PFF1_ARTOC
ID PFF1_ARTOC Reviewed; 976 AA.
AC C5FDH0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 47.
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=MCYG_00832;
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480;
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995701; EEQ27944.1; -; Genomic_DNA.
DR RefSeq; XP_002850728.1; XM_002850682.1.
DR AlphaFoldDB; C5FDH0; -.
DR SMR; C5FDH0; -.
DR STRING; 63405.XP_002850728.1; -.
DR EnsemblFungi; EEQ27944; EEQ27944; MCYG_00832.
DR GeneID; 9226658; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000002035; Unassembled WGS sequence.
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..976
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411696"
FT TOPO_DOM 1..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 52..72
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..399
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 400..420
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 428..448
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..477
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 478..498
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..519
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 520..540
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..550
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 551..571
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..675
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 676..696
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 697..718
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 719..739
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 740..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 746..766
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..976
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 590..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 252
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 206
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 218
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 218
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 253
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 278
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 351
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 350
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 848
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 976 AA; 108474 MW; D5CF1B387DF3F7B0 CRC64;
MPLSTGLTLS SLNVMEKADN HYNMMTKQPP ALSPVDMVSS RRGFNPIAFT PWPVTILSSL
VYLAFIIPII VVHHLVPPAP KESPEGVDLK EAWHDLQHLT RQYHPYNSHS NDEVHQWLLK
RIHAISASSS ARSGDTTGPD IFIFDDNQTN LTFSSVGVAA KSITGVYFES KNILVYIRGA
EDDQEEWWES PDGEPSGKGG VLVNAHYDSV STGYGATDNG VGVISTLQLL KYFTTPGHYP
RKGLVLLFND GEEDFLNGAY AFSQHPLSKF THTFLNIEGA GAGGRAVLFR STDTEVTRFY
GNTEHPFGTV LARDAFQLGF IRSETDYHVF DGVFGMRGLD VAFMEPRSRY HTDQDDARHT
SIDSVWHMLS AAIKTTEGLV SYTGDAFDGD NGNDGKLNNG AGTLGVWFDF YGSSFAVFEL
NTLFGHSVAL LVVAPLLLIA TCVTLYTLDK MYMFSMYTYL SESGGQVSLY GLRGLFRFPL
ILGISTALTI GLAFLLMKAN PFIIYSSPYA VWNPSALHRA YAFTWMFGMM WVLLVIATVY
QKQHGIASSY FIVFYFAGVS IATWISYLEL FGLPTTQDYA RRQIRITDRT PSSDSRLLAP
SADELPPSGS AAGHDFNPED VEDEEPTEST SLLRGQQRTT FANYASARSN SDGNISTNAS
LHPKDHRLEQ RWSINLISSA WILQFLFVAP IVIILLGQLG LFLTSATYQI GADGGSQLVI
YVGIAVLSVL ILLPLFPFIH RFTYHIPTFL LFVLIGTLVY NLTAFPFSHS NRLKVAFVQE
IDLETGKNQA SLVGVEPYIH DIVRTIPSTT GKEVSCISRG YGGRAKCSWD GLKPRVVDAP
YKEWITYNIS QAKDDKHTRF EISGKNTRAC KILFDSPIAD FKVLGSVTDE RIPHTGPKGV
SEIRLWSRTW ENTWTVDVEW TKKNANRQGK VMCIWSDDND LKVIPALDEI RNFAPAWAAI
TKLRDGLVEG SHSFKL
