PFF1_SCHPO
ID PFF1_SCHPO Reviewed; 843 AA.
AC O94479; Q9UU46;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=SPCC1919.12c {ECO:0000312|PomBase:SPCC1919.12c};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 521-705, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
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: Membrane {ECO:0000269|PubMed:10759889}. Vacuole
CC membrane {ECO:0000250|UniProtKB:P38244}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
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DR EMBL; CU329672; CAA22643.1; -; Genomic_DNA.
DR EMBL; AB027788; BAA87092.1; -; Genomic_DNA.
DR EMBL; AB027817; BAA87121.1; -; Genomic_DNA.
DR PIR; T41237; T41237.
DR RefSeq; NP_588494.1; NM_001023484.2.
DR AlphaFoldDB; O94479; -.
DR SMR; O94479; -.
DR BioGRID; 275729; 4.
DR STRING; 4896.SPCC1919.12c.1; -.
DR iPTMnet; O94479; -.
DR MaxQB; O94479; -.
DR PaxDb; O94479; -.
DR PRIDE; O94479; -.
DR EnsemblFungi; SPCC1919.12c.1; SPCC1919.12c.1:pep; SPCC1919.12c.
DR GeneID; 2539157; -.
DR KEGG; spo:SPCC1919.12c; -.
DR PomBase; SPCC1919.12c; -.
DR VEuPathDB; FungiDB:SPCC1919.12c; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; O94479; -.
DR OMA; LTMLWIT; -.
DR PhylomeDB; O94479; -.
DR PRO; PR:O94479; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000329; C:fungal-type vacuole membrane; ISO:PomBase.
DR GO; GO:0016021; C:integral component of membrane; NAS:PomBase.
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 GO; GO:0051603; P:proteolysis involved in protein catabolic process; NAS:PomBase.
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..843
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000174139"
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..347
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 348..368
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 387..407
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..417
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 418..438
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 457..477
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..484
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 485..505
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..566
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 567..587
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..608
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 609..629
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 637..657
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..843
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT ACT_SITE 191
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 147
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 159
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 159
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 192
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 217
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 292
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 291
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 754
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 788
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 521..528
FT /note="HEEDALIG -> IQRRRTDW (in Ref. 2; BAA87092)"
FT /evidence="ECO:0000305"
FT CONFLICT 624..639
FT /note="SGPFIFRALSKKSLAV -> QWTFHISCLVKKVACC (in Ref. 2;
FT BAA87121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 843 AA; 95647 MW; 80E1A404253574E3 CRC64;
MTNSRRHIFE RICAKAFQSS LTCSIFGFTV LLILYLLDWK RIAQVPGPNL LKDLEFQRAW
NDLEYISSLP HPYNSKQNEH VRSYILKSMR ELEATNQSYI TVIDDTLTNI TFESTDNDTL
TYFEGDNILV KFEGKSKDLF PILLSAHFDS VSTGYGATDD GMGVATVMAI ARYYAKNQPN
RDLIININNA EEDYLFGAKA FASHKLSKNV TAFVNLEGAG SGGKAMLFRS SNGHVSSAYF
KGNHYPLASI LGNDFFKRGV IRSQTDYIVY EKMHNHTAGL DIAFYENRDI YHTRKDDINH
LMPSSLRHMM YTASNAVKNL LNDSKSDLTK FRKPMFFLAF GKYWQLNLPI YQVLNIIFAV
ICPIVLLLTL IRFPSLYEQL KKPRYTVCFV VSCIFVSIFD TLTVLLLTWI NPYVINSHTG
LILALFYLTN LIALAFSFRA AATHSKLSSE DLSSIEIVFI WYAQILWYLV FIVSVILSIY
FQLGSTYWVT LSYLCTFTCC IMTIIRINYF VDNVVTTQTT HEEDALIGSS INTSSHQHYG
STLNSTPHRR NSIALSNRAH VKLIDNIWTV IYFIFNVPFP VFLCYDILVE TILPAGSQTL
TDSVFSSKLY KLVIFVVFLS LVNSGPFIFR ALSKKSLAVL TMLWITLFVQ ALSVNPFTES
APLKLSFVQM YDMDRMNNTV YVKNISPFTQ DVLSLNPHFL FSNGSCNTSL CYYESTDPDF
GGLKTPMSIH IEREKHQLDI SINSGSKWCY VDFNTSVFFE AINGNSISGM YSSVRMGQRS
FYAPYTLNLT ITEVVKAEVT CLYDDIHEGI IPAYNTFVEH LPSWVAGVKA STGLLKVKSS
IVI
