRIDLWNNE NLVQDVFLGE IKVPVNVLRN DSSHQAWYLL QPRDNGNKSS
     KPDDLGSLLL TLCYTEDYVL PSEYYGPLKA LLLKSPDVQP VSASAAYILG EICRDQKDAV
     LPLVRLLLHH NKLVPFITAV ADLDLKDTQD ANAIFRGNSL ATQCLTEMMK IVGGHYLKVT
     LKPVLDEICE SSKSCEIDPV KLKEGDNVES NKENLYYYVD KVFSAIVGSS VSCPTVMCDI
     FYSLRQMAAK RFPNNPHVQY SAVSSFVFLR FFAVAILSPH AFHLRPHYPD TQTVRTLTLI
     SKTIQIIGNW GCQSRRKSRF KKSVMCEFLK MFQEERYFTD VKKFLDEISS TETKESSGTS
     EPVHLKEGEM YKRAQGRTRI GKKNFKKRWF CLTSKELTYH KQQGKDAIYT IPVKNILAVE
     KLEESSFNKK NMFQVIHTEK TLYIQANNCV EANEWIDMLC RVSRCNHNRL SSFHPSAYLN
     GNWLCCQETS EGTPGCKPCT AGIPADIQID IDEDRETERI YSVFTLSLLK LQKMEEACGS
     IAVYQGPQKE PGYSKFTIED SVATFKTIQQ IKSTIEKLDE PHEKYRKKRS SSAKYGSKEN
     PIVGKIS