PCYOX_HUMAN
ID PCYOX_HUMAN Reviewed; 505 AA.
AC Q9UHG3; B2RB14; B7Z9P8; O94982; Q8N4N5; Q96QM8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Prenylcysteine oxidase 1 {ECO:0000305};
DE EC=1.8.3.5 {ECO:0000269|PubMed:10585463, ECO:0000269|PubMed:11078725, ECO:0000269|PubMed:12186880};
DE AltName: Full=Prenylcysteine lyase {ECO:0000303|PubMed:10585463};
DE Flags: Precursor;
GN Name=PCYOX1 {ECO:0000312|HGNC:HGNC:20588};
GN Synonyms=KIAA0908 {ECO:0000303|PubMed:10048485}, PCL1;
GN ORFNames=UNQ597/PRO1183 {ECO:0000303|PubMed:12975309};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, CATALYTIC
RP ACTIVITY, FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-149.
RC TISSUE=Brain;
RX PubMed=10048485; DOI=10.1093/dnares/5.6.355;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:355-364(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart, and Lung;
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 [8]
RP PROTEIN SEQUENCE OF 37-54; 256-266 AND 421-430, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (JUN-2005) to UniProtKB.
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND COFACTOR.
RX PubMed=11078725; DOI=10.1074/jbc.c000616200;
RA Tschantz W.R., Digits J.A., Pyun H.J., Coates R.M., Casey P.J.;
RT "Lysosomal prenylcysteine lyase is a FAD-dependent thioether oxidase.";
RL J. Biol. Chem. 276:2321-2324(2001).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=12186880; DOI=10.1074/jbc.m208069200;
RA Digits J.A., Pyun H.J., Coates R.M., Casey P.J.;
RT "Stereospecificity and kinetic mechanism of human prenylcysteine lyase, an
RT unusual thioether oxidase.";
RL J. Biol. Chem. 277:41086-41093(2002).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196; ASN-323 AND ASN-353.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196 AND ASN-353.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Prenylcysteine oxidase that cleaves the thioether bond of
CC prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine
CC (PubMed:10585463, PubMed:11078725, PubMed:12186880). Only active
CC against free prenylcysteines and not prenylcysteine residues within
CC prenylated proteins or peptides (By similarity). Involved in the final
CC step in the degradation of prenylated proteins, by degrading
CC prenylcysteines after the protein has been degraded (PubMed:10585463).
CC {ECO:0000250|UniProtKB:F1N2K1, ECO:0000269|PubMed:10585463,
CC ECO:0000269|PubMed:11078725, ECO:0000269|PubMed:12186880}.
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:10585463,
CC ECO:0000269|PubMed:11078725, ECO:0000269|PubMed:12186880};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53893;
CC Evidence={ECO:0000269|PubMed:10585463, ECO:0000269|PubMed:11078725,
CC ECO:0000269|PubMed:12186880};
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:10585463, ECO:0000269|PubMed:11078725,
CC ECO:0000269|PubMed:12186880};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30232;
CC Evidence={ECO:0000269|PubMed:10585463, ECO:0000269|PubMed:11078725,
CC ECO:0000269|PubMed:12186880};
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:10585463};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70408;
CC Evidence={ECO:0000269|PubMed:10585463};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:11078725};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.0 uM for free farnesylcysteine {ECO:0000269|PubMed:12186880};
CC Note=kcat is 8000 sec(-1) for free farnesylcysteine.
CC {ECO:0000269|PubMed:12186880};
CC -!- INTERACTION:
CC Q9UHG3; P49639: HOXA1; NbExp=3; IntAct=EBI-2908417, EBI-740785;
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:10585463}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UHG3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHG3-2; Sequence=VSP_056701;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10585463}.
CC -!- SIMILARITY: Belongs to the prenylcysteine oxidase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a lyase and was therefore termed
CC prenylcysteine lyase. {ECO:0000305|PubMed:10585463}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA74931.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF181490; AAF16937.1; -; mRNA.
DR EMBL; AB020715; BAA74931.1; ALT_INIT; mRNA.
DR EMBL; AY359063; AAQ89422.1; -; mRNA.
DR EMBL; AK314453; BAG37061.1; -; mRNA.
DR EMBL; AK316013; BAH14384.1; -; mRNA.
DR EMBL; AC016700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99819.1; -; Genomic_DNA.
DR EMBL; BC007029; AAH07029.1; -; mRNA.
DR EMBL; BC033815; AAH33815.1; -; mRNA.
DR EMBL; BC051891; AAH51891.1; -; mRNA.
DR CCDS; CCDS1902.1; -. [Q9UHG3-1]
DR RefSeq; NP_057381.3; NM_016297.3. [Q9UHG3-1]
DR AlphaFoldDB; Q9UHG3; -.
DR BioGRID; 119547; 114.
DR IntAct; Q9UHG3; 22.
DR MINT; Q9UHG3; -.
DR STRING; 9606.ENSP00000387654; -.
DR GlyConnect; 1624; 21 N-Linked glycans (4 sites).
DR GlyGen; Q9UHG3; 5 sites, 27 N-linked glycans (4 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHG3; -.
DR PhosphoSitePlus; Q9UHG3; -.
DR SwissPalm; Q9UHG3; -.
DR BioMuta; PCYOX1; -.
DR DMDM; 115311617; -.
DR EPD; Q9UHG3; -.
DR jPOST; Q9UHG3; -.
DR MassIVE; Q9UHG3; -.
DR MaxQB; Q9UHG3; -.
DR PaxDb; Q9UHG3; -.
DR PeptideAtlas; Q9UHG3; -.
DR PRIDE; Q9UHG3; -.
DR ProteomicsDB; 7041; -.
DR ProteomicsDB; 84350; -. [Q9UHG3-1]
DR TopDownProteomics; Q9UHG3-1; -. [Q9UHG3-1]
DR Antibodypedia; 16314; 88 antibodies from 25 providers.
DR DNASU; 51449; -.
DR Ensembl; ENST00000433351.7; ENSP00000387654.2; ENSG00000116005.12. [Q9UHG3-1]
DR GeneID; 51449; -.
DR KEGG; hsa:51449; -.
DR MANE-Select; ENST00000433351.7; ENSP00000387654.2; NM_016297.4; NP_057381.3.
DR UCSC; uc002sgn.5; human. [Q9UHG3-1]
DR CTD; 51449; -.
DR DisGeNET; 51449; -.
DR GeneCards; PCYOX1; -.
DR HGNC; HGNC:20588; PCYOX1.
DR HPA; ENSG00000116005; Low tissue specificity.
DR MIM; 610995; gene.
DR neXtProt; NX_Q9UHG3; -.
DR OpenTargets; ENSG00000116005; -.
DR PharmGKB; PA134959852; -.
DR VEuPathDB; HostDB:ENSG00000116005; -.
DR eggNOG; ENOG502QSHJ; Eukaryota.
DR GeneTree; ENSGT00390000011206; -.
DR HOGENOM; CLU_021176_1_0_1; -.
DR InParanoid; Q9UHG3; -.
DR OMA; EYPRVTF; -.
DR OrthoDB; 1114069at2759; -.
DR PhylomeDB; Q9UHG3; -.
DR TreeFam; TF329001; -.
DR BRENDA; 1.8.3.5; 2681.
DR PathwayCommons; Q9UHG3; -.
DR SignaLink; Q9UHG3; -.
DR BioGRID-ORCS; 51449; 11 hits in 1078 CRISPR screens.
DR ChiTaRS; PCYOX1; human.
DR GeneWiki; PCYOX1; -.
DR GenomeRNAi; 51449; -.
DR Pharos; Q9UHG3; Tbio.
DR PRO; PR:Q9UHG3; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UHG3; protein.
DR Bgee; ENSG00000116005; Expressed in parotid gland and 200 other tissues.
DR ExpressionAtlas; Q9UHG3; baseline and differential.
DR Genevisible; Q9UHG3; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:BHF-UCL.
DR GO; GO:0071949; F:FAD binding; IDA:UniProtKB.
DR GO; GO:0102149; F:farnesylcysteine lyase activity; IEA:RHEA.
DR GO; GO:0001735; F:prenylcysteine oxidase activity; IDA:UniProtKB.
DR GO; GO:1902476; P:chloride transmembrane transport; IEA:Ensembl.
DR GO; GO:0030327; P:prenylated protein catabolic process; IDA:BHF-UCL.
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 Alternative splicing; Direct protein sequencing; FAD; Flavoprotein;
KW Glycoprotein; Lysosome; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..505
FT /note="Prenylcysteine oxidase 1"
FT /id="PRO_0000023298"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT VAR_SEQ 1..77
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056701"
FT VARIANT 149
FT /note="S -> F (in dbSNP:rs2706762)"
FT /evidence="ECO:0000269|PubMed:10048485"
FT /id="VAR_050469"
FT VARIANT 414
FT /note="T -> S (in dbSNP:rs17005441)"
FT /id="VAR_050470"
FT VARIANT 465
FT /note="S -> G (in dbSNP:rs34041544)"
FT /id="VAR_050471"
FT CONFLICT 341
FT /note="Q -> H (in Ref. 1; AAF16937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 505 AA; 56640 MW; FB388AF70AF229F5 CRC64;
MGRVVAELVS SLLGLWLLLC SCGCPEGAEL RAPPDKIAII GAGIGGTSAA YYLRQKFGKD
VKIDLFEREE VGGRLATMMV QGQEYEAGGS VIHPLNLHMK RFVKDLGLSA VQASGGLLGI
YNGETLVFEE SNWFIINVIK LVWRYGFQSL RMHMWVEDVL DKFMRIYRYQ SHDYAFSSVE
KLLHALGGDD FLGMLNRTLL ETLQKAGFSE KFLNEMIAPV MRVNYGQSTD INAFVGAVSL
SCSDSGLWAV EGGNKLVCSG LLQASKSNLI SGSVMYIEEK TKTKYTGNPT KMYEVVYQIG
TETRSDFYDI VLVATPLNRK MSNITFLNFD PPIEEFHQYY QHIVTTLVKG ELNTSIFSSR
PIDKFGLNTV LTTDNSDLFI NSIGIVPSVR EKEDPEPSTD GTYVWKIFSQ ETLTKAQILK
LFLSYDYAVK KPWLAYPHYK PPEKCPSIIL HDRLYYLNGI ECAASAMEMS AIAAHNAALL
AYHRWNGHTD MIDQDGLYEK LKTEL
