ID   RABL_DICDI              Reviewed;         204 AA.
AC   Q54FK7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Ras-related protein RabL;
GN   Name=rabL; ORFNames=DDB_G0290779;
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; EAL62023.1; -; Genomic_DNA.
DR   RefSeq; XP_635533.1; XM_630441.1.
DR   AlphaFoldDB; Q54FK7; -.
DR   SMR; Q54FK7; -.
DR   STRING; 44689.DDB0191360; -.
DR   PaxDb; Q54FK7; -.
DR   EnsemblProtists; EAL62023; EAL62023; DDB_G0290779.
DR   GeneID; 8627830; -.
DR   KEGG; ddi:DDB_G0290779; -.
DR   dictyBase; DDB_G0290779; rabL.
DR   eggNOG; KOG0394; Eukaryota.
DR   HOGENOM; CLU_041217_10_6_1; -.
DR   InParanoid; Q54FK7; -.
DR   PhylomeDB; Q54FK7; -.
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:Q54FK7; -.
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..204
FT                   /note="Ras-related protein RabL"
FT                   /id="PRO_0000332760"
FT   MOTIF           36..44
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         14..21
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..66
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         120..123
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           203
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           204
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   204 AA;  23619 MW;  B4054C4B7F1EBCBF CRC64;
     MKEEKTMLKI ITLGDSNVGK TSLFYHYVNG EYRYNRPPSI GPDYFIKELK VENKHVFLMV
     WDTCGQERFQ AFSPPYFRGA NCYTLCFDIH NEESFINLGK WMDEIIKYCY GNIPFVLVGT
     KSDIPRTDKS ISKARIEQWC KNIEDQGIID KVHYFETSAK LSQNVTELYN VAAKLALEHY
     SIVKYISIIR PIGPPEEVKV GTCC