ID   IDH3A_MOUSE             Reviewed;         366 AA.
AC   Q9D6R2; Q3UAM8; Q8C8A1; Q9D1L1;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   16-JUN-2009, entry version 71.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and DBA/2;
RC   TISSUE=Bone marrow, Heart, Tongue, Visual cortex, and Wolffian duct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=FVB/N; TISSUE=Liver;
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   [3]
RP   PROTEIN SEQUENCE OF 59-85; 101-188; 206-214 AND 300-336, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B.,
RA   Chen W.-Q.;
RL   Submitted (JAN-2009) 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 (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9D6R2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D6R2-2; Sequence=VSP_014517;
CC   -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate
CC       dehydrogenases family.
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DR   EMBL; AK003393; BAB22760.1; -; mRNA.
DR   EMBL; AK010065; BAB26679.1; -; mRNA.
DR   EMBL; AK032787; BAC28021.1; -; mRNA.
DR   EMBL; AK047951; BAC33199.1; -; mRNA.
DR   EMBL; AK150618; BAE29708.1; -; mRNA.
DR   EMBL; AK151304; BAE30286.1; -; mRNA.
DR   EMBL; AK152353; BAE31145.1; -; mRNA.
DR   EMBL; AK153459; BAE32011.1; -; mRNA.
DR   EMBL; AK158646; BAE34596.1; -; mRNA.
DR   EMBL; AK159051; BAE34785.1; -; mRNA.
DR   EMBL; AK168049; BAE40031.1; -; mRNA.
DR   EMBL; AK168149; BAE40114.1; -; mRNA.
DR   EMBL; AK169152; BAE40931.1; -; mRNA.
DR   EMBL; BC034273; AAH34273.1; -; mRNA.
DR   EMBL; BC049956; AAH49956.1; -; mRNA.
DR   IPI; IPI00459725; -.
DR   IPI; IPI00608078; -.
DR   RefSeq; NP_083849.1; -.
DR   UniGene; Mm.279195; -.
DR   HSSP; P08200; 1ISO.
DR   PhosphoSite; Q9D6R2; -.
DR   REPRODUCTION-2DPAGE; Q9D6R2; -.
DR   PRIDE; Q9D6R2; -.
DR   Ensembl; ENSMUSG00000032279; Mus musculus.
DR   GeneID; 67834; -.
DR   KEGG; mmu:67834; -.
DR   NMPDR; fig|10090.3.peg.20219; -.
DR   MGI; MGI:1915084; Idh3a.
DR   HOGENOM; Q9D6R2; -.
DR   HOVERGEN; Q9D6R2; -.
DR   OMA; Q9D6R2; GGNSKCS.
DR   BRENDA; 1.1.1.41; 244.
DR   NextBio; 325657; -.
DR   Bgee; Q9D6R2; -.
DR   CleanEx; MM_IDH3A; -.
DR   GermOnline; ENSMUSG00000032279; Mus musculus.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0004449; F:isocitrate dehydrogenase (NAD+) activity; IEA:EC.
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:0051287; F:NAD or NADH binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS.
DR   InterPro; IPR001804; Isocitrate/isopropylmalate_DH.
DR   InterPro; IPR004434; Isocitrate_DH_NAD_mit.
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_0000014438.
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_014517.
FT   CONFLICT    306    306       A -> T (in Ref. 1; BAC33199).
SQ   SEQUENCE   366 AA;  39639 MW;  9F1D68C269376955 CRC64;
     MAGSAWVSKV SRLLGAFHNT KQVTRGFAGG VQTVTLIPGD GIGPEISASV MKIFDAAKAP
     IQWEERNVTA IQGPGGKWMI PPEAKESMDK NKMGLKGPLK TPIAAGHPSM NLLLRKTFDL
     YANVRPCVSI EGYKTPYTDV NIVTIRENTE GEYSGIEHVI VDGVVQSIKL ITEEASKRIA
     EFAFEYARNN HRSNVTAVHK ANIMRMSDGL FLQKCREVAE NCKDIKFNEM YLDTVCLNMV
     QDPSQFDVLV MPNLYGDILS DLCAGLIGGL GVTPSGNIGA NGVAIFESVH GTAPDIAGKD
     MANPTALLLS AVMMLRHMGL FDHAAKIEAA CFATIKDGKS LTKDLGGNAK CSDFTEEICR
     RVKDLD
//