Reviewed, UniProtKB/Swiss-Prot Q9UHG3 (PCYOX_HUMAN)

Names and origin

Protein names

Recommended name:
    Prenylcysteine oxidase 1
    EC=1.8.3.5
Alternative name(s):
    Prenylcysteine lyase

Gene names

Name:	PCYOX1
Synonyms:	KIAA0908, PCL1
ORF Names:	UNQ597/PRO1183

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	505 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the degradation of prenylated proteins. Cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine.
Catalytic activity	An S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2.
Cofactor	FAD.
Subcellular location	Lysosome.
Tissue specificity	Ubiquitous.
Post-translational modification	The protein is glycosylated at one or more potential N-glycosylation sites. Ref.8 Ref.11
Sequence similarities	Belongs to the prenylcysteine oxidase family.
Caution	Was originally (Ref.1) thought to be a lyase and was therefore termed prenylcysteine lyase.

Ontologies

Keywords
Cellular component	Lysosome
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	FAD
Molecular function	Oxidoreductase
PTM	Glycoprotein Isopeptide bond Ubl conjugation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW prenylated protein catabolic process Ref.1 Non-traceable author statement. Source: UniProtKB
Cellular component	lysosome Ref.1 Inferred from direct assay. Source: UniProtKB very-low-density lipoprotein particle Inferred from direct assay. Source: UniProtKB
Molecular function	binding Inferred from electronic annotation. Source: InterPro prenylcysteine oxidase activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 27	27	Potential
	Chain	28 – 505	478	Prenylcysteine oxidase 1		PRO_0000023298
Amino acid modifications
	Glycosylation	196	1	N-linked (GlcNAc...) Ref.8 Ref.11
	Glycosylation	323	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	353	1	N-linked (GlcNAc...) Ref.8 Ref.11
	Cross-link	162		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.9
Natural variations
	Natural variant	149	1	S → F: dbSNP rs2706762. Ref.2		VAR_050469
	Natural variant	414	1	T → S: dbSNP rs17005441.		VAR_050470
	Natural variant	465	1	S → G: dbSNP rs34041544.		VAR_050471
Experimental info
	Sequence conflict	341	1	Q → H in AAF16937. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9UHG3-1 [UniParc]. Last modified September 19, 2006. Version 3. Checksum: FB388AF70AF229F5	FASTA	505	56,640
	10 20 30 40 50 60 MGRVVAELVS SLLGLWLLLC SCGCPEGAEL RAPPDKIAII GAGIGGTSAA YYLRQKFGKD 70 80 90 100 110 120 VKIDLFEREE VGGRLATMMV QGQEYEAGGS VIHPLNLHMK RFVKDLGLSA VQASGGLLGI 130 140 150 160 170 180 YNGETLVFEE SNWFIINVIK LVWRYGFQSL RMHMWVEDVL DKFMRIYRYQ SHDYAFSSVE 190 200 210 220 230 240 KLLHALGGDD FLGMLNRTLL ETLQKAGFSE KFLNEMIAPV MRVNYGQSTD INAFVGAVSL 250 260 270 280 290 300 SCSDSGLWAV EGGNKLVCSG LLQASKSNLI SGSVMYIEEK TKTKYTGNPT KMYEVVYQIG 310 320 330 340 350 360 TETRSDFYDI VLVATPLNRK MSNITFLNFD PPIEEFHQYY QHIVTTLVKG ELNTSIFSSR 370 380 390 400 410 420 PIDKFGLNTV LTTDNSDLFI NSIGIVPSVR EKEDPEPSTD GTYVWKIFSQ ETLTKAQILK 430 440 450 460 470 480 LFLSYDYAVK KPWLAYPHYK PPEKCPSIIL HDRLYYLNGI ECAASAMEMS AIAAHNAALL 490 500 AYHRWNGHTD MIDQDGLYEK LKTEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, expression, and cellular localization of a human prenylcysteine lyase." Tschantz W.R., Zhang L., Casey P.J. J. Biol. Chem. 274:35802-35808(1999) [PubMed: 10585463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:355-364(1998) [PubMed: 10048485] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-149. Tissue: Brain.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart and Lung.
[7]	Bienvenut W.V. Submitted (JUN-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 37-54; 256-266 AND 421-430, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[8]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196; ASN-323 AND ASN-353, MASS SPECTROMETRY. Tissue: Plasma.
[9]	"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry." Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D. Proteomics 7:868-874(2007) [PubMed: 17370265] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-162, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196 AND ASN-353, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF181490 mRNA. Translation: AAF16937.1. AB020715 mRNA. Translation: BAA74931.1. Different initiation. AY359063 mRNA. Translation: AAQ89422.1. AK314453 mRNA. Translation: BAG37061.1. CH471053 Genomic DNA. Translation: EAW99819.1. BC007029 mRNA. Translation: AAH07029.1. BC033815 mRNA. Translation: AAH33815.1. BC051891 mRNA. Translation: AAH51891.1.
IPI	IPI00384280.
RefSeq	NP_057381.3.
UniGene	Hs.567502
3D structure databases
SMR	Q9UHG3. Positions 33-338.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9UHG3.
PTM databases
PhosphoSite	Q9UHG3.
Proteomic databases
PeptideAtlas	Q9UHG3.
PRIDE	Q9UHG3.
Genome annotation databases
Ensembl	ENST00000433351; ENSP00000387654; ENSG00000116005; Homo sapiens. [Genome view]
GeneID	51449.
KEGG	hsa:51449.
UCSC	uc002sgn.2. human.
Organism-specific databases
CTD	51449.
GeneCards	GC02P070396.
HGNC	HGNC:20588. PCYOX1.
MIM	610995. gene.
PharmGKB	PA134959852.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG06746.
HOGENOM	HBG447064.
HOVERGEN	Q9UHG3.
InParanoid	Q9UHG3.
OMA	SLRMHMW.
PhylomeDB	Q9UHG3.
Enzyme and pathway databases
BRENDA	1.8.3.5. 247.
Gene expression databases
ArrayExpress	Q9UHG3.
Bgee	Q9UHG3.
CleanEx	HS_PCYOX1.
Genevestigator	Q9UHG3.
GermOnline	ENSG00000116005. Homo sapiens.
Family and domain databases
InterPro	IPR006076. FAD-dep_OxRdtase. IPR016040. NAD(P)-bd_dom. IPR010795. Prenylcys_lyase. IPR017046. Prenylcysteine_Oxase. [Graphical view]
Pfam	PF01266. DAO. 1 hit. PF07156. Prenylcys_lyase. 1 hit. [Graphical view]
PIRSF	PIRSF036292. Prenylcysteine_oxidase. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	55051.
SOURCE	Search...

Entry information

Entry name

PCYOX_HUMAN

Accession

Primary (citable) accession number: Q9UHG3
Secondary accession number(s): B2RB14 , O94982, Q8N4N5, Q96QM8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	September 19, 2006
Last modified:	January 19, 2010
This is version 92 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.