PFF1_ASPOR
ID PFF1_ASPOR Reviewed; 955 AA.
AC Q2UU23;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=AO090009000488;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007150; BAE54942.1; -; Genomic_DNA.
DR RefSeq; XP_001816944.1; XM_001816892.2.
DR AlphaFoldDB; Q2UU23; -.
DR SMR; Q2UU23; -.
DR STRING; 510516.Q2UU23; -.
DR EnsemblFungi; BAE54942; BAE54942; AO090009000488.
DR GeneID; 5988874; -.
DR KEGG; aor:AO090009000488; -.
DR VEuPathDB; FungiDB:AO090009000488; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000006564; Chromosome 1.
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..955
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411703"
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..390
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 391..411
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 443..463
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..473
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 474..494
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 509..529
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..533
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 534..554
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..656
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 657..677
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 678..693
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 694..714
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..721
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 722..742
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 743..955
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 574..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 174
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 186
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 186
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 221
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 246
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 319
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 318
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 826
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 955 AA; 105601 MW; D22514A5DEC98F03 CRC64;
MASLRLPRAN PLAFTRWPVT VITAIVYLAL LIPLLVVHHV VPSAPSSPPS GLNISEAWAD
LQVLTNGFHP YNSRRNDVIH SWLLRRINEI LDSTPLEQEY RALDEEKPDV FVFDDVYSNL
TTYGGTLKDA DLGVYFEGTN VIVYIRGWED DTEHWWEAPN GVPTSRGGVL VNSHYDSVST
GFGATDDGVG VVTCLQLVKY FTTPGHAPRR GLVVLFNNGE EDFLNGARVY SQHPISKLPH
TFLNLEGAGA GGRATLFRSS DFEVTGPYMR SPHPFGSVLS ANGFDTGLIA SQTDYVIFQG
NMGLRGLDVA FMEPRARYHT NQDDTRHTSK DSVWHMLSAA VATTEGLVSD STDRFDGAPN
TDGGVPSGSG SQAVWFDLFG STFVLFQLHT LFALLVTLLI VGPLTLLFTS IALTKADKMY
LFRSSAKSED RLDVVPLQGL RGFFRFPFLF GIPTVVTVGL AYLVTKVNPY IIHSSAYAVW
SMMVAAWVFL AWFVSRVADF ARPSAFHRIY TLTWMYVLSW VSAVIATVYA NQRGLAGGYF
IFFFHAGIFL AKWISYLELF ALPSKTEYAN QLRSASGRAS GHGSRRGTTS GEDDGEEAEE
EPTESTSLLG SGQRTTFANY VRVGGDNHAV AEEEVIDPNV YGREQAWSYA LPKWTWVLQL
LLTAPITLIM VGPLALLTIS AISQTGQDGG HPLFAYVAIA IFTTIMLTPL LPFIHRYTYH
VPLFLLAVFL GTLIYNLVAF PFSDSNRLKL YYVQEVDLDT GVNSATFAGL SPFVKDVSQE
LPSAAGQTVS CEWHTKRRNL LSCSWEGIAP QPVEGDHPMK DWVSFNISKS TDKPQARFEV
SGLNTRACRI LFDTPVKNFH VAGSAYDPRF PYDAAGVNEI RLWSRTWENQ WTVDVDWDEG
ALKGNVVCLW SDHNQPGVLP ALDEAIQFLP VWAAVTKGSD GLVEGRRAFE IGNDD
