ID   IDH3A_HUMAN             Reviewed;         366 AA.
AC   P50213; Q9H3X0;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-DEC-2008, entry version 84.
DE   RecName: Full=Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial;
DE            EC=1.1.1.41;
DE   AltName: Full=Isocitric dehydrogenase;
DE   AltName: Full=NAD(+)-specific ICDH;
DE   Flags: Precursor;
GN   Name=IDH3A;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
RX   MEDLINE=95275260; PubMed=7755589;
RA   Kim Y.O., Oh I.U., Park H.S., Jeng J., Song B.J., Huh T.L.;
RT   "Characterization of a cDNA clone for human NAD(+)-specific isocitrate
RT   dehydrogenase alpha-subunit and structural comparison with its
RT   isoenzymes from different species.";
RL   Biochem. J. 308:63-68(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 135-146 AND 179-188, AND MASS SPECTROMETRY.
RC   TISSUE=Brain, and Cajal-Retzius cell;
RA   Lubec G., Vishwanath V.;
RL   Submitted (MAR-2007) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) +
CC       NADH.
CC   -!- COFACTOR: Binds 1 magnesium or manganese ion per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Heterooligomer of subunits alpha, beta, and gamma in the
CC       apparent ratio of 2:1:1 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P50213-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P50213-2; Sequence=VSP_014516;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; U07681; AAA85639.1; -; mRNA.
DR   EMBL; AL442090; CAC09449.1; -; mRNA.
DR   EMBL; BC021967; AAH21967.1; -; mRNA.
DR   PIR; S55282; S55282.
DR   RefSeq; NP_005521.1; -.
DR   UniGene; Hs.591110; -.
DR   HSSP; P08200; 1ISO.
DR   IntAct; P50213; 6.
DR   PhosphoSite; P50213; -.
DR   OGP; P50213; -.
DR   REPRODUCTION-2DPAGE; IPI00030702; -.
DR   PRIDE; P50213; -.
DR   Ensembl; ENSG00000166411; Homo sapiens.
DR   GeneID; 3419; -.
DR   KEGG; hsa:3419; -.
DR   NMPDR; fig|9606.3.peg.11057; -.
DR   GeneCards; GC15P076228; -.
DR   HGNC; HGNC:5384; IDH3A.
DR   MIM; 601149; gene.
DR   PharmGKB; PA29632; -.
DR   HOGENOM; P50213; -.
DR   HOVERGEN; P50213; -.
DR   Reactome; REACT_1046; Pyruvate metabolism and TCA cycle.
DR   DrugBank; DB00157; NADH.
DR   NextBio; 13478; -.
DR   ArrayExpress; P50213; -.
DR   CleanEx; HS_IDH3A; -.
DR   GermOnline; ENSG00000166411; Homo sapiens.
DR   GO; GO:0005759; C:mitochondrial matrix; EXP:Reactome.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   InterPro; IPR004434; IsoCit_DHase_NAD_mit.
DR   InterPro; IPR001804; IsoCit_IM_DHase.
DR   Gene3D; G3DSA:3.40.718.10; IDH_IMDH; 1.
DR   PANTHER; PTHR11835; IDH_IMDH_dimeric; 1.
DR   Pfam; PF00180; Iso_dh; 1.
DR   TIGRFAMs; TIGR00175; mito_nad_idh; 1.
DR   PROSITE; PS00470; IDH_IMDH; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Direct protein sequencing; Magnesium; Manganese;
KW   Metal-binding; Mitochondrion; NAD; Oxidoreductase; Transit peptide;
KW   Tricarboxylic acid cycle.
FT   TRANSIT       1     27       Mitochondrion (By similarity).
FT   CHAIN        28    366       Isocitrate dehydrogenase [NAD] subunit
FT                                alpha, mitochondrial.
FT                                /FTId=PRO_0000014436.
FT   METAL       233    233       Magnesium or manganese (By similarity).
FT   METAL       257    257       Magnesium or manganese (By similarity).
FT   METAL       261    261       Magnesium or manganese (By similarity).
FT   BINDING     115    115       Substrate (By similarity).
FT   BINDING     125    125       Substrate (By similarity).
FT   BINDING     146    146       Substrate (By similarity).
FT   BINDING     233    233       Substrate (By similarity).
FT   SITE        153    153       Critical for catalysis (By similarity).
FT   SITE        200    200       Critical for catalysis (By similarity).
FT   VAR_SEQ       1     78       Missing (in isoform 2).
FT                                /FTId=VSP_014516.
SQ   SEQUENCE   366 AA;  39592 MW;  695F6A34F97430CF CRC64;
     MAGPAWISKV SRLLGAFHNP KQVTRGFTGG VQTVTLIPGD GIGPEISAAV MKIFDAAKAP
     IQWEERNVTA IQGPGGKWMI PSEAKESMDK NKMGLKGPLK TPIAAGHPSM NLLLRKTFDL
     YANVRPCVSI EGYKTPYTDV NIVTIRENTE GEYSGIEHVI VDGVVQSIKL ITEGASKRIA
     EFAFEYARNN HRSNVTAVHK ANIMRMSDGL FLQKCREVAE SCKDIKFNEM YLDTVCLNMV
     QDPSQFDVLV MPNLYGDILS DLCAGLIGGL GVTPSGNIGA NGVAIFESVH GTAPDIAGKD
     MANPTALLLS AVMMLRHMGL FDHAARIEAA CFATIKDGKS LTKDLGGNAK CSDFTEEICR
     RVKDLD
//