RLGPB_RAT
ID RLGPB_RAT Reviewed; 1484 AA.
AC P86410;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Ral GTPase-activating protein subunit beta;
DE AltName: Full=p170 {ECO:0000303|PubMed:19520869};
GN Name=Ralgapb {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 THR-363, 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: Non-catalytic subunit of the heterodimeric RalGAP1 and
CC RalGAP2 complexes which act as GTPase activators for the Ras-like small
CC GTPases RALA and RALB. {ECO:0000269|PubMed:19520869}.
CC -!- SUBUNIT: Component of the heterodimeric RalGAP1 complex with RALGAPA1
CC and of the heterodimeric RalGAP2 complex with RALGAPA2.
CC Heterodimerization is required for activity.
CC {ECO:0000269|PubMed:19520869}.
CC -!- TISSUE SPECIFICITY: Detected in brain, thymus, lung, heart, spleen,
CC liver and testis (at protein level). {ECO:0000269|PubMed:19520869}.
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 EMBL; AABR03025124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03026826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03027071; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03030442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03031051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03031170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P86410; -.
DR STRING; 10116.ENSRNOP00000020556; -.
DR iPTMnet; P86410; -.
DR jPOST; P86410; -.
DR PaxDb; P86410; -.
DR PRIDE; P86410; -.
DR RGD; 1306861; Ralgapb.
DR eggNOG; KOG3652; Eukaryota.
DR InParanoid; P86410; -.
DR PRO; PR:P86410; -.
DR Proteomes; UP000002494; Unplaced.
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; IPR039930; RALGAPB.
DR InterPro; IPR035974; Rap/Ran-GAP_sf.
DR InterPro; IPR000331; Rap/Ran_GAP_dom.
DR PANTHER; PTHR21344; PTHR21344; 1.
DR SUPFAM; SSF111347; SSF111347; 1.
DR PROSITE; PS50085; RAPGAP; 1.
PE 1: Evidence at protein level;
KW GTPase activation; Phosphoprotein; Reference proteome.
FT CHAIN 1..1484
FT /note="Ral GTPase-activating protein subunit beta"
FT /id="PRO_0000390693"
FT DOMAIN 1138..1382
FT /note="Rap-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00165"
FT REGION 355..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X10"
FT MOD_RES 363
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 379
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86X10"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BQZ4"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X10"
FT MOD_RES 724
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86X10"
FT MOD_RES 1275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86X10"
SQ SEQUENCE 1484 AA; 165367 MW; B551DFD359F59381 CRC64;
MYSEWRSLHL VIQNDQGHTS VLHSYPESVG REVANAVVRP LGQALGHSPV SASQSLLYTD
KDVKWTMEVI CYGLTLPLDG ETVKYCVDVY TDWIMALVLP KDSIPLPVIK EPNLYIQSIL
KHLQNLFVPR QEQGSSQIRL CLQVLRAIQK LARESSIMAR ETWEVLLLFL LQINDILLAP
PTVQGGIAEN LAEKLIGVLF EVWLLACTRC FPTPPYWKTA KEMVANWRHH PAVVEQWSKV
ICALTSRLLR FTYGPSFPPF KVPDEDANLI PPEMDNECIA QTWFRFLHML SNPVDLSNPA
VISSTPKFQE QFLNVSGMPQ ELSQYPCLKH LPQIFFRAMR GISCLVDAFL GISRPRSDSA
PPTPVNRLSM PQSAAVNTTP PHNRRHRAVT VNKATMKTST VTTAHTSKVQ HQASSTSPLS
SPNQTSSEPR PLPAPRRPKV NSILNLFGSW LFDAAFVHCK LHNGINRDSS MTASFIQILL
SYKSSIATQA SMEFRRKGSQ MSTDTMVSNP VFDASEFPDN YEAGRAEACG TLCRIFCSKK
TGEEILPAYL SSVILNSPPL FCCDLKGIDV VVPYFISALE TILPDRELSK FKSYVNPTEL
RRSSINILLS LLPLPHHFGT VRSEVVLEGK FSNDDSSSYD KPITFLSLKL RLVNILIGAL
QTETDPNNTQ MILGAMLNIV QDSALLEALG CQMEMGGGEN NLKSHSRTNS GISSASGGST
EPTTPDSERP AQALLRDYGS TDSAAGLLIR SIHLVTQRLN SQWRQDMSIS LAALELLSGL
AKVKVMVDLG DRKRAISSVC SYIVYQCSRP APLHSRDLHS MIVAAFQCLC VWLTEHPDML
DEKDCLKEVL EIVELGISGS KSKNSEQEVK YKGDKEPNPA SMRVKDAAEA TLTCIMQLLG
AFPSPSGPAS PCSLVNETTL IKYSRLPTIN KHSFRYFVLD NSVILAMLEQ PLGNEQNDFF
PSVTVLVRGM SGRLAWAQQL CLLPRGAKAN QKLFVPEPRP VPKNDVGFKY SVKHRPFPEE
VDKIPFVKAD LSIPDLHEIV TEELEERHEK LRSGMAQQIA YEMHLEQQSE GELQKRSFPD
PVTDCKPPPP AQEFQTARLF LSHFGFLSLE ALKEPANSRL PPHLIALDST IPGFFDDIGY
LDLLPCRPFD TVFIFYMKPG QKTNQEILKN VESSRNVQPH FLEFLLSLGW SVDVGRHPGW
TGHVSTSWSI NSCDDGEGSE QDEVTSSEDV GASIFNGQKK VLYYADALTE IAFVVPSPVE
SLTDSLESNI SDQDSDSNMD LMPGILKQPP LTLELVPNHT DSLNSSQRLS PSSRMKKLPQ
GRPVPPLGPE TRVSVVWVER YDDIENFPLS DLMTEISTGV ETTANSSTSL RSTTLEKEVP
VIFIHPLNTG LFRIKIQGAT GKFNMVIPLV DGMIVSRRAL GFLVRQTVIN ICRRKRLESD
SYSPPHVRRK QKITDIVNKY RNKQLEPEFY TALFQEVGLK NCSS
