ID   RAB4A_ECHMU             Reviewed;         223 AA.
AC   Q9GP33;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Probable Ras-related protein Rab-4A;
OS   Echinococcus multilocularis (Fox tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Echinococcus.
OX   NCBI_TaxID=6211;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=H-95;
RX   PubMed=10973970; DOI=10.1074/jbc.m006091200;
RA   Brehm K., Jensen K., Frosch M.;
RT   "mRNA trans-splicing in the human parasitic cestode Echinococcus
RT   multilocularis.";
RL   J. Biol. Chem. 275:38311-38318(2000).
CC   -!- FUNCTION: Protein transport. Probably involved in vesicular traffic (By
CC       similarity). {ECO:0000250}.
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; AJ292375; CAC18549.1; -; mRNA.
DR   AlphaFoldDB; Q9GP33; -.
DR   SMR; Q9GP33; -.
DR   eggNOG; KOG0086; Eukaryota.
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: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   2: Evidence at transcript level;
KW   Cell membrane; GTP-binding; Lipoprotein; Membrane; Methylation;
KW   Nucleotide-binding; Prenylation; Protein transport; Transport.
FT   CHAIN           1..223
FT                   /note="Probable Ras-related protein Rab-4A"
FT                   /id="PRO_0000121097"
FT   MOTIF           38..46
FT                   /note="Effector region"
FT                   /evidence="ECO:0000250"
FT   BINDING         16..23
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..68
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         122..125
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         223
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000250"
FT   LIPID           221
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           223
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   223 AA;  24454 MW;  9EE6D6166E2089A4 CRC64;
     MESDRFDYLF KFLIIGNAGT GKTCILRRYT ERKFFPNTQH TIGAEFGSRV ISVDGTHVKI
     QIWDTAGQER FRSMARSYYH DAVGTLLVYD ITNRTSFGAV EQWLGDARHL ATPGVVVILV
     GNKKDLRDTD GQVTHWEANT FAQENGLQFI ETSALTGENI DDAFTSCVRV LLSKVKSGEL
     GADRLLVGSN KQHLQAVNLT ASATSVSASQ SSAATAHSDT CLC