PCYOX_MACFA
ID PCYOX_MACFA Reviewed; 505 AA.
AC Q95KC9;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Prenylcysteine oxidase 1;
DE EC=1.8.3.5 {ECO:0000250|UniProtKB:Q9UHG3};
DE Flags: Precursor;
GN Name=PCYOX1 {ECO:0000250|UniProtKB:Q9UHG3};
GN ORFNames=QmoA-10162 {ECO:0000303|Ref.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Medulla oblongata;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Prenylcysteine oxidase that cleaves the thioether bond of
CC prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine
CC (By similarity). Only active against free prenylcysteines and not
CC prenylcysteine residues within prenylated proteins or peptides (By
CC similarity). Involved in the final step in the degradation of
CC prenylated proteins, by degrading prenylcysteines after the protein has
CC been degraded (By similarity). {ECO:0000250|UniProtKB:F1N2K1,
CC ECO:0000250|UniProtKB:Q9UHG3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-prenyl-L-cysteine + H2O + O2 = a prenal + H2O2 + L-
CC cysteine; Xref=Rhea:RHEA:53892, Rhea:RHEA-COMP:13675, Rhea:RHEA-
CC COMP:13676, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:137934, ChEBI:CHEBI:137935;
CC EC=1.8.3.5; Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53893;
CC Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + S-(2E,6E)-farnesyl-L-cysteine = (2E,6E)-farnesal +
CC H2O2 + L-cysteine; Xref=Rhea:RHEA:30231, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:15894, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:62141; EC=1.8.3.5;
CC Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30232;
CC Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(2E,6E,10E)-geranylgeranyl]-L-cysteine + H2O + O2 =
CC (2E,6E,10E)-geranylgeranial + H2O2 + L-cysteine;
CC Xref=Rhea:RHEA:70407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:35235, ChEBI:CHEBI:189549,
CC ChEBI:CHEBI:189554; EC=1.8.3.5;
CC Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70408;
CC Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:Q9UHG3}.
CC -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AB062961; BAB60740.1; -; mRNA.
DR AlphaFoldDB; Q95KC9; -.
DR STRING; 9541.XP_005575714.1; -.
DR PRIDE; Q95KC9; -.
DR eggNOG; ENOG502QSHJ; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0102149; F:farnesylcysteine lyase activity; IEA:RHEA.
DR GO; GO:0001735; F:prenylcysteine oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030328; P:prenylcysteine catabolic process; IEA:InterPro.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR010795; Prenylcys_lyase.
DR InterPro; IPR017046; Prenylcysteine_Oxase.
DR PANTHER; PTHR15944; PTHR15944; 1.
DR Pfam; PF07156; Prenylcys_lyase; 1.
DR PIRSF; PIRSF036292; Prenylcysteine_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 2: Evidence at transcript level;
KW FAD; Flavoprotein; Glycoprotein; Lysosome; Oxidoreductase;
KW Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..505
FT /note="Prenylcysteine oxidase 1"
FT /id="PRO_0000023299"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 505 AA; 56517 MW; 9CC9A113FA132897 CRC64;
MGRAVAELVS SLLGLWLLLC SCGCPEGAEL RAPPDKIAVI GAGIGGTSAA YYLRQKFGKD
VKIDLFEREE VGGRLATMMV QGQEYEAGGS VIHPLNLHMK RFVKDLGLST VQASGGLLGI
YNGEALVFEE SNWFIINVIK LVWRYGFQSL RMHMWVEDVL DKFMRIYRYQ SHDYAFSSVE
KLLHALGGDD FLGMLNRTLL ETLQKAGFSE KFLNEMIAPV MRVDYGQSTD INAFVGAVSL
SCSDSGLWAV EGGNKLVCSG LLQASKSNLI SGSVMYIEEK TKTKHTGNPT KMYEVVYQIG
TETHSDFYDI VLVATPLNRK MSNITFLNFD PPIEEFHQYY QHIVTTLVKG ELNTSIFSSR
PIDKFGLSTV LTTDNSDLFI NSIGIVSSVR EKEDPEPSTD GTYVWKIFSQ ETLTKAQILK
LFLSYDYAVK KPWLAYPHYK PPEKCPSIIL HDRLYYLNGI ECAASAMEMS AIAAHNAALL
AYHRWNGHTD MIDQDGLYEK LKTEL