PFF1_KOMPG
ID PFF1_KOMPG Reviewed; 990 AA.
AC C4R628;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
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=PAS_chr3_0953;
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(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; FN392321; CAY71014.1; -; Genomic_DNA.
DR RefSeq; XP_002493193.1; XM_002493148.1.
DR AlphaFoldDB; C4R628; -.
DR SMR; C4R628; -.
DR STRING; 644223.C4R628; -.
DR PRIDE; C4R628; -.
DR EnsemblFungi; CAY71014; CAY71014; PAS_chr3_0953.
DR GeneID; 8199700; -.
DR KEGG; ppa:PAS_chr3_0953; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; C4R628; -.
DR OMA; IHRFTYH; -.
DR Proteomes; UP000000314; Chromosome 3.
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..990
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411735"
FT TOPO_DOM 1..97
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 98..118
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..433
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 434..454
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..470
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 471..491
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..501
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 502..522
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..534
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 535..555
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 556..565
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 566..586
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..625
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 626..646
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 647..662
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 663..683
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 684..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 691..711
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..990
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 276
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 229
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 241
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 241
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 277
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 302
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 374
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 373
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 651
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 831
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 860
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 884
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 990 AA; 111629 MW; BC7FAD1BD47B24B1 CRC64;
MSNSSPKEQN AAADLQSFRN GEPSLTYTSN HDNDDADESA IIDDDEDEEA HQQEGNTQNQ
GEQSPVRQQQ DTASLDSFSS QPSLFVRFIR STFGFRKTTL TLAVVLSYLF VILVNAAFEK
QSLVIESPEP AILTKAWTDL QVISKDIHPF DSKANDEVHD YILERTRSIA ATKPYIEARG
DNSTVMFNQP DLFNSSSSTN RIIYFESTNV LVRVKGTDPS LEALLISAHY DSVSTSYGTT
DDGMGIASML GILEHLADKK TERPKRDIIF NFNNHEEIGL LGASVFFEHP WSDKVKYFVN
LEGTGTGGRA VLFRATDTGI ISHYSNVRSP FANSFLQQAF NGGMIHSETD YRVYAEHGLR
GVDIAFYRPR SLYHTRRDSI KGANRESLWH MESNALDLVL DLGYNSIDED LSPSIFFDVL
GQQFVYFSLD NLYILNISLL VLIPVLSIVL LLIVKKRHTW HIYSTRGWLR FPITTVFSIT
FVTLVGRFFL FHDAMIISRN WFTPLIALTS LFLIVSYIGL NFANWVVPIH DQKLAILLEL
NSLLWIATLW ATVEIKRYSN VGNYAITIYY ILASLSSLFG LLALALKPRQ RIELPEDLDE
EGDNTRGVQQ RLKEAALKSF SYDWSIQFLL LVPIWLLVTY SFGGLGLEAI NQTIQESNAL
GEISFKFLGA VAVLLGLSVL PFVHKLNAAL TVLLAVTCAI SSFATLVGPV FDYQHPLKLR
FVQQVTRAGE TQVKVFGKHG FIEPVINDLP SVKQLKRNYT CTELSDGNGQ CVYDGQRPWL
VDGSAVQNEF ENLLTVKVLS DTNTGKTRYV PFDSDLEIKA VQSRHCLLLF NTTTFHSGNG
VDKYKNAPVK QVSLYHKLQN NTRPEMKDNF ALSFVPSGHS VDENGTDIYR LNQGIDEFLV
DKTEWNQDTF HVGIEWLYDW SEESDGDKRD RNLGVTVRCY YGEYDAVSVI DGEAKRKIPA
LDELLQYAPV DVEISNLDRG LAYLEQYVEL
