P16116 (ALDR_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aldose reductase
Short name=AR
EC=1.1.1.21

Alternative name(s):
20-alpha-hydroxysteroid dehydrogenase
Short name=20-alpha-HSD
EC=1.1.1.149
Aldehyde reductase

Gene names

Name:

AKR1B1

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	315 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
Catalytic activity	Alditol + NAD(P)+ = aldose + NAD(P)H. 17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)+ = 17-alpha-hydroxyprogesterone + NAD(P)H.
Subunit structure	Monomer.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the aldo/keto reductase family.
Sequence caution	The sequence AAA30370.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	17-alpha,20-alpha-dihydroxypregn-4-en-3-one dehydrogenase activity Inferred from electronic annotation. Source: EC alditol:NADP+ 1-oxidoreductase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 315	315	Aldose reductase		PRO_0000124622
Regions
	Nucleotide binding	9 – 18	10	NADP Potential
	Nucleotide binding	210 – 272	63	NADP By similarity
Sites
	Active site	48	1	Proton donor By similarity
	Binding site	110	1	Substrate By similarity
	Site	77	1	Lowers pKa of active site Tyr By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylalanine Ref.1
	Modified residue	94	1	N6-acetyllysine By similarity
	Modified residue	221	1	N6-acetyllysine By similarity
	Modified residue	262	1	N6-acetyllysine By similarity
Natural variations
	Natural variant	4	1	I → L.
	Natural variant	6	1	L → I.
Experimental info
	Sequence conflict	65	1	Q → K in AAA30370. Ref.2
	Sequence conflict	65	1	Q → K in AAB25333. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P16116 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 18597E7332A3F9C2	FASTA	315	35,919
	10 20 30 40 50 60 AHNIVLYTGA KMPILGLGTW KSPPGKVTEA VKVAIDLGYR HIDCAHVYQN ENEVGLALQA 70 80 90 100 110 120 KLQEQVVKRE DLFIVSKLWC TYHDKDLVKG ACQKTLSDLK LDYLDLYLIH WPTGFKPGKD 130 140 150 160 170 180 FFPLDEDGNV IPSEKDFVDT WTAMEELVDE GLVKAIGVSN FNHLQVEKIL NKPGLKYKPA 190 200 210 220 230 240 VNQIECHPYL TQEKLIQYCN SKGIVVTAYS PLGSPDRPWA KPEDPSILED PRIKAIADKY 250 260 270 280 290 300 NKTTAQVLIR FPIQRNLIVI PKSVTPERIA ENFQVFDFEL DKEDMNTLLS YNRDWRACAL 310 VSCASHRDYP FHEEF

References

[1]	"Sequence analysis of bovine lens aldose reductase." Schade S.Z., Early S.L., Williams T.R., Kezdy F.J., Heinrikson R.L., Grimshaw C.E., Doughty C.C. J. Biol. Chem. 265:3628-3635(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Tissue: Lens.
[2]	"Molecular cloning of testicular 20 alpha-hydroxysteroid dehydrogenase: identity with aldose reductase." Warren J.C., Murdock G.L., Ma Y., Goodman S.R., Zimmer W.E. Biochemistry 32:1401-1406(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-315. Tissue: Testis.
[3]	"Isolation and characterization of cDNA clones encoding aldose reductase." Petrash J.M., Favello A.D. Curr. Eye Res. 8:1021-1027(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-315. Tissue: Lens.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M31463 mRNA. Translation: AAA30370.1. Different initiation.
S54973 mRNA. Translation: AAB25333.1.

IPI

IPI00700920.

PIR

A35452.

UniGene

Bt.63116.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GO6	model	-	A	1-315	[»]

ProteinModelPortal

P16116.

SMR

P16116. Positions 1-315.

ModBase

Search...

Proteomic databases

PaxDb

P16116.

PRIDE

P16116.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Phylogenomic databases

eggNOG

COG0656.

HOVERGEN

HBG000020.

InParanoid

P16116.

OrthoDB

EOG4VMFFR.

Enzyme and pathway databases

SABIO-RK

P16116.

Family and domain databases

Gene3D

3.20.20.100. 1 hit.

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
IPR020471. Aldo/keto_reductase_subgr.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]

PANTHER

PTHR11732. PTHR11732. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

PIRSF

PIRSF000097. AKR. 1 hit.

PRINTS

PR00069. ALDKETRDTASE.

SUPFAM

SSF51430. Aldo/ket_red. 1 hit.

PROSITE

PS00798. ALDOKETO_REDUCTASE_1. 1 hit.
PS00062. ALDOKETO_REDUCTASE_2. 1 hit.
PS00063. ALDOKETO_REDUCTASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P16116.

ChEMBL

CHEMBL3081.

Entry information

Entry name

ALDR_BOVIN

Accession

Primary (citable) accession number: P16116

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program