PFF1_CANAW
ID PFF1_CANAW Reviewed; 837 AA.
AC C4YS59;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 41.
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=CAWG_04918;
OS Candida albicans (strain WO-1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WO-1;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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; CM000312; EEQ46562.1; -; Genomic_DNA.
DR AlphaFoldDB; C4YS59; -.
DR SMR; C4YS59; -.
DR STRING; 5476.C4YS59; -.
DR EnsemblFungi; EEQ46562; EEQ46562; CAWG_04918.
DR VEuPathDB; FungiDB:CAWG_04918; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000001429; Chromosome 6.
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..837
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411706"
FT TOPO_DOM 1..36
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 37..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..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..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 385..405
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..415
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 416..436
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 447..467
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..474
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 475..495
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 540..560
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..572
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 573..593
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 594..598
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244, ECO:0000305"
FT TRANSMEM 599..619
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 620..837
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244, ECO:0000305"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 157
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 169
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 169
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 202
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 227
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 299
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 298
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 837 AA; 93732 MW; AD7D179B4224F203 CRC64;
MSEEEVHDTS SEASEVFTNQ PNAFVRGVRS IFGYRKTSLT LFVILTIVVT AGLSFYDNSL
ELTIELPTSQ LEKEILESSW LDLQNIARYP HTYGSRANDQ VHDYLEEIIQ DMEYDNDGEK
IMFESGKGVV SYYESNNLLV RVNGSDGTLP ALLLSAHYDS VPSSFGVTDD GMGVASLLGV
LRFVAHNQPR RTIIFNFNNN EEFGLFGAHA FVKHPWFKQV GYFLNLEGTG AGGKAVLFRG
TDYGIVKNFG GVRYPYATSI FQQGFNNHVI HSETDYKVYK EAGLRGLDLA FYKPRDKYHT
GEDNIRNVSP KSLWHMMSNA IDFVQMGVVD DSEEPAVYTT FLGYFFATPI SALARVNLVL
LVLFPVVSTP LLFVIVKYKK WKLRVTNFLG VPLAMGLAVA VGQVGNPMLV SSHPMMVVAT
TTSIVVLVYY VVLNGVDWVN TSSDQKLVTM IEVSFVYWVV LVYVTWSGGD HTGEFGVTVL
FFVQASTSLL GLIGWTFTRV RGGDEPLLSG EEERYGTEDE RDTEKPLVEH NYDWSLQYLL
IVPVSSLVVY NSGWLVLEGV NKTVQESLAS EHLIYWIVVV FSQFLVLPVV PFITKFNRYI
VLGLSVVAVV GVLMSMAVHP FNQGSPMKLR FIERVGQNDM VEVYGRQGFV EDVLSDLPSV
KQTQAKLECE ALPDGLEVCK YKSGLTPGNL TVEVTTEPRA ESYGLISGAI TIAAPENRMC
TVHFPPDRVK AVVVGKFGNN FKAIPDGFSR EKGNYIYKDR NGISQLELYK LDWNKDYHVG
FEWLPDIDDE GGMRVEVECF WGDMVPAYQE VVHYSPNWVT WANKERGLVG VVKHVDV
