ID   E9PYG6_MOUSE            Unreviewed;      1038 AA.
AC   E9PYG6;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   SubName: Full=RAS p21 protein activator 1 {ECO:0000313|Ensembl:ENSMUSP00000105179.3};
GN   Name=Rasa1 {ECO:0000313|Ensembl:ENSMUSP00000105179.3,
GN   ECO:0000313|MGI:MGI:97860};
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:ENSMUSP00000105179.3, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000105179.3, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000105179.3,
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   [2] {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   [3] {ECO:0000313|Ensembl:ENSMUSP00000105179.3}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000105179.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; NP_663427.2; NM_145452.3.
DR   AlphaFoldDB; E9PYG6; -.
DR   SMR; E9PYG6; -.
DR   CORUM; E9PYG6; -.
DR   IntAct; E9PYG6; 1.
DR   MINT; E9PYG6; -.
DR   STRING; 10090.ENSMUSP00000105179; -.
DR   iPTMnet; E9PYG6; -.
DR   PhosphoSitePlus; E9PYG6; -.
DR   SwissPalm; E9PYG6; -.
DR   EPD; E9PYG6; -.
DR   MaxQB; E9PYG6; -.
DR   PaxDb; 10090-ENSMUSP00000105179; -.
DR   PeptideAtlas; E9PYG6; -.
DR   ProteomicsDB; 344913; -.
DR   Antibodypedia; 24766; 597 antibodies from 36 providers.
DR   DNASU; 218397; -.
DR   Ensembl; ENSMUST00000109552.3; ENSMUSP00000105179.3; ENSMUSG00000021549.15.
DR   GeneID; 218397; -.
DR   KEGG; mmu:218397; -.
DR   UCSC; uc007rix.2; mouse.
DR   AGR; MGI:97860; -.
DR   CTD; 5921; -.
DR   MGI; MGI:97860; Rasa1.
DR   VEuPathDB; HostDB:ENSMUSG00000021549; -.
DR   eggNOG; KOG3508; Eukaryota.
DR   GeneTree; ENSGT00940000155846; -.
DR   HOGENOM; CLU_010968_1_0_1; -.
DR   InParanoid; E9PYG6; -.
DR   OMA; ICGCLQR; -.
DR   OrthoDB; 22721at2759; -.
DR   PhylomeDB; E9PYG6; -.
DR   TreeFam; TF105301; -.
DR   Reactome; R-MMU-186763; Downstream signal transduction.
DR   Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
DR   Reactome; R-MMU-5218921; VEGFR2 mediated cell proliferation.
DR   Reactome; R-MMU-5658442; Regulation of RAS by GAPs.
DR   Reactome; R-MMU-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR   BioGRID-ORCS; 218397; 2 hits in 80 CRISPR screens.
DR   ChiTaRS; Rasa1; mouse.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; E9PYG6; Protein.
DR   Bgee; ENSMUSG00000021549; Expressed in rostral migratory stream and 263 other cell types or tissues.
DR   ExpressionAtlas; E9PYG6; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR   GO; GO:0001726; C:ruffle; IDA:MGI.
DR   GO; GO:0005096; F:GTPase activator activity; ISO:MGI.
DR   GO; GO:0051020; F:GTPase binding; ISO:MGI.
DR   GO; GO:0019900; F:kinase binding; ISO:MGI.
DR   GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
DR   GO; GO:0005161; F:platelet-derived growth factor receptor binding; ISO:MGI.
DR   GO; GO:0043422; F:protein kinase B binding; ISO:MGI.
DR   GO; GO:1990782; F:protein tyrosine kinase binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:MGI.
DR   GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0048514; P:blood vessel morphogenesis; ISO:MGI.
DR   GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:MGI.
DR   GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0007162; P:negative regulation of cell adhesion; ISO:MGI.
DR   GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISO:MGI.
DR   GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR   GO; GO:0046326; P:positive regulation of glucose import; ISO:MGI.
DR   GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR   GO; GO:0030833; P:regulation of actin filament polymerization; ISO:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR   GO; GO:0007165; P:signal transduction; ISO:MGI.
DR   CDD; cd08400; C2_Ras_p21A1; 1.
DR   CDD; cd13260; PH_RASA1; 1.
DR   CDD; cd05391; RasGAP_p120GAP; 1.
DR   CDD; cd10354; SH2_Cterm_RasGAP; 1.
DR   CDD; cd10353; SH2_Nterm_RasGAP; 1.
DR   CDD; cd11788; SH3_RasGAP; 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   Gene3D; 3.30.505.10; SH2 domain; 2.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
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; 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:SF146; RAS GTPASE-ACTIVATING PROTEIN 1; 1.
DR   PANTHER; PTHR10194; RAS GTPASE-ACTIVATING PROTEINS; 1.
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; 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   SUPFAM; SSF55550; SH2 domain; 2.
DR   SUPFAM; SSF50044; SH3-domain; 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.
DR   PROSITE; PS50001; SH2; 2.
DR   PROSITE; PS50002; SH3; 1.
DR   Genevisible; E9PYG6; MM.
PE   1: Evidence at protein level;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Proteomics identification {ECO:0007829|EPD:E9PYG6,
KW   ECO:0007829|MaxQB:E9PYG6};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}.
FT   DOMAIN          172..263
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          270..332
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          342..432
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          465..568
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          568..681
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          739..933
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1038 AA;  115429 MW;  B6F56F0489252685 CRC64;
     MMAAEAGSEE GGPATAGPGG GAATGSSAYS AACRVKLPAA LPVAAAPCPG LADADLVAAL
     GGGAASGSGF LGTGPVAGVL GGAALTGSAA AGVAGAAAAG PAGDVAFTKG TLSLPAETLG
     PGGGFPPLPP PPQLPPLGSG 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 YTKTNDIR
//