PFF1_CANTT
ID PFF1_CANTT Reviewed; 908 AA.
AC C5M545;
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=CTRG_02023;
OS Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=294747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-3404 / T1;
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; GG692396; EER35161.1; -; Genomic_DNA.
DR RefSeq; XP_002547716.1; XM_002547670.1.
DR AlphaFoldDB; C5M545; -.
DR SMR; C5M545; -.
DR STRING; 5482.XP_002547716.1; -.
DR EnsemblFungi; EER35161; EER35161; CTRG_02023.
DR GeneID; 8296379; -.
DR KEGG; ctp:CTRG_02023; -.
DR VEuPathDB; FungiDB:CTRG_02023; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000002037; Unassembled WGS sequence.
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..908
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411709"
FT TOPO_DOM 1..48
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..381
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 382..402
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..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..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 603..623
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..638
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 639..659
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 660..664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 665..685
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 686..908
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..580
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 221
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 176
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 188
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 188
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 222
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 247
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 319
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 318
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 162
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 627
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 908 AA; 102185 MW; F560E68924195CFE CRC64;
MTSGEEEEGT REQVPVSQPT GTTSIVSTKE KQPNIFIRAI RATFGYRKTS LTLFVLLTIF
FTVAFSSYDN SLDFTIDLPE TKFEKQLLDS SWLDLQNIAR YPHSYGSHAN DKVHDYLESR
ISQTIKGKPF IEFDNGDEKI LYNSSKKVVS YYEGNNLLVR VNGTDSSLPA FLLSAHYDSV
PSSYGVTDDG MGIASLLGVL SYLANNKQPK RTVIFNFNND EEFGLYGAQA FVTHPWFKQI
QYFLNLEGTG AGGKAILFRG TDYGIVKHFD KVRYPYATSI FQQGFNNRLI HSETDYKVYK
EAGLRGLDLA FYKPRDIYHT GEDNIKNINI RSLWHMLSNS IDFTNFISNS IIDNDTGKDE
PAIYLSVLNY FFSTSVTTLN TINMVLIVLF PVLSGPLLFI TVRYKKWNIG TANLFSLPLA
IVITSLVGAV VVNQGFRLVN EFLPASRPML LVTTTTSILL LTYYILLNGI NFVSPSGDQK
LVSIIQISFI YWIALIFVTR GLSQNAIGDD HTGEFAFTIL FLLEATASLF GLIGWTFTRS
VKEPTGDEEP LLNGRMERYV DGSDDEDDVE EEDDEDQSEE ENHQHEMTVK HLMQHFGYDW
SLQFLLIVPI SSLVIYNSGW LVIDGINKSI QESLVAENFI YLIIQLFSQF WILPILPFVY
KLNRFMVLGL IAFALVGVTL ISSVDPFNQD NPLKLRFIER DGVAHVYGRT GVGISNILGD
MPSVKESGVG IKCDSLPDGN EDCSYKAYLP GNSTIPSLSV KSINSTAQQA YINFGAIQIN
APESRECSLE FKKVKAIVVY SGEITAKNFK AIPDGFSEDS KGNLYYKDVS GIDVAQLNKL
GWNKKFNFGF YWLPDIDDDV AALPIHVECF WSDITIPAYD ELLHYTPNWV TWANREKGLV
SLTNRIEV
