GDS1_MOUSE
ID GDS1_MOUSE Reviewed; 607 AA.
AC E9Q912; E9Q6Q4; I6L967; Q3TA69; Q3TLU4; Q3TPS9; Q3TU36;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Rap1 GTPase-GDP dissociation stimulator 1 {ECO:0000305};
GN Name=Rap1gds1 {ECO:0000312|MGI:MGI:2385189};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Head, Hippocampus, Mammary gland, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=Czech II;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Acts as a GEF (guanine nucleotide exchange factor) for the
CC Rho family of small GTP-binding proteins (G proteins) that stimulates
CC the dissociation of GDP to enable subsequent binding of GTP.
CC Additionally, appears to chaperone the processing and/or trafficking of
CC small GTPases containing a C-terminal polybasic region independently of
CC GEF activity. Targets include RAP1A/RAP1B, RHOA, RHOB, RHOC, RAC1 and
CC KRAS. Regulates mitochondrial dynamics by controlling RHOT function to
CC promote mitochondrial fission during high calcium conditions. Able to
CC promote the Ca(2+) release from the endoplasmic reticulum via both
CC inositol trisphosphate (Ins3P) and ryanodine sensitive receptors
CC leading to a enhanced mitochondrial Ca(2+) uptake.
CC {ECO:0000250|UniProtKB:P52306}.
CC -!- FUNCTION: [Isoform 1]: Acts as a GEF (guanine nucleotide exchange
CC factor) for unprenylated RHOA. Chaperones the entry and passage of
CC small GTPases through the prenylation pathway. Recognizes the last
CC amino acid in the GTPase C-terminal CAAX motif with a preference for
CC 'Leu' over 'Met', indicating involvement in the geranylgeranylation
CC pathway. May also recognize prenylated GTPases.
CC {ECO:0000250|UniProtKB:P52306}.
CC -!- FUNCTION: [Isoform 3]: Acts as a GEF (guanine nucleotide exchange
CC factor) for prenylated RHOA. Acts as a GEF for RHOC. Chaperones the
CC downstream trafficking and/or processing of small newly prenylated
CC GTPases. Escorts RAC1 to the nucleus. {ECO:0000250|UniProtKB:P52306}.
CC -!- SUBUNIT: Interacts with RABL3. Interacts with RHOT1.
CC {ECO:0000250|UniProtKB:P52306}.
CC -!- SUBUNIT: [Isoform 1]: Interacts with unprenylated RHOA; the interaction
CC is direct. Interacts with RAP1A. Interacts with KRAS. Interacts with
CC RAC1. Interacts with RAP1B. Preferentially interacts with unprenylated
CC GTPases that will become geranylgeranylated. May also interact with
CC prenylated GTPases. {ECO:0000250|UniProtKB:P52306}.
CC -!- SUBUNIT: [Isoform 3]: Interacts with prenylated RHOA; the interaction
CC is direct and in a 1:1 stoichiometry. Interacts with RAP1A. Interacts
CC with KRAS. Interacts with RAC1. Interacts with RAP1B. Preferentially
CC interacts with prenylated GTPases. {ECO:0000250|UniProtKB:P52306}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P52306}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P52306}. Mitochondrion
CC {ECO:0000250|UniProtKB:P52306}. Nucleus {ECO:0000250|UniProtKB:P52306}.
CC Note=Nuclear import is dependent on complexing with a GTPase containing
CC a C-terminal polybasic region. {ECO:0000250|UniProtKB:P52306}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=E9Q912-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9Q912-2; Sequence=VSP_061009;
CC Name=3;
CC IsoId=E9Q912-3; Sequence=VSP_061008;
CC -!- PTM: Serotonylated on Gln residues by TGM2 in response to hypoxia,
CC leading to its inactivation. {ECO:0000250|UniProtKB:O55143}.
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DR EMBL; AK160989; BAE36135.1; -; mRNA.
DR EMBL; AK164159; BAE37656.1; -; mRNA.
DR EMBL; AK166315; BAE38698.1; -; mRNA.
DR EMBL; AK172052; BAE42801.1; -; mRNA.
DR EMBL; AC110574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC113307; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC119881; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011279; AAH11279.1; -; mRNA.
DR CCDS; CCDS51082.1; -. [E9Q912-3]
DR CCDS; CCDS51083.1; -. [E9Q912-1]
DR CCDS; CCDS80033.1; -. [E9Q912-2]
DR RefSeq; NP_001035780.1; NM_001040690.2. [E9Q912-1]
DR RefSeq; NP_001273688.1; NM_001286759.1. [E9Q912-2]
DR RefSeq; NP_663519.2; NM_145544.3. [E9Q912-3]
DR AlphaFoldDB; E9Q912; -.
DR SMR; E9Q912; -.
DR STRING; 10090.ENSMUSP00000096173; -.
DR iPTMnet; E9Q912; -.
DR PhosphoSitePlus; E9Q912; -.
DR EPD; E9Q912; -.
DR jPOST; E9Q912; -.
DR MaxQB; E9Q912; -.
DR PaxDb; E9Q912; -.
DR PeptideAtlas; E9Q912; -.
DR PRIDE; E9Q912; -.
DR ProteomicsDB; 342782; -.
DR ProteomicsDB; 349181; -.
DR ProteomicsDB; 363855; -.
DR Antibodypedia; 6907; 152 antibodies from 29 providers.
DR DNASU; 229877; -.
DR Ensembl; ENSMUST00000029796; ENSMUSP00000029796; ENSMUSG00000028149. [E9Q912-3]
DR Ensembl; ENSMUST00000098574; ENSMUSP00000096173; ENSMUSG00000028149. [E9Q912-1]
DR Ensembl; ENSMUST00000196280; ENSMUSP00000143181; ENSMUSG00000028149. [E9Q912-2]
DR GeneID; 229877; -.
DR KEGG; mmu:229877; -.
DR UCSC; uc008rnr.2; mouse. [E9Q912-1]
DR UCSC; uc008rnt.2; mouse.
DR CTD; 5910; -.
DR MGI; MGI:2385189; Rap1gds1.
DR VEuPathDB; HostDB:ENSMUSG00000028149; -.
DR eggNOG; KOG4500; Eukaryota.
DR GeneTree; ENSGT00390000014293; -.
DR HOGENOM; CLU_021124_1_0_1; -.
DR InParanoid; E9Q912; -.
DR OMA; IAWLINN; -.
DR OrthoDB; 561489at2759; -.
DR PhylomeDB; E9Q912; -.
DR TreeFam; TF323666; -.
DR BioGRID-ORCS; 229877; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Rap1gds1; mouse.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; E9Q912; protein.
DR Bgee; ENSMUSG00000028149; Expressed in medial dorsal nucleus of thalamus and 271 other tissues.
DR ExpressionAtlas; E9Q912; baseline and differential.
DR Genevisible; E9Q912; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030695; F:GTPase regulator activity; IDA:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0086098; P:angiotensin-activated signaling pathway involved in heart process; IMP:MGI.
DR GO; GO:0080120; P:CAAX-box protein maturation; ISO:MGI.
DR GO; GO:0003300; P:cardiac muscle hypertrophy; IMP:MGI.
DR GO; GO:0031034; P:myosin filament assembly; IEA:Ensembl.
DR GO; GO:0032471; P:negative regulation of endoplasmic reticulum calcium ion concentration; ISO:MGI.
DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0051561; P:positive regulation of mitochondrial calcium ion concentration; ISO:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; ISS:UniProtKB.
DR GO; GO:0070376; P:regulation of ERK5 cascade; IMP:MGI.
DR GO; GO:1904464; P:regulation of matrix metallopeptidase secretion; IMP:MGI.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISO:MGI.
DR GO; GO:0014829; P:vascular associated smooth muscle contraction; IEA:Ensembl.
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; 6.
DR SUPFAM; SSF48371; SSF48371; 2.
DR PROSITE; PS50176; ARM_REPEAT; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cytoplasm; Endoplasmic reticulum;
KW Guanine-nucleotide releasing factor; Mitochondrion; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..607
FT /note="Rap1 GTPase-GDP dissociation stimulator 1"
FT /id="PRO_0000452472"
FT REPEAT 89..131
FT /note="ARM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259"
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"
FT REGION 122..170
FT /note="Prevents binding to prenylated RHOA"
FT /evidence="ECO:0000250|UniProtKB:P52306"
FT MOD_RES 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52306"
FT VAR_SEQ 122..170
FT /note="Missing (in isoform 3)"
FT /id="VSP_061008"
FT VAR_SEQ 434
FT /note="Missing (in isoform 2)"
FT /id="VSP_061009"
FT CONFLICT 70
FT /note="D -> N (in Ref. 1; BAE38698 and 3; AAH11279)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="K -> R (in Ref. 1; BAE38698)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="N -> H (in Ref. 1; BAE38698 and 3; AAH11279)"
FT /evidence="ECO:0000305"
FT CONFLICT 279
FT /note="D -> N (in Ref. 1; BAE42801)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="V -> I (in Ref. 1; BAE37656)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 66076 MW; 1EED21A2C526A17A CRC64;
MDNLSDTLKK LKITAADRTE GSLEGCLDCL LQALAQNNAE TSEKIQGSGI LQLFANLLTP
QASCTAKVAD IIAEVAKNEF MRIPCVDAGL ISPLVQLLNS KDQEVLLQTG RALGNICYDS
HEGRSAVDQA GGAQIVIDHL RSLCGRTDPA SEKLMTVFCG MLMNYSNEND SLQAQLISMG
VIPTLVKLLG IHCHNAALTE MCLVAFGNLA ELESSKEQFA STNIAEELVK LFKKQIEHDK
REMIFEVLAP LAENDAIKLQ LVEAGLVECL LEIVQQKVDS NKEDDVAELK TASDLMVLLL
LGDESMQKLF EGGKGSVFQR VLSWIPSNNH QLQLAGALAI ANFARNDGNC IHMVDNGIVE
KLMDLLDRHV EDGNVTVQHA ALSALRNLAI PVVNKAKMLS AGVTETVLKF LKSEMPPVQF
KLLGTLRMLI DAQAEAAEQL GKNAKLVERL VEWCEAKDHA GVMGESNRLL SALIRHSKSK
DVIKTIVQSG GIKHLVTMAT SEHVIMQNEA LVALALIAAL ELGPAEKDLA SAQLVQILHR
LLADERSAPE IKYNSMVLIC ALMGSESLYK EVQDLAFLDV VSKLRSHENK SVAQQASLTE
QRLTVES
