PFF1_CANGA
ID PFF1_CANGA Reviewed; 947 AA.
AC Q6FK15;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=CAGL0M01936g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380959; CAG62405.1; -; Genomic_DNA.
DR RefSeq; XP_449429.1; XM_449429.1.
DR AlphaFoldDB; Q6FK15; -.
DR SMR; Q6FK15; -.
DR STRING; 5478.XP_449429.1; -.
DR MEROPS; M28.A05; -.
DR EnsemblFungi; CAG62405; CAG62405; CAGL0M01936g.
DR GeneID; 2891755; -.
DR KEGG; cgr:CAGL0M01936g; -.
DR CGD; CAL0136615; CAGL0M01936g.
DR VEuPathDB; FungiDB:CAGL0M01936g; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; Q6FK15; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000002428; Chromosome M.
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; 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..947
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411708"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..358
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 359..379
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 392..412
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..428
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 429..449
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 459..479
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..489
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 490..510
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 602..622
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 623..641
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 642..662
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 670..690
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 691..947
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 522..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 200
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 156
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 168
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 168
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 201
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 226
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 300
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 299
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 92
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 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 742
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 801
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 833
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 947 AA; 107339 MW; 40D31ECDB228E936 CRC64;
MRFKALLRAI FRFRKTNFSI LLIITYAIII ALLVFDRSRY KLDLPNATSD KLRRNLLEQA
WSDLQVITQS PHPYSSRNND VVHDFLLQRV KNITRSNDNI YIDDDYRNKS SILFHQPDVF
NSTSKVSRVV YYESSNIIVK VVGSNNELPA LLISGHFDSV PTSYGATDDG KGIATMLSLL
NHFSSSQPKR SVIFNFNNNE EFGLLGAYAF TYHPWIRDIE YFINLEGMGA GDRAVLFRTS
NVETAEIYKK AVKSRPFGNS IFQQGFNSRY IGSQTDYKVY DEYGLKGWDI SFYKPRDYYH
TAKDSIQYTS KESLWSMLNQ SLQLAIYISN EKLIKKSSSN PAVFFDLLGL FFVVVDTKHL
FYADIFMLIV GPILLMMKAH LDKRRRLERS RLVQLRLLLS LGLSVVFLLL LTKSLNSFNP
FVYSADYRTP LTGLFLLFVT VNYLIVTLAE RLNPTESYKT VAINQIFIIA WLMQLYITLR
MAKSDFTLTG TYPLSIFSGC LIVALSLGLF GTKNKAVNDA PNSSVRYASS QNDEDNPLPS
QDRGENINQV RDTGNQEVTS NTNTDLHSNA EEVDERMPLL SNNHIGDSGK MDKNSDFSKH
YNWIVQFLCI VPISSFIFLF SLDYTLDAIH KMVQETTDDV QLICIIITIG VILLALPILP
FISKLNYQSS VIIAIIGVLL FGKSLVMQPF SEIAPLKVRF LQTVNQHDIS KSSVSLFTAK
DTPIKEMIYD LPSVKSQSTL VNCTVFGGSK ICDYYGLPPN LVDSEGNRQN KNLMKIEVLK
NDNNDTQRSP YAPLSAEIKI NVSENRVCSL AFWSQSSKQS PVKKFSVIKS NNNNTNSVSN
SIKYADGIDE VLIHKLDFNG AHHFSIEWLP NIPFDLDYDP VIDGQGDNNI EITVACFTGE
ADSLSVVNGH PLKKIPAFDE VVKYSPKWYT FTNRDRGLVV IKDKIQL
