YSP3_YEAST
ID YSP3_YEAST Reviewed; 478 AA.
AC P25036; D6W269;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Subtilisin-like protease 3;
DE EC=3.4.21.-;
DE AltName: Full=Subtilisin-like protease III;
DE Flags: Precursor;
GN Name=YSP3; OrderedLocusNames=YOR003W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Mason O.B., Wong P.A., Barr P.J.;
RT "Nucleotide sequence of YSP3, a new subtilisin-like protease from
RT Saccharomyces cerevisiae.";
RL Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8896276;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1091::aid-yea22>3.0.co;2-i;
RA Sterky F., Holmberg A., Pettersson B., Uhlen M.;
RT "The sequence of a 30 kb fragment on the left arm of chromosome XV from
RT Saccharomyces cerevisiae reveals 15 open reading frames, five of which
RT correspond to previously identified genes.";
RL Yeast 12:1091-1095(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP INDUCTION.
RX PubMed=9784122; DOI=10.1126/science.282.5389.699;
RA Chu S., DeRisi J., Eisen M., Mulholland J., Botstein D., Brown P.O.,
RA Herskowitz I.;
RT "The transcriptional program of sporulation in budding yeast.";
RL Science 282:699-705(1998).
RN [6]
RP FUNCTION.
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).
CC -!- FUNCTION: Serine protease with unknown substrate. {ECO:0000250,
CC ECO:0000269|PubMed:11115118}.
CC -!- INDUCTION: Undergoes rapid but transient induction upon transfer to
CC sporulation medium. {ECO:0000269|PubMed:9784122}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M77197; AAA35237.1; -; Genomic_DNA.
DR EMBL; U43491; AAC49482.1; -; Genomic_DNA.
DR EMBL; Z74911; CAA99191.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10785.1; -; Genomic_DNA.
DR PIR; S61986; S61986.
DR RefSeq; NP_014645.1; NM_001183422.1.
DR AlphaFoldDB; P25036; -.
DR SMR; P25036; -.
DR BioGRID; 34406; 64.
DR DIP; DIP-4198N; -.
DR IntAct; P25036; 1.
DR STRING; 4932.YOR003W; -.
DR MEROPS; S08.A51; -.
DR PaxDb; P25036; -.
DR PRIDE; P25036; -.
DR TopDownProteomics; P25036; -.
DR EnsemblFungi; YOR003W_mRNA; YOR003W; YOR003W.
DR GeneID; 854164; -.
DR KEGG; sce:YOR003W; -.
DR SGD; S000005529; YSP3.
DR VEuPathDB; FungiDB:YOR003W; -.
DR eggNOG; KOG1153; Eukaryota.
DR GeneTree; ENSGT00940000176425; -.
DR HOGENOM; CLU_011263_1_4_1; -.
DR InParanoid; P25036; -.
DR OMA; NDIISAW; -.
DR BioCyc; YEAST:G3O-33553-MON; -.
DR PRO; PR:P25036; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P25036; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0000328; C:fungal-type vacuole lumen; HDA:SGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISA:SGD.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; ISA:SGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
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 InterPro; IPR010259; S8pro/Inhibitor_I9.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 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 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Serine protease; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..478
FT /note="Subtilisin-like protease 3"
FT /id="PRO_0000027206"
FT DOMAIN 70..167
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 177..478
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 213
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 245
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 407
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CONFLICT 22
FT /note="D -> E (in Ref. 1; AAA35237)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="N -> D (in Ref. 1; AAA35237)"
FT /evidence="ECO:0000305"
FT CONFLICT 189..205
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="Y -> L (in Ref. 1; AAA35237)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 52089 MW; 3EAB71360235C6FF CRC64;
MKFSTILPIL WANCCLCMII PDFDGIVRFI ENIDGTRSVR AGEGLGQHDP GNFHTEHQHV
AHKTEFLPYR YVIVFNEDIS LQQIQSHMQV VQKDHSTSVG KLTENDAFWR VISSSVSSKS
QFGGIDNFFD INGLFRGYTG YFTDEIIKII SQDPIIKFVE QETTVKISNS SLQEEAPWGL
HRVSHREKPK YGQDLEYLYE DAAGKGVTSY VLDTGIDTEH EDFEGRAEWG AVIPANDEAS
DLNGHGTHCA GIIGSKHFGV AKNTKIVAVK VLRSNGEGTV SDVIKGIEYV TKEHIESSKK
KNKEFKGSTA NLSLGSSKSL AMEMAVNAAV DSGVHFAIAA GNEDEDACLS SPAGAEKSIT
VGASTFSDDR AFFSNWGTCV DVFAPGINIM STYIGSRNAT LSLSGTSMAS PHVAGILSYF
LSLQPAPDSE FFNDAPSPQE LKEKVLKFST QGVLGDIGDD TPNKLIYNGG GKKLDGFW
