IPA3_YEAST
ID IPA3_YEAST Reviewed; 68 AA.
AC P01094; D6VZZ6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Protease A inhibitor 3;
DE AltName: Full=Proteinase inhibitor I(A)3;
DE AltName: Full=Proteinase yscA-inhibitor;
DE AltName: Full=Saccharopepsin inhibitor;
GN Name=PAI3; OrderedLocusNames=YMR174C; ORFNames=YM8010.04C;
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 PROTEIN SEQUENCE, AND ACETYLATION AT MET-1.
RA Biedermann K., Montali U., Martin B., Svendsen I., Ottesen M.;
RT "The amino acid sequence of proteinase A inhibitor 3 from baker's yeast.";
RL Carlsberg Res. Commun. 45:225-235(1980).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2037077; DOI=10.1016/0014-5793(91)80558-k;
RA Schu P., Wolf D.H.;
RT "The proteinase yscA-inhibitor, IA3, gene. Studies of cytoplasmic
RT proteinase inhibitor deficiency on yeast physiology.";
RL FEBS Lett. 283:78-84(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 2-32.
RX PubMed=10655612; DOI=10.1038/72378;
RA Li M., Phylip L.H., Lees W.E., Winther J.R., Dunn B.M., Wlodawer A.,
RA Kay J., Gustchina A.;
RT "The aspartic proteinase from Saccharomyces cerevisiae folds its own
RT inhibitor into a helix.";
RL Nat. Struct. Biol. 7:113-117(2000).
CC -!- FUNCTION: Specific and potent inhibitor for yeast aspartic protease A
CC (yscA). The proteinase acts as a folding template stabilizing the
CC helical conformation in the inhibitor, which results in the potent and
CC specific blockage of the proteolytic activity.
CC -!- SIMILARITY: Belongs to the protease inhibitor I34 family.
CC {ECO:0000305}.
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DR EMBL; X60050; CAA42650.1; -; Genomic_DNA.
DR EMBL; Z49808; CAA89907.1; -; Genomic_DNA.
DR EMBL; AY558120; AAS56446.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10070.1; -; Genomic_DNA.
DR PIR; A01334; IABY3.
DR RefSeq; NP_013899.1; NM_001182680.1.
DR PDB; 1DP5; X-ray; 2.20 A; B=1-68.
DR PDB; 1DPJ; X-ray; 1.80 A; B=2-34.
DR PDB; 1G0V; X-ray; 2.00 A; B=1-31.
DR PDBsum; 1DP5; -.
DR PDBsum; 1DPJ; -.
DR PDBsum; 1G0V; -.
DR AlphaFoldDB; P01094; -.
DR BMRB; P01094; -.
DR SMR; P01094; -.
DR BioGRID; 35352; 95.
DR IntAct; P01094; 4.
DR MINT; P01094; -.
DR STRING; 4932.YMR174C; -.
DR MEROPS; I34.001; -.
DR iPTMnet; P01094; -.
DR MaxQB; P01094; -.
DR PaxDb; P01094; -.
DR PRIDE; P01094; -.
DR EnsemblFungi; YMR174C_mRNA; YMR174C; YMR174C.
DR GeneID; 855212; -.
DR KEGG; sce:YMR174C; -.
DR SGD; S000004786; PAI3.
DR VEuPathDB; FungiDB:YMR174C; -.
DR HOGENOM; CLU_2795383_0_0_1; -.
DR InParanoid; P01094; -.
DR OMA; QDKDELM; -.
DR BioCyc; YEAST:G3O-32862-MON; -.
DR EvolutionaryTrace; P01094; -.
DR PRO; PR:P01094; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P01094; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR GO; GO:0005773; C:vacuole; IEA:GOC.
DR GO; GO:0019828; F:aspartic-type endopeptidase inhibitor activity; IMP:CAFA.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IDA:CAFA.
DR GO; GO:0002020; F:protease binding; IPI:CAFA.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:CAFA.
DR GO; GO:0007039; P:protein catabolic process in the vacuole; IMP:SGD.
DR DisProt; DP00179; -.
DR InterPro; IPR008956; IA3_dom_sf.
DR InterPro; IPR019507; Pai3.
DR Pfam; PF10466; Inhibitor_I34; 1.
DR SUPFAM; SSF48686; SSF48686; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Aspartic protease inhibitor;
KW Direct protein sequencing; Protease inhibitor; Reference proteome.
FT CHAIN 1..68
FT /note="Protease A inhibitor 3"
FT /id="PRO_0000195901"
FT REGION 1..32
FT /note="Inhibitory domain"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.1"
FT HELIX 4..30
FT /evidence="ECO:0007829|PDB:1DPJ"
SQ SEQUENCE 68 AA; 7707 MW; 8295BF7AF3E4A01A CRC64;
MNTDQQKVSE IFQSSKEKLQ GDAKVVSDAF KKMASQDKDG KTTDADESEK HNYQEQYNKL
KGAGHKKE
