PFF1_PICST
ID PFF1_PICST Reviewed; 937 AA.
AC A3LW86;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 61.
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};
DE Flags: Fragment;
GN ORFNames=PICST_46351;
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000499; ABN67242.2; -; Genomic_DNA.
DR RefSeq; XP_001385271.2; XM_001385234.1.
DR AlphaFoldDB; A3LW86; -.
DR SMR; A3LW86; -.
DR STRING; 4924.XP_001385271.2; -.
DR EnsemblFungi; ABN67242; ABN67242; PICST_46351.
DR GeneID; 4839595; -.
DR KEGG; pic:PICST_46351; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; A3LW86; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR Proteomes; UP000002258; Chromosome 5.
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..937
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411736"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..373
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 374..394
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..407
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 408..428
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 429..437
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 438..458
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 476..496
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 497..510
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 511..531
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 532..580
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 581..601
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..618
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 619..639
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 640..643
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 644..664
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 665..937
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT ACT_SITE 201
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 154
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 166
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 166
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 202
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 227
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 300
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 299
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 606
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 870
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 887
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT NON_TER 1
SQ SEQUENCE 937 AA; 104591 MW; 18EC9D168229BC5A CRC64;
PNGFVKFIRS IFGYRKTSLT LFVILTYVAV LLLAYLDHSL YYSVDLPTSH KEQELLHQAW
VDLQHIAKYE HAYGSSGNDY VHDYLESRIV SAVAHKSYVE YDNDLNYTNN IMFGSRSELS
GNSFNSVSYY ESNNLVVRIN GTDETLPALL LSAHFDSVPS SFGVTDDGMG IASLLGVLYY
YTGKSTARPR RTIVLNFNND EEFGLYGATS FLSHPWATGV HYFLNLEGTG AGGKAILFRG
TDYGITKYFK GVRYPYGTSI FQQGFNNHLI HSETDYKIYK EKGGLRGLDV AFYKPRDLYH
TAGDNIKNID IKSLWHMLSN ALDFTAIVTK GKIDLDADSL DSESSKSNTD TAVYTSFLNF
FFAFPTSQVV VASILLLVLI PGISIPFLII IFGYKKNWEL SFVNVTKFPI SLAISAALLN
LFTNGFIVPF NQFLPNSSPF ALVAILFATF LLLNYLILNG INLIFVSYKI VNHDEKLISI
IETSFLYWVV LIYSTAKLAN NVIGDDHSGE FPIIFLCALQ AVASIFGLIG WSFKPVPKEH
YVVVPQEEAE PLLGSSDNFN YGSPDVEDDR LVSDGSYDWS IQFLTIVPIS TYLIYNSGFL
VVDGINKSIQ ESLISQNLIY KLLQTFAISL SIPLLPFIFK VNRLFVLALF LISTIGVLFV
ATADSFNVAN PLKLRFIQYI DLDKSAQDSF VSVIGREASP LQFVLSDIPS VKDSKGAVAC
VPTRDGLQDC SYKSSLDPKL VPGAKSFDDY LKVDILKNSS SNVDYPFGLL TGEIRIRVPK
NRECVLDFKP SESTKIVSPF KDSPVKTVIV YKGKKSATTK EVEAESIPEG FSKDKDGNYV
YKDLVGIDQL QLNKLDWDKS YHVGFQWVPN FSDVDINMKK SATNKLNVSV KCFWAELGKG
EESTIPAYEE LLHYSPNYVS WANSAKGLVS VSKTVEL
