LOCUS NP_004126 393 aa linear PRI 22-OCT-2008
DEFINITION isocitrate dehydrogenase 3 (NAD+) gamma isoform a precursor [Homo
sapiens].
ACCESSION NP_004126
VERSION NP_004126.1 GI:4758582
DBSOURCE REFSEQ: accession NM_004135.2
KEYWORDS .
SOURCE Homo sapiens (human)
ORGANISM Homo sapiens
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
REFERENCE 1 (residues 1 to 393)
AUTHORS Barbe,L., Lundberg,E., Oksvold,P., Stenius,A., Lewin,E.,
Bjorling,E., Asplund,A., Ponten,F., Brismar,H., Uhlen,M. and
Andersson-Svahn,H.
TITLE Toward a confocal subcellular atlas of the human proteome
JOURNAL Mol. Cell Proteomics 7 (3), 499-508 (2008)
PUBMED 18029348
REFERENCE 2 (residues 1 to 393)
AUTHORS Bzymek,K.P. and Colman,R.F.
TITLE Role of alpha-Asp181, beta-Asp192, and gamma-Asp190 in the
distinctive subunits of human NAD-specific isocitrate dehydrogenase
JOURNAL Biochemistry 46 (18), 5391-5397 (2007)
PUBMED 17432878
REMARK GeneRIF: Aspartate-190 is a determinant of IDH gamma subunit
affinity for the manganese (MnII) ion, as well as for
nicotinamide-adenine dinucleotide (NAD), but is not directly
required for the catalytic reaction.
REFERENCE 3 (residues 1 to 393)
AUTHORS Soundar,S., O'hagan,M., Fomulu,K.S. and Colman,R.F.
TITLE Identification of Mn2+-binding aspartates from alpha, beta, and
gamma subunits of human NAD-dependent isocitrate dehydrogenase
JOURNAL J. Biol. Chem. 281 (30), 21073-21081 (2006)
PUBMED 16737955
REMARK GeneRIF: active sites of the human NAD-IDH are shared between alpha
and gamma subunits and between alpha and beta subunits
REFERENCE 4 (residues 1 to 393)
AUTHORS Soundar,S., Park,J.H., Huh,T.L. and Colman,R.F.
TITLE Evaluation by mutagenesis of the importance of 3 arginines in
alpha, beta, and gamma subunits of human NAD-dependent isocitrate
dehydrogenase
JOURNAL J. Biol. Chem. 278 (52), 52146-52153 (2003)
PUBMED 14555658
REFERENCE 5 (residues 1 to 393)
AUTHORS Simpson,J.C., Wellenreuther,R., Poustka,A., Pepperkok,R. and
Wiemann,S.
TITLE Systematic subcellular localization of novel proteins identified by
large-scale cDNA sequencing
JOURNAL EMBO Rep. 1 (3), 287-292 (2000)
PUBMED 11256614
REFERENCE 6 (residues 1 to 393)
AUTHORS Weiss,C., Zeng,Y., Huang,J., Sobocka,M.B. and Rushbrook,J.I.
TITLE Bovine NAD+-dependent isocitrate dehydrogenase: alternative
splicing and tissue-dependent expression of subunit 1
JOURNAL Biochemistry 39 (7), 1807-1816 (2000)
PUBMED 10677231
REFERENCE 7 (residues 1 to 393)
AUTHORS Kim,Y.O., Koh,H.J., Kim,S.H., Jo,S.H., Huh,J.W., Jeong,K.S.,
Lee,I.J., Song,B.J. and Huh,T.L.
TITLE Identification and functional characterization of a novel,
tissue-specific NAD(+)-dependent isocitrate dehydrogenase beta
subunit isoform
JOURNAL J. Biol. Chem. 274 (52), 36866-36875 (1999)
PUBMED 10601238
REFERENCE 8 (residues 1 to 393)
AUTHORS Brenner,V., Nyakatura,G., Rosenthal,A. and Platzer,M.
TITLE Genomic organization of two novel genes on human Xq28: compact head
to head arrangement of IDH gamma and TRAP delta is conserved in rat
and mouse
JOURNAL Genomics 44 (1), 8-14 (1997)
PUBMED 9286695
REFERENCE 9 (residues 1 to 393)
AUTHORS Sandoval,N., Bauer,D., Brenner,V., Coy,J.F., Drescher,B.,
Kioschis,P., Korn,B., Nyakatura,G., Poustka,A., Reichwald,K.,
Rosenthal,A. and Platzer,M.
TITLE The genomic organization of a human creatine transporter (CRTR)
gene located in Xq28
JOURNAL Genomics 35 (2), 383-385 (1996)
PUBMED 8661155
COMMENT REVIEWED REFSEQ: This record has been curated by NCBI staff. The
reference sequence was derived from U40272.1.
Summary: Isocitrate dehydrogenases catalyze the oxidative
decarboxylation of isocitrate to 2-oxoglutarate. These enzymes
belong to two distinct subclasses, one of which utilizes NAD(+) as
the electron acceptor and the other NADP(+). Five isocitrate
dehydrogenases have been reported: three NAD(+)-dependent
isocitrate dehydrogenases, which localize to the mitochondrial
matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of
which is mitochondrial and the other predominantly cytosolic.
NAD(+)-dependent isocitrate dehydrogenases catalyze the
allosterically regulated rate-limiting step of the tricarboxylic
acid cycle. Each isozyme is a heterotetramer that is composed of
two alpha subunits, one beta subunit, and one gamma subunit. The
protein encoded by this gene is the gamma subunit of one isozyme of
NAD(+)-dependent isocitrate dehydrogenase. This gene is a candidate
gene for periventricular heterotopia. Several alternatively spliced
transcript variants of this gene have been described, but only some
of their full length natures have been determined. [provided by
RefSeq].
Transcript Variant: This variant (1) encodes the longer isoform
(a).
FEATURES Location/Qualifiers
source 1..393
/organism="Homo sapiens"
/db_xref="taxon:9606"
/chromosome="X"
/map="Xq28"
Protein 1..393
/product="isocitrate dehydrogenase 3 (NAD+) gamma isoform
a precursor"
/EC_number="1.1.1.41"
/note="isocitric dehydrogenase; IDH-gamma; isocitrate
dehydrogenase, NAD(+)-specific, mitochondrial, gamma
subunit; NAD+-specific ICDH; NAD (H)-specific isocitrate
dehydrogenase gamma subunit"
transit_peptide 1..39
/calculated_mol_wt=3998
mat_peptide 40..393
/product="isocitrate dehydrogenase 3 (NAD+) gamma isoform
a"
/calculated_mol_wt=38815
CDS 1..393
/gene="IDH3G"
/gene_synonym="H-IDHG"
/coded_by="NM_004135.2:187..1368"
/note="isoform a precursor is encoded by transcript
variant 1"
/db_xref="CCDS:CCDS14730.1"
/db_xref="GeneID:3421"
/db_xref="HGNC:5386"
/db_xref="HPRD:02100"
/db_xref="MIM:300089"
ORIGIN
1 malkvatvag saakavlgpa llcrpwevlg ahevpsrnif seqtippsak yggrhtvtmi
61 pgdgigpelm lhvksvfrha cvpvdfeevh vssnadeedi rnaimairrn rvalkgniet
121 nhnlppshks rnnilrtsld lyanvihcks lpgvvtrhkd idilivrent egeysslehe
181 svagvveslk iitkakslri aeyafklaqe sgrkkvtavh kanimklgdg lflqccreva
241 arypqitfen mivdnttmql vsrpqqfdvm vmpnlygniv nnvcaglvgg pglvaganyg
301 hvyavfetat rntgksiank nianptatll ascmmldhlk lhsyatsirk avlasmdnen
361 mhtpdiggqg ttseaiqdvi rhirvingra vea
//