ID   SEC4_CANAX              Reviewed;         210 AA.
AC   P0CY30; O14462; Q5A994;
DT   19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Ras-related protein SEC4;
GN   Name=SEC4;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1161;
RA   Murphy L., Harris D., Barrell B.G., Rajandream M.A.;
RT   "Candida albicans strain 1161 genome pilot sequencing project.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in exocytosis. Maybe by regulating the binding and
CC       fusion of secretory vesicles with the cell surface. The GTP-bound form
CC       of SEC4 may interact with an effector, thereby stimulating its activity
CC       and leading to exocytotic fusion. SEC4 may be an upstream activator of
CC       the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with
CC       SEC8; it could serve as the attachment site for the SEC8/SEC15 particle
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC       {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side
CC       {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC       {ECO:0000305}.
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DR   EMBL; AL033503; CAA22013.1; -; Genomic_DNA.
DR   PIR; T18242; T18242.
DR   AlphaFoldDB; P0CY30; -.
DR   SMR; P0CY30; -.
DR   VEuPathDB; FungiDB:CAWG_01525; -.
DR   VEuPathDB; FungiDB:CR_01750C_A; -.
DR   OMA; SKMEQNE; -.
DR   PhylomeDB; P0CY30; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030658; C:transport vesicle 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:0006887; P:exocytosis; IEA:UniProtKB-KW.
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   Cell membrane; Cytoplasmic vesicle; Exocytosis; GTP-binding; Lipoprotein;
KW   Membrane; Nucleotide-binding; Prenylation; Protein transport; Transport.
FT   CHAIN           1..210
FT                   /note="Ras-related protein SEC4"
FT                   /id="PRO_0000121328"
FT   MOTIF           43..51
FT                   /note="Effector region"
FT                   /evidence="ECO:0000305"
FT   BINDING         21..28
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..73
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         127..130
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   LIPID           209
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
FT   LIPID           210
FT                   /note="S-geranylgeranyl cysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  23077 MW;  4E1890D887DC6131 CRC64;
     MSGKGTSSRA YDMIMKLLLV GDSGVGKSCL LLRFVEDKFN PSFITTIGID FKIRTIESKG
     KRIKLQVWDT AGQERFRTIT TAYYRGAMGI VLIYDVTDSR SFENVENWFQ TVTQHANEDA
     QIFLVGNKCD DEVNRQVSKE QGQELAAKLN VPFLEASAKS NENVDSIFYE LASIIQEKHV
     EENIGGVGGA SGAGGIDVSQ NNSGAKNNCC