ID BIEA_HUMAN STANDARD; PRT; 296 AA. AC P53004; O95019; Q86UX0; Q96QL4; Q9BRW8; DT 01-OCT-1996 (Rel. 34, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Biliverdin reductase A precursor (EC 1.3.1.24) (Biliverdin-IX alpha- DE reductase) (BVR A). GN Name=BLVRA; Synonyms=BLVR, BVR; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Placenta; RX MEDLINE=96202961; PubMed=8631357; RA Maines M.D., Polevoda B.V., Huang T.-J., McCoubrey W.K. Jr.; RT "Human biliverdin IXalpha reductase is a zinc-metalloprotein. RT Characterization of purified and Escherichia coli expressed enzymes."; RL Eur. J. Biochem. 235:372-381(1996). RN [2] RP NUCLEOTIDE SEQUENCE, AND VARIANT THR-3. RA Komuro A., Tobe T., Nakano Y., Yamaguchi T., Tomita M.; RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE, AND VARIANTS THR-3; VAL-37 AND ARG-56. RA Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., RA Nguyen C.P., Nguyen D.A., Poel C.L., Chambers S.W., Schackwitz W.S., RA Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A.; RT "NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department RT of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)."; RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE, AND VARIANT THR-3. RC TISSUE=Brain, and Prostate; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP PROTEIN SEQUENCE OF 3-36; 48-74 AND 228-248. RC TISSUE=Liver; RX MEDLINE=93143333; PubMed=8424666; DOI=10.1006/abbi.1993.1044; RA Maines M.D., Trakshel G.M.; RT "Purification and characterization of human biliverdin reductase."; RL Arch. Biochem. Biophys. 300:320-326(1993). RN [7] RP PROTEIN SEQUENCE OF 3-22. RC TISSUE=Liver; RX MEDLINE=95014177; PubMed=7929092; RA Yamaguchi T., Komoda Y., Nakajima H.; RT "Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from RT human liver. Purification and characterization."; RL J. Biol. Chem. 269:24343-24348(1994). 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. CC -!- CATALYTIC ACTIVITY: Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H. CC -!- COFACTOR: Binds 1 zinc ion per subunit. Has dual pH/cofactor CC (NADH, NADPH) specificity. Uses NADH at the acidic pH range (6- CC 6.7) and NADPH at the alkaline range (8.5-8.7). CC -!- PATHWAY: Heme metabolism; first step. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. CC -!- TISSUE SPECIFICITY: Liver. CC -!- SIMILARITY: Belongs to the gfo/idh/mocA family. Biliverdin CC reductase subfamily. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X93086; CAA63635.1; -. DR EMBL; U34877; AAC35588.1; -. DR EMBL; AY616754; AAT11126.1; -. DR EMBL; AC005189; -; NOT_ANNOTATED_CDS. DR EMBL; AC004939; AAD05025.1; -. DR EMBL; AC004985; AAP21879.1; -. DR EMBL; BC005902; AAH05902.1; -. DR EMBL; BC008456; AAH08456.1; -. DR PIR; G02066; G02066. DR PIR; S62624; S62624. DR HSSP; P46844; 1GCU. DR OGP; P53004; -. DR Genew; HGNC:1062; BLVRA. DR H-InvDB; HIX0006633; -. DR MIM; 109750; -. DR GO; GO:0004074; F:biliverdin reductase activity; TAS. DR GO; GO:0005489; F:electron transporter activity; TAS. DR InterPro; IPR000683; GFO/IDH/MocA_N. DR Pfam; PF01408; GFO_IDH_MocA; 1. KW Direct protein sequencing; NAD; NADP; Oxidoreductase; Polymorphism; KW Zinc. FT PROPEP 1 2 FT CHAIN 3 296 Biliverdin reductase A. FT DOMAIN 11 16 Poly-Val. FT METAL 280 280 Zinc (Potential). FT METAL 281 281 Zinc (Potential). FT METAL 292 292 Zinc (Potential). FT METAL 293 293 Zinc (Potential). FT VARIANT 3 3 A -> T. FT /FTId=VAR_019230. FT VARIANT 37 37 L -> V. FT /FTId=VAR_019231. FT VARIANT 56 56 Q -> R (in dbSNP:1050916). FT /FTId=VAR_014851. FT CONFLICT 121 121 L -> S (in Ref. 5; AAH05902). FT CONFLICT 154 155 AG -> SD (in Ref. 1). FT CONFLICT 160 160 E -> D (in Ref. 1). SQ SEQUENCE 296 AA; 33428 MW; 2CF2AA7F1CDDB707 CRC64; MNAEPERKFG VVVVGVGRAG SVRMRDLRNP HPSSAFLNLI GFVSRRELGS IDGVQQISLE DALSSQEVEV AYICSESSSH EDYIRQFLNA GKHVLVEYPM TLSLAAAQEL WELAEQKGKV LHEEHVELLM EEFAFLKKEV VGKDLLKGSL LFTAGPLEEE RFGFPAFSGI SRLTWLVSLF GELSLVSATL EERKEDQYMK MTVCLETEKK SPLSWIEEKG PGLKRNRYLS FHFKSGSLEN VPNVGVNKNI FLKDQNIFVQ KLLGQFSEKE LAAEKKRILH CLGLAEEIQK YCCSRK //