PFF1_CLAL4
ID PFF1_CLAL4 Reviewed; 1023 AA.
AC C4Y9H0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 43.
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=CLUG_04860;
OS Clavispora lusitaniae (strain ATCC 42720) (Yeast) (Candida lusitaniae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Clavispora.
OX NCBI_TaxID=306902;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42720;
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; CH408081; EEQ40732.1; -; Genomic_DNA.
DR RefSeq; XP_002614845.1; XM_002614799.1.
DR AlphaFoldDB; C4Y9H0; -.
DR SMR; C4Y9H0; -.
DR STRING; 306902.C4Y9H0; -.
DR PRIDE; C4Y9H0; -.
DR EnsemblFungi; EEQ40732; EEQ40732; CLUG_04860.
DR GeneID; 8495413; -.
DR KEGG; clu:CLUG_04860; -.
DR VEuPathDB; FungiDB:CLUG_04860; -.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; C4Y9H0; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000007703; 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..1023
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411711"
FT TOPO_DOM 1..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 81..101
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..425
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 426..446
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..461
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 462..482
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..491
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 492..512
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..529
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 530..550
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 551..564
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 565..585
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 644..664
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..687
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 688..708
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..712
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 713..733
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 734..1023
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 17..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 259
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 214
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 226
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 226
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 260
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 285
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 357
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 356
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 675
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 815
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 858
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 892
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1023 AA; 114211 MW; 0881B7B6941CBE67 CRC64;
MRAAGCGGTG VAALTTKLSR SISQHQPKSM PQASVNSEQN PSVPNSPSAH KPARSQSAQS
APSRAKWFVR FFRSVFGYRK TSLTFLVALV FAATLLLSWA DSSLDFSVDM PTSKHEQAVL
SRSWESLQKI ARTKHTYTSE GNDEVHAYLE AHIASLVAKK PYMELDTDKN GTRRVMFDVK
YLSYDSVSYY ESNNLVVRVN GSDSSLPALL VSAHYDSVPT SYGVTDDGMG VASMLGLLEH
YSSVAQPKRT IIFNFNNNEE FGLYGAQAFL AHPWFSQIAY FLNLEGTGAG GKAILFRGTD
YGIVRHFSSV RFPFASSLFQ QGFNNRLIHS ETDYSVYIKA GLRGLDLAFY KPRDIYHTTR
DSIQNTNIKS LWHMLSSSLD FVEHVSSQTI DLDEEVHAEA GKRDLALYTS FWNHFVVFSV
SQVVSANIAL LVVVPVASLL LLFIIFRCNK GWGFNFVNAI KYPLSLVASV LVLTFVSQVI
IVPSNPFLVN SSIGLLVATL FSLFLLLNYI VLNGLNLVFK SFKGHQHDEK LIVMCESSFL
TWILLLWSTV KLSHNKFGDD HTGELFIPIL FSLQAVACFL GFLGWCFKPS KKVKVSREEH
QPLLSSNGSN YGTQDDDDSL APSSSLSLQS GFSENCEVHE TKSFSYDWLV QFLVIVPISS
LIIFNSGSLI LNGLNKSIQE SLSAQNLIYK FIQIFVIVWS IPFLPFIFKL NRIIVLALSL
VLLYGFFAVN ITDAFNDANP LKLRFLETIS MDTSPPTNLV TVSARSMDVV KDILEDMPSL
KDSKTELSID SLGDGMSLYS YETPLIPHLV PGVKNLTDYL SIDVLKDSSS VSDSPFGLLT
GELKINVPRN RNCKIDFNMS NTVIKVSDTK FMESKRSPVR TVIVYNEDKY ENKSSSVIGA
GVPEGFSRDS KGNSVFKDMD GISQLQLNKL NWDKPYHIGF QWVPEIVESE SVWSEKIRTK
KLGVNIECYW GDLDQLAEKD KAGNPVVQDR VPAFEELLHY SPSYVSWANR DRGMVSVTKY
IEV
