PFF1_KLULA
ID PFF1_KLULA Reviewed; 913 AA.
AC Q6CKC6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=KLLA0F11748g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR382126; CAG98321.1; -; Genomic_DNA.
DR RefSeq; XP_455613.1; XM_455613.1.
DR AlphaFoldDB; Q6CKC6; -.
DR SMR; Q6CKC6; -.
DR STRING; 28985.XP_455613.1; -.
DR MEROPS; M28.A05; -.
DR EnsemblFungi; CAG98321; CAG98321; KLLA0_F11748g.
DR GeneID; 2895957; -.
DR KEGG; kla:KLLA0_F11748g; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; Q6CKC6; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000000598; Chromosome F.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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..913
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411717"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..364
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 365..385
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 395..415
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..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..465
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 466..486
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 487..494
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 495..515
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 601..621
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 622..634
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 635..655
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 656..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 661..681
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 682..913
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 540..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 196
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 152
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 164
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 164
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 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 222
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 296
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 295
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 794
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 810
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 913 AA; 103763 MW; DB1C70D7ABC7E23D CRC64;
MMANYFRSTF KFRKTTVSTL FVLTVLVISI LTWFDANKYK SNLPDDKSSN SLLDAAWHDL
QVITEKPHPY TSHFNDNVHD YLLQRVEQIS KKSKFIEVSD DSANGVSKLF QHLDVFNDSS
TETRLVYYES SNILVKVEGK SPQLPGLLLS AHFDSVPTGY GATDDGKGVV SLLALLQYYS
ENQPERTIVF NFNNNEEFGL LGATIFTYSE WFKLVSYVIN LEGAGAGSKA ALFRTSDTAT
ALLYEKSVKD QPFGNSIYQQ GFYSRFVSSE TDYKIYELNG LRGWDIAFYK PRDMYHTGKD
TVQHTSKAAL WHMLNIAWQL SKYVVADQTT ASQEILDDES NSSPAIYFDI ISKWFFVVSA
RQLYVWNIVL LCVLPITLIL LRIVCNKLGT WRMPTSALFT RIPFALFVSS FTIYFTKELL
LQLNPTIWSR NFILPFLFCI SEFLLINTLV LALFEYLWPI QDFKTLSLLE LSAIAWLFLL
KCTWDLSSSG FKATGVYPVT VFYLFISLAS MFGLCSMCFG KRPNATNDYD NSEFMRPDTN
DTHSIECPRQ PEDSETTETS PLINTPSSSV QSSPIASSKS LPGAVQYLQR TLNYDWSAQY
LLAVPINAFL IWESLFNLFD ALSMTVQESN KATEAVFKFA IYGAIFLCSP LLPFTTKLNR
FVVIILGVVT ILAASFSLFA APYTELAPLK LRFVQRIDIS RETKQNVEIY GRAGANIQEV
LSSLPSRPNV SCKDSGSGTE LCVYEGMWPN FGIPMKVDVV KNTHNDKEHF EYEPYFADLR
INVADNRLCL MKFNTTGKKH LKQVEFKVGN ETTTHSYRTD EGIDSLLLHK LSWNVPYYDV
QLKWIPQYTA EGSSDTLGVS IDCYWGEFDE TIVNGQVVQK IPAYNELLQF LPETFIVSNR
ESGMVTIHKY LEL
