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Protein

Biliverdin reductase A

Gene

BLVRA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Reduces the gamma-methene bridge of the open tetrapyrrole, biliverdin IX alpha, to bilirubin with the concomitant oxidation of a NADH or NADPH cofactor.

Miscellaneous

Uses the reactants NADH or NADPH depending on the pH; NADH is used at the acidic pH range (6-6.9) and NADPH at the alkaline range (8.5-8.7). NADPH, however, is the probable reactant in biological systems.

Catalytic activityi

Bilirubin + NAD(P)+ = biliverdin + NAD(P)H.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Pathwayi: protoheme degradation

This protein is involved in the pathway protoheme degradation, which is part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the pathway protoheme degradation and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei98NAD or NADP; via carbonyl oxygen1
Metal bindingi280ZincSequence analysis1
Metal bindingi281ZincSequence analysis1
Metal bindingi292ZincSequence analysis1
Metal bindingi293ZincSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 20NAD or NADP6
Nucleotide bindingi44 – 46NAD or NADP3
Nucleotide bindingi77 – 80NAD or NADP4

GO - Molecular functioni

  • biliverdin reductase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • heme catabolic process Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB

Keywordsi

Molecular functionOxidoreductase
LigandMetal-binding, NAD, NADP, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:HS02928-MONOMER
BRENDAi1.3.1.24 2681
ReactomeiR-HSA-189483 Heme degradation
SIGNORiP53004
UniPathwayiUPA00684

Names & Taxonomyi

Protein namesi
Recommended name:
Biliverdin reductase A (EC:1.3.1.24)
Short name:
BVR A
Alternative name(s):
Biliverdin-IX alpha-reductase
Gene namesi
Name:BLVRA
Synonyms:BLVR, BVR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000106605.10
HGNCiHGNC:1062 BLVRA
MIMi109750 gene
neXtProtiNX_P53004

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Hyperbiliverdinemia (HBLVD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition characterized by a green discoloration of the skin, urine, serum, and other bodily fluids. It is due to increased biliverdin resulting from inefficient conversion to bilirubin. Affected individuals appear to have symptoms only in the context of obstructive cholestasis and/or liver failure. In some cases, green jaundice can resolve after resolution of obstructive cholestasis.
See also OMIM:614156

Organism-specific databases

DisGeNETi644
MalaCardsiBLVRA
MIMi614156 phenotype
OpenTargetsiENSG00000106605
Orphaneti276405 Hyperbiliverdinemia
PharmGKBiPA25373

Chemistry databases

DrugBankiDB00157 NADH

Polymorphism and mutation databases

BioMutaiBLVRA
DMDMi23830892

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000108521 – 22 Publications2
ChainiPRO_00000108533 – 296Biliverdin reductase A1 PublicationAdd BLAST294

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei174PhosphothreonineCombined sources1
Modified residuei178PhosphoserineCombined sources1
Modified residuei230PhosphoserineCombined sources1
Modified residuei248N6-acetyllysineCombined sources1
Modified residuei253N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP53004
MaxQBiP53004
PaxDbiP53004
PeptideAtlasiP53004
PRIDEiP53004

2D gel databases

OGPiP53004
REPRODUCTION-2DPAGEIPI00294158

PTM databases

iPTMnetiP53004
PhosphoSitePlusiP53004

Expressioni

Tissue specificityi

Liver.

Gene expression databases

BgeeiENSG00000106605
CleanExiHS_BLVRA
ExpressionAtlasiP53004 baseline and differential
GenevisibleiP53004 HS

Organism-specific databases

HPAiHPA019709
HPA042865
HPA054322

Interactioni

Subunit structurei

Monomer.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi107113, 21 interactors
DIPiDIP-42180N
IntActiP53004, 8 interactors
MINTiP53004
STRINGi9606.ENSP00000265523

Structurei

Secondary structure

1296
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 14Combined sources6
Helixi18 – 28Combined sources11
Helixi33 – 36Combined sources4
Beta strandi37 – 43Combined sources7
Beta strandi50 – 53Combined sources4
Helixi59 – 64Combined sources6
Beta strandi70 – 73Combined sources4
Helixi77 – 89Combined sources13
Beta strandi93 – 98Combined sources6
Helixi104 – 117Combined sources14
Beta strandi121 – 124Combined sources4
Helixi126 – 129Combined sources4
Helixi131 – 140Combined sources10
Beta strandi145 – 154Combined sources10
Helixi159 – 162Combined sources4
Helixi165 – 168Combined sources4
Helixi170 – 180Combined sources11
Beta strandi182 – 193Combined sources12
Beta strandi198 – 207Combined sources10
Beta strandi212 – 219Combined sources8
Beta strandi226 – 235Combined sources10
Helixi250 – 262Combined sources13
Helixi268 – 290Combined sources23

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2H63X-ray2.70A/B/C/D7-296[»]
ProteinModelPortaliP53004
SMRiP53004
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53004

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi11 – 16Poly-Val6

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IH7U Eukaryota
ENOG4111FZX LUCA
GeneTreeiENSGT00390000011072
HOGENOMiHOG000231884
HOVERGENiHBG003218
InParanoidiP53004
KOiK00214
OMAiPMTLSWA
OrthoDBiEOG091G0E2N
PhylomeDBiP53004
TreeFamiTF342889

Family and domain databases

InterProiView protein in InterPro
IPR017094 Biliverdin_Rdtase_A
IPR015249 Biliverdin_Rdtase_cat
IPR036291 NAD(P)-bd_dom_sf
IPR000683 Oxidoreductase_N
PfamiView protein in Pfam
PF09166 Biliv-reduc_cat, 1 hit
PF01408 GFO_IDH_MocA, 1 hit
PIRSFiPIRSF037032 Biliverdin_reductase_A, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD040165 Biliverdin_Rdtase_cat, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53004-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAEPERKFG VVVVGVGRAG SVRMRDLRNP HPSSAFLNLI GFVSRRELGS
60 70 80 90 100
IDGVQQISLE DALSSQEVEV AYICSESSSH EDYIRQFLNA GKHVLVEYPM
110 120 130 140 150
TLSLAAAQEL WELAEQKGKV LHEEHVELLM EEFAFLKKEV VGKDLLKGSL
160 170 180 190 200
LFTAGPLEEE RFGFPAFSGI SRLTWLVSLF GELSLVSATL EERKEDQYMK
210 220 230 240 250
MTVCLETEKK SPLSWIEEKG PGLKRNRYLS FHFKSGSLEN VPNVGVNKNI
260 270 280 290
FLKDQNIFVQ KLLGQFSEKE LAAEKKRILH CLGLAEEIQK YCCSRK
Length:296
Mass (Da):33,428
Last modified:October 10, 2002 - v2
Checksum:i2CF2AA7F1CDDB707
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti121L → S in AAH05902 (PubMed:15489334).Curated1
Sequence conflicti154 – 155AG → SD in CAA63635 (PubMed:8631357).Curated2
Sequence conflicti160E → D in CAA63635 (PubMed:8631357).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0192303A → T3 PublicationsCorresponds to variant dbSNP:rs699512Ensembl.1
Natural variantiVAR_01923137L → V1 PublicationCorresponds to variant dbSNP:rs17245918Ensembl.1
Natural variantiVAR_01485156Q → R1 PublicationCorresponds to variant dbSNP:rs1050916Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34877 mRNA Translation: AAC35588.1
X93086 mRNA Translation: CAA63635.1
AK291862 mRNA Translation: BAF84551.1
AY616754 Genomic DNA Translation: AAT11126.1
AC005189 Genomic DNA No translation available.
AC004939 Genomic DNA Translation: AAD05025.1
AC004985 Genomic DNA Translation: AAP21879.1
BC005902 mRNA Translation: AAH05902.1
BC008456 mRNA Translation: AAH08456.1
CCDSiCCDS5472.1
PIRiG02066
S62624
RefSeqiNP_000703.2, NM_000712.3
NP_001240752.1, NM_001253823.1
XP_011513776.1, XM_011515474.2
XP_016868009.1, XM_017012520.1
UniGeneiHs.488143

Genome annotation databases

EnsembliENST00000265523; ENSP00000265523; ENSG00000106605
ENST00000402924; ENSP00000385757; ENSG00000106605
GeneIDi644
KEGGihsa:644
UCSCiuc003tir.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiBIEA_HUMAN
AccessioniPrimary (citable) accession number: P53004
Secondary accession number(s): A8K747
, O95019, Q86UX0, Q96QL4, Q9BRW8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 10, 2002
Last modified: May 23, 2018
This is version 174 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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