RBP1A_XENLA
ID RBP1A_XENLA Reviewed; 655 AA.
AC Q9PT60; Q6NRU6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=RalA-binding protein 1-A {ECO:0000250|UniProtKB:Q62796};
DE Short=RalBP1-A {ECO:0000250|UniProtKB:Q62796};
DE AltName: Full=Dinitrophenyl S-glutathione ATPase {ECO:0000250|UniProtKB:Q15311};
DE Short=DNP-SG ATPase {ECO:0000250|UniProtKB:Q15311};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:Q15311};
DE EC=7.6.2.3 {ECO:0000250|UniProtKB:Q15311};
DE AltName: Full=Ral-interacting protein {ECO:0000303|PubMed:15511640};
DE AltName: Full=Ral-interacting protein 1-A;
DE Short=RIP1-A;
DE AltName: Full=XRLIP2;
DE AltName: Full=XRLIP76-A;
GN Name=ralbp1-a; Synonyms=rlip {ECO:0000312|EMBL:CAB65771.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB65771.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH RALB,
RP SUBCELLULAR LOCATION, TOPOLOGY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte {ECO:0000269|PubMed:15511640};
RX PubMed=15511640; DOI=10.1016/j.mod.2004.07.008;
RA Lebreton S., Boissel L., Iouzalen N., Moreau J.;
RT "RLIP mediates downstream signalling from RalB to the actin cytoskeleton
RT during Xenopus early development.";
RL Mech. Dev. 121:1481-1494(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH70617.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH70617.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP INTERACTION WITH RALA AND RALB.
RX PubMed=9753634; DOI=10.1006/bbrc.1998.9336;
RA Iouzalen N., Camonis J., Moreau J.;
RT "Identification and characterization in Xenopus of XsmgGDS, a RalB-binding
RT protein.";
RL Biochem. Biophys. Res. Commun. 250:359-363(1998).
RN [4]
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND REGION.
RX PubMed=22319010; DOI=10.1096/fj.11-196451;
RA Fillatre J., Delacour D., Van Hove L., Bagarre T., Houssin N., Soulika M.,
RA Veitia R.A., Moreau J.;
RT "Dynamics of the subcellular localization of RalBP1/RLIP through the cell
RT cycle: the role of targeting signals and of protein-protein interactions.";
RL FASEB J. 26:2164-2174(2012).
CC -!- FUNCTION: Multifunctional protein that functions as a downstream
CC effector of ralA and ralB (PubMed:15511640). As a GTPase-activating
CC protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase
CC activity. As part of the Ral signaling pathway, may also regulate
CC ligand-dependent EGF and insulin receptors-mediated endocytosis. During
CC mitosis, may act as a scaffold protein in the phosphorylation of
CC EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1, preventing endocytosis
CC during that phase of the cell cycle. During mitosis, also controls
CC mitochondrial fission as an effector of ralA. Recruited to
CC mitochondrion by ralA, acts as a scaffold to foster the mitotic kinase
CC cyclin B-CDK1-mediated phosphorylation and activation of DNM1L (By
CC similarity). Acts on the cytoskeleton, to regulate pigment distribution
CC and to regulate gastrulation (PubMed:15511640).
CC {ECO:0000250|UniProtKB:Q15311, ECO:0000269|PubMed:15511640}.
CC -!- FUNCTION: Could also function as a primary ATP-dependent active
CC transporter for glutathione conjugates of electrophiles. May also
CC actively catalyze the efflux of a wide range of substrates including
CC xenobiotics like doxorubicin (DOX) contributing to cell multidrug
CC resistance. {ECO:0000250|UniProtKB:Q15311}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC substituted glutathione(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:456216; EC=7.6.2.3;
CC Evidence={ECO:0000250|UniProtKB:Q15311};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000250|UniProtKB:Q15311};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:Q15311};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q15311};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000250|UniProtKB:Q15311};
CC -!- SUBUNIT: Interacts with the active, GTP-bound form of ralB and ralA.
CC {ECO:0000269|PubMed:15511640, ECO:0000269|PubMed:9753634}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15511640};
CC Peripheral membrane protein {ECO:0000269|PubMed:15511640}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:15511640, ECO:0000269|PubMed:22319010}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q62796}.
CC Nucleus {ECO:0000269|PubMed:22319010}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q15311}. Note=Targeted to the plasma membrane
CC through its interaction with ralB, directed by FGF signaling. Docking
CC on the membrane is required to transduce the Ral signal
CC (PubMed:15511640). Nuclear localization is cell cycle dependent while
CC membrane localization is seen in adherent cells (PubMed:22319010).
CC {ECO:0000269|PubMed:15511640, ECO:0000269|PubMed:22319010}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:22319010}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:22319010}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15511640};
CC IsoId=Q9PT60-1; Sequence=Displayed;
CC Name=2; Synonyms=miniRalBP1 {ECO:0000303|PubMed:22319010};
CC IsoId=Q9PT60-2; Sequence=VSP_051990, VSP_051991;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically during
CC oogenesis and early development. {ECO:0000269|PubMed:15511640}.
CC -!- DOMAIN: The Rho-GAP domain mediates the GTPase activator activity
CC toward CDC42. {ECO:0000250|UniProtKB:Q62796}.
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DR EMBL; AJ252165; CAB65771.1; -; mRNA.
DR EMBL; BC070617; AAH70617.1; -; mRNA.
DR RefSeq; NP_001090213.1; NM_001096744.1. [Q9PT60-2]
DR AlphaFoldDB; Q9PT60; -.
DR SMR; Q9PT60; -.
DR GeneID; 779115; -.
DR KEGG; xla:779115; -.
DR CTD; 779115; -.
DR Xenbase; XB-GENE-1016078; ralbp1.S.
DR OMA; CESKDEE; -.
DR OrthoDB; 209269at2759; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 779115; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:UniProtKB.
DR GO; GO:0090141; P:positive regulation of mitochondrial fission; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032489; P:regulation of Cdc42 protein signal transduction; ISS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:UniProtKB.
DR Gene3D; 1.10.555.10; -; 1.
DR InterPro; IPR039767; RALBP1.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR12783; PTHR12783; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Cell projection;
KW Cytoplasm; Cytoskeleton; Developmental protein; GTPase activation;
KW Membrane; Mitochondrion; Nucleotide-binding; Nucleus; Reference proteome;
KW Repeat; Translocase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..655
FT /note="RalA-binding protein 1-A"
FT /id="PRO_0000228812"
FT REPEAT 133..137
FT /note="1"
FT REPEAT 138..142
FT /note="2"
FT DOMAIN 187..383
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..119
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:22319010"
FT REGION 133..142
FT /note="2 X 5 AA tandem repeats of E-[D/E]-K-H-K"
FT REGION 149..214
FT /note="Mediates association with membranes and could form
FT transmembrane domains"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT REGION 398..495
FT /note="Mediates interaction with RALA and RALB"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT REGION 494..510
FT /note="Required to maintain nuclear localization"
FT /evidence="ECO:0000269|PubMed:22319010"
FT REGION 496..655
FT /note="Mediates interaction with REPS1 and REPS2"
FT /evidence="ECO:0000250|UniProtKB:Q62796"
FT REGION 520..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT BINDING 413..420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q15311"
FT VAR_SEQ 347..361
FT /note="ISNRVLYVFFTHVQE -> VQKKHLPELGMGFWF (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_051990"
FT VAR_SEQ 362..655
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_051991"
FT CONFLICT 2..19
FT /note="TECFLPPASSPSEHRRAE -> EFGTR (in Ref. 1; CAB65771)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 76146 MW; 033AE9636407859E CRC64;
MTECFLPPAS SPSEHRRAEH GGGLARTPSS EEISPTKFPG LYRTGEPLPP HDILHEPPDI
VSEDEKDHGK KKGKFKKKEK RTEGYAAFQE DSSGDEAESP SKIKRSKGIH VFKKPSFSKK
KEKDFKIKEK PKEEKHKEDK HKEKKSKDLT AADVVKQWKE KKKKKKPTPE PESLPVDIPR
LRPVFGIPLI EAAERTMIYD GIRLPLVFRE CIDFIEQHGM KCEGIYRVSG IKSKVDELKA
AYDREESPNL EDYEPYTVAS LLKQYLRELP ENVLTKDLMP RFEEACGKTT EGERLQECQR
LLKELPECNF CLTSWLVVHM DHVIEQELET KMNIQNISIV LSPTVQISNR VLYVFFTHVQ
ELFGGVQIKR VIKPLRWSNM ATMPALPETQ ETIKEEIRRQ EFLLNCLHRE LQAGVKDLSK
EERLWEVQRI LTALKRKLRE AKRQDCETKI AQEIASLSKE DVSKEEMTEN EEEVLNILLA
QENEILTEQE ELVAMEQYLR RQIATEKEEI DRLRAEISEI QSRQQHGRSE TEEYSSESES
ESEDEEELQY ILEDLQRQNE ELEIKNTHLN QAIHEEREAI IELRVQLRLL QKQRVKSEQL
QEEEELGKQN VPSQLPRDNL PETKAPKDQP KALMEQMKPS PIKKTGKKLS SETLI
