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Database: UniProt
Entry: A0A2I2YTV7_GORGO
LinkDB: A0A2I2YTV7_GORGO
Original site: A0A2I2YTV7_GORGO 
ID   A0A2I2YTV7_GORGO        Unreviewed;       870 AA.
AC   A0A2I2YTV7;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=RAS p21 protein activator 1 {ECO:0000313|Ensembl:ENSGGOP00000038410.1};
GN   Name=RASA1 {ECO:0000313|Ensembl:ENSGGOP00000038410.1};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000038410.1, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000038410.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Scally A.;
RT   "Insights into the evolution of the great apes provided by the gorilla
RT   genome.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSGGOP00000038410.1, ECO:0000313|Proteomes:UP000001519}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22398555; DOI=10.1038/nature10842;
RA   Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA   Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA   McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA   Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA   Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA   Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA   Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA   Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA   Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA   Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA   Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA   Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA   Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000038410.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; CABD030039534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2YTV7; -.
DR   SMR; A0A2I2YTV7; -.
DR   Ensembl; ENSGGOT00000044953.1; ENSGGOP00000038410.1; ENSGGOG00000001591.3.
DR   GeneTree; ENSGT00940000155846; -.
DR   Proteomes; UP000001519; Chromosome 5.
DR   Bgee; ENSGGOG00000001591; Expressed in testis and 6 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR   CDD; cd08400; C2_Ras_p21A1; 1.
DR   CDD; cd05391; RasGAP_p120GAP; 1.
DR   CDD; cd10354; SH2_Cterm_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; 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.
PE   4: Predicted;
KW   GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
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          4..95
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          102..164
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          174..264
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   DOMAIN          297..400
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          400..513
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          571..765
FT                   /note="Ras-GAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50018"
SQ   SEQUENCE   870 AA;  100398 MW;  B328E701911065F9 CRC64;
     MKGWYHGKLD RTIAEERLRQ AGKSGSYLIR ESDRRPGSFV LSFLSQMNVV NHFRIIAMCG
     DYYIGGRRFS SLSDLIGYYS HVSCLLKGEK LLYPVAPPEP VEDRRRVRAI LPYTKVPDTD
     EISFLKGDMF IVHNELEDGW MWVTNLRTDE QGLIVEDLVE EVGREEDPHE GKIWFHGKIS
     KQEAYNLLMT VGQVCSFLVR PSDNTPGDYS LYFRTNENIQ RFKICPTPNN QFMMGGRYYN
     SIGDIIDHYR KEQIVEGYYL KEPVPMQDQE QVLNDTVDGK EIYNTIRRKT KDAFYKNIVK
     KGYLLKKGKG KRWKNLYFIL EGSDAQLIYF ESEKRATKPK GLIDLSVCSV YVVHDSLFGR
     PNCFQIVVQH FSEEHYIFYF AGETPEQAED WMKGLQAFCN LRKSSPGTSN KRLRQVSSLV
     LHIEEAHKLP VKHFTNPYCN IYLNSVQVAK THAREGQNPV WSEEFVFDDL PPDINRFEIT
     LSNKTKKSKD PDILFMRCQL SRLQKGHATD EWFLLSSHIP LKGIEPGSLR VRARYSMEKI
     MPEEEYSEFK ELILQKELHV VYALSHVCGQ DRTLLASILL RIFLHEKLES LLLCTLNDRE
     ISMEDEATTL FRATTLASTL MEQYMKATAT QFVHHALKDS ILKIMESKQS CELSPSKLEK
     NEDVNTNLTH LLNILSELVE KIFMASEILP PTLRYIYGCL QKSVQHKWPT NTTMRTRVVS
     GFVFLRLICP AILNPRMFNI ISDSPSPIAA RTLILVAKSV QNLANLVEFG AKEPYMEGVN
     PFIKSNKHRM IMFLDELGNV PELPDTTEHS RTDLSRDLAA LHEICVAHSD ELRTLSNERG
     AQQHVLKKLL AITELLQQKQ NQYTKTNDVR
//
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