PFF1_ASHGO
ID PFF1_ASHGO Reviewed; 1011 AA.
AC Q750Z6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 OrderedLocusNames=AGL209W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54282.1; -; Genomic_DNA.
DR RefSeq; NP_986458.1; NM_211520.1.
DR AlphaFoldDB; Q750Z6; -.
DR SMR; Q750Z6; -.
DR STRING; 33169.AAS54282; -.
DR MEROPS; M28.A05; -.
DR EnsemblFungi; AAS54282; AAS54282; AGOS_AGL209W.
DR GeneID; 4622751; -.
DR KEGG; ago:AGOS_AGL209W; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; Q750Z6; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Vacuole;
KW Zinc.
FT CHAIN 1..1011
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411697"
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..352
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 353..373
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 391..411
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..420
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 421..441
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 442..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 452..472
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..487
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 488..508
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..647
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 648..668
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..681
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 682..702
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..708
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 709..729
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..1011
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 534..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..563
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
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 161
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 161
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 194
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 219
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 293
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 292
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 854
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1011 AA; 115899 MW; 5B8AB7987CD73568 CRC64;
MKLTKAVFRF RRTNLSTLLV ITYLVITTLY VWDHFRYHFT LPSDYNYAQM LADAWLDLEI
ITQYPHPYAS HANDKVHDYL LDRVKEITRD SMFAEISDDY GMGLRTLFRQ EDAISGTKES
TVVYYESSNV LARVQGRNSA LDGLLLSAHY DSVPSGYGAT DDGMGVVSML AILTHYVKNQ
PERTLVFNFN NNQEFGLAGA SAFFEHPWSK EISYVINLEG TGAGGKAVLF RTSDVSTAQV
YAEAVRQQPF GNSMYQQGFY NGHIGTETDF QVYEDQGLRG WDIAFYRPRN LYHTAKDTVL
YTSKQALWHM LHTALQLTDY MAINKPDMED TSNAVYFDLF GKWFVVWSAR SLFYWNCIIL
ALFPSILAIL FLVAYDMQLL KFNFWDAMLR LPVSVCLAYF CVKLFQVLVG QLNPYVFSRD
YVSPILAEAS MFIFMNYVIL SSWERLRPLR DFKTVALVEV SMVLWIYLIS VTRWLRDSDY
TATGLYPFTI GYTFVSIGAI IGVFCATFKA KLNPEDDSYV GDSKVDIEQQ QMLMQHQYQQ
HSQKHSNQHS PHHSTHHSAQ HSVHHSPRQS IHQVPSSEQR QRDASETPHV IISVDHTAGH
QEDSEVTPLL NTGTVAPFPK PVPERVSRKS FLRNVVTSIL NYDWSIQFMV VTPWVTYFTW
ICLDLIMGAM NQTIQESAKG TTFVTHMALI GSLLLSLPML PFTYKLHSFA GMLFLLLAVT
TAVWTIVAPP FTESSPLKLR FLQTIDLDKN NSSSVYLYGR ERTFMEPILD DIPSVTKYRC
VEYAGDGVDI CEYNGMPPRM FNNHHEAESD WTKIMTLEIL KDDRNSTSRT PYQPITAELK
INVEENRVCT LNFNSTAFKN WKQGVSPLRE VVILHENPSS NVTPSFYNTA MKNGYYQDEF
GNDHYRWNNG ITELQLHKLD FKRGYYKIGL EWIPQLLYRG YDPATSSSEE DDALGVSVTC
YWGEYDTDSI TDGFATTNVP AYDELRKYSP KNIIYSSKEK GMVSVTKYVE L
