PFF1_VANPO
ID PFF1_VANPO Reviewed; 939 AA.
AC A7TM20;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, 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=Kpol_1052p9;
OS Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS 2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX NCBI_TaxID=436907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC Y-8283 / UCD 57-17;
RX PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT species descended from a whole-genome duplication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(2007).
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; DS480419; EDO16662.1; -; Genomic_DNA.
DR RefSeq; XP_001644520.1; XM_001644470.1.
DR AlphaFoldDB; A7TM20; -.
DR SMR; A7TM20; -.
DR STRING; 436907.A7TM20; -.
DR PRIDE; A7TM20; -.
DR EnsemblFungi; EDO16662; EDO16662; Kpol_1052p9.
DR GeneID; 5544818; -.
DR KEGG; vpo:Kpol_1052p9; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; A7TM20; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR PhylomeDB; A7TM20; -.
DR Proteomes; UP000000267; 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; Reference proteome; Transmembrane; Transmembrane helix; Vacuole;
KW Zinc.
FT CHAIN 1..939
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411747"
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..356
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 357..377
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..388
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 389..409
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..424
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 425..445
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 454..474
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..491
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 492..512
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..588
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 589..609
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 610..636
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 637..657
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..663
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 664..684
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 685..939
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 540..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 193
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
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 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 820
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 939 AA; 107558 MW; A962C2B14A0063AE CRC64;
MGFNSIFKFR KTSLSLLLFA VYFIIGILYF IDKTRYKHSL PIDSEGVALL DNAWLDLQNI
TNKCHPYSSK ENDRVHDYLL NRIADIINKT SYAEVSDDYS TNSRALFKQQ DVFNASSIAS
RIIYFESSNI LVKMEGRNPV LKSLLLSAHY DSTPSSHGVT DDGKGIVSLL ALLEHFSKVQ
PERTLVFNFN NNEEFGLLGA TIFFEHEWSK NVEYFINLEG TGIGGKAVLF RTTDTSTAKI
YQNSVKNSPF GNSIYQQGFY NRYIGSETDY KVYENKGLRG WDIAFYKPRN LYHTIEDSIG
HSSKPALWHM LHTSLQLSKY IAELDNISLG ETQDLSPAVY FDLAGYTFVA IPSTKLFWIN
IALLIIMPII SIFLFSIVKK YNNEIIDSGN IWWRLPISAM SSGTIIIFTT KLIMKWNPYI
LSRNFLLPLI GLTFEFIILN SYILTMFENL SSSFDFKTIA INEISFLFWI VLAYQTWKLY
DNNYQNTGIY PFTICYIVMA TAGNIGYLFL IFKNIEIVED EEASLVQYVS NEQSTIEGRY
RDEINGRDDS SRDSNSASIP TRANDERAPL LTNSVDNINQ RTILKESKLV YNYDWIIEFL
LVVPFSTFLL YNSLELIMDA VNQTIQETGD LYKVYKILAI GSILISIPTL PFAYKIGCQL
GKTLTFISIG CLLISMALAP FTEMNPIKFR FMQVNDKVEI SGVTTHDNNK LRDMINNLPS
VKRDDKKVQC QEITKFSSVC EYEGSPVHLV DNMYRDKLKL MEVIVLKDDR LSPERSPYAP
ITAEVEIRVQ ENRMCNVYFG QNKERIREVN VSIIEGNDRN SSVSLRYRVN NNRNGIDELQ
LHKLRFEANS YIVGIKWMPE ILMSNEEEDD VLPIKVECYW GEYEESSVEV GEGEVGGGAV
IEYYDKIPSY SEILEYKPVD VVIANREKGL VKLTEAMVL
