SEC4_CANAW
ID SEC4_CANAW Reviewed; 210 AA.
AC C4YL11; O14462; Q5A994;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Ras-related protein SEC4;
GN Name=SEC4; ORFNames=CAWG_01525;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=9639314;
RX DOI=10.1002/(sici)1097-0061(199805)14:7<675::aid-yea252>3.0.co;2-9;
RA Clement M., Fournier H., de Repentigny L., Belhumeur P.;
RT "Isolation and characterization of the Candida albicans SEC4 gene.";
RL Yeast 14:675-680(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=10572126; DOI=10.1128/jb.181.23.7235-7242.1999;
RA Mao Y.X., Kalb V.F., Wong B.;
RT "Overexpression of a dominant-negative allele of SEC4 inhibits growth and
RT protein secretion in Candida albicans.";
RL J. Bacteriol. 181:7235-7242(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(2009).
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; AF017183; AAC50022.1; -; Genomic_DNA.
DR EMBL; AF015306; AAB67974.1; -; Genomic_DNA.
DR EMBL; CM000309; EEQ43292.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YL11; -.
DR SMR; C4YL11; -.
DR STRING; 5476.C4YL11; -.
DR EnsemblFungi; EEQ43292; EEQ43292; CAWG_01525.
DR VEuPathDB; FungiDB:CAWG_01525; -.
DR HOGENOM; CLU_041217_23_1_1; -.
DR OMA; SKMEQNE; -.
DR Proteomes; UP000001429; Chromosome R.
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.
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_0000413057"
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
