O88844 (IDHC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Isocitrate dehydrogenase [NADP] cytoplasmic
Short name=IDH
EC=1.1.1.42

Alternative name(s):
Cytosolic NADP-isocitrate dehydrogenase
IDP
NADP(+)-specific ICDH
Oxalosuccinate decarboxylase

Gene names

Name:

Idh1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	414 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.
Cofactor	Binds 1 magnesium or manganese ion per subunit By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the isocitrate and isopropylmalate dehydrogenases family.

Ontologies

Keywords
Biological process	Glyoxylate bypass Tricarboxylic acid cycle
Cellular component	Cytoplasm
Ligand	Magnesium Manganese Metal-binding NADP
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	2-oxoglutarate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB female gonad development Inferred from electronic annotation. Source: Compara glutathione metabolic process Inferred from mutant phenotype PubMed 12031902. Source: MGI glyoxylate cycle Inferred from electronic annotation. Source: UniProtKB-KW isocitrate metabolic process Inferred from sequence or structural similarity. Source: UniProtKB response to oxidative stress Inferred from direct assay PubMed 12031902. Source: MGI response to steroid hormone stimulus Inferred from electronic annotation. Source: Compara tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay PubMed 12031902. Source: MGI mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI peroxisome Inferred from electronic annotation. Source: Compara
Molecular_function	NAD binding Inferred from electronic annotation. Source: InterPro NADP binding Inferred from electronic annotation. Source: Compara isocitrate dehydrogenase (NADP+) activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 414

414

Isocitrate dehydrogenase [NADP] cytoplasmic

PRO_0000083578

Regions

Nucleotide binding

75 – 77

3

NADP By similarity

Nucleotide binding

310 – 315

6

NADP By similarity

Region

94 – 100

7

Substrate binding By similarity

Sites

Metal binding

252

1

Magnesium or manganese By similarity

Metal binding

275

1

Magnesium or manganese By similarity

Binding site

77

1

Substrate By similarity

Binding site

82

1

NADP By similarity

Binding site

109

1

Substrate By similarity

Binding site

132

1

Substrate By similarity

Binding site

260

1

NADP By similarity

Binding site

328

1

NADP; via amide nitrogen and carbonyl oxygen By similarity

Site

139

1

Critical for catalysis By similarity

Site

212

1

Critical for catalysis By similarity

Amino acid modifications

Modified residue

321

1

N6-acetyllysine By similarity

Experimental info

Sequence conflict

243

1

K → N in AAD02919. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

414

Helix Strand Turn

Details...

Beta strand

5 – 14

10

Helix

17 – 30

14

Turn

31 – 34

4

Beta strand

35 – 43

9

Helix

46 – 51

6

Turn

52 – 54

3

Helix

55 – 67

13

Beta strand

68 – 72

5

Helix

80 – 86

7

Helix

95 – 103

9

Beta strand

106 – 111

6

Beta strand

128 – 133

6

Helix

137 – 140

4

Beta strand

142 – 146

5

Beta strand

148 – 162

15

Beta strand

165 – 172

8

Beta strand

177 – 185

9

Helix

186 – 203

18

Beta strand

207 – 211

5

Turn

213 – 215

3

Helix

219 – 234

16

Helix

236 – 241

6

Beta strand

246 – 250

5

Helix

251 – 260

10

Beta strand

265 – 269

5

Helix

271 – 285

15

Beta strand

290 – 296

7

Beta strand

303 – 306

4

Helix

313 – 320

8

Helix

330 – 347

18

Helix

350 – 368

19

Helix

374 – 381

8

Helix

383 – 385

3

Helix

388 – 390

3

Helix

394 – 412

19

Sequences

	Sequence		Length	Mass (Da)
	O88844 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: C7FEF315D042C44C	FASTA	414	46,674
	10 20 30 40 50 60 MSRKIQGGSV VEMQGDEMTR IIWELIKEKL ILPYVELDLH SYDLGIENRD ATNDQVTKDA 70 80 90 100 110 120 AEAIKKYNVG VKCATITPDE KRVEEFKLKQ MWKSPNGTIR NILGGTVFRE AIICKNIPRL 130 140 150 160 170 180 VTGWVKPIII GRHAYGDQYR ATDFVVPGPG KVEITYTPKD GTQKVTYMVH DFEEGGGVAM 190 200 210 220 230 240 GMYNQDKSIE DFAHSSFQMA LSKGWPLYLS TKNTILKKYD GRFKDIFQEI YDKKYKSQFE 250 260 270 280 290 300 AQKICYEHRL IDDMVAQAMK SEGGFIWACK NYDGDVQSDS VAQGYGSLGM MTSVLICPDG 310 320 330 340 350 360 KTVEAEAAHG TVTRHYRMYQ KGQETSTNPI ASIFAWSRGL AHRAKLDNNT ELSFFAKALE 370 380 390 400 410 DVCIETIEAG FMTKDLAACI KGLPNVQRSD YLNTFEFMDK LGENLKAKLA QAKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cytosolic isocitrate dehydrogenase in humans, mice, and voles and phylogenetic analysis of the enzyme family." Nekrutenko A., Hillis D.M., Patton J.C., Bradley R.D., Baker R.J. Mol. Biol. Evol. 15:1674-1684(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Bone marrow, Embryo and Sympathetic ganglion.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Lubec G., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 30-49. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF020039 mRNA. Translation: AAD02919.1.
AK149019 mRNA. Translation: BAE28720.1.
AK151212 mRNA. Translation: BAE30207.1.
AK159173 mRNA. Translation: BAE34873.1.
AK160896 mRNA. Translation: BAE36075.1.
AK167158 mRNA. Translation: BAE39299.1.
CH466548 Genomic DNA. Translation: EDL00223.1.
CH466548 Genomic DNA. Translation: EDL00225.1.

IPI

IPI00762452.

RefSeq

NP_001104790.1. NM_001111320.1.
NP_034627.3. NM_010497.3.

UniGene

Mm.9925.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CMJ	X-ray	1.99	A/B	4-413	[»]
2CMV	X-ray	2.52	A/B	4-413	[»]

ProteinModelPortal

O88844.

SMR

O88844. Positions 4-413.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-1859161.

PTM databases

PhosphoSite

O88844.

2D gel databases

COMPLUYEAST-2DPAGE

O88844.

REPRODUCTION-2DPAGE

O88844.

SWISS-2DPAGE

O88844.

Proteomic databases

PaxDb

O88844.

PRIDE

O88844.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000097709; ENSMUSP00000095316; ENSMUSG00000025950.
ENSMUST00000169032; ENSMUSP00000127307; ENSMUSG00000025950.

GeneID

15926.

KEGG

mmu:15926.

UCSC

uc007bhn.2. mouse.

Organism-specific databases

CTD

3417.

MGI

MGI:96413. Idh1.

Phylogenomic databases

eggNOG

COG0538.

GeneTree

ENSGT00390000012547.

HOGENOM

HOG000019858.

HOVERGEN

HBG006119.

KO

K00031.

OMA

ALGMFNT.

OrthoDB

EOG47M1Z0.

Gene expression databases

ArrayExpress

O88844.

Bgee

O88844.

CleanEx

MM_IDH1.

Genevestigator

O88844.

GermOnline

ENSMUSG00000025950. Mus musculus.

Family and domain databases

Gene3D

3.40.718.10. 1 hit.

InterPro

IPR019818. IsoCit/isopropylmalate_DH_CS.
IPR004790. Isocitrate_DH_NADP.
IPR024084. IsoPropMal-DH-like_dom.
[Graphical view]

PANTHER

PTHR11822. PTHR11822. 1 hit.

Pfam

PF00180. Iso_dh. 1 hit.
[Graphical view]

PIRSF

PIRSF000108. IDH_NADP. 1 hit.

TIGRFAMs

TIGR00127. nadp_idh_euk. 1 hit.

PROSITE

PS00470. IDH_IMDH. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O88844.

NextBio

288640.

SOURCE

Search...

Entry information

Entry name

IDHC_MOUSE

Accession

Primary (citable) accession number: O88844
Secondary accession number(s): Q3UAV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	July 27, 2011
Last modified:	May 29, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program