SEC4_CANGA
ID SEC4_CANGA Reviewed; 215 AA.
AC O42819;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Ras-related protein SEC4;
GN Name=SEC4; OrderedLocusNames=CAGL0F02123g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA McCreath K.J., Gow N.A.R.;
RT "Cloning of the SEC4 homologue from Candida glabrata.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; AJ224685; CAA12071.1; -; Genomic_DNA.
DR EMBL; CR380952; CAG58989.1; -; Genomic_DNA.
DR RefSeq; XP_446065.1; XM_446065.1.
DR AlphaFoldDB; O42819; -.
DR SMR; O42819; -.
DR STRING; 5478.XP_446065.1; -.
DR PRIDE; O42819; -.
DR EnsemblFungi; CAG58989; CAG58989; CAGL0F02123g.
DR GeneID; 2887974; -.
DR KEGG; cgr:CAGL0F02123g; -.
DR CGD; CAL0131066; CAGL0F02123g.
DR VEuPathDB; FungiDB:CAGL0F02123g; -.
DR eggNOG; KOG0078; Eukaryota.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; O42819; -.
DR OMA; HKMLIGN; -.
DR Proteomes; UP000002428; Chromosome F.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0000131; C:incipient cellular bud site; IEA:EnsemblFungi.
DR GO; GO:0043332; C:mating projection tip; IEA:EnsemblFungi.
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:EnsemblFungi.
DR GO; GO:0031321; P:ascospore-type prospore assembly; IEA:EnsemblFungi.
DR GO; GO:0006914; P:autophagy; IEA:EnsemblFungi.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:EnsemblFungi.
DR GO; GO:0007107; P:membrane addition at site of cytokinesis; IEA:EnsemblFungi.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006906; P:vesicle fusion; IEA:EnsemblFungi.
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;
KW Reference proteome; Transport.
FT CHAIN 1..215
FT /note="Ras-related protein SEC4"
FT /id="PRO_0000121329"
FT REGION 187..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 43..51
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 215
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 215 AA; 23681 MW; 0C675877EFACABE1 CRC64;
MSALRTVSGS SGNGKSYDSI MKILLIGDSG VGKSCLLVRF VEDKFNPSFI TTIGIDFKIK
TVDINGKKVK LQLWDTAGQE RFRTITTAYY RGAMGIILVY DVTDERTFAN IKQWFKTVNE
HANDEAQLLL VGNKSDMDTR VVTYEQGEAL AKELGLPFIE SSAKNDDNVN EIFFTLARLI
QEKIDSNKLS GPNSGKDGNI SINANKGDSS KSNCC
