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Reviewed, UniProtKB/Swiss-Prot P12868 (PEP5_YEAST)

Last modified November 24, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Vacuolar membrane protein PEP5
Alternative name(s):
    Vacuolar biogenesis protein END1
    Vacuolar protein sorting-associated protein 11
    Vacuolar morphogenesis protein 1
    Vacuolar protein-targeting protein 11
    Carboxypeptidase Y-deficient protein 5
Gene names
Name: PEP5
Synonyms: END1, VAM1, VPL9, VPS11, VPT11
Ordered Locus Names: YMR231W
ORF Names: YM9959.13
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1029 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Required for vacuolar biogenesis and for trafficking of hydrolase precursors to the vacuole. Mediates transport at the vacuolar membrane where it may be responsible for tethering transport vesicles on the target membranes. It is required for gluconeogenic growth of yeast. Acts as component of the HOPS complex that acts during the docking stage of vacuole fusion. HOPS is an effector for the vacuolar Rab GTPase YPT7 and is required for vacuolar SNARE complex assembly. It remains bound to SNARE complexes after vacuole fusion. Ref.4 Ref.6

Subunit structure

Component of the HOPS complex which is composed of PEP5, VPS16, PEP3, VPS33, VPS39 and VPS41. HOPS associates with phosphoinositides and the PX domain of VAM7. Interacts with PEP3, PEP7 and VAM7. Ref.4 Ref.6

Subcellular location

Vacuole membrane; Peripheral membrane protein; Cytoplasmic side.

Miscellaneous

Present with 1200 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

Belongs to the VPS11 family.

Contains 1 clathrin repeat.

Contains 1 RING-type zinc finger.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VAM7P329121EBI-6450,EBI-20232

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10291029Vacuolar membrane protein PEP5
PRO_0000055995

Regions

Zinc finger928 – 97346RING-type

Amino acid modifications

Modified residue6081Phosphothreonine Ref.7 Ref.8
Modified residue6091Phosphothreonine Ref.8

Experimental info

Sequence conflict371A → R in CAA33413. Ref.2
Sequence conflict619 – 6257VFYSYKT → MFFTVTKH in CAA33413. Ref.2
Sequence conflict769 – 7702TK → KQ in CAA33413. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P12868-1 [UniParc].

Last modified August 1, 1991. Version 2.
Checksum: E5216AD3C285CF34

FASTA1,029117,478
        10         20         30         40         50         60 
MSLSSWRQFQ LFENIPIRDP NFGGDSLLYS DPTLCAATIV DPQTLIIAVN SNIIKVVKLN 

        70         80         90        100        110        120 
QSQVIHEFQS FPHDFQITFL KVINGEFLVA LAESIGKPSL IRVYKLEKLP NREQLYHSQV 

       130        140        150        160        170        180 
ELKNGNNTYP ISVVSISNDL SCIVVGFING KIILIRGDIS RDRGSQQRII YEDPSKEPIT 

       190        200        210        220        230        240 
ALFLNNDATA CFAATTSRIL LFNTTGRNRG RPSLVLNSKN GLDLNCGSFN PATNEFICCL 

       250        260        270        280        290        300 
SNFIEFFSSS GKKHQFAFDL SLRKRIFCVD KDHILIVTEE TGVPTTSISV NELSPTIINR 

       310        320        330        340        350        360 
IFIIDAKNKI ISLNFVVSSA IIDIFSTSQS GKNITYLLTS EGVMHRITPK SLENQINIII 

       370        380        390        400        410        420 
QKELYPFALQ LAKQHSLSPL DVQEIHKKYG DYLFKKGLRK EATDQYIQCL DVVETSEIIS 

       430        440        450        460        470        480 
KFGVKEVPDP ESMRNLADYL WSLIKNSISQ RDHVTLLLIV LIKLKDVEGI DTFIQHFDRK 

       490        500        510        520        530        540 
GIWNEGVVMD DMDDVTFFYS DNDFFDLDLI LELMKESDFK RLSYRLAKKY SKDSLIIVDI 

       550        560        570        580        590        600 
LLNLLHNPVK AIKYIKSLPI DETLRCLVTY SKKLLEESPN ETNALLIEVF TGKFKPSTFE 

       610        620        630        640        650        660 
VDLDRRDTTG DFSENIRTVF YSYKTFFNYM NSNGTSDAMS ESSEASHEHE EPTYHPPKPS 

       670        680        690        700        710        720 
IVFSSFVTKP FEFVVFLEAC LACYQQYEGF DEDRQVILTT LYDLYLNLAQ NDVPERIDDW 

       730        740        750        760        770        780 
RSRATGVLRE SNKLVYSAAS NNTSKRVDNS IMLLISHMDQ SSASAKDKTK IDIASFANDN 

       790        800        810        820        830        840 
PEMDLLSTFR AMTLNEEPST CLKFLEKYGT EEPKLLQVAL SYFVSNKLIF KEMGGNEVLK 

       850        860        870        880        890        900 
EKVLRPIIEG ERMPLLDIIK ALSRTNVAHF GLIQDIIIDH VKTEDTEIKR NEKLIESYDK 

       910        920        930        940        950        960 
ELKEKNKKLK NTINSDQPLH VPLKNQTCFM CRLTLDIPVV FFKCGHIYHQ HCLNEEEDTL 

       970        980        990       1000       1010       1020 
ESERKLFKCP KCLVDLETSN KLFEAQHEVV EKNDLLNFAL NSEEGSRDRF KVITEFLGRG 


AISYSDITI 

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References

« Hide 'large scale' references
[1]"Isolation and characterization of PEP5, a gene essential for vacuolar biogenesis in Saccharomyces cerevisiae."
Woolford C.A., Dixon C.K., Manolson M.F., Wright R., Jones E.W.
Genetics 125:739-752(1990) [PubMed: 2204580] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of the END1 gene required for vacuole biogenesis and gluconeogenic growth of budding yeast."
Dulic V., Riezman H.
EMBO J. 8:1349-1359(1989) [PubMed: 2670552] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII."
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. expand/collapse author list , Skelton J., Walsh S.V., Whitehead S., Barrell B.G.
Nature 387:90-93(1997) [PubMed: 9169872] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"Pep3p/Pep5p complex: a putative docking factor at multiple steps of vesicular transport to the vacuole of Saccharomyces cerevisiae."
Srivastava A., Woolford C.A., Jones E.W.
Genetics 156:105-122(2000) [PubMed: 10978279] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PEP3 AND PEP7.
[5]"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].
[6]"Purification of active HOPS complex reveals its affinities for phosphoinositides and the SNARE Vam7p."
Stroupe C., Collins K.M., Fratti R.A., Wickner W.
EMBO J. 25:1579-1589(2006) [PubMed: 16601699] [Abstract]
Cited for: IDENTIFICATION IN THE HOPS COMPLEX, FUNCTION OF THE HOPS COMPLEX, INTERACTION WITH VAM7.
[7]"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases."
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-608, MASS SPECTROMETRY.
[8]"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-608 AND THR-609, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

X54466 Genomic DNA. Translation: CAA38348.1.
X15355 Genomic DNA. Translation: CAA33413.1.
Z49939 Genomic DNA. Translation: CAA90202.1.
PIRS57598.
RefSeqNP_013958.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:4409N.
IntActP12868. 14 interactions.
STRINGP12868.

Genome annotation databases

EnsemblYMR231W; YMR231W; YMR231W; Saccharomyces cerevisiae. [Genome view]
GeneID855271.
KEGGsce:YMR231W.
NMPDRfig|4932.3.peg.5012.

Organism-specific databases

CYGDYMR231w.
SGDS000004844. PEP5.

Phylogenomic databases

HOGENOMP12868.
OMAYHPPKPS
OrthoDBEOG90K9G6

Gene expression databases

ArrayExpressP12868.
GenevestigatorP12868.
GermOnlineYMR231W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR016528. VPS11.
IPR011046. WD40_repeat-like_dom.
IPR001965. Znf_PHD.
IPR001841. Znf_RING.
[Graphical view]
PIRSFPIRSF007860. VPS11. 1 hit.
SMARTSM00249. PHD. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. False negative.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio978885.

Entry information

Entry namePEP5_YEAST
AccessionPrimary (citable) accession number: P12868
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: August 1, 1991
Last modified: November 24, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Yeast

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

Yeast chromosome XIII

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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents