PFF1_NEUCR
ID PFF1_NEUCR Reviewed; 1072 AA.
AC Q1K7M0; Q9C2E0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 63.
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=9G6.250, NCU04133;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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; AL513463; CAC28773.2; -; Genomic_DNA.
DR EMBL; CM002240; EAA32053.2; -; Genomic_DNA.
DR RefSeq; XP_961289.2; XM_956196.3.
DR AlphaFoldDB; Q1K7M0; -.
DR SMR; Q1K7M0; -.
DR STRING; 5141.EFNCRP00000003961; -.
DR EnsemblFungi; EAA32053; EAA32053; NCU04133.
DR GeneID; 3877453; -.
DR KEGG; ncr:NCU04133; -.
DR VEuPathDB; FungiDB:NCU04133; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; Q1K7M0; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000001805; Chromosome 2, Linkage Group V.
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; IBA:GO_Central.
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..1072
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411727"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 10..30
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..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..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 458..478
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..492
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 493..513
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 524..544
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..554
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 555..575
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 576..747
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 748..768
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..789
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 790..810
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..817
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 818..838
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 839..1072
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 593..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 231
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 185
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 197
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 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 232
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 257
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 330
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 329
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 116
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 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 932
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1072 AA; 118503 MW; 9436F71C686F9024 CRC64;
MINPISFRPG PVTFWTTLIY LALLIPIVII NEKTPAAPKT AEPFKGVNLT EAWLDLTTIT
RAYHPYNSKF NEEVRRYLLE KVETILEENG ASWVSDGQMT TVKDGKSAAV TVFDDNVSNS
TFVMGKSNGT TFTRTDSINN AAYFEGTNIL VYIRGKEDDE GEWWEADYAH GMRRNAKGLT
LVNAHYDSVS TGFGATDDGM GVVTALQVLK YFTAPGHQPQ RGIVVMLNNG EEDWLYGAHA
LGQHKLNPFI HTFLNLEGAG AGGRAIVFRA TDREVMAAYA RTSHPFGTVI ASDAFGLGFI
SSGTDYSVLV DAYGQRGIDL AFFKPRARYH TNQDDTRHTS KGSLWHMLSA AIHTTKQFSG
DTGNTFIGQR PDKAHGKVAN GRSSNGVWFD LFGKSFVLFG LRGMFAWSLT LLIATPLVLV
GITWLLRNLD KDYFFTSTVK TKEHPEYEAV PIGGWKGFFR FPFALGVAVF FTISSALLMN
KVNPLIVYSS RYSVWVMMVS IFYFSFWMIM RGANFVRPSA LHRGYANLWL FVFGWIVLVA
VTALEDRRRI AAGYIFVFLE SAIFLSCLIS FVELLAVPRK SSYALQVQED YDGQEHDHNG
YQGFRDSTDE PSLRARAESS ASAASPPSPT VAQEPSKSKA PAGTTNGLST APSVAAHSSQ
PQPAPTTPIP GRSSGAPSTA SRDENESEDD DEPTERTPLV GGNGTNDRGR TTFATTYRRS
ITALVHGARK MEEDGEPYDH EQEWSGHLPS WAWFFQFLLL GPFMIILAAQ TGLMLTDAVY
QTGSDGSKLI TPYLIIFVFT VLLILPLTPF IHRVTHHIPV FLLVVFIVTL TYNLIAFPFS
ANNRYKTFFG QYIDVATGDN KVCYTGIEEY VRPIIAELPS ASGREVTCGK SLRRGSTIST
CCFDGSAVPP KLGSEDDNGL PEDSYADLIT INATRSTKRG DSSRTTARIE ITADNTKSCF
LQFKKPVSAL AIENGSGWDD RFGQYPEDGV GLVRLWHREF GKTWVVNAEW KGSETRKEYD
ENDGTVICMW SDANTPGTIP ALDEALQFVP SWAAVTKFSE GLVEGRKAFK IV
