ID   RABY_DICDI              Reviewed;         236 AA.
AC   Q54SV1;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Ras-related protein RabY;
DE   Flags: Precursor;
GN   Name=rabY; ORFNames=DDB_G0282203;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000046; EAL66307.1; -; Genomic_DNA.
DR   RefSeq; XP_640284.1; XM_635192.1.
DR   AlphaFoldDB; Q54SV1; -.
DR   SMR; Q54SV1; -.
DR   STRING; 44689.DDB0229421; -.
DR   PaxDb; Q54SV1; -.
DR   EnsemblProtists; EAL66307; EAL66307; DDB_G0282203.
DR   GeneID; 8623461; -.
DR   KEGG; ddi:DDB_G0282203; -.
DR   dictyBase; DDB_G0282203; rabY.
DR   eggNOG; KOG0084; Eukaryota.
DR   HOGENOM; CLU_041217_23_1_1; -.
DR   InParanoid; Q54SV1; -.
DR   OMA; VENTWSE; -.
DR   PhylomeDB; Q54SV1; -.
DR   Reactome; R-DDI-162658; Golgi Cisternae Pericentriolar Stack Reorganization.
DR   Reactome; R-DDI-204005; COPII-mediated vesicle transport.
DR   Reactome; R-DDI-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-DDI-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR   Reactome; R-DDI-6811440; Retrograde transport at the Trans-Golgi-Network.
DR   Reactome; R-DDI-8873719; RAB geranylgeranylation.
DR   Reactome; R-DDI-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   PRO; PR:Q54SV1; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR001806; Small_GTPase.
DR   Pfam; PF00071; Ras; 1.
DR   SMART; SM00174; RHO; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51419; RAB; 1.
PE   3: Inferred from homology;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Reference proteome.
FT   CHAIN           1..233
FT                   /note="Ras-related protein RabY"
FT                   /id="PRO_0000332774"
FT   PROPEP          234..236
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000370839"
FT   REGION          192..236
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           40..48
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         18..25
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..70
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         126..129
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         233
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           233
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   236 AA;  27882 MW;  38F139755B8E36FF CRC64;
     MNSEKPDYNY LFKIVIIGDR KTGKTCLMNR FVENTWSEEY RQTNLLHFKV KTIYIDCKII
     KLQIWDSQAD ENFRFNNNNL SNYRSASGFL VVYDCTNENS FSNLKHWIKD IKLYGRPNAI
     NIVVSNKSDL VNEKVIDSDV AKSYCDSLEI PFIETSSKHS SNVEDCFVLL IKNVMKYLET
     EPTIPQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQHQQSSKTK IGCLIQ