PFF1_SCHCM
ID PFF1_SCHCM Reviewed; 898 AA.
AC D8QAM0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 39.
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=SCHCODRAFT_69280;
OS Schizophyllum commune (strain H4-8 / FGSC 9210) (Split gill fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Schizophyllaceae; Schizophyllum.
OX NCBI_TaxID=578458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H4-8 / FGSC 9210;
RX PubMed=20622885; DOI=10.1038/nbt.1643;
RA Ohm R.A., de Jong J.F., Lugones L.G., Aerts A., Kothe E., Stajich J.E.,
RA de Vries R.P., Record E., Levasseur A., Baker S.E., Bartholomew K.A.,
RA Coutinho P.M., Erdmann S., Fowler T.J., Gathman A.C., Lombard V.,
RA Henrissat B., Knabe N., Kuees U., Lilly W.W., Lindquist E., Lucas S.,
RA Magnuson J.K., Piumi F., Raudaskoski M., Salamov A., Schmutz J.,
RA Schwarze F.W.M.R., vanKuyk P.A., Horton J.S., Grigoriev I.V.,
RA Woesten H.A.B.;
RT "Genome sequence of the model mushroom Schizophyllum commune.";
RL Nat. Biotechnol. 28:957-963(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; GL377308; EFI95857.1; -; Genomic_DNA.
DR RefSeq; XP_003030760.1; XM_003030714.1.
DR AlphaFoldDB; D8QAM0; -.
DR SMR; D8QAM0; -.
DR EnsemblFungi; EFI95857; EFI95857; SCHCODRAFT_69280.
DR GeneID; 9587746; -.
DR KEGG; scm:SCHCODRAFT_69280; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; D8QAM0; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000007431; 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..898
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411740"
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..342
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 343..365
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 366..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 412..432
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 434..454
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 480..500
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..509
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 510..530
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..593
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 594..614
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 615..635
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 636..656
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 665..685
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 686..898
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 139
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 151
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 151
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 184
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 209
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 284
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 283
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 733
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 898 AA; 98026 MW; 98753A3C4ACC49A3 CRC64;
MGIVDYLVAA VSFRTLPTTF VAVLVYLAIF ISVLITDELP ATPKDQRGLN LTQAYSDLRQ
IAARPHPYNS HANDVVHDFI LTRLQDATAG YDYAHVFDDK VSNGSWSSRN NSVYFEGTNI
LVKVDGHDAD KSGALFSAHY DSVSTAPGAT DDGMGVATLL QLVEYYVKHR PQRTAVFNIN
NGEEDWLNGA HAFLEHPWSN LTDTFLNLEG ASSGGRPLLF RATATAPVRA FREKYVTHPH
GNVLSSDAFA RGVVRSGTDY SVYVDGRGMD GADLAFYKGR SRYHTRYDAV QYTDGGVRSL
WAMMEAAQGV SGALLSSEAV HGDKGGAPVY FDLFGQALIV FPLSAMITFN IVFLVVGPIM
LALLVTFDIV ARHRRQEMIG GGYEEQGFFA RAWTSFKSFR WVGGFWKHAK FWVALAVTVG
LQVLLCVGYL YINPLIAYSS SHIVLLSFLS LAYLSTYLVH NIPSPTDTYG SHLPEQQKQA
ALFQLYFFTW ILLLAATVVG AKLSVGSFYI LSLWNAVLFA ACAIGSIAGL LSSHTVEGDA
SYGSRRRIRG VRYDREGEEE GVESETAPTE VTPLIAQPIT VVAPGGKEGE EVSGAIGWWF
VQFVLSVPAV VILVSQLALL MLAATEQTLA DGSPAVTVYG GASLMSVLAI LPLAPFACKL
HRRVAYVALV VLIASTAYAW LVFPFSERAP LKVFFQQQVD LDANITETRI TGHPAYLRQA
IAALPSAGGA PLNCTADDAK AGLQTCGWTP PPALEPSVIA LDFNVSRSEG QNQARFEIAE
TDTRACRVYF DQAVTRFQVH GGTEGVQKGF EIPEEGVREL RLWSRTWDRT WVVDVDREGS
ALTGRVACEW SEYASGSLGV ETRTRIPAYE EVLTFLPSWA VASKFADGLV EGYKAFAV
