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O13849 (CBPY_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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

Short name=CPY
EC=3.4.16.5
Gene names
Name:cpy1
Synonyms:pcy1
ORF Names:SPAC19G12.10c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length1002 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Subunit structure

Heterodimer of two subunits of 32 kDa and 19 kDa derived from the precursor protein and linked by a disulfide bond. Ref.1

Subcellular location

Vacuole. Note: Lysosome-like vacuoles. Ref.1

Sequence similarities

Belongs to the peptidase S10 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Propeptide19 – 521503 Potential
PRO_0000004295
Chain522 – 1002481Carboxypeptidase Y
PRO_0000004296

Regions

Repeat225 – 237131-1
Repeat238 – 250131-2
Repeat251 – 263131-3
Repeat264 – 276131-4
Repeat277 – 289131-5
Repeat290 – 302131-6
Repeat303 – 315131-7
Repeat316 – 328131-8
Repeat329 – 341131-9
Repeat361 – 36992-1
Repeat370 – 37892-2
Repeat379 – 38792-3
Repeat388 – 39692-4
Repeat397 – 40592-5
Repeat406 – 41492-6
Repeat415 – 42392-7; approximate
Region225 – 3411179 X 13 AA tandem repeats of M-H-H-E-P-G-E-H-M-P-P-P-P
Region361 – 423637 X 9 AA tandem repeats of D-K-E-H-H-K-G-P-K
Compositional bias208 – 341134Pro-rich

Sites

Active site7151 By similarity
Active site9211 By similarity
Active site9781 By similarity
Binding site9241Substrate By similarity
Binding site9791Substrate By similarity

Amino acid modifications

Glycosylation6591N-linked (GlcNAc...) Potential
Disulfide bond627 ↔ 880 By similarity
Disulfide bond776 ↔ 789 By similarity
Disulfide bond799 ↔ 822 By similarity
Disulfide bond806 ↔ 815 By similarity
Disulfide bond844 ↔ 851 By similarity

Experimental info

Mutagenesis6271C → T: 36% of original activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O13849 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 4A8D81CFDAB2D854

FASTA1,002114,237
        10         20         30         40         50         60 
MLMKQTFLYF LLTCVVSAQF NGYVPPEQNG GDIVVPKDFY EKFGEDFIRE QEESSAPLMN 

        70         80         90        100        110        120 
PVPERDEAEA PHHPKGHHEF NDDFEDDTAL EHPGFKDKLD SFLQPARDFL HTVSDRLDNI 

       130        140        150        160        170        180 
FDDDEDEHVR EKRPHDSADE DAPRRKHGKC KGKGKHHKGK HAKGKGKKSH PKPEDDSVFF 

       190        200        210        220        230        240 
DDERPKHHEF DDEDREFPAH HEPGEHMPPP PMHHKPGEHM PPPPMHHEPG EHMPPPPMHH 

       250        260        270        280        290        300 
EPGEHMPPPP MHHEPGEHMP PPPMHHEPGE HMPPPPMHHE PGEHMPPPPM HHEPGEHMPP 

       310        320        330        340        350        360 
PPMHHEPGEH MPPPPMHHEP GEHMPPPPMH HEPGEHMPPP PFKHHELEEH EGPEHHRGPE 

       370        380        390        400        410        420 
DKEHHKGPKD KEHHKGPKDK EHHKGPKDKE HHKGPKDKEH HKGPKDKEHH KGPKDKEHHQ 

       430        440        450        460        470        480 
GPKEKHNERP EQNMQSSHEL LVIEAFADLI NSVPVEEIAE EFSRFLDTLG IEYYGNIPVH 

       490        500        510        520        530        540 
IQENAPKDSS IPPLFEFDDD LELSDLTPEQ FAYLEMLKAE GIDPMTAFRD QSHPAKPSNA 

       550        560        570        580        590        600 
QPADSSRPYA VFSQEENGEH VNLKAFPDHT LRVKDSKPES LGIDTVKQYT GYLDVEDDRH 

       610        620        630        640        650        660 
LFFWFFESRN DPENDPVVLW LNGGPGCSSL TGLFMELGPS SINIETLKPE YNPHSWNSNA 

       670        680        690        700        710        720 
SVIFLDQPIN TGFSNGDDSV LDTVTAGKDV YAFLNLFFAK FPQYAHLDFH IAGESYAGHY 

       730        740        750        760        770        780 
IPQFAKEIME HNQGANFFVA SGYEMEKQYI NLKSVLIGNG LTDPLVQYYF YGKMACESPY 

       790        800        810        820        830        840 
GPIMSQEECD RITGAYDTCA KLITGCYQTG FTPVCIGASL YCNNAMIGPF TKTGLNIYDI 

       850        860        870        880        890        900 
REECRDQEHL CYPETGAIES YLNQEFVQEA LGVEYDYKGC NTEVNIGFLF KGDWMRKTFR 

       910        920        930        940        950        960 
DDVTAILEAG LPVLIYAGDA DYICNYMGNE AWTDALEWAG QREFYEAELK PWSPNGKEAG 

       970        980        990       1000 
RGKSFKNFGY LRLYEAGHMV PFNQPEASLE MLNSWIDGSL FA 

« Hide

References

« Hide 'large scale' references
[1]"Vacuolar protein sorting in fission yeast: cloning, biosynthesis, transport, and processing of carboxypeptidase Y from Schizosaccharomyces pombe."
Tabuchi M., Iwaihara O., Ohtani Y., Ohuchi N., Sakurai J., Morita T., Iwahara S., Takegawa K.
J. Bacteriol. 179:4179-4189(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-627.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D86560 Genomic DNA. Translation: BAA25568.1.
CU329670 Genomic DNA. Translation: CAB10121.1.
PIRT43236.
RefSeqNP_594425.1. NM_001019854.2.

3D structure databases

ProteinModelPortalO13849.
SMRO13849. Positions 572-1000.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278926. 4 interactions.
IntActO13849. 1 interaction.
MINTMINT-4668478.
STRING4896.SPAC19G12.10c-1.

Protein family/group databases

MEROPSS10.A66.

Proteomic databases

PaxDbO13849.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC19G12.10c.1; SPAC19G12.10c.1:pep; SPAC19G12.10c.
GeneID2542465.
KEGGspo:SPAC19G12.10c.

Organism-specific databases

PomBaseSPAC19G12.10c.

Phylogenomic databases

eggNOGCOG2939.
KOK13289.
OrthoDBEOG7XDBR1.

Family and domain databases

InterProIPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
PROSITEPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20803521.

Entry information

Entry nameCBPY_SCHPO
AccessionPrimary (citable) accession number: O13849
Secondary accession number(s): O14366
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 104 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

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

Peptidase families

Classification of peptidase families and list of entries