PFF1_COPC7
ID PFF1_COPC7 Reviewed; 1005 AA.
AC A8N513;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 48.
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=CC1G_04591;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(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; AACS02000003; EAU91824.2; -; Genomic_DNA.
DR RefSeq; XP_001829902.2; XM_001829850.2.
DR AlphaFoldDB; A8N513; -.
DR SMR; A8N513; -.
DR STRING; 5346.XP_001829902.2; -.
DR EnsemblFungi; EAU91824; EAU91824; CC1G_04591.
DR GeneID; 6006340; -.
DR KEGG; cci:CC1G_04591; -.
DR VEuPathDB; FungiDB:CC1G_04591; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; A8N513; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001861; 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..1005
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411715"
FT TOPO_DOM 1..14
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 15..35
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..353
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 354..374
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 449..469
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..479
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 480..500
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..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..543
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 544..564
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..644
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 645..665
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 666..686
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 687..707
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 708..713
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 714..734
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 735..1005
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 379..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 152
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 164
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 164
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 197
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 222
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 311
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 310
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 761
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 961
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1005 AA; 110463 MW; 5F7CD4150C2187FE CRC64;
MAKETTARSI LGYQTLPTTA LIALIYVVAF FSVLVSDQLP SIPHPGSKKL KGFDLDLARR
DLEHIAARPH PYNSHANDAV REYLLNRLDD IAWGKDHVHL DNDLRSNGSW ASPKYGVYFE
GTNLLVKIDG TDDDPHTQIP RGVADGVLFS AHYDSVSTAA GATDDGMGVV TLLQLIQYFA
ENRQRKTAIF NINNGEEDWL NGAHAFLQHP WANLTSTFLN LEGAASGGRP ILFRSTSLKP
VKAYDDVPHK LRVRHPHANV IFSDAFARGF VRSGTDYSVY TGIDRHGPAA EGGLLREGLD
IAFYKGRSRY HTRWDAPAYT EGGERSLWSM IDVARGVGVG LLNPEDSAKQ KSKPGVYFDR
PVVLALLWAI GAVLKHNAGS PPPPPKPTVP HSANNASAGT GRPGASTRQP TRSFGSNEDA
NSERGILARI KSVSVKNVLI TVWKQASFWI ALIVTVGLQA LLAWGYVAIN PFTIYSRPYF
VLLSFFALSF FSMTLVLQAA FPSSPVKHAI EVREQEKTTI LLHLHLLSWI ALLLSTILIG
KSQVGSFYVV TVWYLGIWAA TVIGTLQPIL VSKRADDKGK RRARRSRSAS TSSSSSSSSS
SSSGSDTETE RPSTQPASER TPLLFGRANG ASNRRKTNSK SKEDGAIGWW IAQVLLTVPP
VVMLVGQITS IVLEAMNQTL TDGNSAWSIY LLTALLATML VLPVAPFSPK LHRGLIFLSA
AVFVGFTIYL WVVFPFTRQD PFKVFFQQTV SLDREDVFPM NATGNAVTTH GPKIVTELTG
NPAYLRRVLP YLPSSREEDI TCSPHEVRTG LETCRWKSNR LAPFPGGKDP WSTWDSDAQR
TTTDVSFFKA DVTRTAWASA RFIVQGRNTR NCRLYFDPPE KSGVRVVRYV VHGGAKGMQP
GYPVDLVNGV QEIRLWSRTW GKAWEVDVDW ETPLGTGEDE GQLAGRIACE WVEYQSAMVD
NGSFGPDRQP KIPALEEALT FLPEWVAVSK AADGLVEASA PFTVV
