PFF1_LACBS
ID PFF1_LACBS Reviewed; 1019 AA.
AC B0DC53;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, 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=LACBIDRAFT_294465;
OS Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS (Laccaria laccata var. bicolor).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX NCBI_TaxID=486041;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 / ATCC MYA-4686;
RX PubMed=18322534; DOI=10.1038/nature06556;
RA Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA Tuskan G., Grigoriev I.V.;
RT "The genome of Laccaria bicolor provides insights into mycorrhizal
RT symbiosis.";
RL Nature 452:88-92(2008).
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; DS547103; EDR07831.1; -; Genomic_DNA.
DR RefSeq; XP_001881620.1; XM_001881585.1.
DR AlphaFoldDB; B0DC53; -.
DR SMR; B0DC53; -.
DR EnsemblFungi; EDR07831; EDR07831; LACBIDRAFT_294465.
DR GeneID; 6077313; -.
DR KEGG; lbc:LACBIDRAFT_294465; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; B0DC53; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001194; 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..1019
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411718"
FT TOPO_DOM 1..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 70..90
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..404
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 405..425
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 467..487
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..497
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 498..518
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..539
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 540..560
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 561..565
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 566..586
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 652..672
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..692
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 693..713
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..719
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 720..740
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..1019
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 603..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..629
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 239
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 195
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 207
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 207
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 240
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 265
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 341
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 340
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 256
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1019 AA; 113713 MW; 713665A108525AD8 CRC64;
MFLEINFYST FFQRRPSLWK ERCKFEEVDA QGNSISYSHH PPDLTGQRSP LTPTTMRIVD
RIPTVVGFRV IPTTVLVLLT YLTIFTLVIV TDWLPEPPKN QNGLDLKQAY TDLRHITAHP
HPYNSHYNDA VHDYILSRVR PVAASTSFVH ISDDQTSNGS WASPGYGVYF EGTNILVKID
GKSSNGNDGV LFSAHYDSVS TAPGATDDGM GVVTLLQLID YFAKHRPDRT AIFNINNGEE
DWLNGAHAFL QHTWSNLTDT FLNLEGAAAG GRPILFRATS TSPVRAFRSD YVPHPHANVI
SSDAFARGVI RSGTDYEVYT GAGAEMEGLD VAFYKGRSRY HTKYDAVPYT NGGERSLWAM
METAQGAGNA LLNAKRHKQD QGSGGTPVYF DLVKAELVIF YLNDLLIYNV VSLVVGPISL
IFFVVCEYVL RNERARQPNG HPVSRPSVLE WLKQRSWLRA LWRRSKFWIA LVITIALQAL
LVWGYLAFNS FTVYSSPYLV LISFFSLAYL SLVIPLTFTF NQTQSPTAKY IAPEREKHTL
LIQVYIFTWI LLLFSTIAVA RAQVGGLYFV TAWNTGVWIA CLLAAVEGMM LPVPQGGPRV
RFHSAHHHHH HEHEEDQDAD DDDREQRQPP TEATPLIGYS RASLRKPQEG GVVGWWIVHL
LLTIPAPVLL IAQMGSLLLD SLPQTLADGS PAYVVYAAAS LTAVLLAVPL TPFSGKLHRG
LFFLFFLSFL IVTAYLWLAF PFSSADPLKV FFQQKVTLSN VVSERHSSIM GLSNSTVHPT
AGVRKVVTAI TGTPYYLKNE IIPRLPSASG KELKCRDEKA KRGLVTCEWE STLVPSPGGR
NPWEDDFAAA QGRVGATSKS RQSWFKAEVA RTGVRKGQIV LQGRNTRSCR LYFDSRPIIK
YVVEGGHEGM QKGYEVGKVG ASEVRLWSRT RDREFVVDFE WEDDDGREGE GITGRIACEW
VEYESGNLDN GDGQWDLQRG GGERAKIPAF EEVLAFLPEW AVASKTTDGL VEAWSPFSV
