ACD10_MOUSE
ID ACD10_MOUSE Reviewed; 1069 AA.
AC Q8K370; Q8BWQ0; Q8K313;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Acyl-CoA dehydrogenase family member 10;
DE Short=ACAD-10;
DE EC=1.3.99.-;
GN Name=Acad10;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, and Liver;
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 expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-413; LYS-427 AND LYS-1052, 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., Zhang Y.,
RA 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-427 AND LYS-1052, AND
RP IDENTIFICATION BY 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., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Acyl-CoA dehydrogenase only active with R- and S-2-methyl-
CC C15-CoA. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=A + a 2,3-saturated acyl-CoA = a 2,3-dehydroacyl-CoA + AH2;
CC Xref=Rhea:RHEA:48608, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:60015, ChEBI:CHEBI:65111;
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29047.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC34193.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK050332; BAC34193.1; ALT_FRAME; mRNA.
DR EMBL; BC027825; AAH27825.1; -; mRNA.
DR EMBL; BC029047; AAH29047.1; ALT_INIT; mRNA.
DR CCDS; CCDS51643.1; -.
DR RefSeq; NP_082313.2; NM_028037.4.
DR RefSeq; XP_006530521.1; XM_006530458.3.
DR RefSeq; XP_006530523.1; XM_006530460.3.
DR RefSeq; XP_006530524.1; XM_006530461.3.
DR AlphaFoldDB; Q8K370; -.
DR SMR; Q8K370; -.
DR BioGRID; 215074; 5.
DR IntAct; Q8K370; 2.
DR MINT; Q8K370; -.
DR STRING; 10090.ENSMUSP00000107400; -.
DR iPTMnet; Q8K370; -.
DR PhosphoSitePlus; Q8K370; -.
DR SwissPalm; Q8K370; -.
DR EPD; Q8K370; -.
DR jPOST; Q8K370; -.
DR MaxQB; Q8K370; -.
DR PaxDb; Q8K370; -.
DR PeptideAtlas; Q8K370; -.
DR PRIDE; Q8K370; -.
DR ProteomicsDB; 285578; -.
DR DNASU; 71985; -.
DR Ensembl; ENSMUST00000031412; ENSMUSP00000031412; ENSMUSG00000029456.
DR Ensembl; ENSMUST00000111770; ENSMUSP00000107400; ENSMUSG00000029456.
DR GeneID; 71985; -.
DR KEGG; mmu:71985; -.
DR UCSC; uc008zjy.1; mouse.
DR CTD; 80724; -.
DR MGI; MGI:1919235; Acad10.
DR VEuPathDB; HostDB:ENSMUSG00000029456; -.
DR eggNOG; KOG1469; Eukaryota.
DR eggNOG; KOG3085; Eukaryota.
DR GeneTree; ENSGT00940000161620; -.
DR HOGENOM; CLU_007526_2_1_1; -.
DR InParanoid; Q8K370; -.
DR OMA; PGIKVIR; -.
DR OrthoDB; 1028522at2759; -.
DR PhylomeDB; Q8K370; -.
DR TreeFam; TF333953; -.
DR Reactome; R-MMU-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR BioGRID-ORCS; 71985; 6 hits in 60 CRISPR screens.
DR ChiTaRS; Acad10; mouse.
DR PRO; PR:Q8K370; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q8K370; protein.
DR Bgee; ENSMUSG00000029456; Expressed in proximal tubule and 61 other tissues.
DR Genevisible; Q8K370; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
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:0033539; P:fatty acid beta-oxidation using acyl-CoA dehydrogenase; IBA:GO_Central.
DR CDD; cd05154; ACAD10_11_N-like; 1.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 1.10.540.10; -; 1.
DR Gene3D; 2.40.110.10; -; 1.
DR Gene3D; 3.40.50.1000; -; 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; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR011945; HAD-SF_ppase_IA/epoxid_hydro_N.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR023198; PGP-like_dom2.
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 Pfam; PF13419; HAD_2; 1.
DR PRINTS; PR00413; HADHALOGNASE.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02247; HAD-1A3-hyp; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Acetylation; FAD; Flavoprotein; Oxidoreductase; Reference proteome.
FT CHAIN 1..1069
FT /note="Acyl-CoA dehydrogenase family member 10"
FT /id="PRO_0000284771"
FT BINDING 792..802
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 828
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 943
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 1013
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 1044
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT MOD_RES 413
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 427
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 427
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1052
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 1052
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 511..512
FT /note="IL -> MM (in Ref. 2; AAH29047)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1069 AA; 118979 MW; 27A4D0823FDAA3D5 CRC64;
MLVRRLFQPS TLHWAWRTTA LNHPLGRHQG GLRWTHSGGR SYRAVIFDTG GVLVPSPGTV
AVGWEVQNHV PSGTIVKAFI RGGDSGPWIR FIKGEITTEH FLEEFGRLCS EIAKTSVPVS
SYFSLLTSEQ VTKQFPVMTQ AISQIRAKGL QTAVLTNNFH LSSGESFLPL DRKQFDVVVE
SCLEGICKPD PRIFQLCLQR LSLQPSEAIF LDDLGSNLKV AASLGIHTIK VDRPETAVKE
LEALLGFPLH LGVPNTRPVR KTMAIPQDAL EKYLKGLLGT HSTGPMELLQ FDHGQSNPTY
YIRLADRQLV LRKKPSGTLL PSAHAIEREF RIMKALANAG VPVPTVLDLC EDSSIIGTPF
YLMEYCPGII YKDPSLPGLE PSRREAIYTA MNQVLCRIHS VDLQATSLDS FGKQGDYIPR
QVQTWTKQYR AAETSSIPAM ERLIQWLPLH LPRQQRTTLV HGDFRLDNLI FHPEKAEVLA
VLDWELSTLG DPFADVAYSC LAYYLPSSFP ILRGFRDQDV TKLGIPTVEE YFRMYCLNMG
IPPIDNWNFY MAFSFFRVAA ILQGVYKRSL TGQASSATAQ QSGKLTESMA ELAWDFATKE
GFRVFKEMPA TKTLSRSYHA WAGPRSPRTP KGVRGHSTVA AASPSHEAKG GLVISPEGLS
PAVRKLYEQL VQFIEQKVYP LEPELQRHQA SADRWSPSPL IEDLKEKAKA EGLWNLFLPL
ETDPEKKYGA GLTNVEYAHL CEVMGMSLYA SEIFNCSAPD TGNMEILVRY GTEEQKARWL
VPLLEGRIRS CFAMTEPQVA SSDASNIEAS IKEEDGCYVI NGHKWWTSGI LDPRCKLCVF
MGKTDPQAPR HQQQSMLLVP MDSPGITVIR PLSVFGLEDP PGGHGEVRFK DVRVPKENIL
LGPGRGFEIA QGRLGPGRIH HCMRLIGYSE RALALMKTRV MSRTAFGKPL VEQGTILADI
ARSRVEIEQA RLLVLKAAHL MDVAGNKTAA LDIAMIKMVV PSMAYHVIDR AIQAFGAAGL
SSDYPLAQFF GWARALRFAD GPDEVHQLTV AKMELKNQSR MQEPAVPRV
