RASA1_RAT
ID RASA1_RAT Reviewed; 1038 AA.
AC P50904;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 163.
DE RecName: Full=Ras GTPase-activating protein 1;
DE Short=GAP;
DE Short=GTPase-activating protein;
DE Short=RasGAP;
DE AltName: Full=Ras p21 protein activator;
DE AltName: Full=p120GAP;
GN Name=Rasa1; Synonyms=Rasa;
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.
RX PubMed=8262392; DOI=10.1016/0378-1119(93)90114-i;
RA Davis M.M., Catino J.J., Satoh T., Kaziro Y., Perkins L.M.;
RT "Sequence of the cDNA encoding Ras GTPase-activating protein from rat.";
RL Gene 134:305-306(1993).
CC -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway.
CC Stimulates the GTPase of normal but not oncogenic Ras p21 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SQSTM1. Interacts with SPSB1; the interaction
CC does not promote degradation. Interacts with CAV2 (tyrosine
CC phosphorylated form). Directly interacts with NCK1. Interacts with
CC PDGFRB (tyrosine phosphorylated). Interacts (via SH2 domain) with the
CC 'Tyr-9' phosphorylated form of PDPK1. Interacts with tyrosine-
CC phosphorylated EPHB4. {ECO:0000250|UniProtKB:P20936}.
CC -!- INTERACTION:
CC P50904; Q13480: GAB1; Xeno; NbExp=2; IntAct=EBI-5747849, EBI-517684;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Phosphorylated by SRC and LCK. The phosphorylation SRC inhibits
CC its ability to stimulate the Ras-GTPase activity, whereas
CC phosphorylation by LCK does not display any effect on stimulation
CC activity (By similarity). {ECO:0000250}.
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DR EMBL; L13151; AAA16319.1; -; Unassigned_DNA.
DR PIR; JT0663; JT0663.
DR RefSeq; NP_037267.1; NM_013135.1.
DR AlphaFoldDB; P50904; -.
DR BMRB; P50904; -.
DR SMR; P50904; -.
DR BioGRID; 247705; 3.
DR CORUM; P50904; -.
DR IntAct; P50904; 21.
DR MINT; P50904; -.
DR STRING; 10116.ENSRNOP00000047300; -.
DR iPTMnet; P50904; -.
DR PhosphoSitePlus; P50904; -.
DR jPOST; P50904; -.
DR PaxDb; P50904; -.
DR PRIDE; P50904; -.
DR GeneID; 25676; -.
DR KEGG; rno:25676; -.
DR UCSC; RGD:3537; rat.
DR CTD; 5921; -.
DR RGD; 3537; Rasa1.
DR eggNOG; KOG3508; Eukaryota.
DR InParanoid; P50904; -.
DR OrthoDB; 145372at2759; -.
DR PhylomeDB; P50904; -.
DR Reactome; R-RNO-186763; Downstream signal transduction.
DR Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
DR Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-RNO-5658442; Regulation of RAS by GAPs.
DR Reactome; R-RNO-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR PRO; PR:P50904; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IDA:RGD.
DR GO; GO:0051020; F:GTPase binding; ISO:RGD.
DR GO; GO:0001784; F:phosphotyrosine residue binding; ISO:RGD.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IDA:RGD.
DR GO; GO:0043422; F:protein kinase B binding; IPI:RGD.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:RGD.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:RGD.
DR GO; GO:0048514; P:blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IDA:RGD.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEP:RGD.
DR GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:RGD.
DR GO; GO:0030539; P:male genitalia development; IEP:RGD.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IEA:InterPro.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:RGD.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IMP:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISS:UniProtKB.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR CDD; cd10354; SH2_Cterm_RasGAP; 1.
DR CDD; cd10353; SH2_Nterm_RasGAP; 1.
DR CDD; cd11788; SH3_RasGAP; 1.
DR Gene3D; 1.10.506.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR028554; p120-RasGAP.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR039360; Ras_GTPase.
DR InterPro; IPR035842; RasGAP_C_SH2.
DR InterPro; IPR023152; RasGAP_CS.
DR InterPro; IPR001936; RasGAP_dom.
DR InterPro; IPR035841; RasGAP_N_SH2.
DR InterPro; IPR035652; RasGAP_SH3.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR10194; PTHR10194; 2.
DR PANTHER; PTHR10194:SF19; PTHR10194:SF19; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00616; RasGAP; 1.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00323; RasGAP; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
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.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; GTPase activation; Phosphoprotein;
KW Reference proteome; Repeat; SH2 domain; SH3 domain.
FT CHAIN 1..1038
FT /note="Ras GTPase-activating protein 1"
FT /id="PRO_0000056637"
FT DOMAIN 172..263
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 270..332
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 342..432
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 465..568
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 568..681
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 739..933
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..137
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P20936"
FT MOD_RES 606
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20936"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20936"
SQ SEQUENCE 1038 AA; 115440 MW; 242EE47131C1811E CRC64;
MMAAEAGSEE GGPATAGTGG AAATGSSAYP AACRVKLPAA PPMAVAPCPG LADTDLAAAL
GGGAASGSGF LGTGPVSGVL GGAALTGGAA AGVAGAAAAG PAGDIALTKG TLSLPAETLG
PGGGFPPLPP PPLLPPLGSG LGTVDEGDSL DGPEYEEEEV AIPLTAPPTN QWYHGKLDRT
IAEERLRQAG KSGSYLIRES DRRPGSFVLS FLSQTNVVNH FRIIAMCGDY YIGGRRFSSL
SDLIGYYSHV SCLLKGEKLL YPVAPPEPVE DRRRVRAILP YTKVPDTDEI SFLKGDMFIV
HNELEDGWMW VTNLRTDEQG LIVEDLVEEV GREEDPHEGK IWFHGKISKQ EAYNLLMTVG
QVCSFLVRPS DNTPGDYSLY FRTNENIQRF KICPTPNNQF MMGGRYYNSI GDIIDHYRKE
QIVEGYYLKE PVPMQDQGQV LNDTVDGKEI YNTIRRKTKD AFYKNIVKKG YLLKKGKGKR
WKNLYFILEG SDAQLIYFES EKRATKPKGL IDLSVCSVYV VHDSLFGRPN CFQIVVQHFS
EEHYIFYFAG ETPEQAEDWM KGLQAFCSLR KSSPGTSNKR LRQVSSLVLH IEEAHKLPVK
HFTNPYCNIY LNSVQVAKTH AREGQNPVWS EEFVFDDLPP DINRFEITLS NKTKKSKDPD
ILFMRCQLSR LQKGHATDEW FLLSSHIPLK GIEPGSLRVR ARYSMEKIMP EEEYSEFKEL
ILQKELHVVY ALSHVCGQDR TLLASILLKI FLHEKLESLL LCTLNDREIS MEDEATTLFR
ATTLASTLME QYMKATATQF VHHALKDSIL KIMESKQSCE LSPSKLEKNE DVNTNLAHLL
SILSELVEKI FMASEILPPT LRYIYGCLQK SVQHKWPTNN TMRTRVVSGF VFLRLICPAI
LNPRMFNIIS DSPSPIAART LTLVAKSVQN LANLVEFGAK EPYMEGVNPF IKSNKHRMIM
FLDELGNVPE LPDTTEHSRT DLSRDLAALH EICVAHSDEL RTLSNERGVQ QHVLKKLLAI
TELLQQKQNQ YTKTNDVR
