Q811W2 (CP26B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytochrome P450 26B1
EC=1.14.-.-

Alternative name(s):
Cytochrome P450 retinoic acid-inactivating 2
Short name=Cytochrome P450RAI-2

Gene names

Name:

Cyp26b1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	512 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the metabolism of retinoic acid (RA), rendering this classical morphogen inactive through oxidation. Involved in the specific inactivation of all-trans-retinoic acid (all-trans-RA), with a preference for the following substrates: all-trans-RA > 9-cis-RA > 13-cis-RA. Generates several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA, and 18-OH-RA. Esential for postnatal survival. Plays a central role in germ cell development: acts by degrading RA in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required for the maintenance of the undifferentiated state of male germ cells during embryonic development in Sertoli cells, inducing arrest in G0 phase of the cell cycle and preventing meiotic entry. Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints. Ref.6 Ref.7 Ref.8 Ref.9
Cofactor	Heme group By similarity.
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein By similarity. Microsome membrane; Peripheral membrane protein By similarity.
Developmental stage	In the embryonic male gonad, expressed in somatic cells as early as E11.5 and persist throughout development. Expression is detected in peritubular myoepithelial cells in the postnatal testis, while expression is absent in developing and adult ovaries. Ref.6 Ref.7
Disruption phenotype	Germ cells enter meiosis precociously in embryonic testes, due to strong-up-regulation of Stra8. Ref.6
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane Microsome
Ligand	Heme Iron Metal-binding
Molecular function	Monooxygenase Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	bone morphogenesis Inferred from electronic annotation. Source: Compara cell fate determination Inferred from mutant phenotype Ref.6. Source: MGI cellular response to retinoic acid Inferred from expression pattern PubMed 18816858. Source: UniProtKB embryonic limb morphogenesis Inferred from mutant phenotype PubMed 15030763. Source: MGI male meiosis Inferred from mutant phenotype Ref.6. Source: MGI positive regulation of gene expression Inferred from mutant phenotype PubMed 18816858. Source: UniProtKB positive regulation of tongue muscle cell differentiation Inferred from mutant phenotype PubMed 18816858. Source: UniProtKB proximal/distal pattern formation Inferred from mutant phenotype PubMed 15030763. Source: MGI retinoic acid catabolic process Inferred from electronic annotation. Source: Compara retinoic acid metabolic process Inferred by curator PubMed 15030763. Source: MGI retinoic acid receptor signaling pathway Inferred from mutant phenotype PubMed 18816858. Source: UniProtKB spermatogenesis Inferred from mutant phenotype Ref.6. Source: MGI tongue morphogenesis Inferred from mutant phenotype PubMed 18816858. Source: UniProtKB
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro retinoic acid 4-hydroxylase activity Inferred from electronic annotation. Source: Compara retinoic acid binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 512	512	Cytochrome P450 26B1		PRO_0000416905
Sites
	Metal binding	441	1	Iron (heme axial ligand) Potential
Experimental info
	Sequence conflict	67 – 68	2	LQ → TR in BAE38630. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q811W2 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: AAA063DE5718824E	FASTA	512	57,375
	10 20 30 40 50 60 MLFEGLELVS ALATLAACLV SVTLLLAVSQ QLWQLRWAAT RDKSCKLPIP KGSMGFPLIG 70 80 90 100 110 120 ETGHWLLQGS GFQSSRREKY GNVFKTHLLG RPLIRVTGAE NVRKILLGEH QLVSTEWPRS 130 140 150 160 170 180 ARVLLGPNTV ANSIGDIHRN KRKVFSKIFS HEALESYLPK IQLVIQDTLR AWSSQPEAIN 190 200 210 220 230 240 VYQEAQRLTF RMAVRVLLGF SIPEEDLGHL FEVYQQFVEN VFSLPVDLPF SGYRRGIQAR 250 260 270 280 290 300 QILQKGLEKA IREKLQCTQG KDYSDALDIL IESSKEHGKE MTMQELKDGT LELIFAAYAT 310 320 330 340 350 360 TASASTSLIM QLLKHPAVLE KLREELRAQG LLHGGGCPCE GTLRLDTLSS LRYLDCVIKE 370 380 390 400 410 420 VMRLFTPVSG GYRTVLQTFE LDGFQIPKGW SVMYSIRDTH DTAPVFKDVN VFDPDRFSQA 430 440 450 460 470 480 RSEDKDGRFH YLPFGGGVRT CLGKHLAKLF LKVLAVELAS TSRFELATRT FPRITLVPVL 490 500 510 HPVDGLSVKF FGLDSNQNEI LPETEAMLSA TV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sexually dimorphic gene expression in the developing mouse gonad." Menke D.B., Page D.C. Gene Expr. Patterns 2:359-367(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: C57BL/6. Tissue: Testis.
[2]	"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]. Strain: C57BL/6J. Tissue: Embryo and Mammary gland.
[3]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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]. Strain: C57BL/6. Tissue: Brain.
[6]	"Retinoid signaling determines germ cell fate in mice." Bowles J., Knight D., Smith C., Wilhelm D., Richman J., Mamiya S., Yashiro K., Chawengsaksophak K., Wilson M.J., Rossant J., Hamada H., Koopman P. Science 312:596-600(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[7]	"Retinoic acid regulates sex-specific timing of meiotic initiation in mice." Koubova J., Menke D.B., Zhou Q., Capel B., Griswold M.D., Page D.C. Proc. Natl. Acad. Sci. U.S.A. 103:2474-2479(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DEVELOPMENTAL STAGE.
[8]	"Cyp26b1 expression in murine Sertoli cells is required to maintain male germ cells in an undifferentiated state during embryogenesis." Li H., MacLean G., Cameron D., Clagett-Dame M., Petkovich M. PLoS ONE 4:E7501-E7501(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Craniosynostosis and multiple skeletal anomalies in humans and zebrafish result from a defect in the localized degradation of retinoic acid." Laue K., Pogoda H.M., Daniel P.B., van Haeringen A., Alanay Y., von Ameln S., Rachwalski M., Morgan T., Gray M.J., Breuning M.H., Sawyer G.M., Sutherland-Smith A.J., Nikkels P.G., Kubisch C., Bloch W., Wollnik B., Hammerschmidt M., Robertson S.P. Am. J. Hum. Genet. 89:595-606(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN SKELETAL DEVELOPMENT.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY134662 mRNA. Translation: AAN08613.1. AK137124 mRNA. Translation: BAE23242.1. AK166211 mRNA. Translation: BAE38630.1. AC153606 Genomic DNA. No translation available. CH466523 Genomic DNA. Translation: EDK99117.1. BC059246 mRNA. Translation: AAH59246.1.
IPI	IPI00187227.
RefSeq	NP_001171184.1. NM_001177713.1. NP_780684.1. NM_175475.3.
UniGene	Mm.255246.
3D structure databases
ProteinModelPortal	Q811W2.
SMR	Q811W2. Positions 47-493.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000076886.
PTM databases
PhosphoSite	Q811W2.
Proteomic databases
PRIDE	Q811W2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000077705; ENSMUSP00000076886; ENSMUSG00000063415. ENSMUST00000168003; ENSMUSP00000128391; ENSMUSG00000063415.
GeneID	232174.
KEGG	mmu:232174.
UCSC	uc009coy.2. mouse.
Organism-specific databases
CTD	56603.
MGI	MGI:2176159. Cyp26b1.
Phylogenomic databases
GeneTree	ENSGT00660000095370.
HOGENOM	HOG000220829.
HOVERGEN	HBG051099.
InParanoid	Q811W2.
KO	K12664.
OMA	GIQARQT.
Gene expression databases
Bgee	Q811W2.
Genevestigator	Q811W2.
Family and domain databases
Gene3D	1.10.630.10. 1 hit.
InterPro	IPR001128. Cyt_P450. IPR017972. Cyt_P450_CS. IPR002403. Cyt_P450_E_grp-IV. [Graphical view]
Pfam	PF00067. p450. 1 hit. [Graphical view]
PRINTS	PR00465. EP450IV. PR00385. P450.
SUPFAM	SSF48264. Cytochrome_P450. 1 hit.
PROSITE	PS00086. CYTOCHROME_P450. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	380970.
SOURCE	Search...

Entry information

Entry name

CP26B_MOUSE

Accession

Primary (citable) accession number: Q811W2
Secondary accession number(s): Q3TM12

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2012
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program