CARP_YEAST
ID CARP_YEAST Reviewed; 405 AA.
AC P07267; D6W3L4;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Saccharopepsin;
DE EC=3.4.23.25;
DE AltName: Full=Aspartate protease;
DE Short=PrA;
DE Short=Proteinase A;
DE AltName: Full=Carboxypeptidase Y-deficient protein 4;
DE AltName: Full=Proteinase YSCA;
DE Flags: Precursor;
GN Name=PEP4; Synonyms=PHO9, PRA1; OrderedLocusNames=YPL154C; ORFNames=P2585;
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].
RX PubMed=3537721; DOI=10.1128/mcb.6.7.2500-2510.1986;
RA Woolford C.A., Daniels L.B., Park F.J., Jones E.W., van Arsdell J.N.,
RA Innis M.A.;
RT "The PEP4 gene encodes an aspartyl protease implicated in the
RT posttranslational regulation of Saccharomyces cerevisiae vacuolar
RT hydrolases.";
RL Mol. Cell. Biol. 6:2500-2510(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3023936; DOI=10.1128/mcb.6.7.2490-2499.1986;
RA Ammerer G., Hunter C.P., Rothman J.H., Saari G.C., Valls L.A.,
RA Stevens T.H.;
RT "PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar
RT enzyme required for processing of vacuolar precursors.";
RL Mol. Cell. Biol. 6:2490-2499(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8948103;
RX DOI=10.1002/(sici)1097-0061(199611)12:14<1483::aid-yea34>3.0.co;2-o;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a
RT small nuclear RNA, a new putative protein kinase and two new putative
RT regulators.";
RL Yeast 12:1483-1492(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [5]
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 [6]
RP PROTEIN SEQUENCE OF 77-405.
RA Dreyer T., Halkier B., Svendsen I., Ottesen M.;
RT "Primary structure of the aspartic proteinase A from Saccharomyces
RT cerevisiae.";
RL Carlsberg Res. Commun. 51:27-41(1986).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 373-405.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1618910; DOI=10.1083/jcb.118.1.95;
RA Roof D.M., Meluh P.B., Rose M.D.;
RT "Kinesin-related proteins required for assembly of the mitotic spindle.";
RL J. Cell Biol. 118:95-108(1992).
RN [8]
RP PROTEIN SEQUENCE OF 23-31 AND 68-86.
RX PubMed=8840499;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<823::aid-yea975>3.0.co;2-j;
RA Wolff A.M., Dimn N., Petersen J.G.L.;
RT "Vacuolar and extracellular maturation of Saccharomyces cerevisiae
RT proteinase A.";
RL Yeast 12:823-832(1996).
RN [9]
RP MUTAGENESIS OF ASP-294.
RX PubMed=1959673; DOI=10.1016/0014-5793(91)81153-y;
RA Rupp S., Hirsch H.H., Wolf D.H.;
RT "Biogenesis of the yeast vacuole (lysosome). Active site mutation in the
RT vacuolar aspartate proteinase yscA blocks maturation of vacuolar
RT proteinases.";
RL FEBS Lett. 293:62-66(1991).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=9135120; DOI=10.1006/jmbi.1996.0880;
RA Aguilar C.F., Cronin N.B., Badasso M., Dreyer T., Newman M.P., Cooper J.B.,
RA Hoover D.J., Wood S.P., Johnson M.S., Blundell T.L.;
RT "The three-dimensional structure at 2.4-A resolution of glycosylated
RT proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae.";
RL J. Mol. Biol. 267:899-915(1997).
CC -!- FUNCTION: Aspartyl protease implicated in the post-translational
CC regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY
CC and on itself.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate.
CC Does not act on esters of Tyr or Arg.; EC=3.4.23.25;
CC -!- SUBCELLULAR LOCATION: Vacuole. Note=Lysosome-like vacuoles.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; M13358; AAB63975.1; -; Genomic_DNA.
DR EMBL; X96770; CAA65567.1; -; Genomic_DNA.
DR EMBL; Z73510; CAA97859.1; -; Genomic_DNA.
DR EMBL; Z11963; CAA78020.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11280.1; -; Genomic_DNA.
DR PIR; A25379; A25379.
DR RefSeq; NP_015171.1; NM_001183968.1.
DR PDB; 1DP5; X-ray; 2.20 A; A=77-405.
DR PDB; 1DPJ; X-ray; 1.80 A; A=77-405.
DR PDB; 1FMU; X-ray; 2.70 A; A=77-405.
DR PDB; 1FMX; X-ray; 2.61 A; A/B=77-405.
DR PDB; 1FQ4; X-ray; 2.70 A; A=77-405.
DR PDB; 1FQ5; X-ray; 2.40 A; A=77-405.
DR PDB; 1FQ6; X-ray; 2.70 A; A=77-405.
DR PDB; 1FQ7; X-ray; 2.80 A; A=77-405.
DR PDB; 1FQ8; X-ray; 2.80 A; A=77-405.
DR PDB; 1G0V; X-ray; 2.00 A; A=77-405.
DR PDB; 2JXR; X-ray; 2.40 A; A=77-405.
DR PDBsum; 1DP5; -.
DR PDBsum; 1DPJ; -.
DR PDBsum; 1FMU; -.
DR PDBsum; 1FMX; -.
DR PDBsum; 1FQ4; -.
DR PDBsum; 1FQ5; -.
DR PDBsum; 1FQ6; -.
DR PDBsum; 1FQ7; -.
DR PDBsum; 1FQ8; -.
DR PDBsum; 1G0V; -.
DR PDBsum; 2JXR; -.
DR AlphaFoldDB; P07267; -.
DR SMR; P07267; -.
DR BioGRID; 36029; 194.
DR DIP; DIP-4442N; -.
DR IntAct; P07267; 8.
DR MINT; P07267; -.
DR STRING; 4932.YPL154C; -.
DR BindingDB; P07267; -.
DR ChEMBL; CHEMBL4451; -.
DR MEROPS; A01.018; -.
DR iPTMnet; P07267; -.
DR UCD-2DPAGE; P07267; -.
DR MaxQB; P07267; -.
DR PaxDb; P07267; -.
DR PRIDE; P07267; -.
DR EnsemblFungi; YPL154C_mRNA; YPL154C; YPL154C.
DR GeneID; 855949; -.
DR KEGG; sce:YPL154C; -.
DR SGD; S000006075; PEP4.
DR VEuPathDB; FungiDB:YPL154C; -.
DR eggNOG; KOG1339; Eukaryota.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; P07267; -.
DR OMA; DKSHYTG; -.
DR BioCyc; YEAST:YPL154C-MON; -.
DR BRENDA; 3.4.23.25; 984.
DR Reactome; R-SCE-2132295; MHC class II antigen presentation.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; P07267; -.
DR PRO; PR:P07267; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P07267; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:CAFA.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0070492; F:oligosaccharide binding; IDA:CAFA.
DR GO; GO:0008233; F:peptidase activity; IDA:SGD.
DR GO; GO:0006914; P:autophagy; IMP:SGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:SGD.
DR GO; GO:0032258; P:cytoplasm to vacuole transport by the Cvt pathway; IMP:SGD.
DR GO; GO:0016237; P:lysosomal microautophagy; IMP:SGD.
DR GO; GO:0016236; P:macroautophagy; IMP:SGD.
DR GO; GO:0000425; P:pexophagy; IMP:SGD.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IMP:SGD.
DR GO; GO:0006624; P:vacuolar protein processing; IMP:SGD.
DR CDD; cd05488; Proteinase_A_fungi; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033819; Saccharopepsin.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Signal; Vacuole;
KW Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:8840499"
FT PROPEP 23..76
FT /note="Activation peptide"
FT /evidence="ECO:0000269|Ref.6"
FT /id="PRO_0000025873"
FT CHAIN 77..405
FT /note="Saccharopepsin"
FT /id="PRO_0000025874"
FT DOMAIN 91..402
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 109
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 294
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 122..127
FT DISULFID 328..361
FT MUTAGEN 294
FT /note="D->A: Inactivation."
FT /evidence="ECO:0000269|PubMed:1959673"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1DPJ"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1DPJ"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:1DPJ"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:1DPJ"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 142..152
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 155..168
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 171..183
FT /evidence="ECO:0007829|PDB:1DPJ"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1DPJ"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1DPJ"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1DPJ"
FT HELIX 213..219
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:1DPJ"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 240..249
FT /evidence="ECO:0007829|PDB:1DPJ"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:1DPJ"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 271..279
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:1DPJ"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 317..319
FT /evidence="ECO:0007829|PDB:1FQ8"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:1DPJ"
FT HELIX 328..333
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 337..341
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 344..348
FT /evidence="ECO:0007829|PDB:1DPJ"
FT TURN 350..352
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:1DPJ"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 376..380
FT /evidence="ECO:0007829|PDB:1DPJ"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 388..393
FT /evidence="ECO:0007829|PDB:1DPJ"
FT TURN 394..397
FT /evidence="ECO:0007829|PDB:1DPJ"
FT STRAND 398..404
FT /evidence="ECO:0007829|PDB:1DPJ"
SQ SEQUENCE 405 AA; 44499 MW; B0AA36BA098D2BF7 CRC64;
MFSLKALLPL ALLLVSANQV AAKVHKAKIY KHELSDEMKE VTFEQHLAHL GQKYLTQFEK
ANPEVVFSRE HPFFTEGGHD VPLTNYLNAQ YYTDITLGTP PQNFKVILDT GSSNLWVPSN
ECGSLACFLH SKYDHEASSS YKANGTEFAI QYGTGSLEGY ISQDTLSIGD LTIPKQDFAE
ATSEPGLTFA FGKFDGILGL GYDTISVDKV VPPFYNAIQQ DLLDEKRFAF YLGDTSKDTE
NGGEATFGGI DESKFKGDIT WLPVRRKAYW EVKFEGIGLG DEYAELESHG AAIDTGTSLI
TLPSGLAEMI NAEIGAKKGW TGQYTLDCNT RDNLPDLIFN FNGYNFTIGP YDYTLEVSGS
CISAITPMDF PEPVGPLAIV GDAFLRKYYS IYDLGNNAVG LAKAI
