PFF1_CANDC
ID PFF1_CANDC Reviewed; 930 AA.
AC B9WCV6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=CD36_24500;
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841;
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(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; FM992689; CAX44231.1; -; Genomic_DNA.
DR RefSeq; XP_002418923.1; XM_002418878.1.
DR AlphaFoldDB; B9WCV6; -.
DR SMR; B9WCV6; -.
DR STRING; 42374.XP_002418923.1; -.
DR EnsemblFungi; CAX44231; CAX44231; CD36_24500.
DR GeneID; 8046559; -.
DR KEGG; cdu:CD36_24500; -.
DR CGD; CAL0000166311; Cd36_24500.
DR VEuPathDB; FungiDB:CD36_24500; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000002605; Chromosome 2.
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; Transmembrane; Transmembrane helix; Vacuole; Zinc.
FT CHAIN 1..930
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411707"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 50..70
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..379
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 380..400
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 401..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 412..432
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..449
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 450..470
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..480
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 481..501
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 502..514
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 515..535
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 599..619
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..631
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 632..652
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 653..657
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 658..678
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 679..930
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 177
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 189
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 189
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 223
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 248
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 320
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 319
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 697
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 768
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 808
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 890
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 930 AA; 104760 MW; CBBB72679A6E16BF CRC64;
MPQEEVHDTS SVSDDNLTNT GGGGSNYYNS HNQPNVFVRA IRSIFGYRKT SLTLFVILTI
IFTIALSLYD NNLDLTIELP TNKLENEILK SSWLDLQNIA RYPHTYGSRA NDRVHDYLES
RIHDIIKENP YTEYNNDGEK VLYESAKSIV SYYESNNLLV RINGSDASLP ALLLSAHYDS
VPSSFGVTDD GMGIASLLGV LRFFAQNEQP RRTVIFNFNN DEEFGLYGAQ AFVSHPWFKQ
IGFFLNLEGT GAGGKAILFR GTDYGIVKYF NKVRYPYATS IFQQGFNNHL IHSETDYKVY
KEAGLRGLDL AFYKPRDIYH TAEDNIKNIN LKSLWHMLSN SIDFANFVSN QKINDSGKDE
FAVYTSFLGY FFSSPISALV TINSVLIVLF PILSGPLLFI TVRYKKWKIG TSNFLSLPLA
IVLTVAIVMI VVNQGFQIAN PFLPSSHPLL LVATTTSISL LIYYVFLNGV NWVSPSGDQK
LITIIEISFI YWLILIYVTH GLSQNKIGDD HTGEFPFTVL FFLEATASLF GLIGWTFSRS
IKQSSNDGSD EPLLTGTAER YGSDDTDEDE QEEFRHHDGN TVKHLMQHFG YDWSLQYLLI
VPISSLIIFN SGWLVLDGIN KSIQESFAAE NLIYLLIQLF SQFWILPILP FVYKLNRFIV
FGLTIFAISG VALISFLDPF NQENPLKLRF IQKVDLNKSQ DSFVEVYGRK GIFSDILSDM
PSVKETHTKV ECEALSDGLE ACSYKSALAP NVIPGKSLKD YVNVEIVNSS KIESYGLLSG
EIIITAPENR MCTLYFTKKK VKAVVIYNKS KSVNNFKSIP DGFSRDSKGN YIYKDVAGID
QLVLNKLDWN KNYHIGFDWL PNIDDEVNTL SVDVECYWAD LAPGIGGGDN ATNAELAIPA
YNELVHYSPN WVTWANREKG LVSVSLKIEV
