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Protein

Carboxypeptidase Y

Gene

cpy1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei715 – 7151PROSITE-ProRule annotation
Active sitei921 – 9211PROSITE-ProRule annotation
Binding sitei924 – 9241SubstrateBy similarity
Active sitei978 – 9781PROSITE-ProRule annotation
Binding sitei979 – 9791SubstrateBy similarity

GO - Molecular functioni

  1. serine-type carboxypeptidase activity Source: PomBase

GO - Biological processi

  1. protein catabolic process in the vacuole Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Protease

Protein family/group databases

MEROPSiS10.A66.

Names & Taxonomyi

Protein namesi
Recommended name:
Carboxypeptidase Y (EC:3.4.16.5)
Short name:
CPY
Gene namesi
Name:cpy1
Synonyms:pcy1
ORF Names:SPAC19G12.10c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC19G12.10c.

Subcellular locationi

Vacuole 1 Publication
Note: Lysosome-like vacuoles.

GO - Cellular componenti

  1. cytoplasm Source: PomBase
  2. fungal-type vacuole Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi627 – 6271C → T: 36% of original activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Propeptidei19 – 521503Sequence AnalysisPRO_0000004295Add
BLAST
Chaini522 – 1002481Carboxypeptidase YPRO_0000004296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi627 ↔ 880By similarity
Glycosylationi659 – 6591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi776 ↔ 789By similarity
Disulfide bondi799 ↔ 822By similarity
Disulfide bondi806 ↔ 815By similarity
Disulfide bondi844 ↔ 851By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiO13849.
PaxDbiO13849.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi278926. 4 interactions.
IntActiO13849. 1 interaction.
MINTiMINT-4668478.
STRINGi4896.SPAC19G12.10c-1.

Structurei

3D structure databases

ProteinModelPortaliO13849.
SMRiO13849. Positions 572-1000.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati225 – 237131-1Add
BLAST
Repeati238 – 250131-2Add
BLAST
Repeati251 – 263131-3Add
BLAST
Repeati264 – 276131-4Add
BLAST
Repeati277 – 289131-5Add
BLAST
Repeati290 – 302131-6Add
BLAST
Repeati303 – 315131-7Add
BLAST
Repeati316 – 328131-8Add
BLAST
Repeati329 – 341131-9Add
BLAST
Repeati361 – 36992-1
Repeati370 – 37892-2
Repeati379 – 38792-3
Repeati388 – 39692-4
Repeati397 – 40592-5
Repeati406 – 41492-6
Repeati415 – 42392-7; approximate

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni225 – 3411179 X 13 AA tandem repeats of M-H-H-E-P-G-E-H-M-P-P-P-PAdd
BLAST
Regioni361 – 423637 X 9 AA tandem repeats of D-K-E-H-H-K-G-P-KAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi208 – 341134Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S10 family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG2939.
InParanoidiO13849.
KOiK13289.
OrthoDBiEOG7XDBR1.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O13849-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLMKQTFLYF LLTCVVSAQF NGYVPPEQNG GDIVVPKDFY EKFGEDFIRE
60 70 80 90 100
QEESSAPLMN PVPERDEAEA PHHPKGHHEF NDDFEDDTAL EHPGFKDKLD
110 120 130 140 150
SFLQPARDFL HTVSDRLDNI FDDDEDEHVR EKRPHDSADE DAPRRKHGKC
160 170 180 190 200
KGKGKHHKGK HAKGKGKKSH PKPEDDSVFF DDERPKHHEF DDEDREFPAH
210 220 230 240 250
HEPGEHMPPP PMHHKPGEHM PPPPMHHEPG EHMPPPPMHH EPGEHMPPPP
260 270 280 290 300
MHHEPGEHMP PPPMHHEPGE HMPPPPMHHE PGEHMPPPPM HHEPGEHMPP
310 320 330 340 350
PPMHHEPGEH MPPPPMHHEP GEHMPPPPMH HEPGEHMPPP PFKHHELEEH
360 370 380 390 400
EGPEHHRGPE DKEHHKGPKD KEHHKGPKDK EHHKGPKDKE HHKGPKDKEH
410 420 430 440 450
HKGPKDKEHH KGPKDKEHHQ GPKEKHNERP EQNMQSSHEL LVIEAFADLI
460 470 480 490 500
NSVPVEEIAE EFSRFLDTLG IEYYGNIPVH IQENAPKDSS IPPLFEFDDD
510 520 530 540 550
LELSDLTPEQ FAYLEMLKAE GIDPMTAFRD QSHPAKPSNA QPADSSRPYA
560 570 580 590 600
VFSQEENGEH VNLKAFPDHT LRVKDSKPES LGIDTVKQYT GYLDVEDDRH
610 620 630 640 650
LFFWFFESRN DPENDPVVLW LNGGPGCSSL TGLFMELGPS SINIETLKPE
660 670 680 690 700
YNPHSWNSNA SVIFLDQPIN TGFSNGDDSV LDTVTAGKDV YAFLNLFFAK
710 720 730 740 750
FPQYAHLDFH IAGESYAGHY IPQFAKEIME HNQGANFFVA SGYEMEKQYI
760 770 780 790 800
NLKSVLIGNG LTDPLVQYYF YGKMACESPY GPIMSQEECD RITGAYDTCA
810 820 830 840 850
KLITGCYQTG FTPVCIGASL YCNNAMIGPF TKTGLNIYDI REECRDQEHL
860 870 880 890 900
CYPETGAIES YLNQEFVQEA LGVEYDYKGC NTEVNIGFLF KGDWMRKTFR
910 920 930 940 950
DDVTAILEAG LPVLIYAGDA DYICNYMGNE AWTDALEWAG QREFYEAELK
960 970 980 990 1000
PWSPNGKEAG RGKSFKNFGY LRLYEAGHMV PFNQPEASLE MLNSWIDGSL

FA
Length:1,002
Mass (Da):114,237
Last modified:January 1, 1998 - v1
Checksum:i4A8D81CFDAB2D854
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86560 Genomic DNA. Translation: BAA25568.1.
CU329670 Genomic DNA. Translation: CAB10121.1.
PIRiT43236.
RefSeqiNP_594425.1. NM_001019854.2.

Genome annotation databases

EnsemblFungiiSPAC19G12.10c.1; SPAC19G12.10c.1:pep; SPAC19G12.10c.
GeneIDi2542465.
KEGGispo:SPAC19G12.10c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D86560 Genomic DNA. Translation: BAA25568.1.
CU329670 Genomic DNA. Translation: CAB10121.1.
PIRiT43236.
RefSeqiNP_594425.1. NM_001019854.2.

3D structure databases

ProteinModelPortaliO13849.
SMRiO13849. Positions 572-1000.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278926. 4 interactions.
IntActiO13849. 1 interaction.
MINTiMINT-4668478.
STRINGi4896.SPAC19G12.10c-1.

Protein family/group databases

MEROPSiS10.A66.

Proteomic databases

MaxQBiO13849.
PaxDbiO13849.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC19G12.10c.1; SPAC19G12.10c.1:pep; SPAC19G12.10c.
GeneIDi2542465.
KEGGispo:SPAC19G12.10c.

Organism-specific databases

PomBaseiSPAC19G12.10c.

Phylogenomic databases

eggNOGiCOG2939.
InParanoidiO13849.
KOiK13289.
OrthoDBiEOG7XDBR1.

Miscellaneous databases

NextBioi20803521.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR001563. Peptidase_S10.
IPR018202. Peptidase_S10_AS.
[Graphical view]
PANTHERiPTHR11802. PTHR11802. 1 hit.
PfamiPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSiPR00724. CRBOXYPTASEC.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00131. CARBOXYPEPT_SER_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCBPY_SCHPO
AccessioniPrimary (citable) accession number: O13849
Secondary accession number(s): O14366
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: January 1, 1998
Last modified: January 7, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.