ID   BIEA_MOUSE              Reviewed;         295 AA.
AC   Q9CY64; Q3T9C6; Q80WR6; Q9DD21;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   04-NOV-2008, entry version 50.
DE   RecName: Full=Biliverdin reductase A;
DE            Short=BVR A;
DE            EC=1.3.1.24;
DE   AltName: Full=Biliverdin-IX alpha-reductase;
DE   Flags: Precursor;
GN   Name=Blvra;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryonic liver, Kidney, and Spleen;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Reduces the gamma-methene bridge of the open
CC       tetrapyrrole, biliverdin IX alpha, to bilirubin with the
CC       concomitant oxidation of a NADH or NADPH cofactor (By similarity).
CC   -!- CATALYTIC ACTIVITY: Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- PATHWAY: Porphyrin metabolism; protoheme degradation.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- MISCELLANEOUS: Uses the reactants NADH or NADPH depending on the
CC       pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the
CC       alkaline range (8.5-8.7). NADPH, however, is the probable reactant
CC       in biological systems (By similarity).
CC   -!- SIMILARITY: Belongs to the gfo/idh/mocA family. Biliverdin
CC       reductase subfamily.
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DR   EMBL; AK002231; BAB21950.1; -; mRNA.
DR   EMBL; AK010847; BAB27219.1; -; mRNA.
DR   EMBL; AK172620; BAE43098.1; -; mRNA.
DR   EMBL; BC052146; AAH52146.1; -; mRNA.
DR   RefSeq; NP_080954.4; -.
DR   UniGene; Mm.22028; -.
DR   HSSP; P46844; 1GCU.
DR   SMR; Q9CY64; 1-292.
DR   PhosphoSite; Q9CY64; -.
DR   Ensembl; ENSMUSG00000001999; Mus musculus.
DR   GeneID; 109778; -.
DR   KEGG; mmu:109778; -.
DR   NMPDR; fig|10090.3.peg.6848; -.
DR   MGI; MGI:88170; Blvra.
DR   HOGENOM; Q9CY64; -.
DR   HOVERGEN; Q9CY64; -.
DR   NextBio; 362743; -.
DR   ArrayExpress; Q9CY64; -.
DR   CleanEx; MM_BLVRA; -.
DR   GermOnline; ENSMUSG00000001999; Mus musculus.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004074; F:biliverdin reductase activity; IEA:EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR017094; Biliverdin_Rdtase_A.
DR   InterPro; IPR015249; Biliverdin_Rdtase_cat.
DR   InterPro; IPR000683; GFO/IDH/MocA_N.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF09166; Biliv-reduc_cat; 1.
DR   Pfam; PF01408; GFO_IDH_MocA; 1.
DR   PIRSF; PIRSF037032; Biliverdin_reductase_A; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; NAD; NADP; Oxidoreductase; Zinc.
FT   PROPEP        1      2       By similarity.
FT                                /FTId=PRO_0000010854.
FT   CHAIN         3    295       Biliverdin reductase A.
FT                                /FTId=PRO_0000010855.
FT   COMPBIAS     11     16       Poly-Val.
FT   METAL       279    279       Zinc (Potential).
FT   METAL       280    280       Zinc (Potential).
FT   METAL       291    291       Zinc (Potential).
FT   METAL       292    292       Zinc (Potential).
FT   CONFLICT     27     27       L -> S (in Ref. 2; AAH52146).
FT   CONFLICT    295    295       Q -> QWGGSFRYL (in Ref. 1; BAB21950).
SQ   SEQUENCE   295 AA;  33525 MW;  F2E1682BD77032A4 CRC64;
     MSTEPKRKFG VVVVGVGRAG SVRIRDLKDP HSSAFLNLIG YVSRRELGSL DNVRQISLED
     ALRSQEVDVA YICTESSSHE DYIRQFLQAG KHVLVEYPMA LSFAAAQELW ELAAQKGRVL
     HEEHIELLME EFEFLKREVA GKELLKGSLR FTASPLEEEK FGFPAFSGIS RLTWLVSLFG
     ELSLISATME NRKEDQYMKM TVQLETQNKS PLSWIEEKGP GLKRNRHISI HFKSGSLEEV
     PNVGVNKNIF LKDQDIFIQK LLGQVSAEDL AAEKKRILHC LELASDIQRL CHRKQ
//