Skip Header

Contribute Send feedback
Read comments (?) or add your own

P07267 (CARP_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Saccharopepsin
EC=3.4.23.25
Alternative name(s):
Aspartate protease
Short name=Proteinase A
Carboxypeptidase Y-deficient protein 4
Proteinase YSCA
Gene names
Name:PEP4
Synonyms:PHO9, PRA1
Ordered Locus Names:YPL154C
ORF Names:P2585
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.

Catalytic activity

Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.

Subcellular location

Vacuole. Note: Lysosome-like vacuoles.

Sequence similarities

Belongs to the peptidase A1 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RTN1Q049474EBI-4040,EBI-38020

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.8
Propeptide23 – 7654Activation peptide
PRO_0000025873
Chain77 – 405329Saccharopepsin
PRO_0000025874

Sites

Active site1091 By similarity
Active site2941 By similarity

Amino acid modifications

Glycosylation1441N-linked (GlcNAc...)
Glycosylation3451N-linked (GlcNAc...)
Disulfide bond122 ↔ 127
Disulfide bond328 ↔ 361

Experimental info

Mutagenesis2941D → A: Inactivation. Ref.9

Secondary structure

1 ............................................................................ 405
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07267 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: B0AA36BA098D2BF7

FASTA40544,499
        10         20         30         40         50         60 
MFSLKALLPL ALLLVSANQV AAKVHKAKIY KHELSDEMKE VTFEQHLAHL GQKYLTQFEK 

        70         80         90        100        110        120 
ANPEVVFSRE HPFFTEGGHD VPLTNYLNAQ YYTDITLGTP PQNFKVILDT GSSNLWVPSN 

       130        140        150        160        170        180 
ECGSLACFLH SKYDHEASSS YKANGTEFAI QYGTGSLEGY ISQDTLSIGD LTIPKQDFAE 

       190        200        210        220        230        240 
ATSEPGLTFA FGKFDGILGL GYDTISVDKV VPPFYNAIQQ DLLDEKRFAF YLGDTSKDTE 

       250        260        270        280        290        300 
NGGEATFGGI DESKFKGDIT WLPVRRKAYW EVKFEGIGLG DEYAELESHG AAIDTGTSLI 

       310        320        330        340        350        360 
TLPSGLAEMI NAEIGAKKGW TGQYTLDCNT RDNLPDLIFN FNGYNFTIGP YDYTLEVSGS 

       370        380        390        400 
CISAITPMDF PEPVGPLAIV GDAFLRKYYS IYDLGNNAVG LAKAI

« Hide

References

« Hide 'large scale' references
[1]"The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases."
Woolford C.A., Daniels L.B., Park F.J., Jones E.W., van Arsdell J.N., Innis M.A.
Mol. Cell. Biol. 6:2500-2510(1986) [PubMed: 3537721] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors."
Ammerer G., Hunter C.P., Rothman J.H., Saari G.C., Valls L.A., Stevens T.H.
Mol. Cell. Biol. 6:2490-2499(1986) [PubMed: 3023936] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a small nuclear RNA, a new putative protein kinase and two new putative regulators."
Purnelle B., Coster F., Goffeau A.
Yeast 12:1483-1492(1996) [PubMed: 8948103] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed: 9169875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"Primary structure of the aspartic proteinase A from Saccharomyces cerevisiae."
Dreyer T., Halkier B., Svendsen I., Ottesen M.
Carlsberg Res. Commun. 51:27-41(1986)
Cited for: PROTEIN SEQUENCE OF 77-405.
[7]"Kinesin-related proteins required for assembly of the mitotic spindle."
Roof D.M., Meluh P.B., Rose M.D.
J. Cell Biol. 118:95-108(1992) [PubMed: 1618910] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 373-405.
Strain: ATCC 204508 / S288c.
[8]"Vacuolar and extracellular maturation of Saccharomyces cerevisiae proteinase A."
Wolff A.M., Dimn N., Petersen J.G.L.
Yeast 12:823-832(1996) [PubMed: 8840499] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-31 AND 68-86.
[9]"Biogenesis of the yeast vacuole (lysosome). Active site mutation in the vacuolar aspartate proteinase yscA blocks maturation of vacuolar proteinases."
Rupp S., Hirsch H.H., Wolf D.H.
FEBS Lett. 293:62-66(1991) [PubMed: 1959673] [Abstract]
Cited for: MUTAGENESIS OF ASP-294.
[10]"The three-dimensional structure at 2.4-A resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae."
Aguilar C.F., Cronin N.B., Badasso M., Dreyer T., Newman M.P., Cooper J.B., Hoover D.J., Wood S.P., Johnson M.S., Blundell T.L.
J. Mol. Biol. 267:899-915(1997) [PubMed: 9135120] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M13358 Genomic DNA. Translation: AAB63975.1.
X96770 Genomic DNA. Translation: CAA65567.1.
Z73510 Genomic DNA. Translation: CAA97859.1.
Z11963 Genomic DNA. Translation: CAA78020.1.
BK006949 Genomic DNA. Translation: DAA11280.1.
PIRA25379.
RefSeqNP_015171.1. NM_001183968.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DP5X-ray2.20A77-405[»]
1DPJX-ray1.80A77-405[»]
1FMUX-ray2.70A77-405[»]
1FMXX-ray2.61A/B77-405[»]
1FQ4X-ray2.70A77-405[»]
1FQ5X-ray2.40A77-405[»]
1FQ6X-ray2.70A77-405[»]
1FQ7X-ray2.80A77-405[»]
1FQ8X-ray2.80A77-405[»]
1G0VX-ray2.00A78-405[»]
2JXRX-ray2.40A77-405[»]
ProteinModelPortalP07267.
SMRP07267. Positions 77-405.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-4442N.
IntActP07267. 7 interactions.
MINTMINT-382859.
STRINGP07267.

Protein family/group databases

MEROPSA01.018.

2D gel databases

UCD-2DPAGEP07267.

Proteomic databases

PeptideAtlasP07267.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL154C; YPL154C; YPL154C.
GeneID855949.
KEGGsce:YPL154C.
NMPDRfig|4932.3.peg.6300.

Organism-specific databases

CYGDYPL154c.
SGDS000006075. PEP4.

Phylogenomic databases

eggNOGfuNOG05565.
GeneTreeEFGT00050000001345.
HOGENOMHBG590923.
OMANFTIGPY.
OrthoDBEOG4PVS7C.

Gene expression databases

ArrayExpressP07267.
GenevestigatorP07267.
GermOnlineYPL154C. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
KOK01381.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. Pept_Aspartic. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio980726.
PMAP-CutDBP07267.

Entry information

Entry nameCARP_YEAST
AccessionPrimary (citable) accession number: P07267
Secondary accession number(s): D6W3L4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: December 14, 2011
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

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

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents