RASA1_BOVIN
ID RASA1_BOVIN Reviewed; 1044 AA.
AC P09851;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 165.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=2842690; DOI=10.1038/335090a0;
RA Vogel U.S., Dixon R.A.F., Schaber M.D., Diehl R.E., Marshall M.S.,
RA Scolnick E.M., Sigal I.S., Gibbs J.B.;
RT "Cloning of bovine GAP and its interaction with oncogenic ras p21.";
RL Nature 335:90-93(1988).
CC -!- FUNCTION: Inhibitory regulator of the Ras-cyclic AMP pathway.
CC Stimulates the GTPase of normal but not oncogenic Ras p21.
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 -!- 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; X12602; CAA31122.1; -; mRNA.
DR PIR; S01966; S01966.
DR RefSeq; NP_776874.1; NM_174449.2.
DR AlphaFoldDB; P09851; -.
DR BMRB; P09851; -.
DR SMR; P09851; -.
DR BioGRID; 159320; 2.
DR STRING; 9913.ENSBTAP00000012583; -.
DR iPTMnet; P09851; -.
DR PaxDb; P09851; -.
DR PRIDE; P09851; -.
DR GeneID; 282032; -.
DR KEGG; bta:282032; -.
DR CTD; 5921; -.
DR eggNOG; KOG3508; Eukaryota.
DR InParanoid; P09851; -.
DR OrthoDB; 145372at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0051020; F:GTPase binding; ISS:AgBase.
DR GO; GO:0005102; F:signaling receptor binding; ISS:AgBase.
DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:AgBase.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISS:AgBase.
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:0043547; P:positive regulation of GTPase activity; IEA:InterPro.
DR GO; GO:0030833; P:regulation of actin filament polymerization; ISS:AgBase.
DR GO; GO:0007165; P:signal transduction; ISS:AgBase.
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; Direct protein sequencing; GTPase activation;
KW Phosphoprotein; Reference proteome; Repeat; SH2 domain; SH3 domain.
FT CHAIN 1..1044
FT /note="Ras GTPase-activating protein 1"
FT /id="PRO_0000056635"
FT DOMAIN 178..269
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 276..338
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 348..438
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 471..574
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 574..687
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REPEAT 646..664
FT REPEAT 665..683
FT DOMAIN 745..939
FT /note="Ras-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00167"
FT REGION 1..160
FT /note="Hydrophobic"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P20936"
FT MOD_RES 612
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P20936"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20936"
SQ SEQUENCE 1044 AA; 115761 MW; 9B15D1223FA5A61A CRC64;
MMAAEAGGEE GGPVTAGAAG GGAAAASGAY PAVCRVKIPA ALPVAAAAPF PGLAEAGVAA
TLGGGAALGS GFLGAGSVAG TPGGVGLSAG GAAAGVAGVA AAAAGAGGEM AFAKGTTSLP
TETFGAGGGF PPLPPPPPQL PTLGAGLGTV DEGDSLDGPE YEEEEVAIPL TAPPTNQWYH
GKLDRTIAEE RLRQAGKSGS YLIRESDRRP GSFVLSFLSQ TNVVNHFRII AMCGDYYIGG
RRFSSLSDLI GYYSHVSCLL KGEKLLYPVA PPEPVEDRRR VRAILPYTKV PDTDEISFLK
GDMFIVHNEL EDGWMWVTNL RTDEQGLIVE DLVEEVGREE DPHEGKIWFH GKISKQEAYN
LLMTVGQACS FLVRPSDNTP GDYSLYFRTS ENIQRFKICP TPNNQFMMGG RYYNSIGDII
DHYRKEQIVE GYYLKEPVPM QDQEQVLNDA VDGKEIYNTI RRKTKDAFYK NIVKKGYLLK
KGKGKRWKNL YFILEGSDAQ LIYFESEKRA TKPKGLIDLS VCSVYVVHDS LFGRPNCFQI
VVQHFSEEHY IFYFAGETPE QAEDWMKGLQ AFCNLRKSSP GTSNKRLRQV SSLILHIEEA
HKLPVKHFTN PYCNIYLNSV QVAKTHAREG QNPVWSEEFV FDDLPPDINR FEITLSNKTK
KSKDPDILFM RCQLSRLQKG HATDEWFLLS SHIPLKGIEP GSLRVRARYS MEKIMPEEEY
SEFKELILQK ELHVVYALSH VCGQDRTLLA SILLKIFLHE KLESLLLCTL NDREISMEDE
ATTLFRATTL ASTLMEQSMK ATATQFVHHA LKDSILRIME SKQSCELSPS KLEKNEDVNT
NLAHLLNILS ELVEKIFMAS EILPPTLRYI YGCLQKSVQH KWPTNTTMRT RVVSGFVFLR
LICPAILNPR MFNIISDSPS PIAARTLTLV AKSVQNLANL VEFGAKEPYM EGVNPFIKSN
KHRMIMFLDE LGNVPELPDT TEHSRTDLCR DLAALHEICV AHSDELRTLS NERGAQQHVL
KKLLAITELL QQKQNQYTKT NDVR
