GenomeNet

Database: UniProt
Entry: ODO1_MOUSE
LinkDB: ODO1_MOUSE
Original site: ODO1_MOUSE 
ID   ODO1_MOUSE              Reviewed;        1023 AA.
AC   Q60597; Q3UDM7; Q5DTI4; Q5SVX7; Q5SVX9; Q6PFZ2; Q80Y57; Q8K0K7;
AC   Q8K2Z3; Q8R3M2; Q91WP2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 3.
DT   10-OCT-2018, entry version 170.
DE   RecName: Full=2-oxoglutarate dehydrogenase, mitochondrial;
DE            EC=1.2.4.2 {ECO:0000250|UniProtKB:Q02218};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E1;
DE            Short=OGDC-E1;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
DE   Flags: Precursor;
GN   Name=Ogdh; Synonyms=Kiaa4192;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
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] (ISOFORM 3).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene.
RT   The complete nucleotide sequences of mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC   STRAIN=C57BL/6J, and FVB/N;
RC   TISSUE=Brain, Colon, Mammary tumor, and Salivary gland;
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   [5]
RP   PROTEIN SEQUENCE OF 123-135; 185-204; 311-319; 561-568; 616-633 AND
RP   916-925, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 829-958 (ISOFORMS 1/2/3/4).
RC   STRAIN=BALB/cJ;
RX   PubMed=8248240; DOI=10.1073/pnas.90.23.11272;
RA   Udaka K., Tsomides T.J., Walden P., Fukusen N., Eisen H.N.;
RT   "A ubiquitous protein is the source of naturally occurring peptides
RT   that are recognized by a CD8+ T-cell clone.";
RL   Proc. Natl. Acad. Sci. U.S.A. 90:11272-11276(1993).
RN   [7]
RP   PROTEIN SEQUENCE OF 933-939.
RX   PubMed=1606619; DOI=10.1016/0092-8674(92)90617-L;
RA   Udaka K., Tsomides T.J., Eisen H.N.;
RT   "A naturally occurring peptide recognized by alloreactive CD8+
RT   cytotoxic T lymphocytes in association with a class I MHC protein.";
RL   Cell 69:989-998(1992).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
RC   Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-74 AND LYS-564, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
RA   Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-401, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J.,
RA   Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in
RT   mitochondria identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC   -!- FUNCTION: 2-oxoglutarate dehydrogenase (E1) component of the 2-
CC       oxoglutarate dehydrogenase complex, which mediates the
CC       decarboxylation of alpha-ketoglutarate. The 2-oxoglutarate
CC       dehydrogenase complex catalyzes the overall conversion of 2-
CC       oxoglutarate to succinyl-CoA and CO(2). The 2-oxoglutarate
CC       dehydrogenase complex is mainly active in the mitochondrion. A
CC       fraction of the 2-oxoglutarate dehydrogenase complex also
CC       localizes in the nucleus and is required for lysine succinylation
CC       of histones: associates with KAT2A on chromatin and provides
CC       succinyl-CoA to histone succinyltransferase KAT2A.
CC       {ECO:0000250|UniProtKB:Q02218}.
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC       succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC       {ECO:0000250|UniProtKB:Q02218}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:Q02218};
CC   -!- ACTIVITY REGULATION: Calcium ions and ADP stimulate, whereas ATP
CC       and NADH reduce catalytic activity.
CC       {ECO:0000250|UniProtKB:Q02218}.
CC   -!- SUBUNIT: The 2-oxoglutarate dehydrogenase complex is composed of
CC       OGDH (2-oxoglutarate dehydrogenase; E1), DLST (dihydrolipoamide
CC       succinyltransferase; E2) and DLD (dihydrolipoamide dehydrogenase;
CC       E3). It contains multiple copies of the three enzymatic components
CC       (E1, E2 and E3). In the nucleus, the The 2-oxoglutarate
CC       dehydrogenase complex associates with KAT2A.
CC       {ECO:0000250|UniProtKB:Q02218}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q02218}. Nucleus
CC       {ECO:0000250|UniProtKB:Q02218}. Note=Mainly localizes in the
CC       mitochondrion. A small fraction localizes to the nucleus, where
CC       the 2-oxoglutarate dehydrogenase complex is required for histone
CC       succinylation. {ECO:0000250|UniProtKB:Q02218}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q60597-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q60597-2; Sequence=VSP_024799;
CC       Name=3;
CC         IsoId=Q60597-3; Sequence=VSP_024801;
CC         Note=No experimental confirmation available.;
CC       Name=4;
CC         IsoId=Q60597-4; Sequence=VSP_024800;
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH31165.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAD90530.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AK147289; BAE27824.1; -; mRNA.
DR   EMBL; AK150009; BAE29234.1; -; mRNA.
DR   EMBL; AK169286; BAE41044.1; -; mRNA.
DR   EMBL; AK220536; BAD90530.1; ALT_INIT; mRNA.
DR   EMBL; AL607152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC025040; AAH25040.1; -; mRNA.
DR   EMBL; BC013670; AAH13670.1; -; mRNA.
DR   EMBL; BC029143; AAH29143.1; -; mRNA.
DR   EMBL; BC031165; AAH31165.1; ALT_INIT; mRNA.
DR   EMBL; BC049104; AAH49104.1; -; mRNA.
DR   EMBL; BC057354; AAH57354.1; -; mRNA.
DR   EMBL; U02971; AAC52130.1; -; mRNA.
DR   CCDS; CCDS36106.1; -. [Q60597-1]
DR   CCDS; CCDS56758.1; -. [Q60597-4]
DR   PIR; I48884; A41911.
DR   RefSeq; NP_001239211.1; NM_001252282.1. [Q60597-3]
DR   RefSeq; NP_001239212.1; NM_001252283.1. [Q60597-4]
DR   RefSeq; NP_001239216.1; NM_001252287.1. [Q60597-1]
DR   RefSeq; NP_001239217.1; NM_001252288.1.
DR   RefSeq; NP_035086.2; NM_010956.4. [Q60597-1]
DR   RefSeq; XP_006514645.1; XM_006514582.2. [Q60597-4]
DR   RefSeq; XP_006514646.1; XM_006514583.3.
DR   RefSeq; XP_006514647.1; XM_006514584.3. [Q60597-4]
DR   RefSeq; XP_006514648.1; XM_006514585.2.
DR   RefSeq; XP_017169826.1; XM_017314337.1.
DR   UniGene; Mm.276348; -.
DR   UniGene; Mm.479411; -.
DR   UniGene; Mm.490272; -.
DR   PDB; 3E2H; X-ray; 3.80 A; Q=932-940.
DR   PDB; 3TF7; X-ray; 2.75 A; B/F=932-940.
DR   PDBsum; 3E2H; -.
DR   PDBsum; 3TF7; -.
DR   ProteinModelPortal; Q60597; -.
DR   SMR; Q60597; -.
DR   BioGrid; 201905; 4.
DR   IntAct; Q60597; 11.
DR   MINT; Q60597; -.
DR   STRING; 10090.ENSMUSP00000091041; -.
DR   ChEMBL; CHEMBL2176831; -.
DR   iPTMnet; Q60597; -.
DR   PhosphoSitePlus; Q60597; -.
DR   SwissPalm; Q60597; -.
DR   REPRODUCTION-2DPAGE; Q60597; -.
DR   EPD; Q60597; -.
DR   PaxDb; Q60597; -.
DR   PeptideAtlas; Q60597; -.
DR   PRIDE; Q60597; -.
DR   Ensembl; ENSMUST00000003461; ENSMUSP00000003461; ENSMUSG00000020456. [Q60597-1]
DR   Ensembl; ENSMUST00000093350; ENSMUSP00000091041; ENSMUSG00000020456. [Q60597-4]
DR   Ensembl; ENSMUST00000101554; ENSMUSP00000099090; ENSMUSG00000020456. [Q60597-1]
DR   GeneID; 18293; -.
DR   KEGG; mmu:18293; -.
DR   UCSC; uc007hyf.2; mouse. [Q60597-1]
DR   UCSC; uc007hyg.2; mouse. [Q60597-3]
DR   UCSC; uc007hyh.2; mouse. [Q60597-4]
DR   CTD; 4967; -.
DR   MGI; MGI:1098267; Ogdh.
DR   eggNOG; KOG0450; Eukaryota.
DR   eggNOG; COG0567; LUCA.
DR   GeneTree; ENSGT00530000063092; -.
DR   HOVERGEN; HBG001892; -.
DR   InParanoid; Q60597; -.
DR   KO; K00164; -.
DR   OMA; IDMVCYR; -.
DR   OrthoDB; EOG091G025G; -.
DR   PhylomeDB; Q60597; -.
DR   TreeFam; TF300695; -.
DR   Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR   Reactome; R-MMU-71064; Lysine catabolism.
DR   Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR   ChiTaRS; Ogdh; mouse.
DR   PRO; PR:Q60597; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000020456; Expressed in 326 organ(s), highest expression level in heart.
DR   CleanEx; MM_OGDH; -.
DR   ExpressionAtlas; Q60597; baseline and differential.
DR   Genevisible; Q60597; MM.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; ISS:UniProtKB.
DR   GO; GO:0051087; F:chaperone binding; ISO:MGI.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0034602; F:oxoglutarate dehydrogenase (NAD+) activity; IDA:MGI.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; ISS:UniProtKB.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; ISS:UniProtKB.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR   GO; GO:0021695; P:cerebellar cortex development; IEP:UniProtKB.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; ISS:UniProtKB.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0021766; P:hippocampus development; IEP:UniProtKB.
DR   GO; GO:0106077; P:histone succinylation; ISS:UniProtKB.
DR   GO; GO:0006734; P:NADH metabolic process; ISO:MGI.
DR   GO; GO:0061034; P:olfactory bulb mitral cell layer development; IEP:UniProtKB.
DR   GO; GO:0021860; P:pyramidal neuron development; IEP:UniProtKB.
DR   GO; GO:0021756; P:striatum development; IEP:UniProtKB.
DR   GO; GO:0006104; P:succinyl-CoA metabolic process; ISS:UniProtKB.
DR   GO; GO:0022028; P:tangential migration from the subventricular zone to the olfactory bulb; IEP:UniProtKB.
DR   GO; GO:0021794; P:thalamus development; IEP:UniProtKB.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISO:MGI.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; PTHR23152; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Calcium;
KW   Complete proteome; Direct protein sequencing; Glycolysis;
KW   Isopeptide bond; Metal-binding; Mitochondrion; Nucleus;
KW   Oxidoreductase; Phosphoprotein; Reference proteome;
KW   Thiamine pyrophosphate; Transit peptide; Ubl conjugation.
FT   TRANSIT       1     40       Mitochondrion. {ECO:0000255}.
FT   CHAIN        41   1023       2-oxoglutarate dehydrogenase,
FT                                mitochondrial.
FT                                /FTId=PRO_0000020434.
FT   CA_BIND     154    158       {ECO:0000250|UniProtKB:Q02218}.
FT   REGION      933    939       Recognized by alloreactive CD8 cytotoxic
FT                                T-lymphocytes in association with a class
FT                                I MHC protein.
FT   METAL       154    154       Calcium. {ECO:0000250|UniProtKB:Q02218}.
FT   MOD_RES      74     74       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     100    100       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     401    401       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23576753}.
FT   MOD_RES     564    564       N6-succinyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   MOD_RES     970    970       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q02218}.
FT   CROSSLNK    534    534       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin).
FT                                {ECO:0000250|UniProtKB:Q02218}.
FT   VAR_SEQ     139    172       IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRG
FT                                HHIAKSCVNFDDAPVTVSSNV (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_024799.
FT   VAR_SEQ     139    172       IRGHHVAQLDPLGILDADLDSSVPADIISSTDKL -> VRG
FT                                HHIAKLDPLGISCVNFDDAPVTVSSNVDLAVFKERLRMLTV
FT                                G (in isoform 4).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_024800.
FT   VAR_SEQ     172    172       L -> LDLAVFKERLRMLTVG (in isoform 3).
FT                                {ECO:0000303|Ref.2}.
FT                                /FTId=VSP_024801.
FT   CONFLICT    416    416       G -> V (in Ref. 4; AAH49104).
FT                                {ECO:0000305}.
FT   CONFLICT    549    549       V -> F (in Ref. 4; AAH49104).
FT                                {ECO:0000305}.
FT   CONFLICT    552    552       Q -> E (in Ref. 4; AAH57354).
FT                                {ECO:0000305}.
FT   CONFLICT    576    576       E -> K (in Ref. 1; BAE29234).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1023 AA;  116449 MW;  A0F3F8D36C7A76BC CRC64;
     MFHLRTCAAK LRPLTASQTV KTFSQNKPAA IRTFQQIRCY SAPVAAEPFL SGTSSNYVEE
     MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLSLS RSSLATMAHA QSLVEAQPNV
     DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLHES
     DLDKVFHLPT TTFIGGQEPA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET
     PGIMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDMSSAN
     GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDMKYH LGMYHRRINR
     VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV
     YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP
     EAVMYVCKVA AEWRNTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY
     AELLVSQGVV NQPEYEEEIS KYDKICEEAF TRSKDEKILH IKHWLDSPWP GFFTLDGQPR
     SMTCPSTGLE EDVLFHIGKV ASSVPVENFT IHGGLSRILK TRRELVTNRT VDWALAEYMA
     FGSLLKEGIH VRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL
     SEYGVLGFEL GFAMASPNAL VLWEAQFGDF NNMAQCIIDQ FICPGQAKWV RQNGIVLLLP
     HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLQEENFDIN QLYDCNWIVV NCSTPGNFFH
     VLRRQILLPF RKPLIVFTPK SLLRHPEART SFDEMLPGTH FQRVIPENGP AAQDPHKVKR
     LLFCTGKVYY DLTRERKARN MEEEVAITRI EQLSPFPFDL LLKEAQKYPN AELAWCQEEH
     KNQGYYDYVK PRLRTTIDRA KPVWYAGRDP AAAPATGNKK THLTELQRFL DTAFDLDAFK
     KFS
//
DBGET integrated database retrieval system