ID   RABM_DICDI              Reviewed;         202 AA.
AC   Q54FK8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Ras-related protein RabM;
GN   Name=rabM; ORFNames=DDB_G0290829;
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; AAFI02000171; EAL62048.2; -; Genomic_DNA.
DR   RefSeq; XP_635532.2; XM_630440.2.
DR   AlphaFoldDB; Q54FK8; -.
DR   SMR; Q54FK8; -.
DR   STRING; 44689.DDB0230017; -.
DR   PaxDb; Q54FK8; -.
DR   EnsemblProtists; EAL62048; EAL62048; DDB_G0290829.
DR   GeneID; 8627829; -.
DR   KEGG; ddi:DDB_G0290829; -.
DR   dictyBase; DDB_G0290829; rabM.
DR   eggNOG; KOG0394; Eukaryota.
DR   HOGENOM; CLU_041217_10_2_1; -.
DR   InParanoid; Q54FK8; -.
DR   OMA; YEINECT; -.
DR   PhylomeDB; Q54FK8; -.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-8854214; TBC/RABGAPs.
DR   Reactome; R-DDI-8873719; RAB geranylgeranylation.
DR   Reactome; R-DDI-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   Reactome; R-DDI-9706019; RHOBTB3 ATPase cycle.
DR   PRO; PR:Q54FK8; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0005770; C:late endosome; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0045335; C:phagocytic vesicle; IBA:GO_Central.
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; IEA:InterPro.
DR   GO; GO:0090385; P:phagosome-lysosome fusion; 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; Nucleotide-binding;
KW   Prenylation; Reference proteome.
FT   CHAIN           1..202
FT                   /note="Ras-related protein RabM"
FT                   /id="PRO_0000332761"
FT   MOTIF           34..41
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         12..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         59..63
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         117..120
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           201
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           202
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   202 AA;  23358 MW;  6CBEDF53E3484C4B CRC64;
     MSKKSLKIIT LGDSYVGKTS VFNNFVTGKY EINECTVSPS FYSKTLTIEN EPVILNVWDT
     CSQERFNGLS PIYYRWSNCY TLCFDIHNEK SFKNLDKWMD EARKFCIGKV PFVLIGTKKD
     IPRTDKSISK ERIEQWCKNI EDQGIIDRVH YFETSAKFSQ NITESYNAAL KLALEHYNKN
     QKPPITTPAI DSLQEVKPGY CC