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Reviewed, UniProtKB/Swiss-Prot Q10071 (STE24_SCHPO)

Last modified June 16, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Probable CAAX prenyl protease 1
    EC=3.4.24.84
Alternative name(s):
    Prenyl protein-specific endoprotease 1
      Short name=PPSEP 1
Gene names
ORF Names: SPAC3H1.05
OrganismSchizosaccharomyces pombe (Fission yeast) [Complete proteome]
Taxonomic identifier4896 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

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Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Proteolytically removes the C-terminal three residues of farnesylated proteins By similarity.

Catalytic activity

The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the peptidase M48A family.

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Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentendoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Probable CAAX prenyl protease 1
PRO_0000138847

Regions

Transmembrane103 – 12321 Potential
Transmembrane196 – 21621 Potential
Transmembrane230 – 25021 Potential
Transmembrane344 – 36421 Potential
Transmembrane381 – 40121 Potential

Sites

Active site3331 By similarity
Active site4151Proton donor By similarity
Metal binding3321Zinc; catalytic By similarity
Metal binding3361Zinc; catalytic By similarity
Metal binding4111Zinc; catalytic By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q10071-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 50AC2F96E25C76C5

FASTA47454,001
        10         20         30         40         50         60 
MSPGLCFLKE ISVIQATPKP TTRSFANCCK MGILQHLMHI LDIPGFPWKI VIAGFSIGKY 

        70         80         90        100        110        120 
AWDLYLRRRQ VPYLLREKPP AILAEHVDEK KYQKALSYAR DKSWFSTIVS TFTLAVDLLI 

       130        140        150        160        170        180 
IKYDGLSYLW NITKFPWMDK LAASSSRFSL STSITHSCVF MFGLTLFSRL IQIPFNLYST 

       190        200        210        220        230        240 
FVIEEKYGFN KSTLKIFVID LLKELSLGGL LMSVVVGVFV KILTKFGDNF IMYAWGAYIV 

       250        260        270        280        290        300 
FGLILQTIAP SLIMPLFYKF TPLENGSLRT QIEELAASIN FPLKKLYVID ASRRSTHSNA 

       310        320        330        340        350        360 
FFYGLPWNKG IVLFDTLVKN HTEPELIAIL GHELGHWYMS HNLINTIIDY GMSLFHLFLF 

       370        380        390        400        410        420 
AAFIRNNSLY TSFNFITEKP VIVGLLLFSD ALGPLSSILT FASNKVSRLC EYQADAFAKQ 

       430        440        450        460        470 
LGYAKDLGDG LIRIHDDNLS PLEFDSLYTS YYHSHPILVD RLNAIDYTTL KKNN

« Hide

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References

[1]"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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 38366 / 972.

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Cross-references

Sequence databases

CU329670 Genomic DNA. Translation: CAA92258.1.
PIRT38737.
RefSeqNP_593547.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

MEROPSM48.001.

Genome annotation databases

GeneID2543456.
KEGGspo:SPAC3H1.05.
NMPDRfig|4896.1.peg.3517.

Organism-specific databases

GeneDB_SpombeSPAC3H1.05.

Phylogenomic databases

OMAQ10071. KAADYTI.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-001224-MON.
BRENDA3.4.24.84. 653.

Gene expression databases

ArrayExpressQ10071.

Family and domain databases

InterProIPR006025. Pept_M_Zn_BS.
IPR001915. Peptidase_M48.
[Graphical view]
PfamPF01435. Peptidase_M48. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSTE24_SCHPO
AccessionPrimary (citable) accession number: Q10071
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents