PFF1_SCHJY
ID PFF1_SCHJY Reviewed; 847 AA.
AC B6K327;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 46.
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=SJAG_03009;
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936;
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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; KE651167; EEB07884.1; -; Genomic_DNA.
DR RefSeq; XP_002174177.1; XM_002174141.2.
DR AlphaFoldDB; B6K327; -.
DR SMR; B6K327; -.
DR STRING; 4897.EEB07884; -.
DR EnsemblFungi; EEB07884; EEB07884; SJAG_03009.
DR GeneID; 7051778; -.
DR VEuPathDB; FungiDB:SJAG_03009; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR OMA; LTMLWIT; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001744; 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..847
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411741"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 18..38
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..348
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 349..369
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 382..402
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 403..415
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244, ECO:0000305"
FT TRANSMEM 416..436
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..454
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 455..475
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..482
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 483..503
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..560
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 561..581
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..605
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 606..626
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 627..630
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 631..651
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 652..847
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 146
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 158
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 158
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 191
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 216
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 291
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 290
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 726
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 734
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 800
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 834
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 847 AA; 97017 MW; C24FF93F39141B11 CRC64;
MQFGKSLLKH VYTRTFKSSL TCSIFAFTLL MIFFVLDWKR MNVYPRLDEI PGLNVLRAWD
DLQEITKSPH PYNSHASDVV RNYILEELYK LKKQDEGNVE VIDDLSSTTT FIMPDTNIRS
YFEGSNILVR FRGDNERLRP ILLSSHFDSV STGFGATDNG MGVASALELA RYYAEHKPER
DLIINFNNAE EDYLYGARAF TEHEWSKNVT AFLNLEGAGA GGKALLFRST NNHVARSYFK
SNRFAFASVL GIDAFKRGVI KSETDYVVYE KMNNGTAGLD LAFFRNRGIY HTERDDIQHT
SIFSLNHMLV NAFISLRNLL DEKSQHFKGS SPLYFPVFGS YWQINLNLHL FLNVVFLIAC
PAILFMCLFR FPSLYAQLKK PCYLICFTLS SLFVLIFDYV VVQSLTKLNP YVIHSSPDAV
LAFFFLTNLL GLVYSFRYVA THSRMSNEEL SCIEIVLIWY VSMFWYISLL IATLTSIVRG
LGSLYFVNFG FFCSFFCCIL TLIRVRYFVD RMVTINRPAN PEQMPLVQST SGNAYGTSRY
PQHRLKAVVS KSASVKLNDN LWSVLFFSCL VPLPLFTCYN LLSEVFIPAV HQSLIDGPYS
NTCYKFAVIL VFMAIINSSP FVFRALSKKS SAILLMLWVS LLFNILRAEP FNEKAPIKFR
VFQHLNLDTS ENLFHVQNIE PYTQKVLNDY PKIISDTSYQ CVDRDCFYEA EEPTLGFDGP
LQNAINITLH KSLNSSLAEL RVDAFETKWC YFDFSVPVYV DSINGFEVQE EHQSLRLGVR
NFGTPFVVKT VAKDEDSPTN VTVTCMWDEF DHDKIPSYTS LLNYIPAWSV LTKNSTGLLK
MSKTHVM
