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O60123 (KEX1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. 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:
Pheromone-processing carboxypeptidase kex1

EC=3.4.16.6
Alternative name(s):
Carboxypeptidase D
Gene names
Name:kex1
ORF Names:SPBC16G5.09
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Protease with a carboxypeptidase B-like function involved in the C-terminal processing of the lysine and arginine residues from protein precursors. Promotes cell fusion and is involved in the programmed cell death By similarity.

Catalytic activity

Preferential release of a C-terminal arginine or lysine residue.

Subcellular location

Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein By similarity. Vacuole membrane; Single-pass type I membrane protein Ref.2.

Sequence similarities

Belongs to the peptidase S10 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 510489Pheromone-processing carboxypeptidase kex1
PRO_0000314765

Regions

Topological domain22 – 468447Lumenal Potential
Transmembrane469 – 48921Helical; Potential
Topological domain490 – 51021Cytoplasmic Potential

Sites

Active site1751 By similarity
Active site3671 By similarity
Active site4271 By similarity

Amino acid modifications

Glycosylation511N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation3921N-linked (GlcNAc...) Potential
Glycosylation4161N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
O60123 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 9D0D6B82FD1BC9E2

FASTA51057,644
        10         20         30         40         50         60 
MISKLLKIVL LTAGVIGNTL ADSRIHEQYL VKAFPNEPVD YEGRMHAGHL NQTDQLDGDL 

        70         80         90        100        110        120 
FFWMFESVKP EYEHRSILWL NGGPGCSSED GSLMEVGPFR LDDNNTFQLN PGRWDELGNL 

       130        140        150        160        170        180 
LFVDQPLGTG YSYSLAKDFQ SNNEKMANDF SIFFEKFLEE FPERANDEWF IAGESFAGQY 

       190        200        210        220        230        240 
IPHIAAKLKE KNLVNLGGLA IGNGWINPLS HYETYLNYLV EKGMVDFESE LGQYLHHSWA 

       250        260        270        280        290        300 
ECLLAFDKIG SGSGDLSKCE SFLGDILYMV SKEPGKACMN MYDISLESTY PTCGMDWPYD 

       310        320        330        340        350        360 
LSYLTEFLST REAMTSLNVN LEKVHDWEEC NDDVALQYAR EGIESSSKLI QDLVSTVPIL 

       370        380        390        400        410        420 
LFYGENDFLC NYLSGEKLTR SLEWNGAVGF QNQSAQPFYL PGYSDQPSGS YVSSRNLTFA 

       430        440        450        460        470        480 
RIVEASHMVP YDHPNEMKTL ITAFFNNDFA SLPSVPKPSP DLGNGNYKWL YLGLIPVALT 

       490        500        510 
IIILFSIYLC RRFGLFGLSK QRYQPISPTP 

« Hide

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329671 Genomic DNA. Translation: CAA19029.1.
PIRT39601.
RefSeqNP_596758.1. NM_001023778.2.

3D structure databases

ProteinModelPortalO60123.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276735. 6 interactions.
MINTMINT-4677383.
STRING4896.SPBC16G5.09-1.

Protein family/group databases

MEROPSS10.A67.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC16G5.09.1; SPBC16G5.09.1:pep; SPBC16G5.09.
GeneID2540202.
KEGGspo:SPBC16G5.09.

Organism-specific databases

PomBaseSPBC16G5.09.

Phylogenomic databases

eggNOGCOG2939.
KOK01288.
OMAERANDEW.
OrthoDBEOG7TJ3SJ.
PhylomeDBO60123.

Family and domain databases

InterProIPR001563. Peptidase_S10.
[Graphical view]
PANTHERPTHR11802. PTHR11802. 1 hit.
PfamPF00450. Peptidase_S10. 1 hit.
[Graphical view]
PRINTSPR00724. CRBOXYPTASEC.
ProtoNetSearch...

Other

NextBio20801334.

Entry information

Entry nameKEX1_SCHPO
AccessionPrimary (citable) accession number: O60123
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 83 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