BCDO1_MOUSE
ID BCDO1_MOUSE Reviewed; 566 AA.
AC Q9JJS6; Q6K1L5; Q8C6N5; Q9ERN9;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Beta,beta-carotene 15,15'-dioxygenase {ECO:0000305|PubMed:11092891};
DE EC=1.13.11.63 {ECO:0000269|PubMed:11092891, ECO:0000269|PubMed:15951442};
DE AltName: Full=Beta-carotene dioxygenase 1;
DE AltName: Full=Beta-carotene oxygenase 1 {ECO:0000312|MGI:MGI:1926923};
GN Name=Bco1 {ECO:0000312|MGI:MGI:1926923};
GN Synonyms=Bcdo, Bcdo1, Bcmo1 {ECO:0000312|MGI:MGI:1926923};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=11237856; DOI=10.1042/0264-6021:3540521;
RA Wyss A., Wirtz G.M., Woggon W.D., Brugger R., Wyss M., Friedlein A.,
RA Riss G., Bachmann H., Hunziker W.;
RT "Expression pattern and localization of beta,beta-carotene 15,15'-
RT dioxygenase in different tissues.";
RL Biochem. J. 354:521-529(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=11401432; DOI=10.1006/geno.2000.6476;
RA Yan W., Jang G.-F., Haeseleer F., Esumi N., Chang J., Kerrigan M.,
RA Campochiaro M., Campochiaro P., Palczewski K., Zack D.J.;
RT "Cloning and characterization of a human beta,beta-carotene-15,15-prime
RT dioxygenase that is highly expressed in the retinal pigment epithelium.";
RL Genomics 72:193-202(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J;
RX PubMed=11092891; DOI=10.1074/jbc.m009030200;
RA Redmond T.M., Gentleman S., Duncan T., Yu S., Wiggert B., Gantt E.,
RA Cunningham F.X. Jr.;
RT "Identification, expression, and substrate specificity of a mammalian beta-
RT carotene 15,15'-dioxygenase.";
RL J. Biol. Chem. 276:6560-6565(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=12759335; DOI=10.1096/fj.02-0690fje;
RA Boulanger A., McLemore P., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Yu S.S., Gentleman S., Redmond T.M.;
RT "Identification of beta-carotene 15,15'-monooxygenase as a peroxisome
RT proliferator-activated receptor target gene.";
RL FASEB J. 17:1304-1306(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-483.
RC STRAIN=C57BL/6J; TISSUE=Oviduct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP PATHWAY, AND MUTAGENESIS OF HIS-49; ASP-52; HIS-58; GLU-140; HIS-172;
RP HIS-174; HIS-237; HIS-308; HIS-309; GLU-314; GLU-405; GLU-450; GLU-457;
RP GLU-469 AND HIS-514.
RX PubMed=15951442; DOI=10.1074/jbc.m500409200;
RA Poliakov E., Gentleman S., Cunningham F.X. Jr., Miller-Ihli N.J.,
RA Redmond T.M.;
RT "Key role of conserved histidines in recombinant mouse beta-carotene
RT 15,15'-monooxygenase-1 activity.";
RL J. Biol. Chem. 280:29217-29223(2005).
CC -!- FUNCTION: Symmetrically cleaves beta-carotene into two molecules of
CC retinal using a dioxygenase mechanism. {ECO:0000269|PubMed:11092891,
CC ECO:0000269|PubMed:15951442}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-beta-carotene + O2 = 2 all-trans-retinal;
CC Xref=Rhea:RHEA:32887, ChEBI:CHEBI:15379, ChEBI:CHEBI:17579,
CC ChEBI:CHEBI:17898; EC=1.13.11.63;
CC Evidence={ECO:0000269|PubMed:11092891, ECO:0000269|PubMed:15951442};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32888;
CC Evidence={ECO:0000305|PubMed:11092891};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000305|PubMed:15951442};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000305|PubMed:15951442};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 uM for all-trans-beta-carotene (at pH 8.0 and 37 degrees
CC Celsius) {ECO:0000269|PubMed:11092891};
CC Vmax=104.8 pmol/h/ug enzyme for the formation of all-trans-retinal
CC (at pH 8.0 and 37 degrees Celsius) {ECO:0000269|PubMed:11092891};
CC -!- PATHWAY: Cofactor metabolism; retinol metabolism.
CC {ECO:0000305|PubMed:11092891}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9I993}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, kidney, small intestine and
CC testis. {ECO:0000269|PubMed:11092891}.
CC -!- DEVELOPMENTAL STAGE: Abundantly expressed at embryonic day 7 with lower
CC levels at embryonic days 11, 13 and 15. {ECO:0000269|PubMed:11092891}.
CC -!- SIMILARITY: Belongs to the carotenoid oxygenase family. {ECO:0000305}.
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DR EMBL; AJ278064; CAB92531.2; -; mRNA.
DR EMBL; AF271298; AAG33982.1; -; mRNA.
DR EMBL; AF294899; AAG15381.1; -; mRNA.
DR EMBL; AY114302; AAM76677.1; -; Genomic_DNA.
DR EMBL; AY114294; AAM76677.1; JOINED; Genomic_DNA.
DR EMBL; AY114295; AAM76677.1; JOINED; Genomic_DNA.
DR EMBL; AY114296; AAM76677.1; JOINED; Genomic_DNA.
DR EMBL; AY114297; AAM76677.1; JOINED; Genomic_DNA.
DR EMBL; AY114298; AAM76677.1; JOINED; Genomic_DNA.
DR EMBL; AY114299; AAM76677.1; JOINED; Genomic_DNA.
DR EMBL; AY114300; AAM76677.1; JOINED; Genomic_DNA.
DR EMBL; AY114301; AAM76677.1; JOINED; Genomic_DNA.
DR EMBL; AK054171; BAC35679.1; -; mRNA.
DR CCDS; CCDS22697.1; -.
DR RefSeq; NP_067461.2; NM_021486.3.
DR AlphaFoldDB; Q9JJS6; -.
DR SMR; Q9JJS6; -.
DR STRING; 10090.ENSMUSP00000034308; -.
DR iPTMnet; Q9JJS6; -.
DR PhosphoSitePlus; Q9JJS6; -.
DR EPD; Q9JJS6; -.
DR MaxQB; Q9JJS6; -.
DR PaxDb; Q9JJS6; -.
DR PRIDE; Q9JJS6; -.
DR ProteomicsDB; 277117; -.
DR Antibodypedia; 48219; 134 antibodies from 19 providers.
DR DNASU; 63857; -.
DR Ensembl; ENSMUST00000034308; ENSMUSP00000034308; ENSMUSG00000031845.
DR GeneID; 63857; -.
DR KEGG; mmu:63857; -.
DR UCSC; uc009now.2; mouse.
DR CTD; 53630; -.
DR MGI; MGI:1926923; Bco1.
DR VEuPathDB; HostDB:ENSMUSG00000031845; -.
DR eggNOG; KOG1285; Eukaryota.
DR GeneTree; ENSGT00950000182913; -.
DR HOGENOM; CLU_016472_1_1_1; -.
DR InParanoid; Q9JJS6; -.
DR OMA; ENYIIFL; -.
DR OrthoDB; 524712at2759; -.
DR PhylomeDB; Q9JJS6; -.
DR TreeFam; TF314019; -.
DR BRENDA; 1.13.11.63; 3474.
DR Reactome; R-MMU-975634; Retinoid metabolism and transport.
DR SABIO-RK; Q9JJS6; -.
DR UniPathway; UPA00912; -.
DR BioGRID-ORCS; 63857; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q9JJS6; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9JJS6; protein.
DR Bgee; ENSMUSG00000031845; Expressed in gastrula and 76 other tissues.
DR ExpressionAtlas; Q9JJS6; baseline and differential.
DR Genevisible; Q9JJS6; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0003834; F:beta-carotene 15,15'-dioxygenase activity; IDA:UniProtKB.
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:1901810; P:beta-carotene metabolic process; IMP:MGI.
DR GO; GO:0016121; P:carotene catabolic process; IDA:UniProtKB.
DR GO; GO:0042574; P:retinal metabolic process; IMP:UniProtKB.
DR GO; GO:0001523; P:retinoid metabolic process; IDA:UniProtKB.
DR GO; GO:0042572; P:retinol metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004294; Carotenoid_Oase.
DR PANTHER; PTHR10543; PTHR10543; 1.
DR Pfam; PF03055; RPE65; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Dioxygenase; Iron; Lipid metabolism; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..566
FT /note="Beta,beta-carotene 15,15'-dioxygenase"
FT /id="PRO_0000143934"
FT REGION 530..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:15951442"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:15951442"
FT BINDING 308
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:15951442"
FT BINDING 514
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:15951442"
FT MUTAGEN 49
FT /note="H->A: No significant effect on beta-carotene 15,15'-
FT monooxygenase activity. Decreased stability."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 52
FT /note="D->A: Decreased beta-carotene 15,15'-monooxygenase
FT activity. Decreased catalytic efficiency. Loss of beta-
FT carotene 15,15'-monooxygenase activity; when associated
FT with A-140."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 58
FT /note="H->A: No significant effect on beta-carotene 15,15'-
FT monooxygenase activity. Decreased catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 140
FT /note="E->A: Decreased beta-carotene 15,15'-monooxygenase
FT activity. Decreased catalytic efficiency. Loss of beta-
FT carotene 15,15'-monooxygenase activity; when associated
FT with A-52."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 172
FT /note="H->A: No effect on protein abundance. Loss of beta-
FT carotene 15,15'-monooxygenase activity. Decreased iron
FT binding."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 174
FT /note="H->A: No significant effect on beta-carotene 15,15'-
FT monooxygenase activity."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 237
FT /note="H->A: No effect on protein abundance. Loss of beta-
FT carotene 15,15'-monooxygenase activity. Decreased iron
FT binding."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 308
FT /note="H->A: No effect on protein abundance. Loss of beta-
FT carotene 15,15'-monooxygenase activity. Decreased iron
FT binding."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 309
FT /note="H->A: No significant effect on beta-carotene 15,15'-
FT monooxygenase activity."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 314
FT /note="E->A: No significant effect on beta-carotene 15,15'-
FT monooxygenase activity."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 405
FT /note="E->A: Loss of beta-carotene 15,15'-monooxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 450
FT /note="E->A: No significant effect on beta-carotene 15,15'-
FT monooxygenase activity."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 457
FT /note="E->A: Decreased beta-carotene 15,15'-monooxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 469
FT /note="E->A: Decreased beta-carotene 15,15'-monooxygenase
FT activity."
FT /evidence="ECO:0000269|PubMed:15951442"
FT MUTAGEN 514
FT /note="H->A: No effect on protein abundance. Loss of beta-
FT carotene 15,15'-monooxygenase activity. Loss of iron
FT binding."
FT /evidence="ECO:0000269|PubMed:15951442"
FT CONFLICT 409
FT /note="I -> T (in Ref. 2; AAG15381)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 566 AA; 63864 MW; 1B4367815247A8D2 CRC64;
MEIIFGQNKK EQLEPVQAKV TGSIPAWLQG TLLRNGPGMH TVGESKYNHW FDGLALLHSF
SIRDGEVFYR SKYLQSDTYI ANIEANRIVV SEFGTMAYPD PCKNIFSKAF SYLSHTIPDF
TDNCLINIMK CGEDFYATTE TNYIRKIDPQ TLETLEKVDY RKYVAVNLAT SHPHYDEAGN
VLNMGTSVVD KGRTKYVIFK IPATVPDSKK KGKSPVKHAE VFCSISSRSL LSPSYYHSFG
VTENYVVFLE QPFKLDILKM ATAYMRGVSW ASCMSFDRED KTYIHIIDQR TRKPVPTKFY
TDPMVVFHHV NAYEEDGCVL FDVIAYEDSS LYQLFYLANL NKDFEEKSRL TSVPTLRRFA
VPLHVDKDAE VGSNLVKVSS TTATALKEKD GHVYCQPEVL YEGLELPRIN YAYNGKPYRY
IFAAEVQWSP VPTKILKYDI LTKSSLKWSE ESCWPAEPLF VPTPGAKDED DGVILSAIVS
TDPQKLPFLL ILDAKSFTEL ARASVDADMH LDLHGLFIPD ADWNAVKQTP AETQEVENSD
HPTDPTAPEL SHSENDFTAG HGGSSL
