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Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial (ETF-QO) (ETF-ubiquinone oxidoreductase) (EC 1.5.5.1) (Electron-transferring-flavoprotein dehydrogenase) (ETF dehydrogenase)

 ETFD_HUMAN              Reviewed;         617 AA.
Q16134; B4E3R9; J3KND9; Q7Z347;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-MAR-2010, sequence version 2.
07-JUN-2017, entry version 165.
RecName: Full=Electron transfer flavoprotein-ubiquinone oxidoreductase, mitochondrial;
Short=ETF-QO;
Short=ETF-ubiquinone oxidoreductase;
EC=1.5.5.1;
AltName: Full=Electron-transferring-flavoprotein dehydrogenase;
Short=ETF dehydrogenase;
Flags: Precursor;
Name=ETFDH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-31.
TISSUE=Fetal liver;
PubMed=8306995; DOI=10.1111/j.1432-1033.1994.tb19939.x;
Goodman S.I., Axtell K.M., Bindoff L.A., Beard S.E., Gill R.E.,
Frerman F.E.;
"Molecular cloning and expression of a cDNA encoding human electron
transfer flavoprotein-ubiquinone oxidoreductase.";
Eur. J. Biochem. 219:277-286(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ILE-31.
TISSUE=Small intestine;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ILE-31.
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INVOLVEMENT IN GA2C.
PubMed=12815589; DOI=10.1002/humu.10226;
Olsen R.K.J., Andresen B.S., Christensen E., Bross P., Skovby F.,
Gregersen N.;
"Clear relationship between ETF/ETFDH genotype and phenotype in
patients with multiple acyl-CoA dehydrogenation deficiency.";
Hum. Mutat. 22:12-23(2003).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[10]
VARIANTS GA2C CYS-49; PHE-82; PRO-82; ARG-138; ASN-218; PRO-222;
PHE-262; PRO-334; ARG-346; LYS-452; LEU-456; LEU-562 AND GLU-611, AND
VARIANTS CYS-16 AND ILE-31.
PubMed=12359134; DOI=10.1016/S1096-7192(02)00138-5;
Goodman S.I., Binard R.J., Woontner M.R., Frerman F.E.;
"Glutaric acidemia type II: gene structure and mutations of the
electron transfer flavoprotein:ubiquinone oxidoreductase (ETF:QO)
gene.";
Mol. Genet. Metab. 77:86-90(2002).
[11]
VARIANTS GA2C TYR-112 AND THR-456.
PubMed=16527485; DOI=10.1016/j.nmd.2006.01.001;
Beresford M.W., Pourfarzam M., Turnbull D.M., Davidson J.E.;
"So doctor, what exactly is wrong with my muscles? Glutaric aciduria
type II presenting in a teenager.";
Neuromuscul. Disord. 16:269-273(2006).
[12]
VARIANT [LARGE SCALE ANALYSIS] LEU-565.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[13]
VARIANTS GA2C PRO-377; LEU-456; LEU-483 AND GLU-590.
PubMed=17412732; DOI=10.1093/brain/awm054;
Gempel K., Topaloglu H., Talim B., Schneiderat P., Schoser B.G.,
Hans V.H., Palmafy B., Kale G., Tokatli A., Quinzii C., Hirano M.,
Naini A., DiMauro S., Prokisch H., Lochmueller H., Horvath R.;
"The myopathic form of coenzyme Q10 deficiency is caused by mutations
in the electron-transferring-flavoprotein dehydrogenase (ETFDH)
gene.";
Brain 130:2037-2044(2007).
[14]
VARIANTS GA2C THR-84; HIS-127 AND LEU-175.
PubMed=19249206; DOI=10.1016/j.nmd.2009.01.008;
Liang W.C., Ohkuma A., Hayashi Y.K., Lopez L.C., Hirano M., Nonaka I.,
Noguchi S., Chen L.H., Jong Y.J., Nishino I.;
"ETFDH mutations, CoQ10 levels, and respiratory chain activities in
patients with riboflavin-responsive multiple acyl-CoA dehydrogenase
deficiency.";
Neuromuscul. Disord. 19:212-216(2009).
[15]
VARIANTS GA2C THR-84 AND HIS-175.
PubMed=20370797; DOI=10.1111/j.1399-0004.2010.01421.x;
Lan M.Y., Fu M.H., Liu Y.F., Huang C.C., Chang Y.Y., Liu J.S.,
Peng C.H., Chen S.S.;
"High frequency of ETFDH c.250G>A mutation in Taiwanese patients with
late-onset lipid storage myopathy.";
Clin. Genet. 78:565-569(2010).
-!- FUNCTION: Accepts electrons from ETF and reduces ubiquinone.
-!- CATALYTIC ACTIVITY: Reduced electron-transferring flavoprotein +
ubiquinone = electron-transferring flavoprotein + ubiquinol.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Note=Binds 1 [4Fe-4S] cluster.;
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
-!- SUBUNIT: Monomer.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q16134-1; Sequence=Displayed;
Name=2;
IsoId=Q16134-3; Sequence=VSP_055158;
Note=No experimental confirmation available.;
-!- DISEASE: Glutaric aciduria 2C (GA2C) [MIM:231680]: An autosomal
recessively inherited disorder of fatty acid, amino acid, and
choline metabolism. It is characterized by multiple acyl-CoA
dehydrogenase deficiencies resulting in large excretion not only
of glutaric acid, but also of lactic, ethylmalonic, butyric,
isobutyric, 2-methyl-butyric, and isovaleric acids.
{ECO:0000269|PubMed:12359134, ECO:0000269|PubMed:12815589,
ECO:0000269|PubMed:16527485, ECO:0000269|PubMed:17412732,
ECO:0000269|PubMed:19249206, ECO:0000269|PubMed:20370797}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the ETF-QO/FixC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD98030.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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EMBL; S69232; AAC60628.1; -; mRNA.
EMBL; AK304838; BAG65581.1; -; mRNA.
EMBL; BX538129; CAD98030.1; ALT_SEQ; mRNA.
EMBL; AC107219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC011890; AAH11890.1; -; mRNA.
CCDS; CCDS3800.1; -. [Q16134-1]
CCDS; CCDS64090.1; -. [Q16134-3]
PIR; S41115; S41115.
RefSeq; NP_001268666.1; NM_001281737.1. [Q16134-3]
RefSeq; NP_004444.2; NM_004453.3. [Q16134-1]
UniGene; Hs.155729; -.
ProteinModelPortal; Q16134; -.
SMR; Q16134; -.
BioGrid; 108411; 4.
IntAct; Q16134; 8.
STRING; 9606.ENSP00000426638; -.
iPTMnet; Q16134; -.
PhosphoSitePlus; Q16134; -.
SwissPalm; Q16134; -.
BioMuta; ETFDH; -.
DMDM; 292495008; -.
EPD; Q16134; -.
MaxQB; Q16134; -.
PaxDb; Q16134; -.
PeptideAtlas; Q16134; -.
PRIDE; Q16134; -.
Ensembl; ENST00000307738; ENSP00000303552; ENSG00000171503. [Q16134-3]
Ensembl; ENST00000511912; ENSP00000426638; ENSG00000171503. [Q16134-1]
GeneID; 2110; -.
KEGG; hsa:2110; -.
UCSC; uc003iqb.5; human. [Q16134-1]
CTD; 2110; -.
DisGeNET; 2110; -.
GeneCards; ETFDH; -.
H-InvDB; HIX0200647; -.
HGNC; HGNC:3483; ETFDH.
HPA; HPA041978; -.
MalaCards; ETFDH; -.
MIM; 231675; gene.
MIM; 231680; phenotype.
neXtProt; NX_Q16134; -.
OpenTargets; ENSG00000171503; -.
Orphanet; 394532; Multiple acyl-CoA dehydrogenation deficiency, mild type.
Orphanet; 394529; Multiple acyl-CoA dehydrogenation deficiency, severe neonatal type.
PharmGKB; PA27899; -.
eggNOG; KOG2415; Eukaryota.
eggNOG; COG0644; LUCA.
GeneTree; ENSGT00390000010773; -.
HOGENOM; HOG000259450; -.
HOVERGEN; HBG005615; -.
InParanoid; Q16134; -.
KO; K00311; -.
OMA; VPRITTH; -.
OrthoDB; EOG091G03C7; -.
PhylomeDB; Q16134; -.
TreeFam; TF105687; -.
BioCyc; MetaCyc:HS10326-MONOMER; -.
BRENDA; 1.5.5.1; 2681.
Reactome; R-HSA-611105; Respiratory electron transport.
ChiTaRS; ETFDH; human.
GeneWiki; ETFDH; -.
GenomeRNAi; 2110; -.
PRO; PR:Q16134; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000171503; -.
CleanEx; HS_ETFDH; -.
ExpressionAtlas; Q16134; baseline and differential.
Genevisible; Q16134; HS.
GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0017133; C:mitochondrial electron transfer flavoprotein complex; IBA:GO_Central.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB.
GO; GO:0009055; F:electron carrier activity; IDA:UniProtKB.
GO; GO:0004174; F:electron-transferring-flavoprotein dehydrogenase activity; IDA:UniProtKB.
GO; GO:0050660; F:flavin adenine dinucleotide binding; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
GO; GO:0043783; F:oxidoreductase activity, oxidizing metal ions with flavin as acceptor; ISS:UniProtKB.
GO; GO:0048038; F:quinone binding; IDA:UniProtKB.
GO; GO:0048039; F:ubiquinone binding; IDA:UniProtKB.
GO; GO:0022900; P:electron transport chain; IDA:UniProtKB.
GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IMP:BHF-UCL.
GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
Gene3D; 3.50.50.60; -; 1.
InterPro; IPR017896; 4Fe4S_Fe-S-bd.
InterPro; IPR023753; FAD/NAD-binding_dom.
InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2.
PRINTS; PR00469; PNDRDTASEII.
SUPFAM; SSF51905; SSF51905; 2.
PROSITE; PS51379; 4FE4S_FER_2; 1.
1: Evidence at protein level;
4Fe-4S; Acetylation; Alternative splicing; Complete proteome;
Disease mutation; Electron transport; FAD; Flavoprotein;
Glutaricaciduria; Iron; Iron-sulfur; Membrane; Metal-binding;
Mitochondrion; Mitochondrion inner membrane; Oxidoreductase;
Phosphoprotein; Polymorphism; Reference proteome; Transit peptide;
Transport; Ubiquinone.
TRANSIT 1 33 Mitochondrion. {ECO:0000255}.
CHAIN 34 617 Electron transfer flavoprotein-ubiquinone
oxidoreductase, mitochondrial.
/FTId=PRO_0000008661.
INTRAMEM 109 130 {ECO:0000250}.
INTRAMEM 428 447 {ECO:0000250}.
DOMAIN 577 606 4Fe-4S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00711}.
NP_BIND 71 85 FAD. {ECO:0000255}.
METAL 561 561 Iron-sulfur (4Fe-4S). {ECO:0000255}.
METAL 586 586 Iron-sulfur (4Fe-4S). {ECO:0000255}.
METAL 589 589 Iron-sulfur (4Fe-4S). {ECO:0000255}.
METAL 592 592 Iron-sulfur (4Fe-4S). {ECO:0000255}.
BINDING 305 305 Ubiquinone; via carbonyl oxygen.
{ECO:0000250}.
BINDING 306 306 Ubiquinone; via amide nitrogen.
{ECO:0000250}.
MOD_RES 96 96 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q921G7}.
MOD_RES 132 132 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q921G7}.
MOD_RES 223 223 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q921G7}.
MOD_RES 357 357 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q921G7}.
MOD_RES 551 551 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 12 58 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055158.
VARIANT 16 16 F -> C. {ECO:0000269|PubMed:12359134}.
/FTId=VAR_075438.
VARIANT 31 31 T -> I (in dbSNP:rs11559290).
{ECO:0000269|PubMed:12359134,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17974005,
ECO:0000269|PubMed:8306995}.
/FTId=VAR_062966.
VARIANT 49 49 Y -> C (in GA2C; unknown pathological
significance).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075439.
VARIANT 82 82 S -> F (in GA2C).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075440.
VARIANT 82 82 S -> P (in GA2C).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075441.
VARIANT 84 84 A -> T (in GA2C; dbSNP:rs121964954).
{ECO:0000269|PubMed:19249206,
ECO:0000269|PubMed:20370797}.
/FTId=VAR_075442.
VARIANT 94 94 H -> R (in dbSNP:rs1140065).
/FTId=VAR_055711.
VARIANT 112 112 H -> Y (in GA2C).
{ECO:0000269|PubMed:16527485}.
/FTId=VAR_075443.
VARIANT 127 127 L -> H (in GA2C; dbSNP:rs121964956).
{ECO:0000269|PubMed:19249206}.
/FTId=VAR_075444.
VARIANT 138 138 L -> R (in GA2C; unknown pathological
significance; dbSNP:rs779896449).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075445.
VARIANT 175 175 R -> H (in GA2C; dbSNP:rs121964955).
{ECO:0000269|PubMed:20370797}.
/FTId=VAR_075446.
VARIANT 175 175 R -> L (in GA2C; dbSNP:rs121964955).
{ECO:0000269|PubMed:19249206}.
/FTId=VAR_075447.
VARIANT 218 218 D -> N (in GA2C; unknown pathological
significance; dbSNP:rs748289922).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075448.
VARIANT 222 222 Q -> P (in GA2C; unknown pathological
significance).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075449.
VARIANT 262 262 L -> F (in GA2C; unknown pathological
significance).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075450.
VARIANT 334 334 L -> P (in GA2C; unknown pathological
significance; dbSNP:rs377686388).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075451.
VARIANT 346 346 H -> R (in GA2C; unknown pathological
significance).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075452.
VARIANT 377 377 L -> P (in GA2C; unknown pathological
significance; dbSNP:rs387907170).
{ECO:0000269|PubMed:17412732}.
/FTId=VAR_075453.
VARIANT 452 452 R -> K (in GA2C; unknown pathological
significance).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075454.
VARIANT 456 456 P -> L (in GA2C; dbSNP:rs398124152).
{ECO:0000269|PubMed:12359134,
ECO:0000269|PubMed:17412732}.
/FTId=VAR_075455.
VARIANT 456 456 P -> T (in GA2C).
{ECO:0000269|PubMed:16527485}.
/FTId=VAR_075456.
VARIANT 483 483 P -> L (in GA2C; unknown pathological
significance; dbSNP:rs377656387).
{ECO:0000269|PubMed:17412732}.
/FTId=VAR_075457.
VARIANT 562 562 P -> L (in GA2C).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075458.
VARIANT 565 565 V -> L (in a colorectal cancer sample;
somatic mutation; dbSNP:rs769893690).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036134.
VARIANT 590 590 K -> E (in GA2C).
{ECO:0000269|PubMed:17412732}.
/FTId=VAR_075459.
VARIANT 611 611 G -> E (in GA2C; dbSNP:rs761669036).
{ECO:0000269|PubMed:12359134}.
/FTId=VAR_075460.
CONFLICT 109 109 I -> V (in Ref. 3; CAD98030).
{ECO:0000305}.
CONFLICT 456 456 P -> S (in Ref. 2; BAG65581).
{ECO:0000305}.
SEQUENCE 617 AA; 68495 MW; 099EBA36C59AF3D6 CRC64;
MLVPLAKLSC LAYQCFHALK IKKNYLPLCA TRWSSTSTVP RITTHYTIYP RDKDKRWEGV
NMERFAEEAD VVIVGAGPAG LSAAVRLKQL AVAHEKDIRV CLVEKAAQIG AHTLSGACLD
PGAFKELFPD WKEKGAPLNT PVTEDRFGIL TEKYRIPVPI LPGLPMNNHG NYIVRLGHLV
SWMGEQAEAL GVEVYPGYAA AEVLFHDDGS VKGIATNDVG IQKDGAPKAT FERGLELHAK
VTIFAEGCHG HLAKQLYKKF DLRANCEPQT YGIGLKELWV IDEKNWKPGR VDHTVGWPLD
RHTYGGSFLY HLNEGEPLVA LGLVVGLDYQ NPYLSPFREF QRWKHHPSIR PTLEGGKRIA
YGARALNEGG FQSIPKLTFP GGLLIGCSPG FMNVPKIKGT HTAMKSGILA AESIFNQLTS
ENLQSKTIGL HVTEYEDNLK NSWVWKELYS VRNIRPSCHG VLGVYGGMIY TGIFYWILRG
MEPWTLKHKG SDFERLKPAK DCTPIEYPKP DGQISFDLLS SVALSGTNHE HDQPAHLTLR
DDSIPVNRNL SIYDGPEQRF CPAGVYEFVP VEQGDGFRLQ INAQNCVHCK TCDIKDPSQN
INWVVPEGGG GPAYNGM


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