PFF1_YARLI
ID PFF1_YARLI Reviewed; 989 AA.
AC Q6CDE6;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=YALI0C01133g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382129; CAG81611.1; -; Genomic_DNA.
DR RefSeq; XP_501316.1; XM_501316.1.
DR AlphaFoldDB; Q6CDE6; -.
DR SMR; Q6CDE6; -.
DR STRING; 4952.CAG81611; -.
DR MEROPS; M28.A05; -.
DR EnsemblFungi; CAG81611; CAG81611; YALI0_C01133g.
DR GeneID; 2909156; -.
DR KEGG; yli:YALI0C01133g; -.
DR VEuPathDB; FungiDB:YALI0_C01133g; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; Q6CDE6; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000001300; 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; IBA:GO_Central.
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..989
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411749"
FT TOPO_DOM 1..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..383
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 384..404
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 427..447
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..460
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 461..481
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 489..509
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..520
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 521..541
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..611
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 612..632
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 633..648
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 649..669
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 670..673
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 674..694
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 695..989
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 227
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 181
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 193
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 193
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 228
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 253
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 325
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 324
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 793
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 989 AA; 109272 MW; C8EF21E0D18C9751 CRC64;
MDRQSLRTTL RAMDASNENG SAKGAKKTTI GSFVRWTFGF NSVPLTTLVT ITTVLLGLLV
YVSTSVNPPD VTEAQKPLLN YAWAQLGEIS RYPHPYFSHD NDRVRQHILK EVYTLAGREH
FEGAQIEVDD SQTDIFIQKE DVFDKSAPPG KLTYFEGNNV VVRLSSKNSD KSLGAILLSA
HFDSVPSSFG VTDDGAGIAT MLAVLKHALA QNEGPKRDII FNFNNNEEFG LLGAEAFMHH
PWAQNVSAFI NLEGTGAGGK AILFRASDYG VASHYSAAEM PFASSVYQEG FSNGFIHSQT
DYKVYTEGGL RGLDIAFYKP RALYHTRRDN IAETTKNALN HMLVNTIDVT QSMTEADSFD
HADQPAVFSD IGGYLFIILP LQYIFVISCL TLAVGPIFVG FLFLLVLRKQ INAGTSETIL
GGWLRSIVSV LVSVVATYFV VETLHLGNEL YVVRSFYTPL FAGLGTFIFV NYVLLGFFHF
VRPVCDQKLI ILLELSVVLW VLLLLSVIHE ATHKATGEYH FLILYIVVAT ASILGLFGHL
VTSTETSTFV EGPEDEEDTV DASEATETSP LLPEASPDNA APSIHGAVDP ENQQEDKTLQ
KIAVSMGYDW SIQFLLVVPI TFFVTFGLAA SLLDGLHQTP LESEKSADFV YTTITAMSVL
VGITFLPFVH KLQVFVPIVV VGVAVTASFV HILSPPFSSN APAKMRFVQN INLDEGTSYA
NVLGRQDVLQ EVLEYIPSTD TFKPNCSSRG DGVEICNYIA PRPWLIDGEK VSSDGDFAGL
PTNLLDVKVV PVNETSSGPF DRFDGRFKIS ALNNRGCVLR FNTTRFKSGD VETGVSPVKM
VTLRHNRVGK TGITTGSGSR FSMFGWTRDP KTGKDEFRSF MHGVDDVTLH KLDWEDPEYD
IQLSWIPRWY EVGDPEDEGN EALKNRLGVT VTCSWAEYLD PSSIVDEQGR RRTMDKIPAF
TELNNFSPAW SIWSNQGRGL VEVSKYVEL
