Reviewed, UniProtKB/Swiss-Prot P39743 (RV167_YEAST)

Names and origin

Protein names

Recommended name:
    Reduced viability upon starvation protein 167

Gene names

Name:	RVS167
Ordered Locus Names:	YDR388W
ORF Names:	D9509.8

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of a cytoskeletal structure that is required for the formation of endocytic vesicles at the plasma membrane level. Could be implicated in cytoskeletal reorganization in response to environmental stresses and could act in the budding site selection mechanism.
Subunit structure	Binds to actin. Interacts with ABP1, PCL2 and YBR108W.
Subcellular location	Cytoplasm › cytoskeleton.
Post-translational modification	Phosphorylated redundantly by cyclin-dependent kinase PHO85 in association with PCL1,2-type cyclins or by MAP kinase FUS3. Phosphorylation inhibits interaction with complexes involved in actin cytoskeleton function.
Miscellaneous	Present with 14600 molecules/cell in log phase SD medium.
Sequence similarities	Contains 1 BAR domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Domain	Coiled coil SH3 domain
Ligand	Actin-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	bipolar cellular bud site selection Traceable author statement. Source: SGD endocytosis Traceable author statement. Source: SGD response to osmotic stress Traceable author statement. Source: SGD
Cellular component	actin cortical patch Traceable author statement. Source: SGD
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	P31374	1	EBI-14500,EBI-9442
	P38140	2	EBI-14500,EBI-21048
	P38266	3	EBI-14500,EBI-21584
	P40563	1	EBI-14500,EBI-25376
	P47129	1	EBI-14500,EBI-25556
	P53153	1	EBI-14500,EBI-23857
	P53901	1	EBI-14500,EBI-28955
	Q03780	1	EBI-14500,EBI-30094
	Q04322	4	EBI-14500,EBI-27427
	Q06833	1	EBI-14500,EBI-37290
	Q12510	1	EBI-14500,EBI-35343
	Q12532	1	EBI-14500,EBI-33283
ABP1	P15891	1	EBI-14500,EBI-2036
ACF2	Q12168	4	EBI-14500,EBI-32973
ACT1	P60010	2	EBI-14500,EBI-2169
APP1	P53933	4	EBI-14500,EBI-28798
BBP1	Q12365	1	EBI-14500,EBI-3448
BSP1	Q06604	2	EBI-14500,EBI-37047
CUE5	Q08412	1	EBI-14500,EBI-37580
DEM1	P38289	1	EBI-14500,EBI-20869
EAF6	P47128	1	EBI-14500,EBI-25552
GTS1	P40956	1	EBI-14500,EBI-7968
GYP5	Q12344	1	EBI-14500,EBI-38508
LAS17	Q12446	6	EBI-14500,EBI-10022
MRS3	P10566	1	EBI-14500,EBI-11291
RIM101	P33400	1	EBI-14500,EBI-14422
RVS161	P25343	4	EBI-14500,EBI-14490
SML1	Q04964	1	EBI-14500,EBI-27834
SNP1	Q00916	1	EBI-14500,EBI-724

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 482	482	Reduced viability upon starvation protein 167		PRO_0000192961
Regions
	Domain	17 – 254	238	BAR
	Domain	421 – 482	62	SH3
	Coiled coil	31 – 64	34	Potential
	Coiled coil	174 – 204	31	Potential
	Compositional bias	292 – 427	136	Ala/Gly/Pro-rich
Amino acid modifications
	Modified residue	271	1	Phosphothreonine
	Modified residue	299	1	Phosphoserine; by FUS3 and PHO85
	Modified residue	321	1	Phosphoserine; by FUS3 and PHO85
	Modified residue	379	1	Phosphoserine; by FUS3 and PHO85
	Cross-link	481		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)

Sequences

	Sequence		Length	Mass (Da)
	P39743-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 3F0AB53EBCC95A5B	FASTA	482	52,774
	10 20 30 40 50 60 MSFKGFTKAV SRAPQSFRQK FKMGEQTEDP VYEDAERRFQ ELEQETKKLS EESKRYSTAV 70 80 90 100 110 120 NGMLTHQIGF AKSMEEIFKP ISGKMSDPNA TIPEDNPQGI EASEQYRAIV AELQETLKPD 130 140 150 160 170 180 LALVEEKIVT PCQELLKIIT YIRKMATKRN HKKLDLDRHL NTYNKHEKKK EPTAKDEERL 190 200 210 220 230 240 YKAQAQVEVA QQEYDYYNDL LKTQLPILFS LEAEFVKPLF VSFYFMQLNI FYTLYNRLQD 250 260 270 280 290 300 MKIPYFDLNS DIVESYIAKK GNVEEQTDAL TITHFKLGYS KAKLEMTRRK YGVATAEGSP 310 320 330 340 350 360 VSGASSGVGY GAGYDPATAT SPTPTGYGYG AAAPSYAAQP AAQYGTAAAV GTAAAVGTAA 370 380 390 400 410 420 GAAAGAVPGT YPQYAAAQSP PLTGLGFQQS PQQQQGPPPA YSNPLTSPVA GTPAAAVAAA 430 440 450 460 470 480 PGVETVTALY DYQAQAAGDL SFPAGAVIEI VQRTPDVNEW WTGRYNGQQG VFPGNYVQLN KN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Alteration of a yeast SH3 protein leads to conditional viability with defects in cytoskeletal and budding patterns." Bauer F., Urdaci M., Aigle M., Crouzet M. Mol. Cell. Biol. 13:5070-5084(1993) [PubMed: 8336735] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 26109 / X2180.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Defining protein interactions with yeast actin in vivo." Amberg D.C., Basart E., Botstein D. Nat. Struct. Biol. 2:28-35(1995) [PubMed: 7719850] [Abstract] Cited for: INTERACTION WITH ACTIN.
[4]	"In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p function is mediated through multiple protein interactions." Colwill K., Field D., Moore L., Friesen J., Andrews B. Genetics 152:881-893(1999) [PubMed: 10388809] [Abstract] Cited for: INTERACTION WITH ABP1.
[5]	"Interaction of yeast Rvs167 and Pho85 cyclin-dependent kinase complexes may link the cell cycle to the actin cytoskeleton." Lee J., Colwill K., Aneliunas V., Tennyson C.N., Moore L., Ho Y., Andrews B.J. Curr. Biol. 8:1310-1321(1998) [PubMed: 9843683] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH PCL2.
[6]	"Regulation of the yeast amphiphysin homologue Rvs167p by phosphorylation." Friesen H., Murphy K., Breitkreutz A., Tyers M., Andrews B.J. Mol. Biol. Cell 14:3027-3040(2003) [PubMed: 12857883] [Abstract] Cited for: PHOSPHORYLATION AT SER-299; SER-321 AND SER-379.
[7]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[8]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed: 12872131] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-481, MASS SPECTROMETRY.
[9]	"Characterizing the sphingolipid signaling pathway that remediates defects associated with loss of the yeast amphiphysin-like orthologs, Rvs161p and Rvs167p." Germann M., Swain E., Bergman L., Nickels J.T. Jr. J. Biol. Chem. 280:4270-4278(2005) [PubMed: 15561700] [Abstract] Cited for: INTERACTION WITH YBR108W.
[10]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-271, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M92092 Genomic DNA. Translation: AAA35051.1. U32274 Genomic DNA. Translation: AAB64830.1.
PIR	S40887.
RefSeq	NP_010676.1.
3D structure databases
HSSP	HSSP built from PDB template 2HSP based on UniProtKB P19174.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:770N.
IntAct	P39743.
Proteomic databases
PeptideAtlas	P39743.
Genome annotation databases
Ensembl	YDR388W. Saccharomyces cerevisiae. [Contig view]
GeneID	851996.
GenomeReviews	Gene locus YDR388W in contig Z71256_GR.
KEGG	sce:YDR388W.
NMPDR	fig|4932.3.peg.1448.
Organism-specific databases
CYGD	YDR388w.
SGD	S000002796. RVS167.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P39743.
Gene expression databases
ArrayExpress	P39743.
GermOnline	YDR388W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR004148. BAR. IPR001452. SH3. [Graphical view]
Pfam	PF03114. BAR. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00452. SH3DOMAIN.
ProDom	PD000066. SH3. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00721. BAR. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
PROSITE	PS51021. BAR. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	P39743.
NextBio	970172.

Entry information

Entry name

RV167_YEAST

Accession

Primary (citable) accession number: P39743

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 25, 2008
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)