ID   PCYOX_MOUSE             Reviewed;         505 AA.
AC   Q9CQF9; Q3UHV6; Q69ZW0; Q8BZX1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=Prenylcysteine oxidase 1 {ECO:0000305};
DE            EC=1.8.3.5 {ECO:0000250|UniProtKB:Q9UHG3};
DE   AltName: Full=Prenylcysteine lyase {ECO:0000303|PubMed:12151402};
DE   Flags: Precursor;
GN   Name=Pcyox1 {ECO:0000312|MGI:MGI:1914131};
GN   Synonyms=Kiaa0908 {ECO:0000303|PubMed:15368895}, Pcly
GN   {ECO:0000303|PubMed:12151402};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Amnion, Liver, Lung, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-505.
RC   TISSUE=Fetal brain;
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 145-151; 169-193; 292-298; 328-349 AND 421-430, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=12151402; DOI=10.1074/jbc.m205183200;
RA   Beigneux A., Withycombe S.K., Digits J.A., Tschantz W.R., Weinbaum C.A.,
RA   Griffey S.M., Bergo M., Casey P.J., Young S.G.;
RT   "Prenylcysteine lyase deficiency in mice results in the accumulation of
RT   farnesylcysteine and geranylgeranylcysteine in brain and liver.";
RL   J. Biol. Chem. 277:38358-38363(2002).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196.
RC   STRAIN=C57BL/6J; TISSUE=Plasma;
RX   PubMed=16944957; DOI=10.1021/pr060186m;
RA   Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT   "Proteome-wide characterization of N-glycosylation events by diagonal
RT   chromatography.";
RL   J. Proteome Res. 5:2438-2447(2006).
RN   [7]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-353.
RX   PubMed=19349973; DOI=10.1038/nbt.1532;
RA   Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA   Schiess R., Aebersold R., Watts J.D.;
RT   "Mass-spectrometric identification and relative quantification of N-linked
RT   cell surface glycoproteins.";
RL   Nat. Biotechnol. 27:378-386(2009).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Prenylcysteine oxidase that cleaves the thioether bond of
CC       prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine
CC       (PubMed:12151402). 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 (PubMed:12151402). {ECO:0000250|UniProtKB:F1N2K1,
CC       ECO:0000269|PubMed:12151402}.
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: Highly expressed in the liver, kidney, heart and
CC       brain. {ECO:0000269|PubMed:12151402}.
CC   -!- DISRUPTION PHENOTYPE: Mice are healthy and fertile, but show an
CC       accumulation of prenylcysteines within cells (PubMed:12151402).
CC       Significant accumulation of both farnesylcysteine and
CC       geranylgeranylcysteine in the brain and liver (PubMed:12151402).
CC       {ECO:0000269|PubMed:12151402}.
CC   -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
CC       {ECO:0000305}.
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DR   EMBL; AK004799; BAB23572.1; -; mRNA.
DR   EMBL; AK004840; BAB23607.1; -; mRNA.
DR   EMBL; AK031585; BAC27462.1; -; mRNA.
DR   EMBL; AK033373; BAC28252.1; -; mRNA.
DR   EMBL; AK049412; BAC33741.1; -; mRNA.
DR   EMBL; AK145366; BAE26391.1; -; mRNA.
DR   EMBL; AK147190; BAE27750.1; -; mRNA.
DR   EMBL; AK161616; BAE36494.1; -; mRNA.
DR   EMBL; AK169209; BAE40981.1; -; mRNA.
DR   EMBL; BC028308; AAH28308.1; -; mRNA.
DR   EMBL; AK173058; BAD32336.1; -; mRNA.
DR   CCDS; CCDS20311.1; -.
DR   RefSeq; NP_080099.1; NM_025823.4.
DR   AlphaFoldDB; Q9CQF9; -.
DR   BioGRID; 211785; 5.
DR   STRING; 10090.ENSMUSP00000032065; -.
DR   GlyConnect; 2601; 13 N-Linked glycans (3 sites).
DR   GlyCosmos; Q9CQF9; 3 sites, 12 glycans.
DR   GlyGen; Q9CQF9; 3 sites, 12 N-linked glycans (3 sites).
DR   iPTMnet; Q9CQF9; -.
DR   PhosphoSitePlus; Q9CQF9; -.
DR   SwissPalm; Q9CQF9; -.
DR   CPTAC; non-CPTAC-3593; -.
DR   EPD; Q9CQF9; -.
DR   jPOST; Q9CQF9; -.
DR   MaxQB; Q9CQF9; -.
DR   PaxDb; 10090-ENSMUSP00000032065; -.
DR   PeptideAtlas; Q9CQF9; -.
DR   ProteomicsDB; 287896; -.
DR   Pumba; Q9CQF9; -.
DR   Antibodypedia; 16314; 98 antibodies from 26 providers.
DR   DNASU; 66881; -.
DR   Ensembl; ENSMUST00000032065.15; ENSMUSP00000032065.9; ENSMUSG00000029998.15.
DR   GeneID; 66881; -.
DR   KEGG; mmu:66881; -.
DR   UCSC; uc009cro.2; mouse.
DR   AGR; MGI:1914131; -.
DR   CTD; 51449; -.
DR   MGI; MGI:1914131; Pcyox1.
DR   VEuPathDB; HostDB:ENSMUSG00000029998; -.
DR   eggNOG; ENOG502QSHJ; Eukaryota.
DR   GeneTree; ENSGT00390000011206; -.
DR   HOGENOM; CLU_021176_1_0_1; -.
DR   InParanoid; Q9CQF9; -.
DR   OMA; QMWVESI; -.
DR   OrthoDB; 551774at2759; -.
DR   PhylomeDB; Q9CQF9; -.
DR   TreeFam; TF329001; -.
DR   BRENDA; 1.8.3.5; 3474.
DR   BioGRID-ORCS; 66881; 3 hits in 80 CRISPR screens.
DR   ChiTaRS; Pcyox1; mouse.
DR   PRO; PR:Q9CQF9; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9CQF9; Protein.
DR   Bgee; ENSMUSG00000029998; Expressed in metanephric cortical collecting duct and 269 other cell types or tissues.
DR   ExpressionAtlas; Q9CQF9; baseline and differential.
DR   GO; GO:0005764; C:lysosome; IDA:MGI.
DR   GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:MGI.
DR   GO; GO:0071949; F:FAD binding; ISO:MGI.
DR   GO; GO:0102149; F:farnesylcysteine lyase activity; IEA:RHEA.
DR   GO; GO:0001735; F:prenylcysteine oxidase activity; IMP:MGI.
DR   GO; GO:1902476; P:chloride transmembrane transport; ISO:MGI.
DR   GO; GO:0030327; P:prenylated protein catabolic process; ISO:MGI.
DR   GO; GO:0030328; P:prenylcysteine catabolic process; IMP:MGI.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR010795; Prenylcys_lyase.
DR   InterPro; IPR017046; Prenylcysteine_Oxase.
DR   PANTHER; PTHR15944; FARNESYLCYSTEINE LYASE; 1.
DR   PANTHER; PTHR15944:SF3; PRENYLCYSTEINE OXIDASE 1; 1.
DR   Pfam; PF13450; NAD_binding_8; 1.
DR   Pfam; PF07156; Prenylcys_lyase; 1.
DR   PIRSF; PIRSF036292; Prenylcysteine_oxidase; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   Genevisible; Q9CQF9; MM.
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..505
FT                   /note="Prenylcysteine oxidase 1"
FT                   /id="PRO_0000023300"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16944957"
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:0000269|PubMed:19349973"
FT   CONFLICT        114
FT                   /note="S -> T (in Ref. 1; BAC28252)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   505 AA;  56495 MW;  9169BC4CC7D97561 CRC64;
     MGRFAAALVG SLFWLGLLLC GLGSLASAEP RAPPNRIAIV GAGIGGTSSA YYLRKKFGKD
     VKIDVFEREE VGGRLATLKV QGHDYEAGGS VIHPLNLHMK RFVKELGLSS VPASGGLVGV
     YNGKSLVFEE SSWFVINVIK LVWRYGFQSL RMHMWVEDLL DKFMRIYRYQ SHDYAFSSVE
     KLMHAIGGDD YVRLLNQTLR ENLKKAGFSE TFLNEMIAPV MKVNYGQSTD INAFVGAVSL
     TAADSNLWAV EGGNKIVCSG LLQASSSNLI SGSVMSIEEK TRTKQTGNPT KMYEVVYKTG
     SETHSDFYDI VLVAAPLNRK MSNITFRNFD PPIEEFNDPY QQLVTTFIKG ELNSTLFSSR
     PKDQFGLSAI LVTDDSDMFI NSLSIVASVR QKEGPPPAVD GMHVWKTFSR DILTKEQISK
     LFLSYDYAVR KPWLSYPHYE PPQKCPSIIL HDRLYYLNGI EFAASCMEMS AIAGYNAALL
     AYHRWNGNED MIDQDDLYER LKTEL
//