SEC4_CANAL
ID SEC4_CANAL Reviewed; 210 AA.
AC P0CY31; A0A1D8PS21; O14462; Q5A994;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Ras-related protein SEC4;
GN Name=SEC4; OrderedLocusNames=CAALFM_CR01750CA;
GN ORFNames=Ca49C4.03c, CaO19.10103, CaO19.2571;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017630; AOW30934.1; -; Genomic_DNA.
DR RefSeq; XP_718237.1; XM_713144.1.
DR PDB; 6O62; X-ray; 1.88 A; A=1-184.
DR PDBsum; 6O62; -.
DR AlphaFoldDB; P0CY31; -.
DR SMR; P0CY31; -.
DR STRING; 237561.P0CY31; -.
DR PRIDE; P0CY31; -.
DR GeneID; 3640119; -.
DR KEGG; cal:CAALFM_CR01750CA; -.
DR CGD; CAL0000186445; SEC4.
DR VEuPathDB; FungiDB:CR_01750C_A; -.
DR eggNOG; KOG0078; Eukaryota.
DR HOGENOM; CLU_041217_23_1_1; -.
DR InParanoid; P0CY31; -.
DR OMA; SKMEQNE; -.
DR OrthoDB; 1426655at2759; -.
DR PRO; PR:P0CY31; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0005934; C:cellular bud tip; IDA:CGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:CGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0031521; C:spitzenkorper; IDA:CGD.
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; IGI:CGD.
DR GO; GO:0006887; P:exocytosis; IMP:CGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:CGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IMP:CGD.
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 GO; GO:0006906; P:vesicle fusion; IGI:CGD.
DR GO; GO:0006903; P:vesicle targeting; IGI:CGD.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasmic vesicle; Exocytosis; GTP-binding;
KW Lipoprotein; Membrane; Nucleotide-binding; Prenylation; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..210
FT /note="Ras-related protein SEC4"
FT /id="PRO_0000413056"
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"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:6O62"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:6O62"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:6O62"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:6O62"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:6O62"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:6O62"
FT STRAND 88..95
FT /evidence="ECO:0007829|PDB:6O62"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:6O62"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:6O62"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:6O62"
FT HELIX 139..149
FT /evidence="ECO:0007829|PDB:6O62"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6O62"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:6O62"
FT HELIX 164..178
FT /evidence="ECO:0007829|PDB:6O62"
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
