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Protein

Beta,beta-carotene 15,15'-dioxygenase

Gene

Bco1

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

Functioni

Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.By similarity

Catalytic activityi

Beta-carotene + O2 = 2 all-trans-retinal.1 Publication

Cofactori

Fe2+By similarityNote: Binds 1 Fe2+ ion per subunit.By similarity

Pathwayi: retinol metabolism

This protein is involved in the pathway retinol metabolism, which is part of Cofactor metabolism.
View all proteins of this organism that are known to be involved in the pathway retinol metabolism and in Cofactor metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi172 – 1721Iron; catalyticBy similarity
Metal bindingi237 – 2371Iron; catalyticBy similarity
Metal bindingi308 – 3081Iron; catalyticBy similarity
Metal bindingi514 – 5141Iron; catalyticBy similarity

GO - Molecular functioni

  • beta-carotene 15,15'-monooxygenase activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • beta-carotene metabolic process Source: MGI
  • retinal metabolic process Source: MGI
  • retinoid metabolic process Source: UniProtKB
  • retinol metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.13.11.63. 3474.
1.14.99.36. 3474.
ReactomeiR-MMU-975634. Retinoid metabolism and transport.
SABIO-RKQ9JJS6.
UniPathwayiUPA00912.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta,beta-carotene 15,15'-dioxygenase (EC:1.13.11.63By similarity)
Alternative name(s):
Beta-carotene dioxygenase 1
Beta-carotene oxygenase 1By similarity
Gene namesi
Name:Bco1By similarity
Synonyms:Bcdo, Bcdo1, Bcmo1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1926923. Bco1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 566566Beta,beta-carotene 15,15'-dioxygenasePRO_0000143934Add
BLAST

Proteomic databases

EPDiQ9JJS6.
MaxQBiQ9JJS6.
PaxDbiQ9JJS6.
PRIDEiQ9JJS6.

PTM databases

iPTMnetiQ9JJS6.
PhosphoSiteiQ9JJS6.

Expressioni

Tissue specificityi

Expressed in liver, kidney, small intestine and testis.1 Publication

Developmental stagei

Abundantly expressed at embryonic day 7 with lower levels at embryonic days 11, 13 and 15.1 Publication

Gene expression databases

BgeeiQ9JJS6.
CleanExiMM_BCMO1.
ExpressionAtlasiQ9JJS6. baseline and differential.
GenevisibleiQ9JJS6. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034308.

Structurei

3D structure databases

ProteinModelPortaliQ9JJS6.
SMRiQ9JJS6. Positions 10-517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the carotenoid oxygenase family.Curated

Phylogenomic databases

eggNOGiKOG1285. Eukaryota.
COG3670. LUCA.
GeneTreeiENSGT00500000044783.
HOGENOMiHOG000232156.
HOVERGENiHBG050679.
InParanoidiQ9JJS6.
KOiK00515.
OMAiEDKTHIH.
OrthoDBiEOG7353WB.
PhylomeDBiQ9JJS6.
TreeFamiTF314019.

Family and domain databases

InterProiIPR004294. Carotenoid_Oase.
[Graphical view]
PANTHERiPTHR10543. PTHR10543. 2 hits.
PfamiPF03055. RPE65. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JJS6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEIIFGQNKK EQLEPVQAKV TGSIPAWLQG TLLRNGPGMH TVGESKYNHW
60 70 80 90 100
FDGLALLHSF SIRDGEVFYR SKYLQSDTYI ANIEANRIVV SEFGTMAYPD
110 120 130 140 150
PCKNIFSKAF SYLSHTIPDF TDNCLINIMK CGEDFYATTE TNYIRKIDPQ
160 170 180 190 200
TLETLEKVDY RKYVAVNLAT SHPHYDEAGN VLNMGTSVVD KGRTKYVIFK
210 220 230 240 250
IPATVPDSKK KGKSPVKHAE VFCSISSRSL LSPSYYHSFG VTENYVVFLE
260 270 280 290 300
QPFKLDILKM ATAYMRGVSW ASCMSFDRED KTYIHIIDQR TRKPVPTKFY
310 320 330 340 350
TDPMVVFHHV NAYEEDGCVL FDVIAYEDSS LYQLFYLANL NKDFEEKSRL
360 370 380 390 400
TSVPTLRRFA VPLHVDKDAE VGSNLVKVSS TTATALKEKD GHVYCQPEVL
410 420 430 440 450
YEGLELPRIN YAYNGKPYRY IFAAEVQWSP VPTKILKYDI LTKSSLKWSE
460 470 480 490 500
ESCWPAEPLF VPTPGAKDED DGVILSAIVS TDPQKLPFLL ILDAKSFTEL
510 520 530 540 550
ARASVDADMH LDLHGLFIPD ADWNAVKQTP AETQEVENSD HPTDPTAPEL
560
SHSENDFTAG HGGSSL
Length:566
Mass (Da):63,864
Last modified:March 1, 2001 - v2
Checksum:i1B4367815247A8D2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti409 – 4091I → T in AAG15381 (PubMed:11401432).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278064 mRNA. Translation: CAB92531.2.
AF271298 mRNA. Translation: AAG33982.1.
AF294899 mRNA. Translation: AAG15381.1.
AY114302
, AY114294, AY114295, AY114296, AY114297, AY114298, AY114299, AY114300, AY114301 Genomic DNA. Translation: AAM76677.1.
AK054171 mRNA. Translation: BAC35679.1.
CCDSiCCDS22697.1.
RefSeqiNP_067461.2. NM_021486.3.
UniGeneiMm.174133.

Genome annotation databases

EnsembliENSMUST00000034308; ENSMUSP00000034308; ENSMUSG00000031845.
GeneIDi63857.
KEGGimmu:63857.
UCSCiuc009now.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ278064 mRNA. Translation: CAB92531.2.
AF271298 mRNA. Translation: AAG33982.1.
AF294899 mRNA. Translation: AAG15381.1.
AY114302
, AY114294, AY114295, AY114296, AY114297, AY114298, AY114299, AY114300, AY114301 Genomic DNA. Translation: AAM76677.1.
AK054171 mRNA. Translation: BAC35679.1.
CCDSiCCDS22697.1.
RefSeqiNP_067461.2. NM_021486.3.
UniGeneiMm.174133.

3D structure databases

ProteinModelPortaliQ9JJS6.
SMRiQ9JJS6. Positions 10-517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034308.

PTM databases

iPTMnetiQ9JJS6.
PhosphoSiteiQ9JJS6.

Proteomic databases

EPDiQ9JJS6.
MaxQBiQ9JJS6.
PaxDbiQ9JJS6.
PRIDEiQ9JJS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034308; ENSMUSP00000034308; ENSMUSG00000031845.
GeneIDi63857.
KEGGimmu:63857.
UCSCiuc009now.2. mouse.

Organism-specific databases

CTDi53630.
MGIiMGI:1926923. Bco1.

Phylogenomic databases

eggNOGiKOG1285. Eukaryota.
COG3670. LUCA.
GeneTreeiENSGT00500000044783.
HOGENOMiHOG000232156.
HOVERGENiHBG050679.
InParanoidiQ9JJS6.
KOiK00515.
OMAiEDKTHIH.
OrthoDBiEOG7353WB.
PhylomeDBiQ9JJS6.
TreeFamiTF314019.

Enzyme and pathway databases

UniPathwayiUPA00912.
BRENDAi1.13.11.63. 3474.
1.14.99.36. 3474.
ReactomeiR-MMU-975634. Retinoid metabolism and transport.
SABIO-RKQ9JJS6.

Miscellaneous databases

PROiQ9JJS6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JJS6.
CleanExiMM_BCMO1.
ExpressionAtlasiQ9JJS6. baseline and differential.
GenevisibleiQ9JJS6. MM.

Family and domain databases

InterProiIPR004294. Carotenoid_Oase.
[Graphical view]
PANTHERiPTHR10543. PTHR10543. 2 hits.
PfamiPF03055. RPE65. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression pattern and localization of beta,beta-carotene 15,15'-dioxygenase in different tissues."
    Wyss A., Wirtz G.M., Woggon W.D., Brugger R., Wyss M., Friedlein A., Riss G., Bachmann H., Hunziker W.
    Biochem. J. 354:521-529(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "Cloning and characterization of a human beta,beta-carotene-15,15-prime dioxygenase that is highly expressed in the retinal pigment epithelium."
    Yan W., Jang G.-F., Haeseleer F., Esumi N., Chang J., Kerrigan M., Campochiaro M., Campochiaro P., Palczewski K., Zack D.J.
    Genomics 72:193-202(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  3. "Identification, expression, and substrate specificity of a mammalian beta-carotene 15,15'-dioxygenase."
    Redmond T.M., Gentleman S., Duncan T., Yu S., Wiggert B., Gantt E., Cunningham F.X. Jr.
    J. Biol. Chem. 276:6560-6565(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: C57BL/6J.
  4. "Identification of beta-carotene 15,15'-monooxygenase as a peroxisome proliferator-activated receptor target gene."
    Boulanger A., McLemore P., Copeland N.G., Gilbert D.J., Jenkins N.A., Yu S.S., Gentleman S., Redmond T.M.
    FASEB J. 17:1304-1306(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  5. "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] OF 29-483.
    Strain: C57BL/6J.
    Tissue: Oviduct.

Entry informationi

Entry nameiBCDO1_MOUSE
AccessioniPrimary (citable) accession number: Q9JJS6
Secondary accession number(s): Q6K1L5, Q8C6N5, Q9ERN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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 one 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.