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Q2TYA1 (CBPYA_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carboxypeptidase Y homolog A

EC=3.4.16.5
Gene names
Name:cpyA
ORF Names:AO090103000332
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Vacuolar carboxypeptidase involved in degradation of small peptides. Digests preferentially peptides containing an aliphatic or hydrophobic residue in P1' position, as well as methionine, leucine or phenylalanine in P1 position of ester substrate By similarity.

Catalytic activity

Release of a C-terminal amino acid with broad specificity.

Subcellular location

Vacuole. Note: Requires vps10 for correct vacuolar localization. Ref.2 Ref.3 Ref.4

Sequence similarities

Belongs to the peptidase S10 family.

Ontologies

Keywords
   Cellular componentVacuole
   DomainSignal
   Molecular functionCarboxypeptidase
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from direct assay PubMed 21512241. Source: ASPGD

   Cellular_componentfungal-type vacuole lumen

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionserine-type carboxypeptidase activity

Inferred from direct assay PubMed 10427010PubMed 21512241. Source: ASPGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 123106 By similarity
PRO_0000407437
Chain124 – 542419Carboxypeptidase Y homolog A
PRO_0000407438

Sites

Active site2651 By similarity
Active site4571 By similarity
Active site5191 By similarity

Amino acid modifications

Glycosylation2091N-linked (GlcNAc...) Potential
Glycosylation5081N-linked (GlcNAc...) Potential
Disulfide bond178 ↔ 418 By similarity
Disulfide bond312 ↔ 326 By similarity
Disulfide bond336 ↔ 359 By similarity
Disulfide bond343 ↔ 352 By similarity
Disulfide bond381 ↔ 388 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2TYA1 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: BD339D3954E9EB3A

FASTA54260,892
        10         20         30         40         50         60 
MRVLPATLLV GAASAAVPPL QQVLGRPEEG MSFSKPLHAF QEQLKTLSED ARKLWDEVAN 

        70         80         90        100        110        120 
YFPDSMDHSP IFSLPKKHTR RPDSHWDHIV RGSDVQKIWV NNADGEKERE IDGKLEAYDL 

       130        140        150        160        170        180 
RIKKADPSAL GIDPNVKQYT GYLDDNGNDK HLFYWFFESR NDPKNDPVVL WLNGGPGCSS 

       190        200        210        220        230        240 
LTGLFMELGP SSIDENIKPV YNDFSWNSNA SVIFLDQPVN VGYSYSGSAV SDTVAAGKDV 

       250        260        270        280        290        300 
YALLSLFFKQ FPEYAEQDFH IAGESYAGHY IPVFASEILA HKNRNINLKS VLIGNGLTDG 

       310        320        330        340        350        360 
LTQYGYYRPM GCGEGGYKAV LDEATCESMD NALPRCRSMI ESCYNSESAW VCVPASIYCN 

       370        380        390        400        410        420 
NALIGPYQRT GQNVYDVRSK CEDESNLCYK GMGYVSEYLN KAEVREAVGA EVGGYDSCNF 

       430        440        450        460        470        480 
DINRNFLFHG DWMKPYHRLV PGLLEQIPVL IYAGDADYIC NWLGNKAWTE ALEWPGQKEY 

       490        500        510        520        530        540 
ASAELEDLKI EQNEHTGKKI GQVKSHGNFT FMRLYGGGHM VPMDQPEASL EFFNRWLGGE 


WF 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequencing and analysis of Aspergillus oryzae."
Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E. expand/collapse author list , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 42149 / RIB 40.
[2]"Visualization of vacuoles in Aspergillus oryzae by expression of CPY-EGFP."
Ohneda M., Arioka M., Nakajima H., Kitamoto K.
Fungal Genet. Biol. 37:29-38(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[3]"Isolation and characterization of Aspergillus oryzae vacuolar protein sorting mutants."
Ohneda M., Arioka M., Kitamoto K.
Appl. Environ. Microbiol. 71:4856-4861(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[4]"Enhanced production and secretion of heterologous proteins by the filamentous fungus Aspergillus oryzae via disruption of vacuolar protein sorting receptor gene Aovps10."
Yoon J., Aishan T., Maruyama J., Kitamoto K.
Appl. Environ. Microbiol. 76:5718-5727(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007174 Genomic DNA. Translation: BAE65772.1.
RefSeqXP_001826905.1. XM_001826853.2.

3D structure databases

ProteinModelPortalQ2TYA1.
SMRQ2TYA1. Positions 123-539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5062.CADAORAP00010017.

Protein family/group databases

MEROPSS10.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00010224; CADAORAP00010017; CADAORAG00010224.
GeneID5999027.
KEGGaor:AOR_1_542034.

Phylogenomic databases

eggNOGCOG2939.
HOGENOMHOG000198296.
KOK13289.
OMAHYRPMAC.
OrthoDBEOG7XDBR1.

Family and domain databases

InterProIPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
IPR008442. Propeptide_carboxypepY.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF05388. Carbpep_Y_N. 1 hit.
PF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
PROSITEPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBPYA_ASPOR
AccessionPrimary (citable) accession number: Q2TYA1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 3, 2011
Last sequence update: January 24, 2006
Last modified: February 19, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries