PFF1_BOTFB
ID PFF1_BOTFB Reviewed; 1067 AA.
AC A6S8A1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 55.
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=BC1G_08418;
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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; CH476896; EDN29412.1; -; Genomic_DNA.
DR RefSeq; XP_001552553.1; XM_001552503.1.
DR AlphaFoldDB; A6S8A1; -.
DR OMA; IHRFTYH; -.
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..1067
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411704"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..438
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 439..459
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 496..516
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..526
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 527..547
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 558..578
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 579..585
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 586..606
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..740
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 741..761
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 762..773
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 774..794
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 802..822
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..1067
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 114..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 221
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 233
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 233
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 268
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 293
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 365
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 364
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1067 AA; 118502 MW; E3F9300028ABD96C CRC64;
MKCYNPSAFV PMAVTLVTVI IYLGVFIPLL IIQETVPSAP DDPTLYNGLN LTEAWLDLQS
LSDGYHPFNS RKNDDVRNWL LKRIGEILDH NQIQYSTETE SATISETQIK SDFDAEAPES
VPSPSNSNDG SAERYHEDLR ARKESPAVTV FNDLRSNYSS NALTSIGVKG RKLGISTYFE
GNNIICYVRG SDDEEGEWWK TGSVNSKGKV HGKGGVMVNA HFDSVSTGFG ATDDGVGVVT
ALQLIRYFTT PQNVPQKGFV ALFNNGEEDG LYGAKAFLSH PMARFVHTFL NLEGAGAGGR
ATLFRSTDSE VTRAYAHAKH PFGTVVSSDG FSLGYVRSET DYVVFRAEGY RGLDVAFWQP
RSQYHTDQDD AKHTSIDSLW HMLSASVATT RSLTKDTGNT FLGPRGDDKV GKVSNGKGSD
GVWFDIFGTV FAVFKLRTLF AWSLTLLIAA PLMLFAVSYL LNRQDKFYFF AGSIKAKGPE
DEPISLGGWR GAFRYPITLI ITCAITFGCA SLINKINPMI VYSSPYSVWS MSASLFFSIF
WFIMAGCNFV RPSALQRGYA FMWLFVFGWI ILVAATVYED RFKISGGYLF VFYEAAIFLA
TLIAIGEQFA LPKKSTYVEN SQLDHDGNQD SHHQAVMGTD GANGADEANA SNEAGQEEDP
EDNVNDLAVP HETTPLIGGG APTQRSSIST TFANRYRQVV PESYDGPADH HDKKGHKKHP
YGGEQDWSAK LPIWTWLVQY LLVGPFILIV VGQVGLFLVA ALHQTGTDGS PLLLPYLVVA
VFSILLLLPV TPFIHRLTHH MPTFFFLVFI GTLIYNLVAF PFSPNNRYKA YFQQTVDLDT
GLNKVTIVGI EQYIREIIAY IPSAAGQTIN CEENPRIRSG LSFCSYEGIA PRVVDNVVDG
IPPEKGYTDW LTYNVTRVPN ENKATFHISG LETRACILRF DDPFSEFKVH GGAKTEERWD
DVPDSGSDQI KLWSRDWNKE WKVDVEWAVG EDMKPGEEGR TGRVVCLWSD ANERGVIPAL
DEARRFSPDW TSVVKLMDGL VEGSKRRYLD EREVLEFLKV TGGVIES
