Reduced viability upon starvation protein 167 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P39743 (RV167_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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 (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
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. Ref.10
Subunit structure	Binds to actin. Interacts with ABP1, GYL1, GYP5, PCL2 and YBR108W. Ref.4 Ref.5 Ref.6 Ref.10 Ref.11
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. Ref.6 Ref.7
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	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cortical patch localization Inferred from mutant phenotype PubMed 8590801. Source: SGD endocytosis Inferred from mutant phenotype PubMed 8590801. Source: SGD lipid tube assembly Inferred from direct assay PubMed 20610658. Source: SGD
Cellular_component	actin cortical patch Inferred from direct assay PubMed 10393809 PubMed 16239147. Source: SGD mating projection tip Inferred from direct assay PubMed 10393809 PubMed 19053807. Source: SGD
Molecular_function	cytoskeletal protein binding Inferred from sequence or structural similarity Ref.5. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
ABP1	P15891	3	EBI-14500,EBI-2036
ACF2	Q12168	6	EBI-14500,EBI-32973
ACF4	P47129	3	EBI-14500,EBI-25556
AIM3	P38266	5	EBI-14500,EBI-21584
APP1	P53933	7	EBI-14500,EBI-28798
BSP1	Q06604	3	EBI-14500,EBI-37047
ERT1	P38140	2	EBI-14500,EBI-21048
GTS1	P40956	3	EBI-14500,EBI-7968
GYL1	Q04322	5	EBI-14500,EBI-27427
GYP5	Q12344	2	EBI-14500,EBI-38508
LAS17	Q12446	14	EBI-14500,EBI-10022
RVS161	P25343	16	EBI-14500,EBI-14490

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

SH3

Coiled coil

31 – 64

Potential

Coiled coil

174 – 204

Potential

Compositional bias

292 – 427

136

Ala/Gly/Pro-rich

Amino acid modifications

Modified residue

271

Phosphothreonine Ref.12

Modified residue

299

Phosphoserine; by FUS3 and PHO85 Ref.7

Modified residue

321

Phosphoserine; by FUS3 and PHO85 Ref.7

Modified residue

379

Phosphoserine; by FUS3 and PHO85 Ref.7

Cross-link

481

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9

Sequences

Sequence

Length

Mass (Da)

Tools

P39743 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 3F0AB53EBCC95A5B
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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

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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] [Europe PMC] [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. Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Defining protein interactions with yeast actin in vivo." Amberg D.C., Basart E., Botstein D. Nat. Struct. Biol. 2:28-35(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ACTIN.
[5]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ABP1.
[6]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, INTERACTION WITH PCL2.
[7]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-299; SER-321 AND SER-379.
[8]	"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] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"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] [Europe PMC] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-481, MASS SPECTROMETRY. Strain: SUB592.
[10]	"Interaction of the Saccharomyces cerevisiae cortical actin patch protein Rvs167p with proteins involved in ER to Golgi vesicle trafficking." Friesen H., Colwill K., Robertson K., Schub O., Andrews B. Genetics 170:555-568(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GYL1 AND GYP5.
[11]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH YBR108W.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-271, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M92092 Genomic DNA. Translation: AAA35051.1. U32274 Genomic DNA. Translation: AAB64830.1. BK006938 Genomic DNA. Translation: DAA12232.1.
PIR	S40887.
RefSeq	NP_010676.1. NM_001180696.1.
3D structure databases
ProteinModelPortal	P39743.
SMR	P39743. Positions 4-210, 394-482.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-770N.
IntAct	P39743. 87 interactions.
MINT	MINT-369996.
STRING	4932.YDR388W.
Proteomic databases
PaxDb	P39743.
PeptideAtlas	P39743.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDR388W; YDR388W; YDR388W.
GeneID	851996.
KEGG	sce:YDR388W.
Organism-specific databases
CYGD	YDR388w.
SGD	S000002796. RVS167.
Phylogenomic databases
eggNOG	NOG280437.
HOGENOM	HOG000199510.
OMA	QEYDYYN.
OrthoDB	EOG4MD181.
Gene expression databases
Genevestigator	P39743.
GermOnline	YDR388W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	1.20.1270.60. 1 hit.
InterPro	IPR027267. AH/BAR-dom. IPR004148. BAR_dom. IPR001452. SH3_domain. [Graphical view]
Pfam	PF03114. BAR. 1 hit. PF00018. SH3_1. 1 hit. [Graphical view]
PRINTS	PR00452. SH3DOMAIN.
SMART	SM00721. BAR. 1 hit. SM00326. SH3. 1 hit. [Graphical view]
SUPFAM	SSF50044. SH3. 1 hit.
PROSITE	PS51021. BAR. 1 hit. PS50002. SH3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	970172.

Entry information

Entry name

RV167_YEAST

Accession

Primary (citable) accession number: P39743
Secondary accession number(s): D6VT22

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents