B4DJE7 (B4DJE7_HUMAN) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Medium-chain-specific acyl-CoA dehydrogenase, mitochondrial Ensembl ENSP00000446176

Submitted name:
cDNA FLJ52595, highly similar to Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (EC 1.3.99.3) EMBL BAG58809.1

Gene names

Name:

ACADM Ensembl ENSP00000446176

Organism

Homo sapiens (Human) [Reference proteome] EMBL BAG58809.1

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	232 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

Ontologies

Keywords
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cardiac muscle cell differentiation Inferred from electronic annotation. Source: Compara carnitine metabolic process, CoA-linked Inferred from electronic annotation. Source: Compara fatty acid beta-oxidation using acyl-CoA dehydrogenase Inferred from electronic annotation. Source: Compara glycogen biosynthetic process Inferred from electronic annotation. Source: Compara liver development Inferred from electronic annotation. Source: Compara medium-chain fatty acid metabolic process Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara regulation of gluconeogenesis Inferred from electronic annotation. Source: Compara response to cold Inferred from electronic annotation. Source: Compara response to starvation Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	medium-chain-acyl-CoA dehydrogenase activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	B4DJE7 [UniParc]. Last modified September 23, 2008. Version 1. Checksum: B903551ACCD1B68B	FASTA	232	25,663
	10 20 30 40 50 60 MWITNGGKAN WYFLLARSDP DPKAPANKAF TGFIVEADTP GIQIGRKELN MGQRCSDTRG 70 80 90 100 110 120 IVFEDVKVPK ENVLIGDGAG FKVAMGAFDK TRPVVAAGAV GLAQRALDEA TKYALERKTF 130 140 150 160 170 180 GKLLVEHQAI SFMLAEMAMK VELARMSYQR AAWEVDSGRR NTYYASIAKA FAGDIANQLA 190 200 210 220 230 TDAVQILGGN GFNTEYPVEK LMRDAKIYQI YEGTSQIQRL IVAREHIDKY KN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S., McLaren S., Milne S., Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R., Banerjee R., Bryant S.P., Burford D.C., Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., Langford C.F., Pandian R.D., Porter K.M., Prigmore E. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"NEDO human cDNA sequencing project focused on splicing variants." Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T. , Sugano S., Nomura N., Isogai T. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Tissue: Subthalamic nucleus EMBL BAG58809.1.
[3]	Ensembl Submitted (FEB-2012) to UniProtKB Cited for: IDENTIFICATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL357314 Genomic DNA. No translation available. AK296045 mRNA. Translation: BAG58809.1.
IPI	IPI01014812.
UniGene	Hs.445040.
3D structure databases
SMR	B4DJE7. Positions 1-232.
ModBase	Search...
Proteomic databases
PRIDE	B4DJE7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000543667; ENSP00000446176; ENSG00000117054.
Organism-specific databases
HGNC	HGNC:89. ACADM.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG000224.
Gene expression databases
ArrayExpress	B4DJE7.
Family and domain databases
Gene3D	2.40.110.10. 1 hit.
InterPro	IPR006089. Acyl-CoA_DH_CS. IPR006090. Acyl-CoA_Oxase/DH_1. IPR006091. Acyl-CoA_Oxase/DH_cen-dom. IPR009075. AcylCo_DH/oxidase_C. IPR009100. AcylCoA_DH/oxidase. [Graphical view]
Pfam	PF00441. Acyl-CoA_dh_1. 1 hit. [Graphical view]
SUPFAM	SSF56645. AcylCoA_dehyd_NM. 1 hit. SSF47203. AcylCoADH_C_like. 1 hit.
PROSITE	PS00073. ACYL_COA_DH_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	35472513.

Entry information

Entry name

B4DJE7_HUMAN

Accession

Primary (citable) accession number: B4DJE7

Entry history

Integrated into UniProtKB/TrEMBL:	September 23, 2008
Last sequence update:	September 23, 2008
Last modified:	May 1, 2013
This is version 36 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.