(data stored in SCRATCH zone)

SWISSPROT: 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   10-MAY-2017, entry version 39.
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 /
OS   Wisconsin 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.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., 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.
CC       {ECO:0000250|UniProtKB:P80561};
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane
CC       {ECO:0000250|UniProtKB:P38244}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
DR   EMBL; AM920428; CAP91286.1; -; Genomic_DNA.
DR   RefSeq; XP_002558658.1; XM_002558612.1.
DR   EnsemblFungi; CAP91286; CAP91286; PCH_Pc13g02170.
DR   GeneID; 8307825; -.
DR   KEGG; pcs:Pc13g02170; -.
DR   eggNOG; KOG2194; Eukaryota.
DR   eggNOG; COG2234; LUCA.
DR   HOGENOM; HOG000210305; -.
DR   OMA; FAWSLTL; -.
DR   OrthoDB; EOG092C22R5; -.
DR   BioCyc; PCHR:PC13G02170-MONOMER; -.
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:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR007484; Peptidase_M28.
DR   Pfam; PF04389; Peptidase_M28; 1.
PE   3: Inferred from homology;
DR   PRODOM; B6H1I3.
DR   SWISS-2DPAGE; B6H1I3.
KW   Complete proteome; Glycoprotein; Hydrolase; Membrane; Metal-binding;
KW   Metalloprotease; Protease; Reference proteome; Transmembrane;
KW   Transmembrane helix; Vacuole; Zinc.
FT   CHAIN         1    987       Vacuolar membrane protease.
FT                                /FTId=PRO_0000411731.
FT   TOPO_DOM      1     14       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM     15     35       Helical; Name=1. {ECO:0000255}.
FT   TOPO_DOM     36    384       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    385    405       Helical; Name=2. {ECO:0000255}.
FT   TOPO_DOM    406    435       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    436    456       Helical; Name=3. {ECO:0000255}.
FT   TOPO_DOM    457    466       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    467    487       Helical; Name=4. {ECO:0000255}.
FT   TOPO_DOM    488    501       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    502    522       Helical; Name=5. {ECO:0000255}.
FT   TOPO_DOM    523    526       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    527    547       Helical; Name=6. {ECO:0000255}.
FT   TOPO_DOM    548    649       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    650    670       Helical; Name=7. {ECO:0000255}.
FT   TOPO_DOM    671    686       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    687    707       Helical; Name=8. {ECO:0000255}.
FT   TOPO_DOM    708    715       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P38244}.
FT   TRANSMEM    716    736       Helical; Name=9. {ECO:0000255}.
FT   TOPO_DOM    737    987       Vacuolar. {ECO:0000250|UniProtKB:P38244}.
FT   ACT_SITE    213    213       Proton acceptor.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       167    167       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       179    179       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       179    179       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       214    214       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       239    239       Zinc 1; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   METAL       312    312       Zinc 2; catalytic.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   SITE        311    311       Transition state stabilizer.
FT                                {ECO:0000250|UniProtKB:P80561}.
FT   CARBOHYD     51     51       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    117    117       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    781    781       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00498}.
FT   CARBOHYD    871    871       N-linked (GlcNAc...) asparagine.
FT                                {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
//

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