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 27-MAR-2024, entry version 197. 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 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 122. DR IntAct; Q9UHG3; 24. DR MINT; Q9UHG3; -. DR STRING; 9606.ENSP00000387654; -. DR GlyConnect; 1624; 21 N-Linked glycans (4 sites). DR GlyCosmos; Q9UHG3; 4 sites, 23 glycans. 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; 9606-ENSP00000387654; -. DR PeptideAtlas; Q9UHG3; -. DR ProteomicsDB; 7041; -. DR ProteomicsDB; 84350; -. [Q9UHG3-1] DR Pumba; Q9UHG3; -. DR TopDownProteomics; Q9UHG3-1; -. [Q9UHG3-1] DR Antibodypedia; 16314; 98 antibodies from 26 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 AGR; HGNC:20588; -. 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; QMWVESI; -. DR OrthoDB; 551774at2759; -. DR PhylomeDB; Q9UHG3; -. DR TreeFam; TF329001; -. DR BRENDA; 1.8.3.5; 2681. DR PathwayCommons; Q9UHG3; -. DR SignaLink; Q9UHG3; -. DR BioGRID-ORCS; 51449; 13 hits in 1158 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 202 other cell types or tissues. DR ExpressionAtlas; Q9UHG3; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005764; C:lysosome; IDA:BHF-UCL. 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: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; 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; Q9UHG3; HS. 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 //