ID A3LZ45_PICST Unreviewed; 345 AA.
AC A3LZ45;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 27-MAR-2024, entry version 91.
DE RecName: Full=CAAX prenyl protease {ECO:0000256|RuleBase:RU366005};
DE EC=3.4.24.84 {ECO:0000256|RuleBase:RU366005};
GN ORFNames=PICST_33410 {ECO:0000313|EMBL:ABN68273.2};
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 {ECO:0000313|EMBL:ABN68273.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN68273.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
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: Proteolytically removes the C-terminal three residues of
CC farnesylated proteins. {ECO:0000256|RuleBase:RU366005}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR627057-2,
CC ECO:0000256|RuleBase:RU366005};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR627057-2,
CC ECO:0000256|RuleBase:RU366005};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU366005}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU366005}.
CC -!- SIMILARITY: Belongs to the peptidase M48A family.
CC {ECO:0000256|RuleBase:RU366005}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU366005}.
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DR EMBL; CP000501; ABN68273.2; -; Genomic_DNA.
DR RefSeq; XP_001386302.2; XM_001386265.1.
DR AlphaFoldDB; A3LZ45; -.
DR STRING; 322104.A3LZ45; -.
DR GeneID; 4840435; -.
DR KEGG; pic:PICST_33410; -.
DR eggNOG; KOG2719; Eukaryota.
DR HOGENOM; CLU_025947_3_0_1; -.
DR InParanoid; A3LZ45; -.
DR OMA; GHWKFSH; -.
DR OrthoDB; 3080668at2759; -.
DR Proteomes; UP000002258; Chromosome 7.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071586; P:CAAX-box protein processing; IEA:UniProtKB-UniRule.
DR CDD; cd07343; M48A_Zmpste24p_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR InterPro; IPR027057; CAXX_Prtase_1.
DR InterPro; IPR001915; Peptidase_M48.
DR InterPro; IPR032456; Peptidase_M48_N.
DR PANTHER; PTHR10120; CAAX PRENYL PROTEASE 1; 1.
DR PANTHER; PTHR10120:SF24; CAAX PRENYL PROTEASE 1 HOMOLOG; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF16491; Peptidase_M48_N; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU366005};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366005};
KW Membrane {ECO:0000256|RuleBase:RU366005};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR627057-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU366005};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366005};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Transmembrane {ECO:0000256|RuleBase:RU366005};
KW Transmembrane helix {ECO:0000256|RuleBase:RU366005};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR627057-2}.
FT TRANSMEM 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT TRANSMEM 91..113
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU366005"
FT DOMAIN 10..119
FT /note="CAAX prenyl protease 1 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16491"
FT DOMAIN 123..327
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 193
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT ACT_SITE 275
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-1"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
FT BINDING 271
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR627057-2"
SQ SEQUENCE 345 AA; 39620 MW; 0C42248CDA65623D CRC64;
MSRAVFLPKF MKGTITHSLF FYTTISLISE LIDLPFSYYR EFVVEEKFGF NKQTLGLWLR
DHILAFSLNT VIVNVVLSGL LKIFEIYGES FIIYTTGFLV VVSFAVQSLS PFIGRLFYKF
TALQDENLKH QIENLASKFN FPKTNIFVID GSTRSSHSNA YFVGLPWYKE IVIFDTLIEK
QTTEGVVAVL GHELGHWKLN HIPKLMLIQL LDFTQIFGLF GVFIYNKSLY SSFGFTDNQP
AIVGLVLYWI IKEPISTATR FVTNIFSRKF EYQADEFAKS LGYQDELSKS LLKLDINSSS
VTNTDWLYSA YYNGHPLLSE RLSALGYISK EKISRETKSK PLKED
//
