PFF1_ZYGRC
ID PFF1_ZYGRC Reviewed; 950 AA.
AC C5E0G6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
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=ZYRO0G12540g;
OS Zygosaccharomyces rouxii (strain ATCC 2623 / CBS 732 / NBRC 1130 / NCYC 568
OS / NRRL Y-229) (Candida mogii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Zygosaccharomyces.
OX NCBI_TaxID=559307;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2623 / CBS 732 / BCRC 21506 / NBRC 1130 / NCYC 568 / NRRL
RC Y-229;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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; CU928179; CAR29600.1; -; Genomic_DNA.
DR RefSeq; XP_002498533.1; XM_002498488.1.
DR AlphaFoldDB; C5E0G6; -.
DR SMR; C5E0G6; -.
DR STRING; 559307.C5E0G6; -.
DR MEROPS; M28.A05; -.
DR PRIDE; C5E0G6; -.
DR EnsemblFungi; CAR29600; CAR29600; ZYRO0G12540g.
DR GeneID; 8206346; -.
DR KEGG; zro:ZYRO0G12540g; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; C5E0G6; -.
DR Proteomes; UP000008536; Chromosome G.
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..950
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411755"
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..355
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 356..376
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 387..409
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 410..426
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 427..447
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 460..480
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..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..614
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 615..635
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..652
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 653..673
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 674
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 675..695
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 696..950
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 519..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..570
FT /note="Polar residues"
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 65
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 718
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 843
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 931
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 950 AA; 107614 MW; 5566321C0E786022 CRC64;
MFVDFLRSLF RLRKTNVSIL LLLTYLTVGL IYFYDHEHYK HVTPEQSRFK DAPQLVEDAW
LNLQNITYSY HPYFSRDNNR VHDYLLNKIE AIAQRSVHVS VSDDASNNRS VLLRNSFVDG
GAVYFESSNI VVKIEGKNTD LPGLLLSAHY DGVPTSHGAT DDGKGVVSLL GILDHYSRHQ
PERTLVFNFN NNEEFGLLGA VAFMEHPWSK LVHYVINLEG TGIGGKAVLF RTSDVSTAKI
YQNAVKSNPF GNSLFQQGFY EGGVGSETDY RIYESNGLRG FDIAFYKPRD LYHTTKDSVQ
YTSREALWHM FHTAWQLTEY IAREPIDNDD DFTPAVFFDV AGLFFFSTSS KTLFKWCCVI
LVVLPVIAFN FDVISFSQKR SSYNQRHRWG VSIRLPLSFA SSLLLLRFTE RLLSSHNTFI
LSRGHLTPLI ALATEFILSN YLILSFFEYL LPTRDFKTTA LRQVAILTWI VLFVCTMKLY
KSEYKYTGIY GIVILYSFVS LAGIIGLFGR VLKGNISRES TDNKGDSSRP YGSHGVDEEQ
QRSGTSAIEE SAGNLEDSNN EGPLDVSTTN NSEHIDAEER APLLGSNPPS VADQPGITNT
LKIKAVSVVN YDWSLQFLIA VPITTFIVFG CVDLGLDALK QTIQEGAVAT VHVWNLVFLG
GILLTLPVLP FAYKFNYLTA MSFLVAFATT LSLCFLQSPF TEGAPLKVRF SQEININNGT
DAIVNVYGRK GGFLQPMLQD LPSVKQMSKD VWCQDELNGM ERCLYVGYQP NPLDSQRPVS
TEDIFSLKVV SNDKNDHDRS RYAPINAELE INVRENRGCT LWFKNQHLDR PPVRQLTVRH
SDNTSDLIKS SQGFTQLQLH KLDFDQQKYR VGIQWLPKIL LMDGQEDEDN DQLDMQVTCY
WGEYDSESLV NGQHLRKLPA FDELLQYSPL NVSYANRDRG LLTITQSIEL
