ID   RAB7B_DICDI             Reviewed;         197 AA.
AC   Q54K69;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Ras-related protein Rab-7B;
GN   Name=rab7B; ORFNames=DDB_G0287553;
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   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000102; EAL63676.1; -; Genomic_DNA.
DR   RefSeq; XP_637186.1; XM_632094.1.
DR   AlphaFoldDB; Q54K69; -.
DR   SMR; Q54K69; -.
DR   STRING; 44689.DDB0229399; -.
DR   PaxDb; Q54K69; -.
DR   EnsemblProtists; EAL63676; EAL63676; DDB_G0287553.
DR   GeneID; 8626187; -.
DR   KEGG; ddi:DDB_G0287553; -.
DR   dictyBase; DDB_G0287553; rab7B.
DR   eggNOG; KOG0394; Eukaryota.
DR   HOGENOM; CLU_041217_10_6_1; -.
DR   InParanoid; Q54K69; -.
DR   OMA; SYPYFET; -.
DR   PhylomeDB; Q54K69; -.
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:Q54K69; -.
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: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   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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   GTP-binding; Lipoprotein; Nucleotide-binding; Prenylation;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..197
FT                   /note="Ras-related protein Rab-7B"
FT                   /id="PRO_0000312559"
FT   MOTIF           31..39
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         33..38
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..61
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         119..122
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         152..153
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           196
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           197
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   197 AA;  22752 MW;  745BF98B55537E54 CRC64;
     MTKGRKIIKV VIIGEKSVGK TSILRRYVDK RFVTLKPTIG VDFVMVSENM VTLQLWDTSG
     QERFRSLEIS YYRGADYCIL VFDVTNEKTL YDLKLWRDDF IEKTEIRDPI LFPFIILGNK
     IDDPNRVVTE KAAIQWCKDN IGGNLTYFDT SAKDNINIEQ VFKHISNQCE NQPQSNEIPP
     EQLISLTEKK SNQSSCC