CP26B_RAT
ID CP26B_RAT Reviewed; 512 AA.
AC G3V7X8; Q80YE5;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Cytochrome P450 26B1;
DE EC=1.14.13.- {ECO:0000250|UniProtKB:Q9NR63};
GN Name=Cyp26b1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Bengtson M.H., Rodrigues L.O., Colin C., Hasegawa A.P., Maria-Engler S.S.,
RA Sogayar M.C.;
RT "Retinoic acid-induced genes in glioma cells transformed to normal
RT phenotypic reversion.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the metabolism of retinoic acid (RA), rendering
CC this classical morphogen inactive through oxidation. Involved in the
CC specific inactivation of all-trans-retinoic acid (all-trans-RA), with a
CC preference for the following substrates: all-trans-RA > 9-cis-RA > 13-
CC cis-RA. Generates several hydroxylated forms of RA, including 4-OH-RA,
CC 4-oxo-RA, and 18-OH-RA. Essential for postnatal survival. Plays a
CC central role in germ cell development: acts by degrading RA in the
CC developing testis, preventing STRA8 expression, thereby leading to
CC delay of meiosis. Required for the maintenance of the undifferentiated
CC state of male germ cells during embryonic development in Sertoli cells,
CC inducing arrest in G0 phase of the cell cycle and preventing meiotic
CC entry. Plays a role in skeletal development, both at the level of
CC patterning and in the ossification of bone and the establishment of
CC some synovial joints (By similarity). {ECO:0000250|UniProtKB:Q811W2,
CC ECO:0000250|UniProtKB:Q9NR63}.
CC -!- FUNCTION: Has also a significant activity in oxidation of tazarotenic
CC acid and may therefore metabolize that xenobiotic in vivo.
CC {ECO:0000250|UniProtKB:Q9NR63}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=all-trans-retinoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = all-trans-4-hydroxyretinoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:51984, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:35291,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:134178;
CC Evidence={ECO:0000250|UniProtKB:Q9NR63};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51985;
CC Evidence={ECO:0000250|UniProtKB:Q9NR63};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6A2};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43174}. Microsome membrane
CC {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:O43174}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AY245532; AAO92253.1; -; mRNA.
DR EMBL; CH473957; EDL91177.1; -; Genomic_DNA.
DR RefSeq; NP_851601.1; NM_181087.2.
DR AlphaFoldDB; G3V7X8; -.
DR SMR; G3V7X8; -.
DR STRING; 10116.ENSRNOP00000020505; -.
DR iPTMnet; G3V7X8; -.
DR PhosphoSitePlus; G3V7X8; -.
DR PaxDb; G3V7X8; -.
DR PRIDE; G3V7X8; -.
DR Ensembl; ENSRNOT00000020505; ENSRNOP00000020505; ENSRNOG00000015076.
DR GeneID; 312495; -.
DR KEGG; rno:312495; -.
DR CTD; 56603; -.
DR RGD; 631379; Cyp26b1.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00800000124060; -.
DR HOGENOM; CLU_001570_15_6_1; -.
DR InParanoid; G3V7X8; -.
DR OMA; WTATRDR; -.
DR OrthoDB; 871849at2759; -.
DR PhylomeDB; G3V7X8; -.
DR TreeFam; TF105093; -.
DR Reactome; R-RNO-211916; Vitamins.
DR Reactome; R-RNO-5365859; RA biosynthesis pathway.
DR PRO; PR:G3V7X8; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Proteomes; UP000234681; Chromosome 4.
DR Bgee; ENSRNOG00000015076; Expressed in testis and 18 other tissues.
DR Genevisible; G3V7X8; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IBA:GO_Central.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; ISS:UniProtKB.
DR GO; GO:0008401; F:retinoic acid 4-hydroxylase activity; IMP:RGD.
DR GO; GO:0001972; F:retinoic acid binding; ISO:RGD.
DR GO; GO:0060349; P:bone morphogenesis; ISO:RGD.
DR GO; GO:0001709; P:cell fate determination; ISO:RGD.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISO:RGD.
DR GO; GO:0070268; P:cornification; ISO:RGD.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISO:RGD.
DR GO; GO:0061436; P:establishment of skin barrier; ISO:RGD.
DR GO; GO:0001768; P:establishment of T cell polarity; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; ISO:RGD.
DR GO; GO:0001822; P:kidney development; IEP:RGD.
DR GO; GO:0007140; P:male meiotic nuclear division; ISO:RGD.
DR GO; GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:2001037; P:positive regulation of tongue muscle cell differentiation; ISO:RGD.
DR GO; GO:0009954; P:proximal/distal pattern formation; ISO:RGD.
DR GO; GO:0048385; P:regulation of retinoic acid receptor signaling pathway; ISO:RGD.
DR GO; GO:0045580; P:regulation of T cell differentiation; ISO:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR GO; GO:0034653; P:retinoic acid catabolic process; IMP:RGD.
DR GO; GO:0042573; P:retinoic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR GO; GO:0043587; P:tongue morphogenesis; ISO:RGD.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..512
FT /note="Cytochrome P450 26B1"
FT /id="PRO_0000416906"
FT BINDING 441
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255"
FT CONFLICT 251
FT /note="I -> V (in Ref. 1; AAO92253)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 512 AA; 57352 MW; F346AB0F302E4CE7 CRC64;
MLFEGLELVS ALATLAACLV SVTLLLAVSQ QLWQLRWAAT RDKSCKLPIP KGSMGFPLIG
ETGHWLLQGS GFQSSRREKY GNVFKTHLLG RPLIRVTGAE NVRKILLGEH QLVSTEWPRS
ARVLLGPNTV ANSIGDIHRN KRKVFSKIFS HEALESYLPK IQLVIQDTLR AWSSQPEAIN
VYQEAQRLTF RMAVRVLLGF SIPEEDLGNL FEVYQQFVEN VFSLPVDLPF SGYRRGIQAR
QILQKGLEKA IREKLQCTQG KDYSDALDIL IESSKEHGKE MTMQELKDGT LELIFAAYAT
TASASTSLIM QLLKHPAVLE KLREELRAQG LLHGGGCPCE GTLRLDMLSG LRYLDCVIKE
VMRLFTPVSG GYRTVLQTFE LDGFQIPKGW SVMYSIRDTH DTAPVFKDVN VFDPDRFSQA
RSEDKDGRFH YLPFGGGVRT CLGKHLAKLF LKVLAVELAS TSRFELATRT FPRITLVPVL
HPVDGLSVKF FGLDSNQNEI LPETEAMLSA TV
