PFF1_YEAS1
ID PFF1_YEAS1 Reviewed; 976 AA.
AC B3LN75;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Vacuolar membrane protease {ECO:0000250|UniProtKB:P38244};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=FXNA-related family protease 1 {ECO:0000250|UniProtKB:P38244};
GN ORFNames=SCRG_02892;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in vacuolar sorting and osmoregulation.
CC {ECO:0000250|UniProtKB:P38244}.
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:0000250|UniProtKB:P38244};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
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DR EMBL; CH408048; EDV12028.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LN75; -.
DR SMR; B3LN75; -.
DR PRIDE; B3LN75; -.
DR EnsemblFungi; EDV12028; EDV12028; SCRG_02892.
DR HOGENOM; CLU_006412_1_0_1; -.
DR Proteomes; UP000008335; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Transmembrane; Transmembrane helix; Vacuole; Zinc.
FT CHAIN 1..976
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411750"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..359
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 360..380
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 393..412
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..428
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 429..449
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 462..482
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..496
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 497..517
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..627
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 628..648
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..668
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 669..689
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 693..713
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..976
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
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 212
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"
SQ SEQUENCE 976 AA; 111064 MW; 75759B33B050796A CRC64;
MKLKSVFRSV LKYRKTNLSL LLLITYSIIT LLYIFDHERY KLNLPKEDEH PEFNDLLETA
WGDLQIITAS FHPYTSKEND KVHDYLLKRV LEITGNSSFA SVSDDKESER SILFQQQDPF
NESSRFSRVT YFESSNILVK LEGKNPEEEG LLLSAHFDSV PTGYGATDDG MGVVSLLANL
KYHIKHRPNR TLIFNFNNNE EFGLLGASTY FNHSWSNLTK YVINLEGTGA GGKAVLFRTS
DTSTAKIYQQ SVKENPFGNS IYQQGFYSRY VRSETDYKIY EENGMRGWDV AFYKPRNLYH
TIKDSIQYTS KASLWHMLHT SLQLSAYVAS NSLDTADQMP ACYFDFIGLK FFVISAKTLF
YWNCIFLLVS PVVAIGLYLI SRDRMTWKSH SWLSWTRFPL SLAAGIIVQK LFSNDIIRSN
PLTFSRNYFW PISAFFTQVI FTSYVLINCS NFFFPCADMK SLSIIELFII LWTILLFTSK
LLYSSDYRYT GLYPLSIFFL LSTIAAILRL LALALGMRTR KRLGRECRDH HSNYSSHSQI
DMERDGQENL EQPQDQFTSS QDDQASIQDD NVSTTSAGPS HNVDEDHGMD SSSQQHDERV
PLLKGSNSME EGLSTRENSL KLEYTDYAWI IQFLLIVPIP SFILFNSVDV IMDALNHTVQ
EGSKATFDVL RFGMVGSILM ALPILPFFYK VNYITISLTA LLFLISASKT LLVHPFTNSN
PLKVRFSQNI DLSQGNAASV HVLGREGNFL KPMLQDLPSI KYSSTHINCT SVTNGMELCM
YDGMQPNLLS TNGNTNISSM AKVHVLHNNR NSTERSPYEP IVAELLLDVK ENRACTLTFE
SRHQAKSPVR EITVYQKKNS APQKTNITKT IKSASGINEL QLHKLDFDQE TYHIGVQWFP
KLLTDGNLED DKLGTKDELS VSISCYWGEY DSESVVNGTA VRKIPAFDEL INYAPLSFSF
TNEQKGLVIV KDAIIL
