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Protein

Vacuolar segregation protein PEP7

Gene

PEP7

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for vacuole segregation and vacuole protein sorting. Possibly part of a complex which tethers the vacuole membrane to microtubules, either directly or via kinesin or dynein-like motor proteins. Probably functions in several interorganelle traffic pathways.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri6 – 2924C2H2-typeAdd
BLAST
Zinc fingeri72 – 13766FYVE-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri215 – 29783FYVE-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • phosphatidylinositol-3-phosphate binding Source: SGD

GO - Biological processi

  • Golgi to endosome transport Source: SGD
  • Golgi to vacuole transport Source: SGD
  • vacuole inheritance Source: SGD
  • vesicle docking involved in exocytosis Source: SGD
  • vesicle fusion Source: SGD
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-29880-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar segregation protein PEP7
Alternative name(s):
Carboxypeptidase Y-deficient protein 7
Protein VAC1
Vacuolar protein sorting-associated protein 19
Vacuolar protein-targeting protein 19
Gene namesi
Name:PEP7
Synonyms:VAC1, VPL21, VPS19, VPT19
Ordered Locus Names:YDR323C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR323C.
SGDiS000002731. PEP7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoplasmic side of endosome membrane Source: SGD
  • vacuolar membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Vacuole

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515Vacuolar segregation protein PEP7PRO_0000046858Add
BLAST

Proteomic databases

MaxQBiP32609.

Interactioni

Subunit structurei

Interacts with VPS21, VPS45, PEP3 and PEP5.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
VPS45P389323EBI-20208,EBI-20444

Protein-protein interaction databases

BioGridi32381. 104 interactions.
DIPiDIP-5240N.
IntActiP32609. 5 interactions.
MINTiMINT-541674.

Structurei

3D structure databases

ProteinModelPortaliP32609.
SMRiP32609. Positions 66-138, 211-296, 463-504.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Contains 1 C2H2-type zinc finger.Curated
Contains 2 FYVE-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri6 – 2924C2H2-typeAdd
BLAST
Zinc fingeri72 – 13766FYVE-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri215 – 29783FYVE-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

HOGENOMiHOG000001058.
InParanoidiP32609.
KOiK12481.
OMAiQRNFIKL.
OrthoDBiEOG7VB2QK.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR021565. Rbsn_Rab_binding_dom.
IPR007087. Znf_C2H2.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF11464. Rbsn. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS50178. ZF_FYVE. 2 hits.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32609-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLENVSCPI CLRKFDNLQA LNAHLDVEHG FNDNEDSLGS NDSRLVNGKQ
60 70 80 90 100
KKARSVDSSA QKLKRSHWEK FKKGKSCCHT CGRTLNNNIG AINCRKCGKL
110 120 130 140 150
YCRRHLPNMI KLNLSAQYDP RNGKWYNCCH DCFVTKPGYN DYGEVIDLTP
160 170 180 190 200
EFFKVRNIKR EDKNLRLLQL ENRFVRLVDG LITLYNTYSR SIIHNLKMNS
210 220 230 240 250
EMSKLERTVT PWRDDRSVLF CNICSEPFGL LLRKHHCRLC GMVVCDDANR
260 270 280 290 300
NCSNEISIGY LMSAASDLPF EYNIQKDDLL HIPISIRLCS HCIDMLFIGR
310 320 330 340 350
KFNKDVRMPL SGIFAKYDSM QNISKVIDSL LPIFEDSLNS LKVETAKDSE
360 370 380 390 400
NTLDPKNLND LARLRHKLLN SFNLYNTLTR QLLSVEPQSH LERQLQNSIK
410 420 430 440 450
IASAAYINEK ILPLKSLPAI LNPEGHKTNE DGQKAEPEVK KLSQLMIENL
460 470 480 490 500
TIKEVKELRE ELMVLKEQSY LIESTIQDYK KQRRLEEIVT LNKNLEELHS
510
RIHTVQSKLG DHGFN
Length:515
Mass (Da):59,443
Last modified:September 27, 2004 - v2
Checksum:i53C304F1ADA5B7A1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti366 – 3661H → Y in AAA35203 (PubMed:1730622).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80596 Genomic DNA. Translation: AAA35203.1.
U22070 Genomic DNA. Translation: AAB60290.1.
U32517 Genomic DNA. Translation: AAB64759.1.
BK006938 Genomic DNA. Translation: DAA12166.1.
PIRiS59811.
RefSeqiNP_010610.3. NM_001180631.3.

Genome annotation databases

EnsemblFungiiYDR323C; YDR323C; YDR323C.
GeneIDi851923.
KEGGisce:YDR323C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80596 Genomic DNA. Translation: AAA35203.1.
U22070 Genomic DNA. Translation: AAB60290.1.
U32517 Genomic DNA. Translation: AAB64759.1.
BK006938 Genomic DNA. Translation: DAA12166.1.
PIRiS59811.
RefSeqiNP_010610.3. NM_001180631.3.

3D structure databases

ProteinModelPortaliP32609.
SMRiP32609. Positions 66-138, 211-296, 463-504.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32381. 104 interactions.
DIPiDIP-5240N.
IntActiP32609. 5 interactions.
MINTiMINT-541674.

Proteomic databases

MaxQBiP32609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR323C; YDR323C; YDR323C.
GeneIDi851923.
KEGGisce:YDR323C.

Organism-specific databases

EuPathDBiFungiDB:YDR323C.
SGDiS000002731. PEP7.

Phylogenomic databases

HOGENOMiHOG000001058.
InParanoidiP32609.
KOiK12481.
OMAiQRNFIKL.
OrthoDBiEOG7VB2QK.

Enzyme and pathway databases

BioCyciYEAST:G3O-29880-MONOMER.

Miscellaneous databases

NextBioi969971.
PROiP32609.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
InterProiIPR021565. Rbsn_Rab_binding_dom.
IPR007087. Znf_C2H2.
IPR000306. Znf_FYVE.
IPR017455. Znf_FYVE-rel.
IPR011011. Znf_FYVE_PHD.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF01363. FYVE. 1 hit.
PF11464. Rbsn. 1 hit.
[Graphical view]
SMARTiSM00064. FYVE. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 2 hits.
PROSITEiPS50178. ZF_FYVE. 2 hits.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of VAC1, a gene required for vacuole inheritance and vacuole protein sorting."
    Weisman L.S., Wickner W.
    J. Biol. Chem. 267:618-623(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: LWY148.
  2. "Pep7p provides a novel protein that functions in vesicle-mediated transport between the yeast Golgi and endosome."
    Webb G.C., Zhang J., Garlow S.J., Wesp A., Riezman H., Jones E.W.
    Mol. Biol. Cell 8:871-895(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: ATCC 204508 / S288c.
  3. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "The phosphatidylinositol 3-phosphate binding protein Vac1p interacts with a Rab GTPase and a Sec1p homologue to facilitate vesicle-mediated vacuolar protein sorting."
    Tall G.G., Hama H., DeWald D.B., Horazdovsky B.F.
    Mol. Biol. Cell 10:1873-1889(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VPS21 AND VPS45, SUBCELLULAR LOCATION.
  6. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PEP3 AND PEP5.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPEP7_YEAST
AccessioniPrimary (citable) accession number: P32609
Secondary accession number(s): D6VSV6, Q99229
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: September 27, 2004
Last modified: May 11, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 768 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.