PCYOX_MOUSE
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 03-AUG-2022, entry version 153.
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},
GN Pcly {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, Pancreas,
RC 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; 3.
DR STRING; 10090.ENSMUSP00000032065; -.
DR GlyConnect; 2601; 13 N-Linked glycans (3 sites).
DR GlyGen; Q9CQF9; 3 sites, 12 N-linked glycans (3 sites).
DR iPTMnet; Q9CQF9; -.
DR PhosphoSitePlus; Q9CQF9; -.
DR CPTAC; non-CPTAC-3593; -.
DR EPD; Q9CQF9; -.
DR jPOST; Q9CQF9; -.
DR MaxQB; Q9CQF9; -.
DR PaxDb; Q9CQF9; -.
DR PeptideAtlas; Q9CQF9; -.
DR PRIDE; Q9CQF9; -.
DR ProteomicsDB; 287896; -.
DR Antibodypedia; 16314; 88 antibodies from 25 providers.
DR DNASU; 66881; -.
DR Ensembl; ENSMUST00000032065; ENSMUSP00000032065; ENSMUSG00000029998.
DR GeneID; 66881; -.
DR KEGG; mmu:66881; -.
DR UCSC; uc009cro.2; mouse.
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; EYPRVTF; -.
DR OrthoDB; 1114069at2759; -.
DR PhylomeDB; Q9CQF9; -.
DR TreeFam; TF329001; -.
DR BRENDA; 1.8.3.5; 3474.
DR BioGRID-ORCS; 66881; 3 hits in 75 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 265 other tissues.
DR ExpressionAtlas; Q9CQF9; baseline and differential.
DR Genevisible; Q9CQF9; MM.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO: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; -; 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..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
