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Protein

Prenylcysteine oxidase

Gene

Pcyox1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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

FADBy similarity

GO - Molecular functioni

  • chloride-transporting ATPase activity Source: Ensembl
  • prenylcysteine oxidase activity Source: MGI

GO - Biological processi

  • prenylated protein catabolic process Source: MGI
  • prenylcysteine catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BRENDAi1.8.3.5. 3474.

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 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1914131. Pcyox1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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

BgeeiQ9CQF9.
CleanExiMM_PCYOX1.
ExpressionAtlasiQ9CQF9. baseline and differential.
GenevisibleiQ9CQF9. MM.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9CQF9.
SMRiQ9CQF9. Positions 35-72.
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]
PANTHERiPTHR15944. PTHR15944. 1 hit.
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

« Hide

        10         20         30         40         50
MGRFAAALVG SLFWLGLLLC GLGSLASAEP RAPPNRIAIV GAGIGGTSSA
60 70 80 90 100
YYLRKKFGKD VKIDVFEREE VGGRLATLKV QGHDYEAGGS VIHPLNLHMK
110 120 130 140 150
RFVKELGLSS VPASGGLVGV YNGKSLVFEE SSWFVINVIK LVWRYGFQSL
160 170 180 190 200
RMHMWVEDLL DKFMRIYRYQ SHDYAFSSVE KLMHAIGGDD YVRLLNQTLR
210 220 230 240 250
ENLKKAGFSE TFLNEMIAPV MKVNYGQSTD INAFVGAVSL TAADSNLWAV
260 270 280 290 300
EGGNKIVCSG LLQASSSNLI SGSVMSIEEK TRTKQTGNPT KMYEVVYKTG
310 320 330 340 350
SETHSDFYDI VLVAAPLNRK MSNITFRNFD PPIEEFNDPY QQLVTTFIKG
360 370 380 390 400
ELNSTLFSSR PKDQFGLSAI LVTDDSDMFI NSLSIVASVR QKEGPPPAVD
410 420 430 440 450
GMHVWKTFSR DILTKEQISK LFLSYDYAVR KPWLSYPHYE PPQKCPSIIL
460 470 480 490 500
HDRLYYLNGI EFAASCMEMS AIAGYNAALL AYHRWNGNED MIDQDDLYER

LKTEL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9CQF9.
SMRiQ9CQF9. Positions 35-72.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ9CQF9.

Proteomic databases

MaxQBiQ9CQF9.
PaxDbiQ9CQF9.
PRIDEiQ9CQF9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51449.
MGIiMGI:1914131. Pcyox1.
RougeiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi1.8.3.5. 3474.

Miscellaneous databases

NextBioi322917.
PROiQ9CQF9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CQF9.
CleanExiMM_PCYOX1.
ExpressionAtlasiQ9CQF9. baseline and differential.
GenevisibleiQ9CQF9. MM.

Family and domain databases

InterProiIPR010795. Prenylcys_lyase.
IPR017046. Prenylcysteine_Oxase.
[Graphical view]
PANTHERiPTHR15944. PTHR15944. 1 hit.
PfamiPF07156. Prenylcys_lyase. 1 hit.
[Graphical view]
PIRSFiPIRSF036292. Prenylcysteine_oxidase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 112 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.