ID   GDS1B_XENLA             Reviewed;         607 AA.
AC   Q5PPZ9;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Rap1 GTPase-GDP dissociation stimulator 1-B;
DE            Short=Rap1gds1-B protein;
DE   AltName: Full=RalB-binding protein B;
DE   AltName: Full=XsmgGDS-B;
DE            Short=smgGDS-B;
GN   Name=rap1gds1-b;
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:0000312|EMBL:AAH87423.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis {ECO:0000312|EMBL:AAH87423.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-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. Probably interacts with the post-
CC       translationally isoprenylated (geranyl-geranylation) forms of ral
CC       proteins. Interacts with both GDP-bound and GTP-bound forms of ralA,
CC       but interaction is much stronger with ralA-GDP (By similarity).
CC       {ECO:0000250|UniProtKB:O93614}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P52306}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P52306}. Mitochondrion
CC       {ECO:0000250|UniProtKB:P52306}.
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DR   EMBL; BC087423; AAH87423.1; -; mRNA.
DR   RefSeq; NP_001088766.1; NM_001095297.1.
DR   AlphaFoldDB; Q5PPZ9; -.
DR   SMR; Q5PPZ9; -.
DR   DNASU; 496030; -.
DR   GeneID; 496030; -.
DR   KEGG; xla:496030; -.
DR   CTD; 496030; -.
DR   Xenbase; XB-GENE-6252826; rap1gds1.S.
DR   OrthoDB; 561489at2759; -.
DR   Proteomes; UP000186698; Chromosome 1S.
DR   Bgee; 496030; Expressed in brain and 20 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; ISS:UniProtKB.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; ISS: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   2: Evidence at transcript level;
KW   Cytoplasm; Endoplasmic reticulum; GTPase activation; Mitochondrion;
KW   Reference proteome; Repeat.
FT   CHAIN           1..607
FT                   /note="Rap1 GTPase-GDP dissociation stimulator 1-B"
FT                   /id="PRO_0000228811"
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;  66648 MW;  A905ED57C23F4F43 CRC64;
     MDNLNDALEK LKLTGTECTS DKLDGCLDCL LQALGHNNTE SSEKIQQSGI LQLFASILNS
     QSSCASKVAH IVAEIAKNEL MRIPCVEADL IPPLVQLLHS KDQEVLLQTG RALGNICYDN
     HEGRRTVDQE GGAQIVVDHL RSRCTLTDPS SEKLMTVFCG MLMNYSSEND SLQTQLIQMG
     VIPILVDLLA VHSQNTALTE MCLVAFGNLA ELESSKEQFA ATNVAEVIVK LFKKQTEHEK
     REVIFEVLAP LAENDAIKMQ LVEAGLVECL LDIVQQTVNS EKDDDVAELK TSSDLMVLLL
     LGDESMQKLF EGGKGSVFQR VLSWLPSNNH QLQLAGALAI ANFARNDGNC IHMVDSEIVQ
     KLLDLLDRHV EDGNVTVQHA ALSALRNLAI PVVNKAKMLS AGVTEEVLKF LPSEMPPVQF
     KLLGTLRMLI DAQAEAAEQL GKNEKLVERL VEWCEAKDHA GVMGESNRLL SALIRHSKSK
     DVIRTTVQSG GIKHLVTMAT SEHVIMQNEA LVALGLIAAL ELQAAERDLE SAKLVEVLHR
     LLSDERSAPE IKYNSMVLIC AVMGSEPLHK EVQKLAFLDV VSKLRSHENK TVAQQASLTE
     QKFTVQS