PCYOX_RAT
ID PCYOX_RAT Reviewed; 504 AA.
AC Q99ML5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Prenylcysteine oxidase 1 {ECO:0000305};
DE EC=1.8.3.5 {ECO:0000250|UniProtKB:Q9UHG3};
DE AltName: Full=Chloride ion pump-associated 55 kDa protein {ECO:0000303|PubMed:11716481};
DE Flags: Precursor;
GN Name=Pcyox1 {ECO:0000312|RGD:628652};
GN Synonyms=Clp55 {ECO:0000303|PubMed:11716481};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=11716481; DOI=10.1006/bbrc.2001.5997;
RA Kitagawa K., Yagyu K., Yamamoto A., Hattori N., Omori K., Zeng X.-T.,
RA Inagaki C.;
RT "Molecular cloning and characterization of the Cl(-) pump-associated 55-kDa
RT protein in rat brain.";
RL Biochem. Biophys. Res. Commun. 289:363-371(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 291-318 AND 420-429, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196 AND ASN-352, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
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 -!- TISSUE SPECIFICITY: Expressed mainly in cerebrum.
CC {ECO:0000269|PubMed:11716481}.
CC -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
CC {ECO:0000305}.
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DR EMBL; AF332142; AAK16548.1; -; mRNA.
DR EMBL; BC078719; AAH78719.1; -; mRNA.
DR PIR; JC7782; JC7782.
DR RefSeq; NP_659553.1; NM_145085.2.
DR AlphaFoldDB; Q99ML5; -.
DR STRING; 10116.ENSRNOP00000022532; -.
DR GlyGen; Q99ML5; 3 sites, 9 N-linked glycans (2 sites).
DR iPTMnet; Q99ML5; -.
DR SwissPalm; Q99ML5; -.
DR jPOST; Q99ML5; -.
DR PaxDb; Q99ML5; -.
DR PRIDE; Q99ML5; -.
DR GeneID; 246302; -.
DR KEGG; rno:246302; -.
DR UCSC; RGD:628652; rat.
DR CTD; 51449; -.
DR RGD; 628652; Pcyox1.
DR VEuPathDB; HostDB:ENSRNOG00000016704; -.
DR eggNOG; ENOG502QSHJ; Eukaryota.
DR HOGENOM; CLU_021176_1_0_1; -.
DR InParanoid; Q99ML5; -.
DR OMA; EYPRVTF; -.
DR OrthoDB; 1114069at2759; -.
DR PhylomeDB; Q99ML5; -.
DR TreeFam; TF329001; -.
DR PRO; PR:Q99ML5; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000016704; Expressed in skeletal muscle tissue and 18 other tissues.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:RGD.
DR GO; GO:0071949; F:FAD binding; ISO:RGD.
DR GO; GO:0102149; F:farnesylcysteine lyase activity; IEA:RHEA.
DR GO; GO:0001735; F:prenylcysteine oxidase activity; ISO:RGD.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:RGD.
DR GO; GO:0030327; P:prenylated protein catabolic process; ISO:RGD.
DR GO; GO:0030328; P:prenylcysteine catabolic process; ISO:RGD.
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..28
FT /evidence="ECO:0000255"
FT CHAIN 29..504
FT /note="Prenylcysteine oxidase 1"
FT /id="PRO_0000023302"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
SQ SEQUENCE 504 AA; 56288 MW; D2778026128FE9D4 CRC64;
MGRFAATLVG SLFGLGLLLC GLGRLASAEP RAPPEKIAIV GAGIGGTSSA YYLRKKFGKD
VKIDVFEREE IGGRLATLKV QGHDYEAGGS VIHPLNLHMK RFVKELGLSS VPASGGLVGV
YNGKSLVFEE SSWFIINVIK LVWRYGFQSL RMHMWVEDLL DKFMRIYRYQ SHDYAFSSVE
KLMYAIGGDD YVRLLNQTLR ENLKKAGFSE TFLNEMIAPV MKVNFGQSTD LNAFVGAVSM
TAADSNLWAV EGGNKVVCSG LLQASNSNLI SGSVMSIEKT RTKQTGTPPK MYEVVYKTGS
EIHSDFYDIV LVAAPLNRKM SNITFRNFDP PIEEFNDPYQ QLVTTLIKGE LNSTLFSSRH
KDQFGLSAIL VTDDSDMFIN SLSIVASVSH KEGPPPAVDG MHVWKTFSKD ILTKEQISKL
FLSYDYAVRK PWLSYPYYNP PQKCPSIILH DRLYYLNGIE FAASCMEMSA IAGYNAALLA
YHRWNGNEDM IDQDDLYEKL KTEL
