PFF1_PODAN
ID PFF1_PODAN Reviewed; 1011 AA.
AC B2B585; A0A090CCT1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
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 OrderedLocusNames=Pa_2_3840; ORFNames=PODANS_2_3840;
OS Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS (Pleurage anserina).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC Podospora anserina.
OX NCBI_TaxID=515849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL Genome Biol. 9:R77.1-R77.22(2008).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383;
RX PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA Couloux A., Wincker P., Debuchy R., Silar P.;
RT "Maintaining two mating types: Structure of the mating type locus and its
RT role in heterokaryosis in Podospora anserina.";
RL Genetics 197:421-432(2014).
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; CU640366; CAP72960.1; -; Genomic_DNA.
DR EMBL; FO904937; CDP25360.1; -; Genomic_DNA.
DR RefSeq; XP_001911135.1; XM_001911100.1.
DR AlphaFoldDB; B2B585; -.
DR SMR; B2B585; -.
DR STRING; 5145.XP_001911135.1; -.
DR EnsemblFungi; CAP72960; CAP72960; PODANS_2_3840.
DR GeneID; 6196458; -.
DR KEGG; pan:PODANSg8177; -.
DR VEuPathDB; FungiDB:PODANS_2_3840; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001197; 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; Reference proteome; Transmembrane; Transmembrane helix; Vacuole;
KW Zinc.
FT CHAIN 1..1011
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411737"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..395
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 396..416
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 417..449
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 450..470
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..483
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 484..504
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 505..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 515..535
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..546
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 547..567
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 568..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 700..720
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..742
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 743..763
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 764..769
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 770..790
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 791..1011
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 587..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..630
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 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 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 321
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 320
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 31
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 837
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1011 AA; 111715 MW; 6AA4A8922AB0FF84 CRC64;
MINPISFRPG PVTFWTTLVY LALLIPIVII NETVPPAPAA ADDGKIEGVN LTEAWLDLTR
ITRGYHPYNS RFNEEVRGYL LGRVGEILEG SGVGGKKGNV TVFDDLRSNV TGLMAGSVVP
TPGSAQVAAY FEGTNILVYV RGKGDDEGDW WRRSAEGGEM EGVRKNERGL VLVNAHYDSV
STGYGATDDG MGVVTCLQVI KYFAHPDHQP ERGIVVMLNN GEEDYLYGAR ALGQHPLNPY
IHTFLNLEGA GAGGRANLFR TTDREVTAAY AGTSDPFGTV IASDAFGLGF IRSGTDYSVL
YDVYGQRGLD LAFFKPRSRY HTNRDDATHT SKASLWHMLS AAIHTASKLS GDTGDTFVGA
RPDGARNKVR NGSPSNGVWF DLFGKGFVNF GLRGMFAWSL TVLVATPLIL VLATYILHKL
DKYYFFTSSV RTYDQPDFEP VLVGGWKGAF RFPFAFIVSG ALSLAVAFLM RKVNPFIIYS
HRYSVIAMIF SLFYFTFWSI MRGANFARPS ALHRGYVNIW LFILGWATLV AVTVTEDRFK
LGAGYPIVFL QTAVCLTTFL TLCELFALPK KTAWGQQVRE DHEVHDYYQP QSGNNNTRTE
SPPPLPQIPH QPSLVPPATR DSNASTLRQG DGNDTDDEDA AVPTERTPLV GGGNATSEHF
RTTFATTYRR SITALVNGAR KYGQDGDEPF EHEQAWSGRL PSWLWFFQFL ILGPFTIILA
AQTGLMLVDA VHQTGADGSN LLLPYLIVFA FTVLVLLPIT PVIHRISHHI PVFLLVVFVG
TLIYNLVAFP FSEESRYKVY FVQQIDLDTA DNRVCYNGVD EYVHKIIAEL PSASGRNVTC
GESKRAELVS CCYDGVDVAP RLGSETPEED TPIEEIYKSL ATVTATRGEG NKAQLEIEAD
NTKACFLEFK QPISGFNVQG GSEWDDRFGQ FPEGGIKQLK LWHRQRGERW VVDVEWKDAE
KLEGQVVCAW SDANEAGTIP ALDEGLRYSP VWAAITKFAE GLVEGRKGFS V
