PFF1_TUBMM
ID PFF1_TUBMM Reviewed; 969 AA.
AC D5GI81;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, 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=GSTUM_00008325001;
OS Tuber melanosporum (strain Mel28) (Perigord black truffle).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Tuber.
OX NCBI_TaxID=656061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mel28;
RX PubMed=20348908; DOI=10.1038/nature08867;
RA Martin F., Kohler A., Murat C., Balestrini R., Coutinho P.M., Jaillon O.,
RA Montanini B., Morin E., Noel B., Percudani R., Porcel B., Rubini A.,
RA Amicucci A., Amselem J., Anthouard V., Arcioni S., Artiguenave F.,
RA Aury J.M., Ballario P., Bolchi A., Brenna A., Brun A., Buee M.,
RA Cantarel B., Chevalier G., Couloux A., Da Silva C., Denoeud F.,
RA Duplessis S., Ghignone S., Hilselberger B., Iotti M., Marcais B., Mello A.,
RA Miranda M., Pacioni G., Quesneville H., Riccioni C., Ruotolo R.,
RA Splivallo R., Stocchi V., Tisserant E., Viscomi A.R., Zambonelli A.,
RA Zampieri E., Henrissat B., Lebrun M.H., Paolocci F., Bonfante P.,
RA Ottonello S., Wincker P.;
RT "Perigord black truffle genome uncovers evolutionary origins and mechanisms
RT of symbiosis.";
RL Nature 464:1033-1038(2010).
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; FN430324; CAZ84224.1; -; Genomic_DNA.
DR RefSeq; XP_002840033.1; XM_002839987.1.
DR AlphaFoldDB; D5GI81; -.
DR SMR; D5GI81; -.
DR STRING; 656061.D5GI81; -.
DR EnsemblFungi; CAZ84224; CAZ84224; GSTUM_00008325001.
DR GeneID; 9181942; -.
DR KEGG; tml:GSTUM_00008325001; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; D5GI81; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000006911; 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..969
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411746"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 13..33
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..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..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 439..459
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..469
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 470..490
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..505
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 506..526
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..531
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 532..552
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 553..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 663..683
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 684..698
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 699..719
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..727
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 728..748
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 749..969
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 571..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 216
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 166
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 178
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 178
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 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 355
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 969 AA; 106569 MW; F4A545AF55AA9078 CRC64;
MTRVNSIIGF RPIPVTLLTV ITYVSLFSAL LFIDRQPPAV AKKGELDYWG VDIEEAWSDL
EVLTRDFHPY NSRPNDDVRA YLLGRVQEIL SRNGVSGFGN ELQSSGYSGT VDLFDDGIPG
KPGSNVTFVG AGSEDLTVYF EGTNIIVYIH GERPADELSP VLVSAHYDSV STGYGATDDG
AAVVSILQII KSFTRPESQG GKRPKRGLVA LLNNGEEDFL NGARAFAMHP VAKLPHSFLN
LEGAGAGGRA TLFRSTDAEV TKYYKRAKRP FGTIVSGDGF KAGLIRSGTD YSVFVENLGM
RGLDVAFYQP RSRYHTTEDD ARHSSKRSLW HMLGGSLATL RGMTDDTSKV FDSPNGSAGK
GHNAVWFDLF GRAFSVLHLH TIFAFTITLI VVPFVVVLVA MWALGHFDKL YFFSNTAYIP
PPPEHSIASR TTQGWRGVLR FPVAFVAASA GVVGMAFLIN KINPMVVYAS QYTVWTCFLS
TWWIIAWVIL RGADAVRPTA LARGYGFLEQ WLLWLVAMIG VAISIGKSHL GSGYWVLVFY
SGFFTSAFIS LLEMAALQKK SEVKIAVSGD DQAYPPEEHS QTGASGNISN RAANDDDDAG
EHATEETPLF RGPNRPLSFA PHRNPRYDNG DHDSGDILVE EKDEAVYGGE QGWSKDLPSW
TWILQFLATV PLQLVLAGSV ALLLGNALAQ TGADGSDMLT VLLGFGVFSI ILLLPVAPFL
HRITYHVTLF IFVIFVGTFI YNLAAPPFSP NARLKVYFQQ TVDLQTGENN VHLVGHPDYI
DRIVSKHIPS AKGKVDICQA DKLKSGLRRC SWKGIAPRVV PQAPGGMPPE YGFSDWISYN
VTKTGDGKAT IKLRGRNTRA CKLLFNKPLA KSPTLGNPIP GFPNTRELRL WSRDWERGWS
VELTWEKEED QEENKDSHSS AIVVCLWSDG NKVSDEIPAL HEIRRYLPVW AIASKLADGL
VEGSVPFMI
