PFF1_YEAST
ID PFF1_YEAST Reviewed; 976 AA.
AC P38244; D6VQ74; P38245; Q86ZS2;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Vacuolar membrane protease {ECO:0000305|PubMed:23679341};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=FXNA-related family protease 1 {ECO:0000303|PubMed:23679341};
GN Name=PFF1 {ECO:0000303|PubMed:23679341};
GN OrderedLocusNames=YBR074W {ECO:0000312|SGD:S000000278};
GN ORFNames=YBR0718, YBR0719, YBR075W;
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7985423; DOI=10.1002/yea.320100711;
RA van der Aart Q.J.M., Barthe C., Doignon F., Aigle M., Crouzet M.,
RA Steensma H.Y.;
RT "Sequence analysis of a 31 kb DNA fragment from the right arm of
RT Saccharomyces cerevisiae chromosome II.";
RL Yeast 10:959-964(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 832.
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 381-503.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION.
RX PubMed=23679341; DOI=10.1111/1567-1364.12050;
RA Hecht K.A., Wytiaz V.A., Ast T., Schuldiner M., Brodsky J.L.;
RT "Characterization of an M28 metalloprotease family member residing in the
RT yeast vacuole.";
RL FEMS Yeast Res. 13:471-484(2013).
CC -!- FUNCTION: May be involved in vacuolar sorting and osmoregulation.
CC {ECO:0000269|PubMed:23679341}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P80561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:23679341};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:23679341}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA53931.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA53932.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA85018.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA85019.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X76294; CAA53931.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X76294; CAA53932.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z35943; CAA85018.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z35944; CAA85019.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY260891; AAP21759.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07194.2; -; Genomic_DNA.
DR PIR; S45467; S45467.
DR PIR; S45470; S45470.
DR RefSeq; NP_009630.3; NM_001178422.2.
DR AlphaFoldDB; P38244; -.
DR SMR; P38244; -.
DR BioGRID; 32777; 60.
DR DIP; DIP-4914N; -.
DR IntAct; P38244; 2.
DR STRING; 4932.YBR074W; -.
DR MEROPS; M28.A05; -.
DR iPTMnet; P38244; -.
DR MaxQB; P38244; -.
DR PaxDb; P38244; -.
DR PRIDE; P38244; -.
DR EnsemblFungi; YBR074W_mRNA; YBR074W; YBR074W.
DR GeneID; 852366; -.
DR KEGG; sce:YBR074W; -.
DR SGD; S000000278; PFF1.
DR VEuPathDB; FungiDB:YBR074W; -.
DR eggNOG; KOG2194; Eukaryota.
DR GeneTree; ENSGT00530000063839; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; P38244; -.
DR OMA; IHRFTYH; -.
DR BioCyc; YEAST:G3O-29043-MON; -.
DR PRO; PR:P38244; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38244; protein.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Vacuole;
KW Zinc.
FT CHAIN 1..976
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000174140"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:23679341"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..359
FT /note="Vacuolar"
FT /evidence="ECO:0000269|PubMed:23679341"
FT TRANSMEM 360..380
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23679341"
FT TRANSMEM 393..412
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..428
FT /note="Vacuolar"
FT /evidence="ECO:0000305|PubMed:23679341"
FT TRANSMEM 429..449
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23679341"
FT TRANSMEM 462..482
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..496
FT /note="Vacuolar"
FT /evidence="ECO:0000305|PubMed:23679341"
FT TRANSMEM 497..517
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23679341"
FT TRANSMEM 628..648
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..668
FT /note="Vacuolar"
FT /evidence="ECO:0000305|PubMed:23679341"
FT TRANSMEM 669..689
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23679341"
FT TRANSMEM 693..713
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..976
FT /note="Vacuolar"
FT /evidence="ECO:0000269|PubMed:23679341"
FT REGION 528..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 299
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 656
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 796
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 811
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 866
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 832
FT /note="N -> F (in Ref. 1; CAA53932 and 2; CAA85019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 976 AA; 111035 MW; 8D25D5CBFE98A315 CRC64;
MKLKSVFRSV LKYRKTNLSL LLLITYSIIT LLYIFDHERY KLNLPKEDEH PEFNDLLETA
WGDLQIITAS FHPYTSKEND KVHDYLLKRV LEITGNSSFA SVSDDKESER SILFQQQDPF
NESSRFSRVT YFESSNILVK LEGKNPEEEG LLLSAHFDSV PTGYGATDDG MGVVSLLANL
KYHIKHRPNR TLIFNFNNNE EFGLLGASTY FDHSWSNLTK YVINLEGTGA GGKAVLFRTS
DTSTARIYQQ SVKENPFGNS IYQQGFYSRY VRSETDYKIY EENGMRGWDV AFYKPRNLYH
TIKDSIQYTS KASLWHMLHT SLQLSAYVAS NSLDTADQTP ACYFDFIGLK FFVISAKTLF
YWNCIFLLVS PVVAIGLYLI SRDRMTWKSY SWLSWTRFPL SLAAGIIVQK LFSNDIIRSN
PLTFSRNYFW PISAFFTQVI FTSYVLINCS NFFFPCADMK SLSIIELFII LWTILLFTSK
LLYSSDYRYT GLYPLSIFFL LSTIAAILRL LALALGMRTR KRLGRECRDH HSNYSSHSQI
DMERDGQENL EQPQDQLTSS QDDQASIQDD NVSTTSAGPS HNVDEDHGMD SSSQQHDERV
PLLKGSNSME EGLSTRENSL KLEYTDYAWI IQFLLIVPIP SFILFNSVDV IMDALNHTVQ
EGSKATFDVL RFGMVGSILI ALPILPFFYK VNYITISLTA LLFLISASKT LLVHPFTNSN
PLKVRFSQNI DLSQGNAASV HVLGREGNFL KPMLQDLPSI KYSSTHINCT SVTNGMELCM
YDGMQPNLLS TNGNTNISSM VKVHVLHNNR NSTERSPYEP IVAELLLEVK ENRACTLTFE
SRHQAKSPVR EITVYQKKNS APQKANITKT IKSASGINEL QLHKLDFDQE TYHIGVQWFP
KLLTDGNVED DKLGTKDELS VSISCYWGEY DSESVVNGTA VRKIPAFDEL INYAPLSFSF
TNEQKGLVIV KDAIIL
