ACD11_HUMAN
ID ACD11_HUMAN Reviewed; 780 AA.
AC Q709F0; Q08AF0; Q658N9; Q658Y2; Q6ZND2; Q8WUT6; Q9H9R3;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Acyl-CoA dehydrogenase family member 11;
DE Short=ACAD-11;
DE EC=1.3.8.- {ECO:0000269|PubMed:21237683};
GN Name=ACAD11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Mahieu V., Van Veldhoven P.P.;
RT "Presence of an acyl-CoA dehydrogenase in mammalian peroxisomes ?";
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 35-780 (ISOFORM 1).
RC TISSUE=Lymph node, and Stomach;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-563 (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 343-780 (ISOFORM 1).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21237683; DOI=10.1016/j.ymgme.2010.12.005;
RA He M., Pei Z., Mohsen A.W., Watkins P., Murdoch G., Van Veldhoven P.P.,
RA Ensenauer R., Vockley J.;
RT "Identification and characterization of new long chain acyl-CoA
RT dehydrogenases.";
RL Mol. Genet. Metab. 102:418-429(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 355-780 IN COMPLEX WITH FAD,
RP COFACTOR, AND SUBUNIT.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human acyl-CoA dehydrogenase 11.";
RL Submitted (MAY-2009) to the PDB data bank.
CC -!- FUNCTION: Acyl-CoA dehydrogenase, that exhibits maximal activity
CC towards saturated C22-CoA (PubMed:21237683). Probably participates in
CC beta-oxydation and energy production but could also play a role in the
CC metabolism of specific fatty acids to control fatty acids composition
CC of cellular lipids in brain (Probable). {ECO:0000269|PubMed:21237683,
CC ECO:0000305|PubMed:21237683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2,3-saturated acyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = a (2E)-enoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:44704, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:58856, ChEBI:CHEBI:65111;
CC Evidence={ECO:0000269|PubMed:21237683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44705;
CC Evidence={ECO:0000305|PubMed:21237683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=docosanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-docosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47228, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:65059, ChEBI:CHEBI:74692;
CC Evidence={ECO:0000269|PubMed:21237683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47229;
CC Evidence={ECO:0000305|PubMed:21237683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + reduced [electron-
CC transfer flavoprotein]; Xref=Rhea:RHEA:47232, Rhea:RHEA-COMP:10685,
CC Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:65052, ChEBI:CHEBI:74693;
CC Evidence={ECO:0000269|PubMed:21237683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47233;
CC Evidence={ECO:0000305|PubMed:21237683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=eicosanoyl-CoA + H(+) + oxidized [electron-transfer
CC flavoprotein] = (2E)-eicosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:47236, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57380, ChEBI:CHEBI:57692,
CC ChEBI:CHEBI:58307, ChEBI:CHEBI:74691;
CC Evidence={ECO:0000269|PubMed:21237683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47237;
CC Evidence={ECO:0000305|PubMed:21237683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + hexacosanoyl-CoA + oxidized [electron-transfer
CC flavoprotein] = (2E)-hexacosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48216, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:64868, ChEBI:CHEBI:74281;
CC Evidence={ECO:0000269|PubMed:21237683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48217;
CC Evidence={ECO:0000305|PubMed:21237683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + oxidized [electron-transfer flavoprotein] +
CC tricosanoyl-CoA = (2E)-tricosenoyl-CoA + reduced [electron-transfer
CC flavoprotein]; Xref=Rhea:RHEA:48220, Rhea:RHEA-COMP:10685, Rhea:RHEA-
CC COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,
CC ChEBI:CHEBI:90118, ChEBI:CHEBI:90119;
CC Evidence={ECO:0000269|PubMed:21237683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48221;
CC Evidence={ECO:0000305|PubMed:21237683};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|Ref.9};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000305|PubMed:21237683}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.9}.
CC -!- INTERACTION:
CC Q709F0; O95400: CD2BP2; NbExp=4; IntAct=EBI-2880718, EBI-768015;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:Q80XL6}.
CC Mitochondrion membrane {ECO:0000269|PubMed:21237683}. Note=Has been
CC detected associated with mitochondrial membrane, but no matrix, in
CC kidney and cerebellum, as well as in a neuroblastoma cell line, but not
CC in skin fibroblasts, where it is observed in cytoplasmic vesicles
CC (PubMed:21237683). No mitochondrial targeting signals could be
CC predicted for any known isoform, including a putative isoform starting
CC at Met-316. {ECO:0000269|PubMed:21237683}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q709F0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q709F0-2; Sequence=VSP_021188;
CC Name=3;
CC IsoId=Q709F0-3; Sequence=VSP_021187;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain
CC followed by liver, heart and kidney. {ECO:0000269|PubMed:21237683}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14158.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ608287; CAE55233.1; -; mRNA.
DR EMBL; AL833721; CAH56228.1; -; mRNA.
DR EMBL; AL832873; CAH56354.1; -; mRNA.
DR EMBL; AK022654; BAB14158.1; ALT_INIT; mRNA.
DR EMBL; AK131265; BAD18443.1; -; mRNA.
DR EMBL; AC020632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF457683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF457684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019607; AAH19607.2; -; mRNA.
DR EMBL; BC125204; AAI25205.1; -; mRNA.
DR CCDS; CCDS3074.1; -. [Q709F0-1]
DR RefSeq; NP_115545.3; NM_032169.4. [Q709F0-1]
DR PDB; 2WBI; X-ray; 2.80 A; A/B=355-780.
DR PDBsum; 2WBI; -.
DR AlphaFoldDB; Q709F0; -.
DR SMR; Q709F0; -.
DR BioGRID; 123902; 142.
DR IntAct; Q709F0; 55.
DR MINT; Q709F0; -.
DR STRING; 9606.ENSP00000264990; -.
DR ChEMBL; CHEMBL4105707; -.
DR SwissLipids; SLP:000001326; -.
DR iPTMnet; Q709F0; -.
DR PhosphoSitePlus; Q709F0; -.
DR BioMuta; ACAD11; -.
DR DMDM; 117949774; -.
DR EPD; Q709F0; -.
DR jPOST; Q709F0; -.
DR MassIVE; Q709F0; -.
DR MaxQB; Q709F0; -.
DR PaxDb; Q709F0; -.
DR PeptideAtlas; Q709F0; -.
DR PRIDE; Q709F0; -.
DR ProteomicsDB; 68516; -. [Q709F0-1]
DR ProteomicsDB; 68517; -. [Q709F0-2]
DR ProteomicsDB; 68518; -. [Q709F0-3]
DR Antibodypedia; 34898; 111 antibodies from 21 providers.
DR DNASU; 84129; -.
DR Ensembl; ENST00000264990.11; ENSP00000264990.6; ENSG00000240303.8. [Q709F0-1]
DR GeneID; 84129; -.
DR KEGG; hsa:84129; -.
DR MANE-Select; ENST00000264990.11; ENSP00000264990.6; NM_032169.5; NP_115545.3.
DR UCSC; uc003eov.5; human. [Q709F0-1]
DR CTD; 84129; -.
DR DisGeNET; 84129; -.
DR GeneCards; ACAD11; -.
DR HGNC; HGNC:30211; ACAD11.
DR HPA; ENSG00000240303; Group enriched (kidney, liver).
DR MalaCards; ACAD11; -.
DR MIM; 614288; gene.
DR neXtProt; NX_Q709F0; -.
DR OpenTargets; ENSG00000240303; -.
DR PharmGKB; PA142672658; -.
DR VEuPathDB; HostDB:ENSG00000240303; -.
DR eggNOG; KOG1469; Eukaryota.
DR GeneTree; ENSGT00940000160993; -.
DR HOGENOM; CLU_007526_3_1_1; -.
DR InParanoid; Q709F0; -.
DR OMA; IWAPQIF; -.
DR OrthoDB; 1028522at2759; -.
DR PhylomeDB; Q709F0; -.
DR TreeFam; TF333953; -.
DR PathwayCommons; Q709F0; -.
DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SignaLink; Q709F0; -.
DR UniPathway; UPA00659; -.
DR BioGRID-ORCS; 84129; 12 hits in 1080 CRISPR screens.
DR EvolutionaryTrace; Q709F0; -.
DR GenomeRNAi; 84129; -.
DR Pharos; Q709F0; Tbio.
DR PRO; PR:Q709F0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q709F0; protein.
DR Bgee; ENSG00000240303; Expressed in right lobe of liver and 94 other tissues.
DR ExpressionAtlas; Q709F0; baseline and differential.
DR Genevisible; Q709F0; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; ISS:HGNC.
DR GO; GO:0003995; F:acyl-CoA dehydrogenase activity; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004466; F:long-chain-acyl-CoA dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0070991; F:medium-chain-acyl-CoA dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0017099; F:very-long-chain-acyl-CoA dehydrogenase activity; IDA:UniProtKB.
DR GO; GO:0006635; P:fatty acid beta-oxidation; TAS:Reactome.
DR GO; GO:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IDA:UniProtKB.
DR CDD; cd05154; ACAD10_11_N-like; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR InterPro; IPR041726; ACAD10_11_N.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; FAD;
KW Fatty acid metabolism; Flavoprotein; Lipid metabolism; Membrane;
KW Mitochondrion; Oxidoreductase; Peroxisome; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..780
FT /note="Acyl-CoA dehydrogenase family member 11"
FT /id="PRO_0000254145"
FT BINDING 504..514
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 514
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 538..540
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 629..632
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 657
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 727..731
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 727
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.9"
FT BINDING 755
FT /ligand="substrate"
FT BINDING 756..758
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|Ref.9"
FT MOD_RES 177
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
FT MOD_RES 324
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
FT MOD_RES 391
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80XL6"
FT VAR_SEQ 1..120
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021187"
FT VAR_SEQ 564..667
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_021188"
FT VARIANT 362
FT /note="V -> L (in dbSNP:rs6776576)"
FT /id="VAR_028826"
FT CONFLICT 414
FT /note="K -> T (in Ref. 2; CAH56354)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="I -> V (in Ref. 1; CAE55233 and 3; BAB14158)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="S -> SRLT (in Ref. 2; CAH56228)"
FT /evidence="ECO:0000305"
FT HELIX 377..392
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 394..402
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 404..408
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 419..430
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 446..456
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 462..465
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 472..482
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 485..490
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 492..497
FT /evidence="ECO:0007829|PDB:2WBI"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:2WBI"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:2WBI"
FT STRAND 529..540
FT /evidence="ECO:0007829|PDB:2WBI"
FT TURN 541..543
FT /evidence="ECO:0007829|PDB:2WBI"
FT STRAND 547..555
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 563..565
FT /evidence="ECO:0007829|PDB:2WBI"
FT STRAND 567..573
FT /evidence="ECO:0007829|PDB:2WBI"
FT STRAND 579..584
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:2WBI"
FT STRAND 598..609
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 620..656
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 664..666
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 668..702
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 704..728
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 730..734
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 740..750
FT /evidence="ECO:0007829|PDB:2WBI"
FT TURN 751..754
FT /evidence="ECO:0007829|PDB:2WBI"
FT HELIX 757..776
FT /evidence="ECO:0007829|PDB:2WBI"
SQ SEQUENCE 780 AA; 87264 MW; E4DC30F6ABE70463 CRC64;
MKPGATGESD LAEVLPQHKF DSKSLEAYLN QHLSGFGAER EATLTIAQYR AGKSNPTFYL
QKGFQTYVLR KKPPGSLLPK AHQIDREFKV QKALFSIGFP VPKPILYCSD TSVIGTEFYV
MEHVQGRIFR DLTIPGLSPA ERSAIYVATV ETLAQLHSLN IQSLQLEGYG IGAGYCKRQV
STWTKQYQAA AHQDIPAMQQ LSEWLMKNLP DNDNEENLIH GDFRLDNIVF HPKECRVIAV
LDWELSTIGH PLSDLAHFSL FYFWPRTVPM INQGSYSENS GIPSMEELIS IYCRCRGINS
ILPNWNFFLA LSYFKMAGIA QGVYSRYLLG NNSSEDSFLF ANIVQPLAET GLQLSKRTFS
TVLPQIDTTG QLFVQTRKGQ EVLIKVKHFM KQHILPAEKE VTEFYVQNEN SVDKWGKPLV
IDKLKEMAKV EGLWNLFLPA VSGLSHVDYA LIAEETGKCF FAPDVFNCQA PDTGNMEVLH
LYGSEEQKKQ WLEPLLQGNI TSCFCMTEPD VASSDATNIE CSIQRDEDSY VINGKKWWSS
GAGNPKCKIA IVLGRTQNTS LSRHKQHSMI LVPMNTPGVK IIRPLSVFGY TDNFHGGHFE
IHFNQVRVPA TNLILGEGRG FEISQGRLGP GRIHHCMRTV GLAERALQIM CERATQRIAF
KKKLYAHEVV AHWIAESRIA IEKIRLLTLK AAHSMDTLGS AGAKKEIAMI KVAAPRAVSK
IVDWAIQVCG GAGVSQDYPL ANMYAITRVL RLADGPDEVH LSAIATMELR DQAKRLTAKI
