SEC4_YEAST
ID SEC4_YEAST Reviewed; 215 AA.
AC P07560; D6VTM4;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Ras-related protein SEC4;
DE AltName: Full=Suppressor of RHO3 protein 6;
GN Name=SEC4; Synonyms=SRO6; OrderedLocusNames=YFL005W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3552249; DOI=10.1016/0092-8674(87)90455-7;
RA Salminen A., Novick P.J.;
RT "A ras-like protein is required for a post-Golgi event in yeast
RT secretion.";
RL Cell 49:527-538(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8789262;
RX DOI=10.1002/(sici)1097-0061(199601)12:1<77::aid-yea887>3.0.co;2-5;
RA Naitou M., Ozawa M., Sasanuma S., Kobayashi M., Hagiwara H., Shibata T.,
RA Hanaoka F., Watanabe K., Ono A., Yamazaki M., Tashiro H., Eki T.,
RA Murakami Y.;
RT "Sequencing of a 23 kb fragment from Saccharomyces cerevisiae chromosome
RT VI.";
RL Yeast 12:77-84(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP INTERACTION WITH SEC2.
RX PubMed=9199166; DOI=10.1083/jcb.137.7.1495;
RA Walch-Solimena C., Collins R.N., Novick P.J.;
RT "Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized
RT delivery of post-Golgi vesicles.";
RL J. Cell Biol. 137:1495-1509(1997).
RN [7]
RP INTERACTION WITH YIP3.
RX PubMed=11785952; DOI=10.1006/bbrc.2001.6242;
RA Calero M., Collins R.N.;
RT "Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab
RT proteins.";
RL Biochem. Biophys. Res. Commun. 290:676-681(2002).
RN [8]
RP INTERACTION WITH YIF1; YIP4 AND YIP5.
RX PubMed=11943201; DOI=10.1016/s0014-5793(02)02442-0;
RA Calero M., Winand N.J., Collins R.N.;
RT "Identification of the novel proteins Yip4p and Yip5p as Rab GTPase
RT interacting factors.";
RL FEBS Lett. 515:89-98(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH SRO7.
RX PubMed=16390997; DOI=10.1083/jcb.200510016;
RA Grosshans B.L., Andreeva A., Gangar A., Niessen S., Yates J.R. III,
RA Brennwald P., Novick P.;
RT "The yeast lgl family member Sro7p is an effector of the secretory Rab
RT GTPase Sec4p.";
RL J. Cell Biol. 172:55-66(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-204, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-204, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-187 IN COMPLEX WITH GDP AND GTP
RP ANALOG.
RX PubMed=11099382; DOI=10.1006/jmbi.2000.4236;
RA Stroupe C., Brunger A.T.;
RT "Crystal structures of a Rab protein in its inactive and active
RT conformations.";
RL J. Mol. Biol. 304:585-598(2000).
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
CC particle. {ECO:0000269|PubMed:16390997}.
CC -!- SUBUNIT: Interacts with the guanyl-nucleotide exchange factor SEC2.
CC Interacts with SRO7, YIF1, YIP3, YIP4 and YIP5.
CC {ECO:0000269|PubMed:11099382, ECO:0000269|PubMed:11785952,
CC ECO:0000269|PubMed:11943201, ECO:0000269|PubMed:16390997,
CC ECO:0000269|PubMed:9199166}.
CC -!- INTERACTION:
CC P07560; P39958: GDI1; NbExp=3; IntAct=EBI-16858, EBI-7517;
CC P07560; P17065: SEC2; NbExp=4; IntAct=EBI-16858, EBI-16842;
CC P07560; P53845: YIF1; NbExp=2; IntAct=EBI-16858, EBI-28230;
CC P07560; P53633: YIP3; NbExp=2; IntAct=EBI-16858, EBI-25301;
CC P07560; P53093: YIP4; NbExp=2; IntAct=EBI-16858, EBI-24124;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane;
CC Lipid-anchor; Cytoplasmic side. Cell membrane; Lipid-anchor;
CC Cytoplasmic side. Cytoplasm. Note=A small fraction is soluble.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; M16507; AAA35032.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09233.1; -; Genomic_DNA.
DR EMBL; AY692843; AAT92862.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12434.1; -; Genomic_DNA.
DR PIR; A25959; TVBYQ4.
DR RefSeq; NP_116650.1; NM_001179961.1.
DR PDB; 1G16; X-ray; 1.80 A; A/B/C/D=18-187.
DR PDB; 1G17; X-ray; 2.00 A; A/B=18-187.
DR PDB; 2EQB; X-ray; 2.70 A; A=19-187.
DR PDB; 2OCY; X-ray; 3.30 A; C=18-187.
DR PDB; 3CPH; X-ray; 2.90 A; A=1-213.
DR PDB; 4Z8Y; X-ray; 1.90 A; A/B=19-187.
DR PDB; 4ZDW; X-ray; 2.90 A; A=19-187.
DR PDBsum; 1G16; -.
DR PDBsum; 1G17; -.
DR PDBsum; 2EQB; -.
DR PDBsum; 2OCY; -.
DR PDBsum; 3CPH; -.
DR PDBsum; 4Z8Y; -.
DR PDBsum; 4ZDW; -.
DR AlphaFoldDB; P07560; -.
DR SMR; P07560; -.
DR BioGRID; 31141; 280.
DR DIP; DIP-2492N; -.
DR IntAct; P07560; 15.
DR MINT; P07560; -.
DR STRING; 4932.YFL005W; -.
DR iPTMnet; P07560; -.
DR MaxQB; P07560; -.
DR PaxDb; P07560; -.
DR PRIDE; P07560; -.
DR TopDownProteomics; P07560; -.
DR EnsemblFungi; YFL005W_mRNA; YFL005W; YFL005W.
DR GeneID; 850543; -.
DR KEGG; sce:YFL005W; -.
DR SGD; S000001889; SEC4.
DR VEuPathDB; FungiDB:YFL005W; -.
DR eggNOG; KOG0078; Eukaryota.
DR GeneTree; ENSGT00940000169395; -.
DR HOGENOM; CLU_041217_10_1_1; -.
DR InParanoid; P07560; -.
DR OMA; HKMLIGN; -.
DR BioCyc; YEAST:G3O-30450-MON; -.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-8873719; RAB geranylgeranylation.
DR Reactome; R-SCE-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR EvolutionaryTrace; P07560; -.
DR PRO; PR:P07560; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P07560; protein.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0030133; C:transport vesicle; IDA:SGD.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031982; C:vesicle; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IDA:SGD.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0031321; P:ascospore-type prospore assembly; IMP:SGD.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; IDA:SGD.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IMP:SGD.
DR GO; GO:0007107; P:membrane addition at site of cytokinesis; IMP:SGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IBA:GO_Central.
DR GO; GO:0009306; P:protein secretion; IBA:GO_Central.
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; IMP:SGD.
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; Cytoplasm; Cytoplasmic vesicle; Exocytosis;
KW GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Phosphoprotein;
KW Prenylation; Protein transport; Reference proteome; Transport.
FT CHAIN 1..215
FT /note="Ras-related protein SEC4"
FT /id="PRO_0000121330"
FT MOTIF 49..57
FT /note="Effector region"
FT /evidence="ECO:0000305"
FT BINDING 27..34
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 75..79
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT BINDING 133..136
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 201
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT LIPID 214
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 215
FT /note="S-geranylgeranyl cysteine"
FT /evidence="ECO:0000250"
FT STRAND 20..28
FT /evidence="ECO:0007829|PDB:1G16"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:2EQB"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:1G16"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2EQB"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:4Z8Y"
FT STRAND 57..66
FT /evidence="ECO:0007829|PDB:1G16"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:1G16"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1G16"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:4Z8Y"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:1G16"
FT STRAND 93..101
FT /evidence="ECO:0007829|PDB:1G16"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:1G16"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:1G16"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:3CPH"
FT STRAND 127..133
FT /evidence="ECO:0007829|PDB:1G16"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2EQB"
FT HELIX 144..154
FT /evidence="ECO:0007829|PDB:1G16"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:1G16"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:1G16"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:1G16"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:2EQB"
SQ SEQUENCE 215 AA; 23506 MW; 7DEDF7DCC7533BA7 CRC64;
MSGLRTVSAS SGNGKSYDSI MKILLIGDSG VGKSCLLVRF VEDKFNPSFI TTIGIDFKIK
TVDINGKKVK LQLWDTAGQE RFRTITTAYY RGAMGIILVY DVTDERTFTN IKQWFKTVNE
HANDEAQLLL VGNKSDMETR VVTADQGEAL AKELGIPFIE SSAKNDDNVN EIFFTLAKLI
QEKIDSNKLV GVGNGKEGNI SINSGSGNSS KSNCC
