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Reviewed, UniProtKB/Swiss-Prot Q9CQF9 (PCYOX_MOUSE)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Prenylcysteine oxidase
    EC=1.8.3.5
Gene names
Name: Pcyox1
Synonyms: Kiaa0908
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Involved in the degradation of prenylated proteins. Cleaves the thioether bond of prenyl-L-cysteines, such as farnesylcysteine and geranylgeranylcysteine By similarity.

Catalytic activity

An S-prenyl-L-cysteine + O2 + H2O = a prenal + L-cysteine + H2O2.

Cofactor

FAD By similarity.

Subcellular location

Lysosome By similarity.

Sequence similarities

Belongs to the prenylcysteine oxidase family.

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Ontologies

Keywords
   Cellular componentLysosome
   DomainSignal
   LigandFAD
   Molecular functionOxidoreductase
   PTMGlycoprotein
Isopeptide bond
Ubl conjugation
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

prenylcysteine catabolic process

Inferred from mutant phenotype. Source: MGI

   Cellular componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprenylcysteine oxidase activity

Inferred from mutant phenotype. Source: MGI

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2828 Potential
Chain29 – 505477Prenylcysteine oxidase
PRO_0000023300

Amino acid modifications

Glycosylation1961N-linked (GlcNAc...) Ref.5
Glycosylation3231N-linked (GlcNAc...) Potential
Glycosylation3531N-linked (GlcNAc...) Potential
Cross-link162Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict1141S → T in BAC28252. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
Q9CQF9-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 9169BC4CC7D97561

FASTA50556,495
        10         20         30         40         50         60 
MGRFAAALVG SLFWLGLLLC GLGSLASAEP RAPPNRIAIV GAGIGGTSSA YYLRKKFGKD 

        70         80         90        100        110        120 
VKIDVFEREE VGGRLATLKV QGHDYEAGGS VIHPLNLHMK RFVKELGLSS VPASGGLVGV 

       130        140        150        160        170        180 
YNGKSLVFEE SSWFVINVIK LVWRYGFQSL RMHMWVEDLL DKFMRIYRYQ SHDYAFSSVE 

       190        200        210        220        230        240 
KLMHAIGGDD YVRLLNQTLR ENLKKAGFSE TFLNEMIAPV MKVNYGQSTD INAFVGAVSL 

       250        260        270        280        290        300 
TAADSNLWAV EGGNKIVCSG LLQASSSNLI SGSVMSIEEK TRTKQTGNPT KMYEVVYKTG 

       310        320        330        340        350        360 
SETHSDFYDI VLVAAPLNRK MSNITFRNFD PPIEEFNDPY QQLVTTFIKG ELNSTLFSSR 

       370        380        390        400        410        420 
PKDQFGLSAI LVTDDSDMFI NSLSIVASVR QKEGPPPAVD GMHVWKTFSR DILTKEQISK 

       430        440        450        460        470        480 
LFLSYDYAVR KPWLSYPHYE PPQKCPSIIL HDRLYYLNGI EFAASCMEMS AIAGYNAALL 

       490        500 
AYHRWNGNED MIDQDDLYER LKTEL

« Hide

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References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Amnion, Liver, Lung and Testis.
[2]"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].
Strain: FVB/N.
Tissue: Mammary tumor.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H.
DNA Res. 11:205-218(2004) [PubMed: 15368895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-505.
Tissue: Fetal brain.
[4]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 145-151; 169-193; 292-298; 328-349 AND 421-430, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[5]"Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
J. Proteome Res. 5:2438-2447(2006) [PubMed: 16944957] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196, MASS SPECTROMETRY.
Tissue: Plasma.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AK004799 mRNA. Translation: BAB23572.1.
AK004840 mRNA. Translation: BAB23607.1.
AK031585 mRNA. Translation: BAC27462.1.
AK033373 mRNA. Translation: BAC28252.1.
AK049412 mRNA. Translation: BAC33741.1.
AK145366 mRNA. Translation: BAE26391.1.
AK147190 mRNA. Translation: BAE27750.1.
AK161616 mRNA. Translation: BAE36494.1.
AK169209 mRNA. Translation: BAE40981.1.
BC028308 mRNA. Translation: AAH28308.1.
AK173058 mRNA. Translation: BAD32336.1.
IPIIPI00460063.
RefSeqNP_080099.1.
UniGeneMm.30849

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ9CQF9.

Proteomic databases

PRIDEQ9CQF9.

Genome annotation databases

EnsemblENSMUSG00000029998. Mus musculus. [Contig view]
GeneID66881.
KEGGmmu:66881.

Organism-specific databases

MGIMGI:1914131. Pcyox1.
RougeSearch...

Phylogenomic databases

HOGENOMQ9CQF9.
HOVERGENQ9CQF9.
OMAQ9CQF9. SLRMHMW.

Enzyme and pathway databases

BRENDA1.8.3.5. 244.

Gene expression databases

ArrayExpressQ9CQF9.
BgeeQ9CQF9.
CleanExMM_PCYOX1.
GermOnlineENSMUSG00000029998. Mus musculus.

Family and domain databases

InterProIPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR010795. Prenylcys_lyase.
IPR017046. Prenylcysteine_Oxase.
[Graphical view]
PfamPF07156. Prenylcys_lyase. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
PIRSFPIRSF036292. Prenylcysteine_oxidase. 1 hit.
ProtoNetSearch...

Other Resources

NextBio322917.
SOURCESearch...

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Entry information

Entry namePCYOX_MOUSE
AccessionPrimary (citable) accession number: Q9CQF9
Secondary accession number(s): Q3UHV6, Q69ZW0, Q8BZX1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2005
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents