PFF1_ARTGP
ID PFF1_ARTGP Reviewed; 963 AA.
AC E5QYX6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, 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=MGYG_01137;
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893;
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; DS989822; EFQ98099.1; -; Genomic_DNA.
DR RefSeq; XP_003177051.1; XM_003177003.1.
DR AlphaFoldDB; E5QYX6; -.
DR SMR; E5QYX6; -.
DR STRING; 63402.XP_003177051.1; -.
DR EnsemblFungi; EFQ98099; EFQ98099; MGYG_01137.
DR GeneID; 10032376; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; E5QYX6; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000002669; 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..963
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411695"
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..391
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 392..412
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 413..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 442..462
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..473
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 474..494
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 505..525
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 526..535
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 536..556
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..668
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 669..689
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..705
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 706..726
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 727..732
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 733..753
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..963
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 569..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 170
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 182
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 182
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 217
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 242
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 315
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 314
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 963 AA; 107271 MW; 2EFF02B92393E2DC CRC64;
MVSSRRGFNP IAFTPWPVTI LTSLVYLALI IPIIVVHHLV PPAPKQSPPG VDLEEAWHDL
QHLTRQYHPY NSHSNDEVHQ WLLKRIRAIS ATTSARSESQ GGPEVFVFDD NQTNLTFSSA
GVAATAITGV YFESKNIVVY IRGTEDEPGE WWKSPDGEPS GKGGVLVNAH YDSVSTGYGA
TDNGVGVITT LQLLKYFTTP GHYPRKGLVL LFNNGEEDFL NGAYAYSQHP MSKFTHTFLN
LEGAGAGGRA VLFRSTDTEI TRFYGKSQHP FGTVLARDAF KLGFIRSETD YHVFDGVFGM
RGLDVAFMEP RSRYHTDQDD ARHTSIDSVW HMLSAAITTT EGLVSYTGNE FDGDSGEGGK
LNNGVGTLGV WFDFFGSSLA VFQLNTLFGL SVALLVVAPL LLILTSVALF AVDKMYMFSM
YTYLSESGGQ VSLYGLRGMF RFPLILGIST ALTVALAFLI MKVNPFIIYS SPYAVWSMML
STCMFFAWFI SCVADFARPS ALHRAYAFSW MFGILWVFLV IATVYQRQHG IASSYFIVFY
FAGVSVATWI SYLELFGLST TQDYARRQSR LSDRTPSSDS HLLAPSADEL PSSGSVAGRD
FNPEDVEDEE PTESTSLLRG QQRTTFANYA SARGSQESNI SNQGSSLLHP KNNRLEQKWS
IYLVSSAWIL QFLLVAPIVL ILLGQLGLFL TSATYQIGAD GGSQFIIYIG IAVLSVLILL
PLFPFIHRFT YHIPTFMLFV LIGTLVYNLT AFPFSHNSRL KVAFVQEMDL GTGKNQASLV
GVEPYIRDIV HAIPFVNDEE ISCTSKGYGG RTKCSWPGLR PTVVDGPYKD WVTYNISQTK
EDKTTRFEVS GKNTRACKLL FDSPISDFHV HGSVVDKRIP HTGSKGVSEV RLWSRNWENT
WTVDVEWTKK SAERTGRVMC LWSDDNDLNL IPELDMIRKF APWWVAITKL RDGLVEGSYS
FKL
