PFF1_LODEL
ID PFF1_LODEL Reviewed; 960 AA.
AC A5DZ28;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=LELG_02615;
OS Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS 1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC Lodderomyces.
OX NCBI_TaxID=379508;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC YB-4239;
RX PubMed=19465905; DOI=10.1038/nature08064;
RA Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA Birren B.W., Kellis M., Cuomo C.A.;
RT "Evolution of pathogenicity and sexual reproduction in eight Candida
RT genomes.";
RL Nature 459:657-662(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; CH981526; EDK44436.1; -; Genomic_DNA.
DR RefSeq; XP_001526057.1; XM_001526007.1.
DR AlphaFoldDB; A5DZ28; -.
DR SMR; A5DZ28; -.
DR STRING; 379508.A5DZ28; -.
DR EnsemblFungi; EDK44436; EDK44436; LELG_02615.
DR GeneID; 5233296; -.
DR KEGG; lel:LELG_02615; -.
DR VEuPathDB; FungiDB:LELG_02615; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; A5DZ28; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000001996; 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..960
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411721"
FT TOPO_DOM 1..57
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 58..78
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 79..401
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 402..422
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 433..453
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..476
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 477..497
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 498..502
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 503..523
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..535
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 536..556
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 636..656
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..668
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 669..689
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..696
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 697..717
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..960
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 22..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 235
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 189
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 201
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 201
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 236
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 261
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 333
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 332
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 763
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 803
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 875
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 960 AA; 107646 MW; 466DAE7E7ADBBAB8 CRC64;
MADNNSSSGS LVIDEQDYDV HEAGQQGQQG QQKHQQRQQE RPSLITRVFR SVFGYRKTSL
SLFVVATIAL CVSLSYIDNS VDFISFPTVE SEVNLLNAAW LDLQVIAKEQ HPYGSIGNDR
VHDFLERRIQ ELITGANFIT WDNDINGNNS FMFESSSNPK TVSYYESNNL LVKIEGKNAK
LPGILLSSHF DSVPTSYGVT DDGMGVASML GILNYFSQQK KQPERTIVMN FNNNEEFGLL
GATAFTRHPW FKLVKYFLNL EGTGAGGKAI LFRATDYGIA KYFQNVRTPY ASSIFQQGFA
NGLVHSETDY KVYKEAGMRG LDLAFFKPRD YYHTAEDNIR RTSEKSLWHM LSNSLDFIDY
LSKDKEFGMN LEEKPNLLEE PAVFASFLNY FFTISTSQLF KINVALLTVF PILNGLLLLY
TIRSRKWQVS FSSAISIPVA LLVTMFIVVY LVVESYKSFN QYLPSSRPLL LVATITSILL
LVFSIILVAF SFFSIIAEEN LRLLAIVELS FAYWVGLAFT THGLSGAESA RHSGEFAVSI
LFTLEAVASF LGLIGWSLCR NRSHLQVAEG ESVPLLNGID ARYSSDNDHD HEHRHGHEDN
EHGEAHVQQQ SQSRHKKQCK ETVHSFGYDW SLQYLITVPL SIFIIYNSGW LVLEGVNKTL
QESAKAETFV YNLLWIVSVS LVLPLIPFAG KLNRYMVFVL IAIGVLGTLL VHVVQPFNEA
NPLKLRFLQR IDGKNNASSV HVYARKGLAT EVLEQLPSVR QSNETIHCSQ LADGMEDCSF
VSALAPQILP GYELGNYIEV TNNGSAPSQL FGVNYNQIKI VALKSQSCSL HFGDSKVKAV
VVGSSLESAP AFKHLPSGYS FNKDHFYKDT SGIWNLTLNK LDSHSSFDIS LYWLPGIDDE
ANTLQFDVEC FWADLSPVAL NNTVFEAIPA FNEVQQYSPI SVSWANREKG LVAYTKQVHV
