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Q9CQF9

- PCYOX_MOUSE

UniProt

Q9CQF9 - PCYOX_MOUSE

Protein

Prenylcysteine oxidase

Gene

Pcyox1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

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

    Cofactori

    FAD.By similarity

    GO - Molecular functioni

    1. chloride-transporting ATPase activity Source: Ensembl
    2. prenylcysteine oxidase activity Source: MGI

    GO - Biological processi

    1. prenylated protein catabolic process Source: Ensembl
    2. prenylcysteine catabolic process Source: MGI

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prenylcysteine oxidase (EC:1.8.3.5)
    Gene namesi
    Name:Pcyox1
    Synonyms:Kiaa0908
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1914131. Pcyox1.

    Subcellular locationi

    Lysosome By similarity

    GO - Cellular componenti

    1. lysosome Source: UniProtKB-SubCell
    2. plasma membrane Source: Ensembl
    3. very-low-density lipoprotein particle Source: Ensembl

    Keywords - Cellular componenti

    Lysosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 505477Prenylcysteine oxidasePRO_0000023300Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki162 – 162Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Glycosylationi196 – 1961N-linked (GlcNAc...)1 Publication
    Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi353 – 3531N-linked (GlcNAc...)1 Publication

    Keywords - PTMi

    Glycoprotein, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ9CQF9.
    PaxDbiQ9CQF9.
    PRIDEiQ9CQF9.

    PTM databases

    PhosphoSiteiQ9CQF9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9CQF9.
    BgeeiQ9CQF9.
    CleanExiMM_PCYOX1.
    GenevestigatoriQ9CQF9.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9CQF9. 5 interactions.
    MINTiMINT-1858396.
    STRINGi10090.ENSMUSP00000032065.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CQF9.
    SMRiQ9CQF9. Positions 34-111.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the prenylcysteine oxidase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG73316.
    GeneTreeiENSGT00390000011206.
    HOGENOMiHOG000241149.
    HOVERGENiHBG053532.
    InParanoidiQ9CQF9.
    KOiK05906.
    OMAiNGIECAA.
    OrthoDBiEOG7VB2F5.
    PhylomeDBiQ9CQF9.
    TreeFamiTF329001.

    Family and domain databases

    InterProiIPR010795. Prenylcys_lyase.
    IPR017046. Prenylcysteine_Oxase.
    [Graphical view]
    PfamiPF07156. Prenylcys_lyase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036292. Prenylcysteine_oxidase. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9CQF9-1 [UniParc]FASTAAdd to Basket

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    MGRFAAALVG SLFWLGLLLC GLGSLASAEP RAPPNRIAIV GAGIGGTSSA    50
    YYLRKKFGKD VKIDVFEREE VGGRLATLKV QGHDYEAGGS VIHPLNLHMK 100
    RFVKELGLSS VPASGGLVGV YNGKSLVFEE SSWFVINVIK LVWRYGFQSL 150
    RMHMWVEDLL DKFMRIYRYQ SHDYAFSSVE KLMHAIGGDD YVRLLNQTLR 200
    ENLKKAGFSE TFLNEMIAPV MKVNYGQSTD INAFVGAVSL TAADSNLWAV 250
    EGGNKIVCSG LLQASSSNLI SGSVMSIEEK TRTKQTGNPT KMYEVVYKTG 300
    SETHSDFYDI VLVAAPLNRK MSNITFRNFD PPIEEFNDPY QQLVTTFIKG 350
    ELNSTLFSSR PKDQFGLSAI LVTDDSDMFI NSLSIVASVR QKEGPPPAVD 400
    GMHVWKTFSR DILTKEQISK LFLSYDYAVR KPWLSYPHYE PPQKCPSIIL 450
    HDRLYYLNGI EFAASCMEMS AIAGYNAALL AYHRWNGNED MIDQDDLYER 500
    LKTEL 505
    Length:505
    Mass (Da):56,495
    Last modified:June 1, 2001 - v1
    Checksum:i9169BC4CC7D97561
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti114 – 1141S → T in BAC28252. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS20311.1.
    RefSeqiNP_080099.1. NM_025823.4.
    UniGeneiMm.30849.

    Genome annotation databases

    EnsembliENSMUST00000032065; ENSMUSP00000032065; ENSMUSG00000029998.
    GeneIDi66881.
    KEGGimmu:66881.
    UCSCiuc009cro.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS20311.1.
    RefSeqi NP_080099.1. NM_025823.4.
    UniGenei Mm.30849.

    3D structure databases

    ProteinModelPortali Q9CQF9.
    SMRi Q9CQF9. Positions 34-111.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9CQF9. 5 interactions.
    MINTi MINT-1858396.
    STRINGi 10090.ENSMUSP00000032065.

    PTM databases

    PhosphoSitei Q9CQF9.

    Proteomic databases

    MaxQBi Q9CQF9.
    PaxDbi Q9CQF9.
    PRIDEi Q9CQF9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032065 ; ENSMUSP00000032065 ; ENSMUSG00000029998 .
    GeneIDi 66881.
    KEGGi mmu:66881.
    UCSCi uc009cro.2. mouse.

    Organism-specific databases

    CTDi 51449.
    MGIi MGI:1914131. Pcyox1.
    Rougei Search...

    Phylogenomic databases

    eggNOGi NOG73316.
    GeneTreei ENSGT00390000011206.
    HOGENOMi HOG000241149.
    HOVERGENi HBG053532.
    InParanoidi Q9CQF9.
    KOi K05906.
    OMAi NGIECAA.
    OrthoDBi EOG7VB2F5.
    PhylomeDBi Q9CQF9.
    TreeFami TF329001.

    Miscellaneous databases

    NextBioi 322917.
    PROi Q9CQF9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9CQF9.
    Bgeei Q9CQF9.
    CleanExi MM_PCYOX1.
    Genevestigatori Q9CQF9.

    Family and domain databases

    InterProi IPR010795. Prenylcys_lyase.
    IPR017046. Prenylcysteine_Oxase.
    [Graphical view ]
    Pfami PF07156. Prenylcys_lyase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036292. Prenylcysteine_oxidase. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-196.
      Strain: C57BL/6.
      Tissue: Plasma.
    6. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-353.

    Entry informationi

    Entry nameiPCYOX_MOUSE
    AccessioniPrimary (citable) accession number: Q9CQF9
    Secondary accession number(s): Q3UHV6, Q69ZW0, Q8BZX1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 104 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3