RGPA2_RAT
ID RGPA2_RAT Reviewed; 1872 AA.
AC P86411;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Ral GTPase-activating protein subunit alpha-2;
DE AltName: Full=250 kDa substrate of Akt {ECO:0000250|UniProtKB:Q2PPJ7};
DE Short=AS250 {ECO:0000250|UniProtKB:Q2PPJ7};
DE AltName: Full=p220 {ECO:0000303|PubMed:19520869};
GN Name=Ralgapa2 {ECO:0000303|PubMed:19520869};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15057822};
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 [2] {ECO:0000305}
RP FUNCTION, SUBUNIT, AND 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-486; SER-696; SER-819 AND
RP SER-820, AND IDENTIFICATION BY 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 RalGAP2 complex which
CC acts as a GTPase activator for the Ras-like small GTPases RALA and
CC RALB. {ECO:0000269|PubMed:19520869}.
CC -!- SUBUNIT: Component of the heterodimeric RalGAP2 complex with RALGAPB.
CC Heterodimerization is required for activity.
CC {ECO:0000269|PubMed:19520869}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q2PPJ7}.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, liver, testis and thymus
CC with lower levels in brain and heart (at protein level).
CC {ECO:0000269|PubMed:19520869}.
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DR EMBL; AABR03024064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03024168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03024328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03026408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03026968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03029878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P86411; -.
DR SMR; P86411; -.
DR STRING; 10116.ENSRNOP00000015637; -.
DR iPTMnet; P86411; -.
DR PhosphoSitePlus; P86411; -.
DR PaxDb; P86411; -.
DR PRIDE; P86411; -.
DR Ensembl; ENSRNOT00000113019; ENSRNOP00000084183; ENSRNOG00000036964.
DR UCSC; RGD:1308023; rat.
DR RGD; 1308023; Ralgapa2.
DR eggNOG; KOG3686; Eukaryota.
DR GeneTree; ENSGT00950000183139; -.
DR InParanoid; P86411; -.
DR PhylomeDB; P86411; -.
DR PRO; PR:P86411; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0032484; P:Ral protein signal transduction; ISO:RGD.
DR GO; GO:0060178; P:regulation of exocyst localization; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:InterPro.
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 Cytoplasm; GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..1872
FT /note="Ral GTPase-activating protein subunit alpha-2"
FT /id="PRO_0000390695"
FT DOMAIN 1634..1842
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 446..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..473
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..813
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A3KGS3"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A3KGS3"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A3KGS3"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 715
FT /note="Phosphothreonine; by PKB"
FT /evidence="ECO:0000250|UniProtKB:Q2PPJ7"
FT MOD_RES 819
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 1592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2PPJ7"
SQ SEQUENCE 1872 AA; 210333 MW; A64C5E16327A27EA CRC64;
MFSRRSHGDV KKSTQKVLDP KKDVLTRLKH LRALLDNVDA SDLKQFFETN YSQIYFIFYE
NFITLENSLK LKGNNKSQRE ELDSILFLFE KILQFLPERI FFRWHYQSIG STLKKLLHTG
NSIKIRCEGI RLFLLWLQAL QTNCAEEQVL IFACLVPGFP AVLSSRGPCT LETLINPSPS
VVDAKIYPEE ITPLLPAVSG EKIAEDQTCF FLQILLKYMV IQAASLEWKN KENQDTGFKF
LFTLFRKYYL PHLFPSFTKL TNIYKPVLEI PHLRPKPLYV TVTRDNETIY STKIPYMAAR
VVFIKWIVTF FLEKKYLTAT QNTKNGVDVL PKIIQTVGGG AIQEKVPELD GAGATEQDKS
HSNSSTLSDR RLSNSSLCSI EEEHRTVYEM VQRILLSTRG YVNFVNEVFR QAFLLPSCEI
SITRKVVQVY RKWILQNKPV FMEEPDKKDV AEEDADKLGL SETDSKEVSS ESSGHKRSSS
WGRTYSFTSA MSRGCVTEED NTNVKAGAQA MLQVFLTNAA NVFLLEPCVE VPMLLREQVD
ACKAVLIIFR RMIMELTMNQ KTWEQMLQIL LRITEAVMQK PKDKLVQDSF ARSLAGLLFR
TLIVAWIRAN LCVYISRELW DDFLRVLSSL TEWEELITEW SNIMDSLTAV LARTVYGVEM
TNLPLDKLSE QKEKKQRGKG CVLEPQKGTA VGRSFSLSWR SHPDVTEPMR FRSATTSGAP
GVEKARNTVR QKATEVEEFQ QAESTAAADC DYLVVGQQPV PRSSSTSDIT ERLYSDSSQG
QKVENSQNLS SSEPKSVQES KGHVTHEHEG VTILVRRSSS PAELDLKEES QQTHGRCRER
QKSESTGSDM AVGYSNEAEL PVSPWQTCEE DPELSTPTDA VADSDARHWL QLSPTDASNL
TESRECLADD CSIIAGGNLT GWHPDSAAVL WRRVLGILGD VNNIQSPKIH AKVFSYLYEL
WYKLAKIRDN LAISLDNQSS PSPPLLIPPL RMFASWLFKA TTLPNEYKEG KLQAYKLICA
MMTRRQDVLP NSDFLVHFYL VMHLGLTSED QDVLNTIIKN CSPRFFSLGL PGFSMLVGDF
ITAAARVLST DMLAAPRSEA LTLLGSLVCF PNTYQEIPLL QSVPEVSDVV TGAEDVKHYL
INILLKNATE EPNECARCIA ICSLGVWICE ELAQCASHPQ VKDAINVIGV TLKFPNKIVA
QVACDVLQLL VSYWEKLQMF ETALPRKMAE ILVATIAFLL PSAEYSSVET DKKFIVSLLL
CLLDWCMALP VSALLHPVST AVIEELHPSR APLLDYIYRV LHCCVCGSST YTQQSHYTLT
LADLSSTDYD PFLPLANVRN SEPVQYHSSA DLGNLLTVEE EKKRRSVELI PLTARMVMAH
LVNHLGHYPL SGGPAVLHSL VSENHDNAHV EGTELSSEVF RSPNLQLFVF NDSTLISYLQ
TPAEGPAGGT SGGSLSDVRV IVRDISGKYS WDGKVLYGPL EGRLAPSGRN PSFQISGWHH
HTCGPQSNLF HGEEGDDVLD KLLENIGHTS PECLLPSQLN LNEPSPTPSA MNCDQEKEII
EVILRQSTQE DEYVQRCHSN SAVKVTSQGQ PSPVEPRGPF YFCRLLLDDL GMNSWDRRKN
FHLLKKNSKL LRELKNLDSR QCRETHKIAV FYIAEGQEDK CSILANERGS QAYEDFVAGL
GWEVDLSTHC GFMGGLQRNG STGQTAPYYA TSTVEVIFHV STRMPSDSDD SLTKKLRHLG
NDEVHIVWSE HSRDYRRGII PTAFGDVSII IYPMKNHMFF ITITKKPEVP FFGPLFDGAI
VSGKLLPSLI CATCINASRA VKCLIPLYQS FYEERALYLE AIIQNHREVM TFEDFAAQVF
SPSPSYSLSG TD
