PFF1_PENRW
ID PFF1_PENRW Reviewed; 987 AA.
AC B6H1I3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 49.
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=Pc13g02170;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
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; AM920428; CAP91286.1; -; Genomic_DNA.
DR RefSeq; XP_002558658.1; XM_002558612.1.
DR AlphaFoldDB; B6H1I3; -.
DR SMR; B6H1I3; -.
DR STRING; 1108849.XP_002558658.1; -.
DR EnsemblFungi; CAP91286; CAP91286; PCH_Pc13g02170.
DR GeneID; 8307825; -.
DR KEGG; pcs:Pc13g02170; -.
DR VEuPathDB; FungiDB:PCH_Pc13g02170; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR BioCyc; PCHR:PC13G02170-MON; -.
DR Proteomes; UP000000724; Contig Pc00c13.
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; Reference proteome; Transmembrane; Transmembrane helix; Vacuole;
KW Zinc.
FT CHAIN 1..987
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411731"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 15..35
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..384
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 385..405
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..435
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 436..456
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 457..466
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 467..487
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..501
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 502..522
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..526
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 527..547
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 650..670
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..686
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 687..707
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 716..736
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 737..987
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 572..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 167
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 179
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 179
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 214
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 239
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 312
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 311
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 781
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 871
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 987 AA; 110113 MW; 7636E3A3484CF437 CRC64;
MATRKARNPL AFMPWPVTIL TTAMYLALII PLLVIHHNVP PAPRTSPNGL NLTEAWQDLQ
SLTKGFHPYN SHQNDEVRSW LLERIDAIKQ STPSTEEYRD AKEEKPDVFV FDDLVSNLTF
IDKSVGVYFE GTNILVYIRG SEDNKQNWWE TPGRAPVGKG GVLVNAHYDS VSTGYGATDD
GVGVVTCLQL VKYFLTPGHA PRRGLVVLFN NGEEDYLNGA RVYSQHPMAR FAHTFLNLEG
AGAGGRATLF RSSDTEVTQA YAKSEHPFGS VLSANGFEKG LISSQTDYVV LEGILGLRGL
DVAFFEPRAR YHTDQDDARH TSIDSLWHML STAVATTEEL VSDTTDRFDG HIRDDGTVPS
GSGTRAVWFD LFGSAFAVFR LHTLFALSVT LLIVAPLTLL VTSVILSRAD KMYLFRSSVY
SEINDDYIPL RGLRGFFRFP FLISIPTGVT VGLAYMVTKV NPFIAHSSSY AVWSMMISAW
IFLAWFVSRV ANSARPSAFH RVYTWTWMFV LTWSLMVVCT VYEHEEGLAG GYFIFFYFAG
TFLATWISYL ELFALPTKSE YVGRLAESRR PSTQGSRLAA SGDEHQDDAA EEDPTESTSL
LHGRHRPTFA NYVRVGVDRA SQDEEEEEED PNVYEHEQGW SGVLPRWTWL LQLLITAPVI
LMLIVPLALL TTSALSQTGQ DGSPQLLIYL FISCLTALLF APMLPFIHRY TYHLPIFLLF
VFIGTMIYNL VAFPFADSNR LKLFFLQEVD LDNGISTASL TGMPPFVSDV TYGLPSAAGQ
NESCDWTFRG KRKLQRCSWS APLPHVVPDG DSLSVSSEDA DSLLDATELS PDWISFSISH
PQRDSSSVRF EVSGQNTRNC RINMDGNSIT NFSVIGSSAP DHRFLNPSPD GLNRIQLWSR
TWDNKWTVDV DFSKHDSSET DEVDESSITG RITCLWSDNN RVGLIPALDE VRQFSPAWVA
VTKFSDGLIE GSRAFEIKRS SLGALGS
