RGPA1_RAT
ID RGPA1_RAT Reviewed; 2035 AA.
AC O55007; F1LSW3; O55008;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ral GTPase-activating protein subunit alpha-1;
DE AltName: Full=GAP-related-interacting partner to E12;
DE Short=GRIPE;
DE AltName: Full=GTPase-activating RapGAP domain-like 1;
DE AltName: Full=Tuberin-like protein 1;
DE AltName: Full=p240;
GN Name=Ralgapa1; Synonyms=Garnl1, Tulip1;
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] (ISOFORMS 1 AND 2).
RA Hirao K., Hata Y., Takai Y.;
RT "Tuberin-like proteins identified through the yeast two-hybrid screening
RT using rat lin-10 as a bait.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=19520869; DOI=10.1074/jbc.m109.012112;
RA Shirakawa R., Fukai S., Kawato M., Higashi T., Kondo H., Ikeda T.,
RA Nakayama E., Okawa K., Nureki O., Kimura T., Kita T., Horiuchi H.;
RT "Tuberous sclerosis tumor suppressor complex-like complexes act as GTPase-
RT activating proteins for Ral GTPases.";
RL J. Biol. Chem. 284:21580-21588(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-796; SER-859; SER-860;
RP SER-863; SER-999; THR-1001; SER-1003 AND SER-1477, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalytic subunit of the heterodimeric RalGAP1 complex which
CC acts as a GTPase activator for the Ras-like small GTPases RALA and
CC RALB. {ECO:0000250}.
CC -!- SUBUNIT: Component of the heterodimeric RalGAP1 complex with RALGAPB.
CC Heterodimerization is required for activity. Interacts with the HLH
CC region of TCF3/isoform E12 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Translocated to the nucleus, when associated with TCF3/E12.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=O55007-4; Sequence=Displayed;
CC Name=2; Synonyms=Tulip 2;
CC IsoId=O55007-3; Sequence=VSP_056780, VSP_056783;
CC Name=1; Synonyms=Tulip 1;
CC IsoId=O55007-1; Sequence=VSP_056779, VSP_056781, VSP_056782;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, thymus and testis with
CC lower levels in lung and spleen and barely detectable in heart or liver
CC (at protein level). {ECO:0000269|PubMed:19520869}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB97076.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF041106; AAB97075.1; -; mRNA.
DR EMBL; AF041107; AAB97076.1; ALT_FRAME; mRNA.
DR EMBL; AABR06044125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044127; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044128; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044130; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044133; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044134; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044136; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06044137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_064468.3; NM_020083.3.
DR AlphaFoldDB; O55007; -.
DR IntAct; O55007; 2.
DR MINT; O55007; -.
DR STRING; 10116.ENSRNOP00000059440; -.
DR iPTMnet; O55007; -.
DR PhosphoSitePlus; O55007; -.
DR PaxDb; O55007; -.
DR PRIDE; O55007; -.
DR Ensembl; ENSRNOT00000065230; ENSRNOP00000059440; ENSRNOG00000046256. [O55007-1]
DR GeneID; 56785; -.
DR KEGG; rno:56785; -.
DR UCSC; RGD:620642; rat. [O55007-4]
DR CTD; 253959; -.
DR RGD; 620642; Ralgapa1.
DR VEuPathDB; HostDB:ENSRNOG00000046256; -.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00950000183139; -.
DR HOGENOM; CLU_001676_0_0_1; -.
DR InParanoid; O55007; -.
DR OrthoDB; 157372at2759; -.
DR Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR PRO; PR:O55007; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000046256; Expressed in ovary and 20 other tissues.
DR ExpressionAtlas; O55007; baseline and differential.
DR Genevisible; O55007; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR Gene3D; 3.40.50.11210; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR InterPro; IPR027107; Tuberin/Ral-act_asu.
DR PANTHER; PTHR10063; PTHR10063; 1.
DR Pfam; PF02145; Rap_GAP; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; GTPase activation; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..2035
FT /note="Ral GTPase-activating protein subunit alpha-1"
FT /id="PRO_0000056755"
FT DOMAIN 1795..2003
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 343..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 807..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 986..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..2034
FT /note="Minimal domain that binds to TCF3/E12"
FT /evidence="ECO:0000250|UniProtKB:Q6GYP7"
FT COILED 1713..1746
FT /evidence="ECO:0000255"
FT COMPBIAS 348..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 714..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..832
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..911
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 753
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 777
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 796
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 859
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 863
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 985
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 993
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6GYQ0"
FT MOD_RES 999
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1001
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..1174
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_056779"
FT VAR_SEQ 1..1134
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056780"
FT VAR_SEQ 1897..1921
FT /note="LRHLGNDEVHIVWSEHTRDYRRGII -> INWRIALSFSIKDSVGILMGIPL
FT TL (in isoform 1)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_056781"
FT VAR_SEQ 1922..2035
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_056782"
FT VAR_SEQ 2034..2035
FT /note="DH -> GKNKREC (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_056783"
FT CONFLICT 1150
FT /note="L -> F (in Ref. 1; AAB97076)"
FT CONFLICT 1406
FT /note="L -> I (in Ref. 1; AAB97076)"
FT CONFLICT 1688
FT /note="G -> R (in Ref. 1; AAB97075/AAB97076)"
FT CONFLICT 1691
FT /note="S -> N (in Ref. 1; AAB97076)"
FT CONFLICT 1992
FT /note="L -> F (in Ref. 1; AAB97076)"
SQ SEQUENCE 2035 AA; 229447 MW; 7BF777C25ADDDA4E CRC64;
MFSKKPHGDV KKSTQKVLDT KKDALTRLKH LRIVIENADS IDLKQFFDQH FSHIYYVFFE
NFVTIEASLK QKGHKSQREE LDAILFIFEK ILQLLPERIH QRWQFHSIGL ILKKLLHTGN
SLKIRREGVR LFLLWLQALQ DNCSKEQLWM FSCLIPGFSA PQSEYGPRTL DNLINPPLNL
QETQVTIEEV TPLVPPQSGD KGQEDLTSYF LEALLKYIVI QVKSLEWKNK ENQERGFSFL
FSHFKKFYLP YIFPNLCKEN SLYHPVLDIP QVRPKPHYVM VKKDAETNET IYCTKEPFIQ
ARVIVIRWLV SFWLEPKPHS GPNIPGMEGE VLPKNIQRAA ASLVSREESK NDTVDKADKT
AEPEQSHSNT STLTEREPSS SSLCSIDEEH LTDIEIVRRV FSSKRSNVNF VTEIFRQAFL
LPICEAAAMR KVVKVYQEWI QQEGKPLFMQ EPEETVITSS DIPCSENVTD HDISIEDGEK
REEENGTNIS EHVRNSTWTK NGSYQEAFHV SEEATEQNIQ AGTQAVLQVF IINSSNIFLL
EPANEIKNLL DEHTDMCKRI LNIYRYMVVQ VSMDKKTWEQ MLLVLLRVTE SVLKMSSQAF
LQFQGKKNMT LAGRLAGPLF QTLIVAWIKA NLNVYISREL WDDLLSVLSS LTYWEELATE
WSLTMETLTK VLARNLYSLD LSDLPLDKLS EQKQKKHKGK GVGHEFQKVS VDKSFSRGWS
RDQPGQAPMR QRSATTTGSP GTEKARSIVR QKTVDIDDSQ ILPRSTRVRH FSQSEDTGNE
VFGALHEEQP LPRSSSTSDI LEPFTVERAK VNKEDTSPKL PPLNSETGGS SANVPDLMDE
FIAERLRSGN ASTMTRRGSS PGSLEIPKDL PDILNKQNQM RPVDDPGVPS EWTSPASAGS
SDLMSSDSHS DSFSAFQCEG RKFDNFGFGT DIGIPSSADV DSGSGHHQST EEQEVASLTT
LHLDSETSSL NQQAFSAEVA TVTGSESASP VHSALGSRSQ TPSPSTLNID HMEQKDLQLD
EKLHHSVLQT PDDLEISEFP SECCSVMAGG TLTGWHADVA TVMWRRMLGI LGDVNAIMDP
EIHAQVFDYL CELWQNLAKI RDNLGISADN LTSPSPPVLI PPLRILTPWL FKATMLTDKY
KQGKLHAYKL ICNTMKRRQD VSPNRDFLTH FYNIMHCGLL HIDQDIVNTI IKHCSPQFFS
LGLPGATMLI MDFIIAAGRV ASSAFLNAPR VEAQVLLGSL VCFPNLYCEL PALHPSTPDI
AVSQFTDVKE LIIKTVLSSA RDEPSGPARC VALCSLGIWI CEELVHESHH PQIKEALNVI
CVSLKFTNKT VAHVACNMLH MLVHYAPRLQ TYQPDSPLKI IQILIATITH LLPSTEASSY
EMDKRLVVSL LLCLLDWIMA LPLKTLLQSV HSTGAENEKT EKSVLNCIYK VLHGCVYGAQ
SFSHPKYFPI SLSDLASVDY DPFMHLESLR EPEPLHSPDS ERSSKLQPVT EVKTQMQQGL
ISIAARTVIT HLVNHLGHYP MSGGPAMLTS QVCENHDNHY SESTELSPEL FDSPNIQFFV
LNNTTLVSCI QIRSEESVPG GGLAAGLVSA NSNVRIIVRD LSGKYSWDSA ILYGPPIVSG
LPEPTSFILS MSYQEKPEEP PTSNECLEDI TVKDGLSLQL RRFRETVPTW STIREEEDVL
DELLQYLGTT SPECLQRTGI SLNVPAPQPV CISEKQENDV INAILKQYTE EKEFVEKHFN
DLNMKASEQD EPTPQKPQSA FYYCRLLLSI LGMNSWDKRR SFHLLKKNEK LLRELRNLDS
RQCRETHKIA VFYVAEGQED KYSILTNIGG SQAYEDFVAG LGWEVNLTNH CGFMGGLQKN
KSTGLTTPYF ATSTVEVIFH VSTRMPSESD DSLTKKLRHL GNDEVHIVWS EHTRDYRRGI
IPTEFGDVLI VIYPMKNHMF SIQIMKKPEV PFFGPLFDGA IVNGKVLPIM VRSTAINASR
ALKSLIPLYQ NLYEERARYL QTIVQHHLEP TTFEDFAAQV FSPAPYHHFP ADADH
