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Protein

Beta,beta-carotene 15,15'-monooxygenase

Gene

BCO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Symmetrically cleaves beta-carotene into two molecules of retinal. The reaction proceeds in three stages, epoxidation of the 15,15'-double bond, hydration of the double bond leading to ring opening, and oxidative cleavage of the diol formed.

Catalytic activityi

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

Cofactori

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

Pathwayi

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

  1. beta-carotene 15,15'-monooxygenase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW
  3. monooxygenase activity Source: UniProtKB-KW

GO - Biological processi

  1. phototransduction, visible light Source: Reactome
  2. retinal metabolic process Source: BHF-UCL
  3. retinoid metabolic process Source: UniProtKB
  4. retinol metabolic process Source: UniProtKB-UniPathway
  5. vitamin A biosynthetic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS06050-MONOMER.
ReactomeiREACT_24968. Retinoid metabolism and transport.
SABIO-RKQ9HAY6.
UniPathwayiUPA00912.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta,beta-carotene 15,15'-monooxygenase (EC:1.14.99.36)
Alternative name(s):
Beta-carotene dioxygenase 1
Beta-carotene oxygenase 1Imported
Gene namesi
Name:BCO1Imported
Synonyms:BCDO, BCDO1, BCMO1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:13815. BCO1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Hypercarotenemia and vitamin A deficiency, autosomal dominant1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by increased serum beta-carotene, decreased conversion of beta-carotene to vitamin A and decreased serum vitamin A.

See also OMIM:115300
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1701T → M in ADHVAD; has about 90% decreased enzyme activity compared to wild-type; no evidence for a dominant-negative effect; consistent with a loss-of-function mutation resulting in haploinsufficiency. 1 Publication
Corresponds to variant rs119478057 [ dbSNP | Ensembl ].
VAR_058112

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi115300. phenotype.
Orphaneti199285. Hereditary hypercarotenemia and vitamin A deficiency.
PharmGKBiPA37812.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 547547Beta,beta-carotene 15,15'-monooxygenasePRO_0000143933Add
BLAST

Proteomic databases

PaxDbiQ9HAY6.
PRIDEiQ9HAY6.

PTM databases

PhosphoSiteiQ9HAY6.

Expressioni

Tissue specificityi

Highly expressed in retinal pigment epithelium. Also expressed in kidney, testis, liver, brain, small intestine and colon.1 Publication

Gene expression databases

BgeeiQ9HAY6.
CleanExiHS_BCMO1.
ExpressionAtlasiQ9HAY6. baseline and differential.
GenevestigatoriQ9HAY6.

Organism-specific databases

HPAiHPA043811.

Interactioni

Protein-protein interaction databases

IntActiQ9HAY6. 1 interaction.
STRINGi9606.ENSP00000258168.

Structurei

3D structure databases

ProteinModelPortaliQ9HAY6.
SMRiQ9HAY6. Positions 10-517.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the carotenoid oxygenase family.Curated

Phylogenomic databases

eggNOGiCOG3670.
GeneTreeiENSGT00500000044783.
HOGENOMiHOG000232156.
HOVERGENiHBG050679.
KOiK00515.
OMAiNIMRCGE.
OrthoDBiEOG7353WB.
PhylomeDBiQ9HAY6.
TreeFamiTF314019.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9HAY6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDIIFGRNRK EQLEPVRAKV TGKIPAWLQG TLLRNGPGMH TVGESRYNHW
60 70 80 90 100
FDGLALLHSF TIRDGEVYYR SKYLRSDTYN TNIEANRIVV SEFGTMAYPD
110 120 130 140 150
PCKNIFSKAF SYLSHTIPDF TDNCLINIMK CGEDFYATSE TNYIRKINPQ
160 170 180 190 200
TLETLEKVDY RKYVAVNLAT SHPHYDEAGN VLNMGTSIVE KGKTKYVIFK
210 220 230 240 250
IPATVPEGKK QGKSPWKHTE VFCSIPSRSL LSPSYYHSFG VTENYVIFLE
260 270 280 290 300
QPFRLDILKM ATAYIRRMSW ASCLAFHREE KTYIHIIDQR TRQPVQTKFY
310 320 330 340 350
TDAMVVFHHV NAYEEDGCIV FDVIAYEDNS LYQLFYLANL NQDFKENSRL
360 370 380 390 400
TSVPTLRRFA VPLHVDKNAE VGTNLIKVAS TTATALKEED GQVYCQPEFL
410 420 430 440 450
YEGLELPRVN YAHNGKQYRY VFATGVQWSP IPTKIIKYDI LTKSSLKWRE
460 470 480 490 500
DDCWPAEPLF VPAPGAKDED DGVILSAIVS TDPQKLPFLL ILDAKSFTEL
510 520 530 540
ARASVDVDMH MDLHGLFITD MDWDTKKQAA SEEQRDRASD CHGAPLT
Length:547
Mass (Da):62,637
Last modified:March 1, 2001 - v1
Checksum:iF94BC8B01D56F9CB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti302 – 3021D → G in BAA91776. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti170 – 1701T → M in ADHVAD; has about 90% decreased enzyme activity compared to wild-type; no evidence for a dominant-negative effect; consistent with a loss-of-function mutation resulting in haploinsufficiency. 1 Publication
Corresponds to variant rs119478057 [ dbSNP | Ensembl ].
VAR_058112
Natural varianti267 – 2671R → S.2 Publications
Corresponds to variant rs12934922 [ dbSNP | Ensembl ].
VAR_048406
Natural varianti379 – 3791A → V.
Corresponds to variant rs7501331 [ dbSNP | Ensembl ].
VAR_048407

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF294900 mRNA. Translation: AAG15380.1.
AK001592 mRNA. Translation: BAA91776.1.
CH471114 Genomic DNA. Translation: EAW95537.1.
BC126210 mRNA. Translation: AAI26211.1.
BC126212 mRNA. Translation: AAI26213.1.
CCDSiCCDS10934.1.
RefSeqiNP_059125.2. NM_017429.2.
UniGeneiHs.212172.

Genome annotation databases

EnsembliENST00000258168; ENSP00000258168; ENSG00000135697.
GeneIDi53630.
KEGGihsa:53630.
UCSCiuc002fgn.1. human.

Polymorphism databases

DMDMi41688803.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF294900 mRNA. Translation: AAG15380.1.
AK001592 mRNA. Translation: BAA91776.1.
CH471114 Genomic DNA. Translation: EAW95537.1.
BC126210 mRNA. Translation: AAI26211.1.
BC126212 mRNA. Translation: AAI26213.1.
CCDSiCCDS10934.1.
RefSeqiNP_059125.2. NM_017429.2.
UniGeneiHs.212172.

3D structure databases

ProteinModelPortaliQ9HAY6.
SMRiQ9HAY6. Positions 10-517.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9HAY6. 1 interaction.
STRINGi9606.ENSP00000258168.

PTM databases

PhosphoSiteiQ9HAY6.

Polymorphism databases

DMDMi41688803.

Proteomic databases

PaxDbiQ9HAY6.
PRIDEiQ9HAY6.

Protocols and materials databases

DNASUi53630.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258168; ENSP00000258168; ENSG00000135697.
GeneIDi53630.
KEGGihsa:53630.
UCSCiuc002fgn.1. human.

Organism-specific databases

CTDi53630.
GeneCardsiGC16P081272.
HGNCiHGNC:13815. BCO1.
HPAiHPA043811.
MIMi115300. phenotype.
605748. gene.
neXtProtiNX_Q9HAY6.
Orphaneti199285. Hereditary hypercarotenemia and vitamin A deficiency.
PharmGKBiPA37812.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3670.
GeneTreeiENSGT00500000044783.
HOGENOMiHOG000232156.
HOVERGENiHBG050679.
KOiK00515.
OMAiNIMRCGE.
OrthoDBiEOG7353WB.
PhylomeDBiQ9HAY6.
TreeFamiTF314019.

Enzyme and pathway databases

UniPathwayiUPA00912.
BioCyciMetaCyc:HS06050-MONOMER.
ReactomeiREACT_24968. Retinoid metabolism and transport.
SABIO-RKQ9HAY6.

Miscellaneous databases

ChiTaRSiBCMO1. human.
GenomeRNAii53630.
NextBioi56108.
PROiQ9HAY6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HAY6.
CleanExiHS_BCMO1.
ExpressionAtlasiQ9HAY6. baseline and differential.
GenevestigatoriQ9HAY6.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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], TISSUE SPECIFICITY.
    Tissue: Retinal pigment epithelium.
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-267.
  4. "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], VARIANT SER-267.
    Tissue: Colon.
  5. "Loss-of-function mutation in carotenoid 15,15'-monooxygenase identified in a patient with hypercarotenemia and hypovitaminosis A."
    Lindqvist A., Sharvill J., Sharvill D.E., Andersson S.
    J. Nutr. 137:2346-2350(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ADHVAD MET-170.

Entry informationi

Entry nameiBCDO1_HUMAN
AccessioniPrimary (citable) accession number: Q9HAY6
Secondary accession number(s): A0AV48, A0AV50, Q9NVH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: March 1, 2001
Last modified: January 7, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. 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.