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Protein

Dibasic-processing endoprotease

Gene

krp1

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

Membrane-bound, subtilisin-like serine protease that processes the P-factor precursor and other precursor proteins. Essential for cell viability.1 Publication

Catalytic activityi

Cleaves substrate on the C-terminal side of dibasic residues.

Cofactori

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei162 – 1621Charge relay systemBy similarity
Active sitei200 – 2001Charge relay systemBy similarity
Active sitei371 – 3711Charge relay systemBy similarity

GO - Molecular functioni

  • endopeptidase activity Source: PomBase
  • peptidase activity, acting on L-amino acid peptides Source: PomBase
  • serine-type endopeptidase activity Source: PomBase
  • serine-type endopeptidase inhibitor activity Source: PomBase

GO - Biological processi

  • dibasic protein processing Source: PomBase
  • negative regulation of endopeptidase activity Source: GOC
  • peptide mating pheromone maturation involved in conjugation with cellular fusion Source: PomBase
  • protein autoprocessing Source: PomBase
  • proteolysis Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

Calcium

Protein family/group databases

MEROPSiS08.A55.

Names & Taxonomyi

Protein namesi
Recommended name:
Dibasic-processing endoprotease (EC:3.4.21.-)
Alternative name(s):
KEX2-related protease
Gene namesi
Name:krp1
Synonyms:krp
ORF Names:SPAC22E12.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC22E12.09c.
PomBaseiSPAC22E12.09c. krp1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini103 – 668566LumenalSequence analysisAdd
BLAST
Transmembranei669 – 69325HelicalSequence analysisAdd
BLAST
Topological domaini694 – 70916CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cell surface Source: PomBase
  • Golgi apparatus Source: PomBase
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi425 – 4251F → S in JY965; temperature-sensitive. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence analysisAdd
BLAST
Propeptidei23 – 8260Sequence analysisPRO_0000027046Add
BLAST
Propeptidei83 – 10220Sequence analysisPRO_0000027047Add
BLAST
Chaini103 – 709607Dibasic-processing endoproteasePRO_0000027048Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence analysis
Disulfide bondi216 ↔ 363By similarity
Disulfide bondi308 ↔ 338By similarity
Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence analysis
Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence analysis
Glycosylationi620 – 6201N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ09175.

Miscellaneous databases

PMAP-CutDBQ09175.

Interactioni

Protein-protein interaction databases

BioGridi279032. 5 interactions.
MINTiMINT-4693762.

Structurei

3D structure databases

ProteinModelPortaliQ09175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini157 – 440284Peptidase S8Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S8 family. Furin subfamily.Curated
Contains 1 peptidase S8 domain.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMiHOG000192536.
InParanoidiQ09175.
KOiK01341.
OMAiVEWHEEQ.
OrthoDBiEOG7CK3GC.
PhylomeDBiQ09175.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q09175-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHPALLCGPI LAIFLQFLVS SCSPLENDDL FLVQVEPEVD PVVAAEAIGA
60 70 80 90 100
KYVRPLLNLK YHHLIKLHKG SDDSVQSSIR KRGIDAGILE LERQTPRWRY
110 120 130 140 150
KRDASESDEL LNEFSNHFGI SDPLFYGQWH IFNSNNPGHD LNLREVWDAG
160 170 180 190 200
YFGENVTVAF VDDGIDFKHP DLQAAYTSLG SWDFNDNIAD PLPKLSDDQH
210 220 230 240 250
GTRCAGEVAA AWNDVCGVGI APRAKVAGLR ILSAPITDAV ESEALNYGFQ
260 270 280 290 300
TNHIYSCSWG PADDGRAMDA PNTATRRALM NGVLNGRNGL GSIFVFASGN
310 320 330 340 350
GGHYHDNCNF DGYTNSIFSA TIGAVDAEHK IPFYSEVCAA QLVSAYSSGS
360 370 380 390 400
HLSILTTNPE GTCTRSHGGT SAAAPLASAV YALALSIRPD LSWRDIQHIT
410 420 430 440 450
VYSASPFDSP SQNAEWQKTP AGFQFSHHFG FGKLDASKFV EVAKDWQVVN
460 470 480 490 500
PQTWLIAPEI NVNKSFGSVN NETITEMVSE FTVTKDMIEK SNFKRLEHVT
510 520 530 540 550
VRVCIPFNRR GALEILLESP SGIRSILASE RPYDENSKGF LDWTFMTVQH
560 570 580 590 600
WAEPPEGVWK LLVNDRSGGK HEGTFENWQL ALWGESENPS NTAPLPYDTL
610 620 630 640 650
ELPKEMVLGI YSEPNSDLTN SSTLLSPTST SFTSYTVSAT ATPTSTSHIP
660 670 680 690 700
IPTVLPPTQP VLEPSYREIV AFITFFLLFA FIFVAVIWTW ISAFWKAKAP

PPLSQQEIA
Length:709
Mass (Da):78,127
Last modified:November 1, 1995 - v1
Checksum:i414FE9B89CBE0840
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82435 Genomic DNA. Translation: CAA57818.1.
CU329670 Genomic DNA. Translation: CAA93896.1.
PIRiS51793.
RefSeqiNP_594835.1. NM_001020264.2.

Genome annotation databases

EnsemblFungiiSPAC22E12.09c.1; SPAC22E12.09c.1:pep; SPAC22E12.09c.
GeneIDi2542576.
KEGGispo:SPAC22E12.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82435 Genomic DNA. Translation: CAA57818.1.
CU329670 Genomic DNA. Translation: CAA93896.1.
PIRiS51793.
RefSeqiNP_594835.1. NM_001020264.2.

3D structure databases

ProteinModelPortaliQ09175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi279032. 5 interactions.
MINTiMINT-4693762.

Protein family/group databases

MEROPSiS08.A55.

Proteomic databases

MaxQBiQ09175.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC22E12.09c.1; SPAC22E12.09c.1:pep; SPAC22E12.09c.
GeneIDi2542576.
KEGGispo:SPAC22E12.09c.

Organism-specific databases

EuPathDBiFungiDB:SPAC22E12.09c.
PomBaseiSPAC22E12.09c. krp1.

Phylogenomic databases

HOGENOMiHOG000192536.
InParanoidiQ09175.
KOiK01341.
OMAiVEWHEEQ.
OrthoDBiEOG7CK3GC.
PhylomeDBiQ09175.

Miscellaneous databases

PMAP-CutDBQ09175.
PROiQ09175.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
3.40.50.200. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
IPR002884. PrprotnconvertsP.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 1 hit.
PfamiPF01483. P_proprotein. 1 hit.
PF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of krp, a dibasic endopeptidase required for cell viability in the fission yeast Schizosaccharomyces pombe."
    Davey J., Davis K., Imai Y., Yamamoto M., Matthews G.
    EMBO J. 13:5910-5921(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: EG545.
  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.
  3. "Identification of proteases with shared functions to the proprotein processing protease Krp1 in the fission yeast Schizosaccharomyces pombe."
    Ladds G., Davey J.
    Mol. Microbiol. 38:839-853(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF PHE-425.
  4. "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].

Entry informationi

Entry nameiKRP1_SCHPO
AccessioniPrimary (citable) accession number: Q09175
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 8, 2016
This is version 125 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

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 one 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.