ID   RABZ_DICDI              Reviewed;         229 AA.
AC   Q1ZXE7;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Ras-related protein RabZ;
GN   Name=rabZ; ORFNames=DDB_G0286169;
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   -!- PTM: Although this sequence lacks the C-terminal cysteine motifs
CC       subject to isoprenylation in other Rab proteins, it does have N-
CC       terminal myristoylation and S-palmitoylation sequence motifs.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000085; EAS66851.2; -; Genomic_DNA.
DR   RefSeq; XP_001134534.2; XM_001134534.2.
DR   AlphaFoldDB; Q1ZXE7; -.
DR   SMR; Q1ZXE7; -.
DR   STRING; 44689.DDB0233188; -.
DR   PaxDb; Q1ZXE7; -.
DR   EnsemblProtists; EAS66851; EAS66851; DDB_G0286169.
DR   GeneID; 8625453; -.
DR   KEGG; ddi:DDB_G0286169; -.
DR   dictyBase; DDB_G0286169; rabZ.
DR   eggNOG; KOG0084; Eukaryota.
DR   HOGENOM; CLU_041217_10_6_1; -.
DR   InParanoid; Q1ZXE7; -.
DR   OMA; YLCTVGV; -.
DR   PhylomeDB; Q1ZXE7; -.
DR   Reactome; R-DDI-210500; Glutamate Neurotransmitter Release Cycle.
DR   Reactome; R-DDI-6798695; Neutrophil degranulation.
DR   Reactome; R-DDI-8873719; RAB geranylgeranylation.
DR   PRO; PR:Q1ZXE7; -.
DR   Proteomes; UP000002195; Chromosome 4.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0009306; P:protein secretion; IBA:GO_Central.
DR   GO; GO:0017157; P:regulation of exocytosis; IBA:GO_Central.
DR   GO; GO:0006904; P:vesicle docking involved in exocytosis; 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   GTP-binding; Lipoprotein; Myristate; Nucleotide-binding; Palmitate;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000255"
FT   CHAIN           2..229
FT                   /note="Ras-related protein RabZ"
FT                   /id="PRO_0000332775"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           79..88
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        10..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         57..64
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         106..110
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         164..167
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           2
FT                   /note="N-myristoyl glycine"
FT                   /evidence="ECO:0000255"
FT   LIPID           3
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   229 AA;  25874 MW;  8484C11D4B578500 CRC64;
     MGCFHSREPT ATGKTKKEEP TSAVKTNKEE KSSNYVSEPT TMEKIKKDDV YTIILIGDQA
     TGKSSVLQRF KNNQFEVCHK PSPIIIDCFT KKIQIEGKKI SLKCYDTAGQ EKFRALSQSY
     YRCADGIMLF YDIANQKTFD NVGRWLEEVH RLAGPNVPIL IIANKCDLNE KRVVNFNNAK
     KFADDKNIPI IEVSAKESLG VEEAFIKLAS EINKTWKPLP DNETVTIGM