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 27-MAR-2024, entry version 238. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 286. DR DIP; DIP-2492N; -. DR IntAct; P07560; 15. DR MINT; P07560; -. DR STRING; 4932.YFL005W; -. DR iPTMnet; P07560; -. DR MaxQB; P07560; -. DR PaxDb; 4932-YFL005W; -. DR PeptideAtlas; P07560; -. DR TopDownProteomics; P07560; -. DR EnsemblFungi; YFL005W_mRNA; YFL005W; YFL005W. DR GeneID; 850543; -. DR KEGG; sce:YFL005W; -. DR AGR; SGD:S000001889; -. 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; ENIRTWF; -. DR OrthoDB; 3487147at2759; -. DR BioCyc; YEAST:G3O-30450-MONOMER; -. 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 BioGRID-ORCS; 850543; 2 hits in 10 CRISPR screens. 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: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 CDD; cd01867; Rab8_Rab10_Rab13_like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR001806; Small_GTPase. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR47980; LD44762P; 1. DR PANTHER; PTHR47980:SF24; LD44762P; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00177; ARF; 1. DR SMART; SM00175; RAB; 1. DR SMART; SM00176; RAN; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 //