PCYOX_BOVIN
ID PCYOX_BOVIN Reviewed; 508 AA.
AC F1N2K1; A6QPR1;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Prenylcysteine oxidase 1 {ECO:0000305};
DE EC=1.8.3.5 {ECO:0000269|PubMed:9287348};
DE AltName: Full=Prenylcysteine lyase {ECO:0000303|PubMed:9287348};
DE Flags: Precursor;
GN Name=PCYOX1 {ECO:0000250|UniProtKB:Q9UHG3};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 32-57; 172-184; 215-225; 383-390 AND 402-409.
RX PubMed=10585463; DOI=10.1074/jbc.274.50.35802;
RA Tschantz W.R., Zhang L., Casey P.J.;
RT "Cloning, expression, and cellular localization of a human prenylcysteine
RT lyase.";
RL J. Biol. Chem. 274:35802-35808(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9287348; DOI=10.1074/jbc.272.37.23354;
RA Zhang L., Tschantz W.R., Casey P.J.;
RT "Isolation and characterization of a prenylcysteine lyase from bovine
RT brain.";
RL J. Biol. Chem. 272:23354-23359(1997).
CC -!- FUNCTION: Prenylcysteine oxidase that cleaves the thioether bond of
CC prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine
CC (PubMed:9287348). Only active against free prenylcysteines and not
CC prenylcysteine residues within prenylated proteins or peptides
CC (PubMed:9287348). Involved in the final step in the degradation of
CC prenylated proteins, by degrading prenylcysteines after the protein has
CC been degraded (PubMed:9287348). {ECO:0000269|PubMed:9287348}.
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:0000269|PubMed:9287348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53893;
CC Evidence={ECO:0000269|PubMed:9287348};
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:0000269|PubMed:9287348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30232;
CC Evidence={ECO:0000269|PubMed:9287348};
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:0000269|PubMed:9287348};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70408;
CC Evidence={ECO:0000269|PubMed:9287348};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:Q9UHG3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.69 uM for free farnesylcysteine {ECO:0000269|PubMed:9287348};
CC KM=0.84 uM for free geranylgeranylcysteine
CC {ECO:0000269|PubMed:9287348};
CC Vmax=3910 nmol/h/mg enzyme with free farnesylcysteine as substrate
CC {ECO:0000269|PubMed:9287348};
CC Vmax=1790 nmol/h/mg enzyme with free geranylgeranylcysteine as
CC substrate {ECO:0000269|PubMed:9287348};
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; BC149440; AAI49441.1; -; mRNA.
DR RefSeq; NP_001098944.1; NM_001105474.2.
DR STRING; 9913.ENSBTAP00000042008; -.
DR PaxDb; F1N2K1; -.
DR PRIDE; F1N2K1; -.
DR Ensembl; ENSBTAT00000044517; ENSBTAP00000042008; ENSBTAG00000002783.
DR GeneID; 100125835; -.
DR KEGG; bta:100125835; -.
DR CTD; 51449; -.
DR VEuPathDB; HostDB:ENSBTAG00000002783; -.
DR VGNC; VGNC:32650; PCYOX1.
DR eggNOG; ENOG502QSHJ; Eukaryota.
DR GeneTree; ENSGT00390000011206; -.
DR HOGENOM; CLU_021176_1_0_1; -.
DR InParanoid; F1N2K1; -.
DR OMA; EYPRVTF; -.
DR OrthoDB; 1114069at2759; -.
DR TreeFam; TF329001; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000002783; Expressed in oviduct epithelium and 107 other tissues.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0071949; F:FAD binding; IEA:Ensembl.
DR GO; GO:0001735; F:prenylcysteine oxidase activity; IDA:UniProtKB.
DR GO; GO:0030327; P:prenylated protein catabolic process; IBA:GO_Central.
DR GO; GO:0030328; P:prenylcysteine catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Direct protein sequencing; FAD; Flavoprotein; Glycoprotein; Lysosome;
KW Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:10585463"
FT CHAIN 32..508
FT /note="Prenylcysteine oxidase 1"
FT /id="PRO_5003269986"
FT CARBOHYD 199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 34
FT /note="R -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="F -> Y (in Ref. 2; AAI49441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 56776 MW; 02C334BAE7750CA1 CRC64;
MDPAAPGLAC SILRLGLGLL LLCSWWYPGS AEPRAPPEKI AVIGAGIGGT SAAYYLRQKF
GKDVKIDVFE KGKVGGRLAT LNVQGQEFES GGSVIHPLNL HMKRFVKDLG LSAVQSPSGL
VGVYNGETLV YEESSWFIIN MIKLIWHYGF QSLRMHMWVE DILDKFMRIY RYQSHDYAFS
SVEKLLHSLG GDDYLGLFNR SLLETLQKAG FSEKFLDEII TPVMRVNYGQ TTNINGFVGA
VSMAGTDPGL WAVKGGNKLV CSRLLQASRS NLVSGLVMSI EEKTRTKQTG NPSKVYEVVY
QTGSETHSDF YDIVLVATPL NRKMSNINFL NFDPPIEEFH QHYEPLVTTL IKGELNSTVF
SSRALNEFHL GTVLTTDNPD LFINSIGLVS PVEEDNNPQP KADTAHVWKI FSAAALTKEQ
ILKLFVSYDY AVKQSWLAYP HYTPPEKCPS IILHDQLYYL NGIEFAASAM EMSAIAGYNA
ALLAYHRWNG NTHMIDQEDL YERLKTEL
