[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0092-8674(87)90455-7; PubMed=3552249 [NCBI, ExPASy, EBI, Israel, Japan] Salminen A., Novick P.J.; "A ras-like protein is required for a post-Golgi event in yeast secretion."; Cell 49:527-538(1987).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; DOI=10.1038/ng0795-261; PubMed=7670463 [NCBI, ExPASy, EBI, Israel, Japan] Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., Eki T.; "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces cerevisiae."; Nat. Genet. 10:261-268(1995).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; DOI=10.1002/(SICI)1097-0061(199601)12:1<77::AID-YEA887>3.0.CO;2-5; PubMed=8789262 [NCBI, ExPASy, EBI, Israel, Japan] Naitou M., Ozawa M., Sasanuma S., Kobayashi M., Hagiwara H., Shibata T., Hanaoka F., Watanabe K., Ono A., Yamazaki M., Tashiro H., Eki T., Murakami Y.; "Sequencing of a 23 kb fragment from Saccharomyces cerevisiae chromosome VI."; Yeast 12:77-84(1996).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 204508 / S288c; DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan] Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.; "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."; Genome Res. 17:536-543(2007).
[5]	INTERACTION WITH SEC2. DOI=10.1083/jcb.137.7.1495; PubMed=9199166 [NCBI, ExPASy, EBI, Israel, Japan] Walch-Solimena C., Collins R.N., Novick P.J.; "Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles."; J. Cell Biol. 137:1495-1509(1997).
[6]	INTERACTION WITH YIP3. DOI=10.1006/bbrc.2001.6242; PubMed=11785952 [NCBI, ExPASy, EBI, Israel, Japan] Calero M., Collins R.N.; "Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab proteins."; Biochem. Biophys. Res. Commun. 290:676-681(2002).
[7]	INTERACTION WITH YIF1; YIP4 AND YIP5. DOI=10.1016/S0014-5793(02)02442-0; PubMed=11943201 [NCBI, ExPASy, EBI, Israel, Japan] Calero M., Winand N.J., Collins R.N.; "Identification of the novel proteins Yip4p and Yip5p as Rab GTPase interacting factors."; FEBS Lett. 515:89-98(2002).
[8]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-11; SER-201 AND SER-204, AND MASS SPECTROMETRY. DOI=10.1038/nbt0302-301; PubMed=11875433 [NCBI, ExPASy, EBI, Israel, Japan] Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M., Shabanowitz J., Hunt D.F., White F.M.; "Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae."; Nat. Biotechnol. 20:301-305(2002).
[9]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-204, AND MASS SPECTROMETRY. DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan] Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.; "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."; J. Proteome Res. 6:1190-1197(2007).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-201 AND SER-204, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).
[11]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 18-187 IN COMPLEX WITH GDP AND GTP ANALOG. DOI=10.1006/jmbi.2000.4236; PubMed=11099382 [NCBI, ExPASy, EBI, Israel, Japan] Stroupe C., Brunger A.T.; "Crystal structures of a Rab protein in its inactive and active conformations."; J. Mol. Biol. 304:585-598(2000).

Comments

FUNCTION: Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP-bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as the attachment site for the SEC8/SEC15 particle.
SUBUNIT: Interacts with the guanyl-nucleotide exchange factor SEC2. Interacts with YIF1, YIP3, YIP4 and YIP5.
INTERACTION:
P53633:YIP3; NbExp=1; IntAct=EBI-16858, EBI-25301;
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane; Lipid-anchor; Cytoplasmic side. Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasm. Note=A small fraction is soluble.
SIMILARITY: Belongs to the small GTPase superfamily. Rab family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M16507; AAA35032.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D50617; BAA09233.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY692843; AAT92862.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A25959; TVBYQ4.

RefSeq

NP_116650.1; -.

3D structure databases

PDB

1G16; X-ray; 1.80 A; A/B/C/D=18-187.	[ExPASy / RCSB / EBI]
1G17; X-ray; 2.00 A; A/B=18-187.	[ExPASy / RCSB / EBI]
2EQB; X-ray; 2.70 A; A=19-187.	[ExPASy / RCSB / EBI]
2OCY; X-ray; 3.30 A; C=18-187.	[ExPASy / RCSB / EBI]
3CPH; X-ray; 2.90 A; A=1-213.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1G16; -.
1G17; -.
2EQB; -.
2OCY; -.
3CPH; -.

ModBase

P07560.

Protein-protein interaction databases

DIP

DIP:2492N; -.

IntAct

P07560; -.

Organism-specific databases

YFL005w; -.

S000001889; SEC4.

Gene expression databases

GermOnline

YFL005W; Saccharomyces cerevisiae.

Ontologies

GO:0030478;	Cellular component: actin cap (traceable author statement from SGD).
GO:0000131;	Cellular component: incipient cellular bud site (inferred from direct assay from SGD).
GO:0005741;	Cellular component: mitochondrial outer membrane (inferred from direct assay from SGD).
GO:0030133;	Cellular component: transport vesicle (traceable author statement from SGD).
GO:0005525;	Molecular function: GTP binding (inferred from direct assay from SGD).
GO:0003924;	Molecular function: GTPase activity (inferred from direct assay from SGD).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0031321;	Biological process: ascospore-type prospore formation (inferred from mutant phenotype from SGD).
GO:0007121;	Biological process: bipolar cellular bud site selection (traceable author statement from SGD).
GO:0006887;	Biological process: exocytosis (inferred from direct assay from SGD).
GO:0006893;	Biological process: Golgi to plasma membrane transport (inferred from mutant phenotype from SGD).
GO:0007107;	Biological process: membrane addition at site of cytokinesis (inferred from expression pattern from SGD).
GO:0007264;	Biological process: small GTPase mediated signal transduction (traceable author statement from SGD).
GO:0006906;	Biological process: vesicle fusion (inferred from mutant phenotype from SGD).
QuickGo view.

Family and domain databases

InterPro

IPR003579; GTPase_Rab.
IPR013753; Ras.
IPR001806; Ras_trnsfrmng.
IPR005225; Small_GTP_bd.
Graphical view of domain structure.

Pfam

PF00071; Ras; 1.
Pfam graphical view of domain structure.

PRINTS

PR00449; RASTRNSFRMNG.

SMART

SM00175; RAB; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00231; small_GTP; 1.

Proteomic databases

P07560; -.

Genome annotation databases

Ensembl

YFL005W; Saccharomyces cerevisiae. [Contig view]

850543; -.

D50617_GR; YFL005W.

sce:YFL005W; -.

fig|4932.3.peg.2280; -.

Phylogenomic databases

HOGENOM

P07560; -.

Other

LinkHub

P07560; -.

NextBio

966307; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell membrane; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Exocytosis; GTP-binding; Lipoprotein; Membrane; Nucleotide-binding; Palmitate; Phosphoprotein; Prenylation; Protein transport; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 215`	`215`	`Ras-related protein SEC4.`	`PRO_0000121330`
`NP_BIND`	`27 34`	`8`	`GTP.`
`NP_BIND`	`75 79`	`5`	`GTP.`
`NP_BIND`	`133 136`	`4`	`GTP (By similarity).`
`MOTIF`	`49 57`	`9`	`Effector region (Probable).`
`MOD_RES`	`8 8`		`Phosphoserine.`
`MOD_RES`	`11 11`		`Phosphoserine.`
`MOD_RES`	`201 201`		`Phosphoserine.`
`MOD_RES`	`204 204`		`Phosphoserine.`
`LIPID`	`214 214`		`S-palmitoyl cysteine (By similarity).`
`LIPID`	`215 215`		`S-geranylgeranyl cysteine (By similarity).`
`STRAND`	`20 28`	`9`
`HELIX`	`33 42`	`10`
`STRAND`	`57 66`	`10`
`STRAND`	`68 74`	`7`
`HELIX`	`79 81`	`3`
`HELIX`	`87 90`	`4`
`STRAND`	`93 101`	`9`
`HELIX`	`105 109`	`5`
`HELIX`	`111 121`	`11`
`STRAND`	`127 133`	`7`
`HELIX`	`144 154`	`11`
`STRAND`	`158 160`	`3`
`TURN`	`163 166`	`4`
`HELIX`	`169 182`	`14`

Sequence information

Length: 215 AA [This is the length of the unprocessed precursor]

Molecular weight: 23506 Da [This is the MW of the unprocessed precursor]

CRC64: 7DEDF7DCC7533BA7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGLRTVSAS SGNGKSYDSI MKILLIGDSG VGKSCLLVRF VEDKFNPSFI TTIGIDFKIK 

        70         80         90        100        110        120 
TVDINGKKVK LQLWDTAGQE RFRTITTAYY RGAMGIILVY DVTDERTFTN IKQWFKTVNE 

       130        140        150        160        170        180 
HANDEAQLLL VGNKSDMETR VVTADQGEAL AKELGIPFIE SSAKNDDNVN EIFFTLAKLI 

       190        200        210 
QEKIDSNKLV GVGNGKEGNI SINSGSGNSS KSNCC

P07560 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools