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UniProtKB/Swiss-Prot entry P53004


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name BIEA_HUMAN
Primary accession number P53004
Secondary accession numbers A8K747 O95019 Q86UX0 Q96QL4 Q9BRW8
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 10, 2002 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 83)
Name and origin of the protein
Protein name Biliverdin reductase A [Precursor]
Synonyms BVR A
EC 1.3.1.24
Biliverdin-IX alpha-reductase
Gene name
Name: BLVRA
Synonyms: BLVR, BVR
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-3.
PubMed=8950184 [NCBI, ExPASy, EBI, Israel, Japan]
Komuro A., Tobe T., Nakano Y., Yamaguchi T., Tomita M.;
"Cloning and characterization of the cDNA encoding human biliverdin-IX alpha reductase.";
Biochim. Biophys. Acta 1309:89-99(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8631357 [NCBI, ExPASy, EBI, Israel, Japan]
Maines M.D., Polevoda B.V., Huang T.-J., McCoubrey W.K. Jr.;
"Human biliverdin IXalpha reductase is a zinc-metalloprotein. Characterization of purified and Escherichia coli expressed enzymes.";
Eur. J. Biochem. 235:372-381(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-3; VAL-37 AND ARG-56.
NIEHS SNPs program;
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-3.
TISSUE=Brain, and Prostate;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 3-36; 48-74 AND 228-248.
TISSUE=Liver;
DOI=10.1006/abbi.1993.1044; PubMed=8424666 [NCBI, ExPASy, EBI, Israel, Japan]
Maines M.D., Trakshel G.M.;
"Purification and characterization of human biliverdin reductase.";
Arch. Biochem. Biophys. 300:320-326(1993).
[8]
PROTEIN SEQUENCE OF 3-22.
TISSUE=Liver;
PubMed=7929092 [NCBI, ExPASy, EBI, Israel, Japan]
Yamaguchi T., Komoda Y., Nakajima H.;
"Biliverdin-IX alpha reductase and biliverdin-IX beta reductase from human liver. Purification and characterization.";
J. Biol. Chem. 269:24343-24348(1994).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U34877; AAC35588.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X93086; CAA63635.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291862; BAF84551.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY616754; AAT11126.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC005189; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AC004939; AAD05025.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004985; AAP21879.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005902; AAH05902.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008456; AAH08456.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G02066; G02066.
S62624; S62624.
RefSeq NP_000703.2; -.
UniGene Hs.488143
3D structure databases
PDB
2H63; X-ray; 2.70 A; A/B/C/D=7-296.[ExPASy / RCSB / EBI]
PDBsum 2H63; -.
SMR P53004; 1-292.
ModBase P53004.
PTM databases
PhosphoSite P53004; -.
Enzyme and pathway databases
BioCyc MetaCyc:MON-13862; -.
2D gel databases
OGP P53004; -.
REPRODUCTION-2DPAGE IPI00294158; -.
Organism-specific databases
GeneCards GC07P043764; -.
H-InvDB HIX0006633; -.
HGNC HGNC:1062; BLVRA.
GenAtlas BLVRA.
MIM 109750; gene. [NCBI / EBI]
PharmGKB PA25373; -.
GeneCards P53004.
Gene expression databases
ArrayExpress P53004; -.
CleanEx HS_BLVRA; -.
GermOnline ENSG00000106605; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0004074; Molecular function: biliverdin reductase activity (inferred from direct assay from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0042167; Biological process: heme catabolic process (traceable author statement from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR017094; Biliverdin_Rdtase_A.
IPR015249; Biliverdin_Rdtase_cat.
IPR000683; GFO/IDH/MocA_N.
IPR016040; NAD(P)-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.720; NAD(P)-bd; 1.
Pfam PF09166; Biliv-reduc_cat; 1.
PF01408; GFO_IDH_MocA; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF037032; Biliverdin_reductase_A; 1.
Proteomic databases
PeptideAtlas P53004; -.
Proteomics databases
PRIDE P53004; -.
Genome annotation databases
Ensembl ENSG00000106605; Homo sapiens. [Contig view]
GeneID 644; -.
KEGG hsa:644; -.
Phylogenomic databases
HOGENOM P53004; -.
HOVERGEN P53004; -.
Other
DrugBank DB00157; NADH.
NextBio 2614; -.
SOURCE BLVRA; Homo sapiens.
ProtoNet P53004.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Metal-binding; NAD; NADP; Oxidoreductase; Phosphoprotein; Polymorphism; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
PROPEP   1     2  2      PRO_0000010852
CHAIN   3   296  294     Biliverdin reductase A. PRO_0000010853
COMPBIAS   11    16  6     Poly-Val. 
METAL   280   280        Zinc (Potential). 
METAL   281   281        Zinc (Potential). 
METAL   292   292        Zinc (Potential). 
METAL   293   293        Zinc (Potential). 
MOD_RES   230   230        Phosphoserine. 
VARIANT   3     3  1     A -> T (in dbSNP:rs699512 [NCBI]). VAR_019230 
VARIANT   37    37  1     L -> V (in dbSNP:rs17245918 [NCBI]). VAR_019231 [3D]
VARIANT   56    56  1     Q -> R (in dbSNP:rs1050916 [NCBI]). VAR_014851 [3D]
CONFLICT   121   121        L -> S (in Ref. 6; AAH05902). 
CONFLICT   154   155        AG -> SD (in Ref. 2; CAA63635). 
CONFLICT   160   160        E -> D (in Ref. 2; CAA63635). 
STRAND   9    14  6      
HELIX   18    28  11      
HELIX   33    36  4      
STRAND   37    43  7      
STRAND   50    53  4      
HELIX   59    64  6      
STRAND   70    73  4      
HELIX   77    89  13      
STRAND   93    98  6      
HELIX   104   117  14      
STRAND   121   124  4      
HELIX   126   129  4      
HELIX   131   140  10      
STRAND   145   154  10      
HELIX   159   162  4      
HELIX   165   168  4      
HELIX   170   180  11      
STRAND   182   193  12      
STRAND   198   207  10      
STRAND   212   219  8      
STRAND   226   235  10      
HELIX   250   262  13      
HELIX   268   290  23      
Sequence information
Length: 296 AA [This is the length of the unprocessed precursor] Molecular weight: 33428 Da [This is the MW of the unprocessed precursor] CRC64: 2CF2AA7F1CDDB707 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNAEPERKFG VVVVGVGRAG SVRMRDLRNP HPSSAFLNLI GFVSRRELGS IDGVQQISLE 

        70         80         90        100        110        120 
DALSSQEVEV AYICSESSSH EDYIRQFLNA GKHVLVEYPM TLSLAAAQEL WELAEQKGKV 

       130        140        150        160        170        180 
LHEEHVELLM EEFAFLKKEV VGKDLLKGSL LFTAGPLEEE RFGFPAFSGI SRLTWLVSLF 

       190        200        210        220        230        240 
GELSLVSATL EERKEDQYMK MTVCLETEKK SPLSWIEEKG PGLKRNRYLS FHFKSGSLEN 

       250        260        270        280        290 
VPNVGVNKNI FLKDQNIFVQ KLLGQFSEKE LAAEKKRILH CLGLAEEIQK YCCSRK 

P53004 in FASTA format

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