KRP1_SCHPO
ID KRP1_SCHPO Reviewed; 709 AA.
AC Q09175;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 157.
DE RecName: Full=Dibasic-processing endoprotease;
DE EC=3.4.21.-;
DE AltName: Full=KEX2-related protease;
DE Flags: Precursor;
GN Name=krp1; Synonyms=krp; ORFNames=SPAC22E12.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EG545;
RX PubMed=7813430; DOI=10.1002/j.1460-2075.1994.tb06936.x;
RA Davey J., Davis K., Imai Y., Yamamoto M., Matthews G.;
RT "Isolation and characterization of krp, a dibasic endopeptidase required
RT for cell viability in the fission yeast Schizosaccharomyces pombe.";
RL EMBO J. 13:5910-5921(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP FUNCTION, AND MUTAGENESIS OF PHE-425.
RX PubMed=11115118; DOI=10.1046/j.1365-2958.2000.02180.x;
RA Ladds G., Davey J.;
RT "Identification of proteases with shared functions to the proprotein
RT processing protease Krp1 in the fission yeast Schizosaccharomyces pombe.";
RL Mol. Microbiol. 38:839-853(2000).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Membrane-bound, subtilisin-like serine protease that
CC processes the P-factor precursor and other precursor proteins.
CC Essential for cell viability. Cleaves substrate on the C-terminal side
CC of dibasic residues. {ECO:0000269|PubMed:11115118}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:16823372}.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. Furin subfamily.
CC {ECO:0000305}.
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DR EMBL; X82435; CAA57818.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA93896.1; -; Genomic_DNA.
DR PIR; S51793; S51793.
DR RefSeq; NP_594835.1; NM_001020264.2.
DR AlphaFoldDB; Q09175; -.
DR SMR; Q09175; -.
DR BioGRID; 279032; 5.
DR STRING; 4896.SPAC22E12.09c.1; -.
DR MEROPS; S08.A55; -.
DR iPTMnet; Q09175; -.
DR MaxQB; Q09175; -.
DR PaxDb; Q09175; -.
DR EnsemblFungi; SPAC22E12.09c.1; SPAC22E12.09c.1:pep; SPAC22E12.09c.
DR GeneID; 2542576; -.
DR KEGG; spo:SPAC22E12.09c; -.
DR PomBase; SPAC22E12.09c; krp1.
DR VEuPathDB; FungiDB:SPAC22E12.09c; -.
DR eggNOG; KOG3525; Eukaryota.
DR HOGENOM; CLU_002976_2_1_1; -.
DR InParanoid; Q09175; -.
DR OMA; PFMTDVI; -.
DR PhylomeDB; Q09175; -.
DR PRO; PR:Q09175; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0009986; C:cell surface; NAS:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; IDA:PomBase.
DR GO; GO:0030173; C:integral component of Golgi membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:PomBase.
DR GO; GO:0005802; C:trans-Golgi network; IBA:GO_Central.
DR GO; GO:0004175; F:endopeptidase activity; IDA:PomBase.
DR GO; GO:0008233; F:peptidase activity; IDA:PomBase.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:PomBase.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IMP:PomBase.
DR GO; GO:0071432; P:peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion; EXP:PomBase.
DR GO; GO:0016540; P:protein autoprocessing; IDA:PomBase.
DR GO; GO:0016485; P:protein processing; IBA:GO_Central.
DR CDD; cd04059; Peptidases_S8_Protein_convertases_Kexins_Furin-like; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR034182; Kexin/furin.
DR InterPro; IPR002884; P_dom.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR Pfam; PF01483; P_proprotein; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease; Signal; Transmembrane; Transmembrane helix; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..82
FT /evidence="ECO:0000255"
FT /id="PRO_0000027046"
FT PROPEP 83..102
FT /evidence="ECO:0000255"
FT /id="PRO_0000027047"
FT CHAIN 103..709
FT /note="Dibasic-processing endoprotease"
FT /id="PRO_0000027048"
FT TOPO_DOM 103..668
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..693
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 694..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 128..440
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT DOMAIN 449..588
FT /note="P/Homo B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01173"
FT ACT_SITE 162
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 200
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 371
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 216..363
FT /evidence="ECO:0000250"
FT DISULFID 308..338
FT /evidence="ECO:0000250"
FT MUTAGEN 425
FT /note="F->S: In JY965; temperature-sensitive."
FT /evidence="ECO:0000269|PubMed:11115118"
SQ SEQUENCE 709 AA; 78127 MW; 414FE9B89CBE0840 CRC64;
MHPALLCGPI LAIFLQFLVS SCSPLENDDL FLVQVEPEVD PVVAAEAIGA KYVRPLLNLK
YHHLIKLHKG SDDSVQSSIR KRGIDAGILE LERQTPRWRY KRDASESDEL LNEFSNHFGI
SDPLFYGQWH IFNSNNPGHD LNLREVWDAG YFGENVTVAF VDDGIDFKHP DLQAAYTSLG
SWDFNDNIAD PLPKLSDDQH GTRCAGEVAA AWNDVCGVGI APRAKVAGLR ILSAPITDAV
ESEALNYGFQ TNHIYSCSWG PADDGRAMDA PNTATRRALM NGVLNGRNGL GSIFVFASGN
GGHYHDNCNF DGYTNSIFSA TIGAVDAEHK IPFYSEVCAA QLVSAYSSGS HLSILTTNPE
GTCTRSHGGT SAAAPLASAV YALALSIRPD LSWRDIQHIT VYSASPFDSP SQNAEWQKTP
AGFQFSHHFG FGKLDASKFV EVAKDWQVVN PQTWLIAPEI NVNKSFGSVN NETITEMVSE
FTVTKDMIEK SNFKRLEHVT VRVCIPFNRR GALEILLESP SGIRSILASE RPYDENSKGF
LDWTFMTVQH WAEPPEGVWK LLVNDRSGGK HEGTFENWQL ALWGESENPS NTAPLPYDTL
ELPKEMVLGI YSEPNSDLTN SSTLLSPTST SFTSYTVSAT ATPTSTSHIP IPTVLPPTQP
VLEPSYREIV AFITFFLLFA FIFVAVIWTW ISAFWKAKAP PPLSQQEIA
