PFF1_LACTC
ID PFF1_LACTC Reviewed; 962 AA.
AC C5DDZ2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 54.
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 OrderedLocusNames=KLTH0C04972g;
OS Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS (Yeast) (Kluyveromyces thermotolerans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=559295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284;
RX PubMed=19525356; DOI=10.1101/gr.091546.109;
RG The Genolevures Consortium;
RA Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P., Jubin C.,
RA Poulain J., Barbe V., Segurens B., Artiguenave F., Anthouard V.,
RA Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R., Durrens P.,
RA Jean G., Marck C., Martin T., Nikolski M., Rolland T., Seret M.-L.,
RA Casaregola S., Despons L., Fairhead C., Fischer G., Lafontaine I., Leh V.,
RA Lemaire M., de Montigny J., Neuveglise C., Thierry A., Blanc-Lenfle I.,
RA Bleykasten C., Diffels J., Fritsch E., Frangeul L., Goeffon A.,
RA Jauniaux N., Kachouri-Lafond R., Payen C., Potier S., Pribylova L.,
RA Ozanne C., Richard G.-F., Sacerdot C., Straub M.-L., Talla E.;
RT "Comparative genomics of protoploid Saccharomycetaceae.";
RL Genome Res. 19:1696-1709(2009).
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; CU928167; CAR22003.1; -; Genomic_DNA.
DR RefSeq; XP_002552441.1; XM_002552395.1.
DR AlphaFoldDB; C5DDZ2; -.
DR SMR; C5DDZ2; -.
DR STRING; 559295.C5DDZ2; -.
DR MEROPS; M28.A05; -.
DR EnsemblFungi; CAR22003; CAR22003; KLTH0C04972g.
DR GeneID; 8291308; -.
DR KEGG; lth:KLTH0C04972g; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; C5DDZ2; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000002036; Chromosome C.
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..962
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411719"
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..359
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 360..380
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 381..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 391..411
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..431
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 432..452
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 461..481
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..489
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 490..510
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 511..601
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 602..622
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 623..639
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 640..660
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 661
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 662..682
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 683..962
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 531..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 197
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 153
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 165
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 165
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 198
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 223
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 297
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 296
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 812
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 962 AA; 108220 MW; CA3003FE583CB404 CRC64;
MLAQFLRSLF RFRKTTVSVL LVATYVVVFL LNVWDRIRYQ YSLPEDNKHH KQLLDASWID
LQSITRKPHP YTSRENDAVH DFLLHRVTEL VEGAPHAEVS DDYKEGNHLV FKQPDVFNSS
STESRIVSFE SSNIVVKITG SQPELPGLLI SAHFDSVPTA LGATDDGVGI VTLLALITRY
AKKQPRRTLV FNLNNNEEFG LLGASAFLNH RWRPLVDYVL NLEGTGAGGK AVLFRTSDTN
TASIYKNAVK TQPFGNSIYQ QAFYDRYISS ETDYKVYEQA GLRGWDIAFY KPRALYHTIK
DSTQFTSQAS LWNMMHASLQ LADFIAFESF EDEPKDRSPA VYFDIIGTFF VTASTKDLFT
LNCVVLSVIP VIILVLEFVI QRRKTRERNP LLVWLRLPFS MFISYLVTAT FRSSLFRVNP
LIFSRDYVSP TIGFSFTFLI LNYLVLSLLE YLAPSRDLKT VSFVELFFGM WIALLWATIR
LCTSKYTATG VYPITVLYLL MSFGAIVGLV CSAFKRKHSV VKAKDSEETA APNTYSSIEE
SPQQATNTEA PNENSPEEHD ERAPLLRASN SSQVSSVTNV SEAPSSALKA FVVSALNYDW
SVQFLAVVPL ASFFVIMCLS LILDGIYQTC QEGFQATWNV SKISMLGGML LAIPVLPFCY
KLNYFVSMVL LFAAASAGIF SFERAPFTES SPLKLRFSQE LNLHDELGFS TVNVFGRQGA
GIEQILRNIP STQNAHSNVE CTSNGQGSET CRYAGPRPHL VSSSSIPELS DILSIKVLSN
NRKSSGRSSY EPINAELVIN VKENRLCTIG FNSSQFAEHD YGQSPVKQVT IFGNAHHDNR
TRSQLSTLDG LSRDDEENRI FKWNRGINSL QLHKLDFERN YYHVGIQWMP TILSQDADEE
SSDALGLKIR CFWGEYDSVS IINGEVKRKV PALDELLAYS PKEVSFSNRE AGLVIVNDYI
EL
