PFF1_ASPNC
ID PFF1_ASPNC Reviewed; 986 AA.
AC A2RAN5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
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=An18g03780;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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; AM270404; CAK97416.1; -; Genomic_DNA.
DR RefSeq; XP_001398837.1; XM_001398800.2.
DR AlphaFoldDB; A2RAN5; -.
DR SMR; A2RAN5; -.
DR PaxDb; A2RAN5; -.
DR EnsemblFungi; CAK97416; CAK97416; An18g03780.
DR GeneID; 4989942; -.
DR KEGG; ang:ANI_1_484164; -.
DR VEuPathDB; FungiDB:An18g03780; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 8L.
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..986
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411702"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..392
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 393..413
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 445..465
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..475
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 476..496
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..510
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 511..531
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..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..704
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 705..725
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 726..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..986
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 573..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 840..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..614
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..857
FT /note="Basic and acidic 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 121
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 799
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"
FT CARBOHYD 948
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 986 AA; 108883 MW; ACA29A173E2742AB CRC64;
MAPLRLSRAN PLAFARWPVT LITAVVYLAF LIPLLIVHHV VPSPPTANPN GLDLTQAWAD
LQVLTDGFHP YNSRRNDEVH TWLLQRIHEI LDAAPPADQY LSVDEEKPKP AVFVFDDTQS
NLSFVGNSLS SSNTAVYFEG TNILVYIRGS DDDHENWWEE PNGVPSGKGG VLVNAHYDSV
STGYGATDDG VGVVTCLQLI QYFMTPGHAP RRGLVVLLNN GEEDYLNGAR VYGQHPISKF
PHTFLNLEGA GAGGRAILFR SSDTEVTRPY MSSKYPFGSV LAADGFATGL IGSQTDYVVF
EVDLGLRGLD VAFMEPRARY HTEQDDSRHT SKSSLWHMLS AAVATTEGLV SDKSDQFEGA
PTDDAKVASG SGSKAVWFDL FGTTFVLFEL HTLFALSVTL LVVAPLALLV TGIALTRADK
MYLFRTSAKA DESLDSVPLQ GLRGFFRFPF LFAIPTAVTV GLAYLVTKVN PLIIHSSEYA
VWSMMLSAWT FLAWFVSRMA DFARPTALHR IYTLTWMFVL AWVLLVISTV YQNQRGLAGS
YSVFFFFSGT FLATWISYLE LFSLPRKSEY ANQNRPTSRR ASSYGGSRLG TASGEDHEED
DHDAEEEEEE QEPTESTSLL GGGQRTTFAN YVRVAGDHRD SDTDHHYYPG VYKHEQRWSA
SLPTWTWTLQ FLLMAPLVLI MVGPLALLLT SALHQTGQDG SSSLFIYVAI AALTTFLLTP
LLPFIHRHTY HLPVFLLLVF LGTLIYNLVA FPFSPTNRLK LFFIQDIDLS TGSTTASLAG
VQPYVHAAAS TLPSTANQNI TCTEHTTRGT KCAWPGLAPR VVPDTPYSDW LDFTISQQHN
TTDDKEGDED THHPRKARIT LSGRNTRACK LLFDSPISSF AVLGSSTDPR FPTSSPHGTK
EIRLWSREWE NEWVVDVAWT TSTNDDSEEG DEGEGKLNGK AVCLWSDNNS AGVIPALDEV
RQFAPSWVAV SKAADGLVEG WKGFSI
