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Protein

Acyl-CoA dehydrogenase family member 10

Gene

Acad10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Acyl-CoA dehydrogenase only active with R- and S-2-methyl-C15-CoA.By similarity

Catalytic activityi

Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.

Cofactori

FADBy similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei828 – 8281FADBy similarity
Binding sitei943 – 9431FADBy similarity
Binding sitei1013 – 10131FADBy similarity
Binding sitei1044 – 10441FADBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi792 – 80211FADBy similarityAdd
BLAST

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-MMU-77289. Mitochondrial Fatty Acid Beta-Oxidation.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA dehydrogenase family member 10 (EC:1.3.99.-)
Short name:
ACAD-10
Gene namesi
Name:Acad10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1919235. Acad10.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10691069Acyl-CoA dehydrogenase family member 10PRO_0000284771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei413 – 4131N6-succinyllysineCombined sources
Modified residuei427 – 4271N6-acetyllysine; alternateCombined sources
Modified residuei427 – 4271N6-succinyllysine; alternateCombined sources
Modified residuei1052 – 10521N6-acetyllysine; alternateCombined sources
Modified residuei1052 – 10521N6-succinyllysine; alternateCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ8K370.
MaxQBiQ8K370.
PaxDbiQ8K370.
PRIDEiQ8K370.

PTM databases

iPTMnetiQ8K370.
SwissPalmiQ8K370.

Expressioni

Gene expression databases

BgeeiQ8K370.
CleanExiMM_ACAD10.
GenevisibleiQ8K370. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8K370. 2 interactions.
MINTiMINT-1839952.
STRINGi10090.ENSMUSP00000031412.

Structurei

3D structure databases

ProteinModelPortaliQ8K370.
SMRiQ8K370. Positions 41-599, 659-1055.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG1469. Eukaryota.
KOG3085. Eukaryota.
COG3173. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131666.
HOVERGENiHBG057142.
InParanoidiQ8K370.
KOiK11729.
OMAiAIGLQKY.
OrthoDBiEOG7JDQWS.
TreeFamiTF333953.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
1.10.540.10. 1 hit.
3.40.50.1000. 1 hit.
InterProiIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
IPR002575. Aminoglycoside_PTrfase.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
IPR011009. Kinase-like_dom.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
PF01636. APH. 1 hit.
PF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF56645. SSF56645. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02247. HAD-1A3-hyp. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8K370-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLVRRLFQPS TLHWAWRTTA LNHPLGRHQG GLRWTHSGGR SYRAVIFDTG
60 70 80 90 100
GVLVPSPGTV AVGWEVQNHV PSGTIVKAFI RGGDSGPWIR FIKGEITTEH
110 120 130 140 150
FLEEFGRLCS EIAKTSVPVS SYFSLLTSEQ VTKQFPVMTQ AISQIRAKGL
160 170 180 190 200
QTAVLTNNFH LSSGESFLPL DRKQFDVVVE SCLEGICKPD PRIFQLCLQR
210 220 230 240 250
LSLQPSEAIF LDDLGSNLKV AASLGIHTIK VDRPETAVKE LEALLGFPLH
260 270 280 290 300
LGVPNTRPVR KTMAIPQDAL EKYLKGLLGT HSTGPMELLQ FDHGQSNPTY
310 320 330 340 350
YIRLADRQLV LRKKPSGTLL PSAHAIEREF RIMKALANAG VPVPTVLDLC
360 370 380 390 400
EDSSIIGTPF YLMEYCPGII YKDPSLPGLE PSRREAIYTA MNQVLCRIHS
410 420 430 440 450
VDLQATSLDS FGKQGDYIPR QVQTWTKQYR AAETSSIPAM ERLIQWLPLH
460 470 480 490 500
LPRQQRTTLV HGDFRLDNLI FHPEKAEVLA VLDWELSTLG DPFADVAYSC
510 520 530 540 550
LAYYLPSSFP ILRGFRDQDV TKLGIPTVEE YFRMYCLNMG IPPIDNWNFY
560 570 580 590 600
MAFSFFRVAA ILQGVYKRSL TGQASSATAQ QSGKLTESMA ELAWDFATKE
610 620 630 640 650
GFRVFKEMPA TKTLSRSYHA WAGPRSPRTP KGVRGHSTVA AASPSHEAKG
660 670 680 690 700
GLVISPEGLS PAVRKLYEQL VQFIEQKVYP LEPELQRHQA SADRWSPSPL
710 720 730 740 750
IEDLKEKAKA EGLWNLFLPL ETDPEKKYGA GLTNVEYAHL CEVMGMSLYA
760 770 780 790 800
SEIFNCSAPD TGNMEILVRY GTEEQKARWL VPLLEGRIRS CFAMTEPQVA
810 820 830 840 850
SSDASNIEAS IKEEDGCYVI NGHKWWTSGI LDPRCKLCVF MGKTDPQAPR
860 870 880 890 900
HQQQSMLLVP MDSPGITVIR PLSVFGLEDP PGGHGEVRFK DVRVPKENIL
910 920 930 940 950
LGPGRGFEIA QGRLGPGRIH HCMRLIGYSE RALALMKTRV MSRTAFGKPL
960 970 980 990 1000
VEQGTILADI ARSRVEIEQA RLLVLKAAHL MDVAGNKTAA LDIAMIKMVV
1010 1020 1030 1040 1050
PSMAYHVIDR AIQAFGAAGL SSDYPLAQFF GWARALRFAD GPDEVHQLTV
1060
AKMELKNQSR MQEPAVPRV
Length:1,069
Mass (Da):118,979
Last modified:October 1, 2002 - v1
Checksum:i27A4D0823FDAA3D5
GO

Sequence cautioni

The sequence AAH29047.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC34193.1 differs from that shown. Reason: Frameshift at position 59. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti511 – 5122IL → MM in AAH29047 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050332 mRNA. Translation: BAC34193.1. Frameshift.
BC027825 mRNA. Translation: AAH27825.1.
BC029047 mRNA. Translation: AAH29047.1. Different initiation.
CCDSiCCDS51643.1.
RefSeqiNP_082313.2. NM_028037.4.
XP_006530521.1. XM_006530458.2.
XP_006530523.1. XM_006530460.2.
XP_006530524.1. XM_006530461.2.
UniGeneiMm.45423.

Genome annotation databases

EnsembliENSMUST00000031412; ENSMUSP00000031412; ENSMUSG00000029456.
ENSMUST00000111770; ENSMUSP00000107400; ENSMUSG00000029456.
GeneIDi71985.
KEGGimmu:71985.
UCSCiuc008zjy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050332 mRNA. Translation: BAC34193.1. Frameshift.
BC027825 mRNA. Translation: AAH27825.1.
BC029047 mRNA. Translation: AAH29047.1. Different initiation.
CCDSiCCDS51643.1.
RefSeqiNP_082313.2. NM_028037.4.
XP_006530521.1. XM_006530458.2.
XP_006530523.1. XM_006530460.2.
XP_006530524.1. XM_006530461.2.
UniGeneiMm.45423.

3D structure databases

ProteinModelPortaliQ8K370.
SMRiQ8K370. Positions 41-599, 659-1055.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K370. 2 interactions.
MINTiMINT-1839952.
STRINGi10090.ENSMUSP00000031412.

PTM databases

iPTMnetiQ8K370.
SwissPalmiQ8K370.

Proteomic databases

EPDiQ8K370.
MaxQBiQ8K370.
PaxDbiQ8K370.
PRIDEiQ8K370.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031412; ENSMUSP00000031412; ENSMUSG00000029456.
ENSMUST00000111770; ENSMUSP00000107400; ENSMUSG00000029456.
GeneIDi71985.
KEGGimmu:71985.
UCSCiuc008zjy.1. mouse.

Organism-specific databases

CTDi80724.
MGIiMGI:1919235. Acad10.

Phylogenomic databases

eggNOGiKOG1469. Eukaryota.
KOG3085. Eukaryota.
COG3173. LUCA.
GeneTreeiENSGT00760000119007.
HOGENOMiHOG000131666.
HOVERGENiHBG057142.
InParanoidiQ8K370.
KOiK11729.
OMAiAIGLQKY.
OrthoDBiEOG7JDQWS.
TreeFamiTF333953.

Enzyme and pathway databases

ReactomeiR-MMU-77289. Mitochondrial Fatty Acid Beta-Oxidation.

Miscellaneous databases

PROiQ8K370.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K370.
CleanExiMM_ACAD10.
GenevisibleiQ8K370. MM.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
1.10.540.10. 1 hit.
3.40.50.1000. 1 hit.
InterProiIPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
IPR002575. Aminoglycoside_PTrfase.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
IPR011009. Kinase-like_dom.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
PF01636. APH. 1 hit.
PF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF56645. SSF56645. 1 hit.
SSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02247. HAD-1A3-hyp. 1 hit.
TIGR01509. HAD-SF-IA-v3. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney and Liver.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-413; LYS-427 AND LYS-1052, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-427 AND LYS-1052, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiACD10_MOUSE
AccessioniPrimary (citable) accession number: Q8K370
Secondary accession number(s): Q8BWQ0, Q8K313
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 1, 2002
Last modified: June 8, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.