ID   GDS1A_XENLA             Reviewed;         607 AA.
AC   O93614;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Rap1 GTPase-GDP dissociation stimulator 1-A;
DE            Short=Rap1gds1-A protein;
DE   AltName: Full=RalB-binding protein A;
DE   AltName: Full=XsmgGDS-A;
DE            Short=smgGDS-A;
GN   Name=rap1gds1-a;
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:CAA06746.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH RALB, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   TISSUE=Oocyte {ECO:0000269|PubMed:9753634};
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   [2] {ECO:0000312|EMBL:AAH79775.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye {ECO:0000312|EMBL:AAH79775.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Stimulates GDP/GTP exchange reaction of a group of small GTP-
CC       binding proteins (G proteins) including Rap1a/Rap1b, RhoA, RhoB and
CC       KRas, by stimulating the dissociation of GDP from and the subsequent
CC       binding of GTP to each small G protein. {ECO:0000250|UniProtKB:P52306}.
CC   -!- SUBUNIT: Interacts with ralB (PubMed:9753634). Probably interacts with
CC       the post-translationally isoprenylated (geranyl-geranylation) forms of
CC       ral proteins. Interacts with both GDP-bound and GTP-bound forms of
CC       ralA, but interaction is much stronger with ralA-GDP (PubMed:9753634).
CC       {ECO:0000269|PubMed:9753634}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P52306}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P52306}. Mitochondrion
CC       {ECO:0000250|UniProtKB:P52306}.
CC   -!- TISSUE SPECIFICITY: Weakly expressed in adult tissues with highest
CC       levels found in spleen, kidney, skin and A6 cells.
CC       {ECO:0000269|PubMed:9753634}.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically from
CC       oogenesis through to late embryogenesis at a constant level.
CC       {ECO:0000269|PubMed:9753634}.
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DR   EMBL; AJ005870; CAA06746.1; -; mRNA.
DR   EMBL; BC079775; AAH79775.1; -; mRNA.
DR   RefSeq; NP_001081078.1; NM_001087609.1.
DR   AlphaFoldDB; O93614; -.
DR   SMR; O93614; -.
DR   IntAct; O93614; 2.
DR   DNASU; 394369; -.
DR   GeneID; 394369; -.
DR   KEGG; xla:394369; -.
DR   CTD; 394369; -.
DR   Xenbase; XB-GENE-1004458; rap1gds1.L.
DR   OrthoDB; 561489at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 394369; Expressed in brain and 19 other tissues.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IPI:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IPI:UniProtKB.
DR   Gene3D; 1.25.10.10; -; 3.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR040144; RAP1GDS1.
DR   PANTHER; PTHR10957; PTHR10957; 1.
DR   Pfam; PF00514; Arm; 4.
DR   SMART; SM00185; ARM; 5.
DR   SUPFAM; SSF48371; SSF48371; 2.
DR   PROSITE; PS50176; ARM_REPEAT; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endoplasmic reticulum; GTPase activation; Mitochondrion;
KW   Reference proteome; Repeat.
FT   CHAIN           1..607
FT                   /note="Rap1 GTPase-GDP dissociation stimulator 1-A"
FT                   /id="PRO_0000228810"
FT   REPEAT          79..118
FT                   /note="ARM 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          170..211
FT                   /note="ARM 2"
FT                   /evidence="ECO:0000255"
FT   REPEAT          347..390
FT                   /note="ARM 3"
FT                   /evidence="ECO:0000255"
FT   REPEAT          391..431
FT                   /note="ARM 4"
FT                   /evidence="ECO:0000255"
FT   REPEAT          479..519
FT                   /note="ARM 5"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   607 AA;  66527 MW;  5850F23101F38618 CRC64;
     MDNLNDALEK LKLTGTECTS DKLDGCFDCL LQALGHNNTE SSEKIQQSGI LQLFASILNS
     QSSCASKVAH IVAEIAKNEL MRIPCVEAGL IPPLVQLLHS KDQEVLLQTG RALGNICYDN
     HEGRRAVDQE GGAQIVVDHL RSMCTLTDPS SEKLMTVFCG MLMNYSSEND SLQTQLIQMG
     VIPILVDLLG VHSQNTALTE MCLVAFGNLA ELESSKEQFA GTNIAEEIVK LFKKQTEHEK
     REIIFEVLAP LAENDAIKMQ LVEAGLVECL LDVVQQTVNS EKDDDIAELK TSSDLMVLLL
     LGDESMQKLF EGGKGSVFQR VLSWLPSNNH QLQLAGALAI ANFARNDGNC IHMVDSEIVQ
     KLLDLLDRHV EDGNVTVQHA ALSALRNLAI PVVNKAKMLS AGVAEEVLKF LRSEMPPVQF
     KLLGTLRMLI DAQAEAAEQI GKNEKLAERL VEWCEAKDHA GVMGESNRLL SALIRHSKSK
     DVIRTIVQSG GIKHLVTMAT SEHVIMQNEA LVALGLIAAL ELQAAEHDLE SAKLVEVLHR
     LLLDERSAPE IKYNSMVLIC AAMGSVPLHK EVQKLAFLDV VSKLRSHENK TVAQQASLTE
     QKLTVQS