Alcohol dehydrogenase [NADP+] - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P14550 (AK1A1_HUMAN)

Last modified June 16, 2009. Version 103. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Alcohol dehydrogenase [NADP+]
    EC=1.1.1.2
Alternative name(s):
    Aldehyde reductase
    Aldo-keto reductase family 1 member A1

Gene names

Name:	AKR1A1
Synonyms:	ALDR1, ALR

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	325 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Catalyzes the NADPH-dependent reduction of a variety of aldehydes to their corresponding alcohols By similarity.
Catalytic activity	An alcohol + NADP⁺ = an aldehyde + NADPH.
Subunit structure	Monomer By similarity.
Sequence similarities	Belongs to the aldo/keto reductase family.

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Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	glucose metabolic process Ref.1 Traceable author statement. Source: ProtInc oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	alcohol dehydrogenase (NADP+) activity Inferred from electronic annotation. Source: EC aldehyde reductase activity Ref.1 Traceable author statement. Source: ProtInc electron carrier activity Ref.1 Traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
EXOSC4	Q9NPD3	1	EBI-372388,EBI-371823

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 325

324

Alcohol dehydrogenase [NADP+]

PRO_0000124617

Regions

Nucleotide binding

211 – 273

NADP By similarity

Sites

Active site

Proton donor

Binding site

113

Substrate

Site

Lowers pKa of active site Tyr

Amino acid modifications

Modified residue

N-acetylalanine

Natural variations

Natural variant

N → S: dbSNP rs2229540.

VAR_048212

Experimental info

Mutagenesis

Y → F: Complete loss of enzymatic activity. Ref.7

Mutagenesis

Y → H: Complete loss of enzymatic activity. Ref.7

Mutagenesis

K → M: Complete loss of enzymatic activity. Ref.7

Mutagenesis

113

H → Q: Strong decrease in enzymatic activity. Ref.7

Mutagenesis

299

I → A: No change in enzymatic activity. Ref.7

Mutagenesis

299

I → C: No change in enzymatic activity. Ref.7

Mutagenesis

300

V → C: No change in enzymatic activity. Ref.7

Secondary structure

325

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P14550-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: F6B27517EB754E37
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FASTA

325

36,573

        10         20         30         40         50         60 
MAASCVLLHT GQKMPLIGLG TWKSEPGQVK AAVKYALSVG YRHIDCAAIY GNEPEIGEAL 

        70         80         90        100        110        120 
KEDVGPGKAV PREELFVTSK LWNTKHHPED VEPALRKTLA DLQLEYLDLY LMHWPYAFER 

       130        140        150        160        170        180 
GDNPFPKNAD GTICYDSTHY KETWKALEAL VAKGLVQALG LSNFNSRQID DILSVASVRP 

       190        200        210        220        230        240 
AVLQVECHPY LAQNELIAHC QARGLEVTAY SPLGSSDRAW RDPDEPVLLE EPVVLALAEK 

       250        260        270        280        290        300 
YGRSPAQILL RWQVQRKVIC IPKSITPSRI LQNIKVFDFT FSPEEMKQLN ALNKNWRYIV 

       310        320 
PMLTVDGKRV PRDAGHPLYP FNDPY

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases." Bohren K.M., Bullock B., Wermuth B., Gabbay K.H. J. Biol. Chem. 264:9547-9551(1989) [PubMed: 2498333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Liver.
[2]	"The structural organization of the human aldehyde reductase gene, AKR1A1, and mapping to chromosome 1p33-->p32." Fujii J., Hamaoka R., Matsumoto A., Fujii T., Yamaguchi Y., Egashira M., Miyoshi O., Niikawa N., Taniguchi N. Cytogenet. Cell Genet. 84:230-232(1999) [PubMed: 10393438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Characterization of the human aldehyde reductase gene and promoter." Barski O.A., Gabbay K.H., Bohren K.M. Genomics 60:188-198(1999) [PubMed: 10486210] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon and Kidney.
[6]	"Primary structure of aldehyde reductase from human liver." Wermuth B., Omar A., Forster A., di Francesco C., Wolf M., von Wartburg J.-P., Bullock B., Gabbay K.H. Prog. Clin. Biol. Res. 232:297-307(1987) [PubMed: 3615425] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-325. Tissue: Liver.
[7]	"Mechanism of human aldehyde reductase: characterization of the active site pocket." Barski O.A., Gabbay K.H., Grimshaw C.E., Bohren K.M. Biochemistry 34:11264-11275(1995) [PubMed: 7669785] [Abstract] Cited for: MUTAGENESIS OF TYR-50; LYS-80; HIS-113; ILE-299 AND VAL-300.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]	"Structures of human and porcine aldehyde reductase: an enzyme implicated in diabetic complications." El-Kabbani O., Green N.C., Lin G., Carson M., Narayana S.V.L., Moore K.M., Flynn T.G., DeLucas L.J. Acta Crystallogr. D 50:859-868(1994) [PubMed: 15299353] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

J04794 mRNA. Translation: AAA51711.1.
AF036683

AF036682 Genomic DNA. Translation: AAB92369.1.
AF112485, AF112484 Genomic DNA. Translation: AAF01260.1.
BT007003 mRNA. Translation: AAP35649.1.
BC000670 mRNA. Translation: AAH00670.1.
BC005394 mRNA. Translation: AAH05394.1.

IPI

IPI00220271.

PIR

A33851.

RefSeq

NP_006057.1.
NP_697021.1.

UniGene

Hs.654435

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ALR	X-ray	2.48	A	2-325	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P14550. 1 interaction.

PTM databases

PhosphoSite

P14550.

2-D gel databases

SWISS-2DPAGE

P14550.

REPRODUCTION-2DPAGE

IPI00220271.
P14550.

Proteomic databases

PeptideAtlas

P14550.

PRIDE

P14550.

Genome annotation databases

Ensembl

ENSG00000117448. Homo sapiens. [Contig view]

GeneID

10327.

KEGG

hsa:10327.

Organism-specific databases

GeneCards

GC01P045789.

H-InvDB

HIX0000534.

HGNC

HGNC:380. AKR1A1.

HPA

CAB006246.
HPA017919.

MIM

103830. gene.

PharmGKB

PA24674.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P14550.

HOVERGEN

P14550.

OMA

P14550. WRHPDEP.

Enzyme and pathway databases

BRENDA

1.1.1.2. 247.

Gene expression databases

ArrayExpress

P14550.

Bgee

P14550.

CleanEx

HS_AKR1A1.

GermOnline

ENSG00000117448. Homo sapiens.

Family and domain databases

InterPro

IPR001395. Aldo/ket_red.
IPR018170. Aldo/ket_reductase_CS.
[Graphical view]

Gene3D

G3DSA:3.20.20.100. Aldo/ket_red. 1 hit.

PANTHER

PTHR11732. Aldo/ket_red. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

ProDom

PD000288. Aldo/ket_red. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

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

ProtoNet

Search...

Other Resources

NextBio

39151.

SOURCE

Search...

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Entry information

Entry name

AK1A1_HUMAN

Accession

Primary (citable) accession number: P14550

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 103 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents