BCDO2_HUMAN
ID BCDO2_HUMAN Reviewed; 579 AA.
AC Q9BYV7; B0YIX5; B4DNC3; E9PBI8; E9PJJ1; Q8IUS0; Q96JC8; Q96JY5;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 5.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Carotenoid-cleaving dioxygenase, mitochondrial {ECO:0000250|UniProtKB:Q99NF1};
DE EC=1.13.11.- {ECO:0000250|UniProtKB:Q99NF1};
DE EC=1.13.11.71 {ECO:0000250|UniProtKB:Q99NF1};
DE AltName: Full=B-diox-II {ECO:0000303|PubMed:11278918};
DE AltName: Full=Beta,beta-carotene 9',10'-oxygenase {ECO:0000303|PubMed:11278918};
DE AltName: Full=Beta-carotene dioxygenase 2 {ECO:0000312|HGNC:HGNC:18503};
GN Name=BCO2 {ECO:0000312|HGNC:HGNC:18503};
GN Synonyms=BCDO2 {ECO:0000312|HGNC:HGNC:18503};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS PRO-231 AND LEU-548.
RC TISSUE=Uterus;
RA Cunningham F.X. Jr.;
RT "An ortholog of the human retinal pigment epithelium protein RPE65.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 6), AND VARIANTS
RP PRO-231 AND LEU-548.
RC TISSUE=Heart, and Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G);
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-548.
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT LEU-548.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-579 (ISOFORM 1), AND VARIANTS PRO-231 AND
RP LEU-548.
RC TISSUE=Liver;
RX PubMed=11278918; DOI=10.1074/jbc.m011510200;
RA Kiefer C., Hessel S., Lampert J.M., Vogt K., Lederer M.O., Breithaupt D.E.,
RA von Lintig J.;
RT "Identification and characterization of a mammalian enzyme catalyzing the
RT asymmetric oxidative cleavage of provitamin A.";
RL J. Biol. Chem. 276:14110-14116(2001).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=15983114; DOI=10.1369/jhc.5a6705.2005;
RA Lindqvist A., He Y.-G., Andersson S.;
RT "Cell type-specific expression of beta-carotene 9',10'-monooxygenase in
RT human tissues.";
RL J. Histochem. Cytochem. 53:1403-1412(2005).
CC -!- FUNCTION: Broad specificity mitochondrial dioxygenase that mediates the
CC asymmetric oxidative cleavage of carotenoids. Cleaves carotenes (pure
CC hydrocarbon carotenoids) such as all-trans-beta-carotene and lycopene
CC as well as xanthophylls (oxygenated carotenoids) such as zeaxanthin,
CC lutein and beta-cryptoxanthin at both the 9,10 and the 9',10' carbon-
CC carbon double bond. Through its function in carotenoids metabolism
CC regulates oxidative stress and the production of important signaling
CC molecules. {ECO:0000250|UniProtKB:Q99NF1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-beta-carotene + O2 = all-trans-10'-apo-beta-
CC carotenal + beta-ionone; Xref=Rhea:RHEA:26389, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:17579, ChEBI:CHEBI:32325, ChEBI:CHEBI:53153;
CC EC=1.13.11.71; Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26390;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-cis-lycopene + O2 = (3E,5E)-6,10-dimethylundeca-3,5,9-trien-
CC 2-one + 5-cis-10'-apo-lycopenal; Xref=Rhea:RHEA:68444,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:67207, ChEBI:CHEBI:177905,
CC ChEBI:CHEBI:177906; Evidence={ECO:0000250|UniProtKB:Q6QT07};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68445;
CC Evidence={ECO:0000250|UniProtKB:Q6QT07};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-cis-lycopene + O2 = (3E,5E)-6,10-dimethylundeca-3,5,9-
CC trien-2-one + 13-cis-10'-apo-lycopenal; Xref=Rhea:RHEA:68448,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:67207, ChEBI:CHEBI:177907,
CC ChEBI:CHEBI:177908; Evidence={ECO:0000250|UniProtKB:Q6QT07};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68449;
CC Evidence={ECO:0000250|UniProtKB:Q6QT07};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lutein + O2 = (3R)-3-hydroxy-10'-apo-beta-carotenal + (3R,6R)-
CC hydroxy-alpha-ionone; Xref=Rhea:RHEA:68428, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28838, ChEBI:CHEBI:177902, ChEBI:CHEBI:177904;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68429;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lutein + O2 = (3R)-hydroxy-beta-ionone + (3R,6R)-3-hydroxy-
CC 10'-apo-alpha-carotenal; Xref=Rhea:RHEA:68432, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:28838, ChEBI:CHEBI:53173, ChEBI:CHEBI:177903;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68433;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-zeaxanthin + 2 O2 = 2 (3R)-hydroxy-beta-ionone +
CC 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial; Xref=Rhea:RHEA:26393,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:53171,
CC ChEBI:CHEBI:53173; Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:26394;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-zeaxanthin + O2 = (3R)-3-hydroxy-10'-apo-beta-
CC carotenal + (3R)-hydroxy-beta-ionone; Xref=Rhea:RHEA:68104,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:27547, ChEBI:CHEBI:53173,
CC ChEBI:CHEBI:177902; Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68105;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-cryptoxanthin + O2 = (3R)-hydroxy-beta-ionone + all-
CC trans-10'-apo-beta-carotenal; Xref=Rhea:RHEA:68440,
CC ChEBI:CHEBI:10362, ChEBI:CHEBI:15379, ChEBI:CHEBI:53153,
CC ChEBI:CHEBI:53173; Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68441;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-10'-apo-beta-carotenal + O2 = 4,9-dimethyldodeca-
CC 2,4,6,8,10-pentaenedial + beta-ionone; Xref=Rhea:RHEA:68452,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:32325, ChEBI:CHEBI:53153,
CC ChEBI:CHEBI:53171; Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68453;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-3-hydroxy-10'-apo-beta-carotenal + O2 = (3R)-hydroxy-
CC beta-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial;
CC Xref=Rhea:RHEA:68424, ChEBI:CHEBI:15379, ChEBI:CHEBI:53171,
CC ChEBI:CHEBI:53173, ChEBI:CHEBI:177902;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68425;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R,6R)-3-hydroxy-10'-apo-alpha-carotenal + O2 = (3R,6R)-
CC hydroxy-alpha-ionone + 4,9-dimethyldodeca-2,4,6,8,10-pentaenedial;
CC Xref=Rhea:RHEA:68436, ChEBI:CHEBI:15379, ChEBI:CHEBI:53171,
CC ChEBI:CHEBI:177903, ChEBI:CHEBI:177904;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68437;
CC Evidence={ECO:0000250|UniProtKB:Q99NF1};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q6QT07};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q6QT07};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:Q99NF1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9BYV7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BYV7-2; Sequence=VSP_008599;
CC Name=4;
CC IsoId=Q9BYV7-4; Sequence=VSP_008599, VSP_008600;
CC Name=5;
CC IsoId=Q9BYV7-5; Sequence=VSP_046916;
CC Name=6;
CC IsoId=Q9BYV7-6; Sequence=VSP_046915;
CC -!- TISSUE SPECIFICITY: Highly expressed in retinal pigment epithelium.
CC Also expressed in stomach, small intestine, liver, testis, kidney,
CC adrenal gland, pancreas, heart, skeletal muscle and prostate (at
CC protein level). {ECO:0000269|PubMed:15983114}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC27994.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF276432; AAK69433.1; -; mRNA.
DR EMBL; AK027801; BAB55379.1; -; mRNA.
DR EMBL; AK297853; BAG60185.1; -; mRNA.
DR EMBL; EF444956; ACA05952.1; -; Genomic_DNA.
DR EMBL; AP002884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67192.1; -; Genomic_DNA.
DR EMBL; BC041656; AAH41656.2; -; mRNA.
DR EMBL; AJ290393; CAC27994.1; ALT_INIT; mRNA.
DR CCDS; CCDS41716.1; -. [Q9BYV7-2]
DR CCDS; CCDS58181.1; -. [Q9BYV7-5]
DR CCDS; CCDS58182.1; -. [Q9BYV7-4]
DR CCDS; CCDS58183.1; -. [Q9BYV7-6]
DR CCDS; CCDS8358.2; -. [Q9BYV7-1]
DR RefSeq; NP_001032367.2; NM_001037290.2. [Q9BYV7-2]
DR RefSeq; NP_001243326.1; NM_001256397.1. [Q9BYV7-4]
DR RefSeq; NP_001243327.1; NM_001256398.1. [Q9BYV7-5]
DR RefSeq; NP_001243329.1; NM_001256400.1. [Q9BYV7-6]
DR RefSeq; NP_114144.4; NM_031938.5. [Q9BYV7-1]
DR AlphaFoldDB; Q9BYV7; -.
DR SMR; Q9BYV7; -.
DR STRING; 9606.ENSP00000350314; -.
DR iPTMnet; Q9BYV7; -.
DR PhosphoSitePlus; Q9BYV7; -.
DR SwissPalm; Q9BYV7; -.
DR BioMuta; BCO2; -.
DR DMDM; 308153680; -.
DR MassIVE; Q9BYV7; -.
DR PaxDb; Q9BYV7; -.
DR PeptideAtlas; Q9BYV7; -.
DR PRIDE; Q9BYV7; -.
DR ProteomicsDB; 19234; -.
DR ProteomicsDB; 21156; -.
DR ProteomicsDB; 79718; -. [Q9BYV7-1]
DR ProteomicsDB; 79719; -. [Q9BYV7-2]
DR ProteomicsDB; 79720; -. [Q9BYV7-4]
DR Antibodypedia; 45628; 118 antibodies from 19 providers.
DR DNASU; 83875; -.
DR Ensembl; ENST00000357685.11; ENSP00000350314.5; ENSG00000197580.13. [Q9BYV7-1]
DR Ensembl; ENST00000361053.8; ENSP00000354338.4; ENSG00000197580.13. [Q9BYV7-5]
DR Ensembl; ENST00000438022.5; ENSP00000414843.1; ENSG00000197580.13. [Q9BYV7-2]
DR Ensembl; ENST00000526088.5; ENSP00000436615.1; ENSG00000197580.13. [Q9BYV7-4]
DR Ensembl; ENST00000531169.5; ENSP00000437053.1; ENSG00000197580.13. [Q9BYV7-2]
DR Ensembl; ENST00000532593.5; ENSP00000431802.1; ENSG00000197580.13. [Q9BYV7-6]
DR GeneID; 83875; -.
DR KEGG; hsa:83875; -.
DR MANE-Select; ENST00000357685.11; ENSP00000350314.5; NM_031938.7; NP_114144.5.
DR UCSC; uc001pnf.4; human. [Q9BYV7-1]
DR CTD; 83875; -.
DR DisGeNET; 83875; -.
DR GeneCards; BCO2; -.
DR HGNC; HGNC:18503; BCO2.
DR HPA; ENSG00000197580; Tissue enhanced (heart muscle, liver, retina).
DR MIM; 611740; gene.
DR neXtProt; NX_Q9BYV7; -.
DR OpenTargets; ENSG00000197580; -.
DR PharmGKB; PA162377424; -.
DR VEuPathDB; HostDB:ENSG00000197580; -.
DR eggNOG; KOG1285; Eukaryota.
DR GeneTree; ENSGT00950000182913; -.
DR OMA; RAHGKVC; -.
DR OrthoDB; 895046at2759; -.
DR PhylomeDB; Q9BYV7; -.
DR TreeFam; TF314019; -.
DR BioCyc; MetaCyc:G66-33846-MON; -.
DR BRENDA; 1.13.11.71; 2681.
DR PathwayCommons; Q9BYV7; -.
DR Reactome; R-HSA-975634; Retinoid metabolism and transport.
DR BioGRID-ORCS; 83875; 9 hits in 1072 CRISPR screens.
DR ChiTaRS; BCO2; human.
DR GenomeRNAi; 83875; -.
DR Pharos; Q9BYV7; Tbio.
DR PRO; PR:Q9BYV7; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BYV7; protein.
DR Bgee; ENSG00000197580; Expressed in right lobe of liver and 139 other tissues.
DR ExpressionAtlas; Q9BYV7; baseline and differential.
DR Genevisible; Q9BYV7; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0010437; F:9,10 (9', 10')-carotenoid-cleaving dioxygenase activity; ISS:UniProtKB.
DR GO; GO:0102076; F:beta,beta-carotene-9',10'-cleaving oxygenase activity; ISS:UniProtKB.
DR GO; GO:0003834; F:beta-carotene 15,15'-dioxygenase activity; IBA:GO_Central.
DR GO; GO:0010436; F:carotenoid dioxygenase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:UniProtKB.
DR GO; GO:0016121; P:carotene catabolic process; IDA:BHF-UCL.
DR GO; GO:0016119; P:carotene metabolic process; IDA:UniProtKB.
DR GO; GO:0016116; P:carotenoid metabolic process; ISS:BHF-UCL.
DR GO; GO:0062172; P:lutein catabolic process; ISS:UniProtKB.
DR GO; GO:1901176; P:lycopene catabolic process; ISS:UniProtKB.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:BHF-UCL.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISS:BHF-UCL.
DR GO; GO:0042574; P:retinal metabolic process; IBA:GO_Central.
DR GO; GO:0042573; P:retinoic acid metabolic process; NAS:UniProtKB.
DR GO; GO:0016124; P:xanthophyll catabolic process; ISS:UniProtKB.
DR GO; GO:1901826; P:zeaxanthin catabolic process; ISS:UniProtKB.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Dioxygenase; Iron; Lipid metabolism; Metal-binding;
KW Mitochondrion; Oxidoreductase; Reference proteome.
FT CHAIN 1..579
FT /note="Carotenoid-cleaving dioxygenase, mitochondrial"
FT /id="PRO_0000143937"
FT BINDING 226
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 286
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 357
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT BINDING 573
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9JJS6"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046915"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_008599"
FT VAR_SEQ 173..245
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046916"
FT VAR_SEQ 501..506
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008600"
FT VARIANT 231
FT /note="L -> P (in dbSNP:rs10891338)"
FT /evidence="ECO:0000269|PubMed:11278918,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.1"
FT /id="VAR_047047"
FT VARIANT 289
FT /note="G -> E (in dbSNP:rs17113607)"
FT /id="VAR_047048"
FT VARIANT 548
FT /note="I -> L (in dbSNP:rs2217401)"
FT /evidence="ECO:0000269|PubMed:11278918,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.1, ECO:0000269|Ref.5"
FT /id="VAR_047049"
FT CONFLICT 26
FT /note="H -> Y (in Ref. 7; CAC27994)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="N -> D (in Ref. 7; CAC27994)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="K -> E (in Ref. 7; CAC27994)"
FT /evidence="ECO:0000305"
FT CONFLICT 429
FT /note="P -> Q (in Ref. 2; BAG60185)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="W -> C (in Ref. 7; CAC27994)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 579 AA; 65674 MW; B14F54FCEC1092CE CRC64;
MFFRVFLHFI RSHSATAVDF LPVMVHRLPV FKRYMGNTPQ KKAVFGQCRG LPCVAPLLTT
VEEAPRGISA RVWGHFPKWL NGSLLRIGPG KFEFGKDKYN HWFDGMALLH QFRMAKGTVT
YRSKFLQSDT YKANSAKNRI VISEFGTLAL PDPCKNVFER FMSRFELPGK AAAMTDNTNV
NYVRYKGDYY LCTETNFMNK VDIETLEKTE KVDWSKFIAV NGATAHPHYD LDGTAYNMGN
SFGPYGFSYK VIRVPPEKVD LGETIHGVQV ICSIASTEKG KPSYYHSFGM TRNYIIFIEQ
PLKMNLWKIA TSKIRGKAFS DGISWEPQCN TRFHVVEKRT GQLLPGRYYS KPFVTFHQIN
AFEDQGCVII DLCCQDNGRT LEVYQLQNLR KAGEGLDQVH NSAAKSFPRR FVLPLNVSLN
APEGDNLSPL SYTSASAVKQ ADGTIWCSHE NLHQEDLEKE GGIEFPQIYY DRFSGKKYHF
FYGCGFRHLV GDSLIKVDVV NKTLKVWRED GFYPSEPVFV PAPGTNEEDG GVILSVVITP
NQNESNFILV LDAKNFEELG RAEVPVQMPY GFHGTFIPI
