PFF1_DEBHA
ID PFF1_DEBHA Reviewed; 1016 AA.
AC Q6BMD6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 73.
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=DEHA2F06380g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382138; CAG88967.2; -; Genomic_DNA.
DR RefSeq; XP_460635.2; XM_460635.1.
DR AlphaFoldDB; Q6BMD6; -.
DR SMR; Q6BMD6; -.
DR STRING; 4959.XP_460635.2; -.
DR EnsemblFungi; CAG88967; CAG88967; DEHA2F06380g.
DR GeneID; 2903146; -.
DR KEGG; dha:DEHA2F06380g; -.
DR VEuPathDB; FungiDB:DEHA2F06380g; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; Q6BMD6; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000000599; Chromosome F.
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..1016
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411716"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 58..78
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..408
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 409..429
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 439..459
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..481
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 482..502
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..511
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 512..532
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..547
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 548..568
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 569..646
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 647..667
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..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..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 707..727
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 728..1016
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 598..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 191
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 203
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 203
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="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 264
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 337
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 336
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 778
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 850
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 977
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1016 AA; 114986 MW; F51C4B51B3C8CF9E CRC64;
MAETESGTGN SPSHRLSETS NASGNRSHQQ SKQIASYKSS KPNVFIRFIR AIFGYRKTSV
TLFVFITIIA TLILVELSNS LDFSVKLPTN NLERTILDNS WLDLQKIGKE EHPYTSKGND
YVHDYLEAKI TELIGKSLFI ECDNDVNYTN NIIFKTENDL YNQVTYYESN NLLVRINGSD
SSLPALLVSA HFDSVPSSFG VTDDGMGIAS LLGILNYYSS DGIDQPMRTI ILNFNNNEEF
GLMGATSFLH HPWFKQVRYF LNLEGTGAGG KAVLFRGTDY GIVKYFKHVR YPFGTSLFQQ
GFNNHLIHSE TDYKIYKENG GIRGIDLAFY KPRDIYHTAS DSIKNIDIKS LWHMLSNSLD
FVEIVSSQRI DLDDEDTSPE SDEKSREFAI FSSFFNWFFV IPASQLVLIN VTCLAVIPLI
SLPLLVIIFN YKKNWHIGFI NAIKFPVSLV LSICILNIIT HNVIASINEF LPNSSYDSIV
STLYSLFLLL NYLFLNGINF IFKGYKGLYH DEKLILIIQT SFIYWVLLIV STNKLSKNKI
GNDHTGEFPL IMLFLLQSIG ALFGLFSWSF KKTTPDELRN NDDEACQALL SREEHNNYGS
NEAELESGEP ISSNSSVSLN SSSSQVTNNL VKNLRKSFSY DWSIQYVVIV PLSSLIVYNT
GSLLLSGLNK SIQESLNAEK LIFDLIQLVA VTLAIPFLPF IFKINRLLVT ALVLVFCSGF
ISIFLKSPFD QLNPLKLRFV QSINLDESSD ISVVNVFGRY GSPMNNVLLD LPSLKETNES
LECNNLQDGM QLCSYKTLLS PNLSPDVTDF NDYLDVQVLK NSSSDYPYGL LSGEIKINVP
ENRVCRLSFN NSNFENSKQS LVRTILVYED NNYENSSNKL FPFEVSEFQL ANLPEGFSRD
KKGTYIYKNL NGIDKLELNK LSWDKPYHVG FQWMPKFVDS VSAENENTNV PYTTDFNNLG
IQVECFWGNL GYANNENKSE DERIPAYGEV LHYSPNYVSW ANKESGLVSV SKYVEI
