Q709F0 (ACD11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyl-CoA dehydrogenase family member 11
Short name=ACAD-11
EC=1.3.99.-

Gene names

Name:

ACAD11

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	780 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA. Ref.7
Catalytic activity	Acyl-CoA + acceptor = 2,3-dehydroacyl-CoA + reduced acceptor.
Cofactor	FAD. Ref.8
Subunit structure	Homodimer. Ref.8
Subcellular location	Peroxisome By similarity. Mitochondrion. Note: Has been detected associated with mitochondrial membrane, but no matrix, in kidney and cerebellum, as well as in a neuroblastoma cell line, but not in skin fibroblasts, where it is observed in cytoplasmic vesicles (Ref.7). No mitochondrial targeting signals could be predicted for any known isoform, including a putative isoform starting at Met-316. Ref.7
Tissue specificity	Widely expressed with highest levels in brain followed by liver, heart and kidney. Ref.7
Sequence similarities	Belongs to the acyl-CoA dehydrogenase family.
Sequence caution	The sequence BAB14158.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Mitochondrion Peroxisome
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	fatty acid beta-oxidation using acyl-CoA dehydrogenase Inferred from direct assay Ref.7. Source: UniProtKB
Cellular component	mitochondrial membrane Inferred from direct assay Ref.7. Source: UniProtKB nucleus Inferred from direct assay Ref.7. Source: UniProtKB peroxisome Inferred from sequence or structural similarity. Source: HGNC
Molecular function	flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro long-chain-acyl-CoA dehydrogenase activity Inferred from direct assay Ref.7. Source: UniProtKB medium-chain-acyl-CoA dehydrogenase activity Inferred from direct assay Ref.7. Source: UniProtKB transferase activity, transferring phosphorus-containing groups Inferred from electronic annotation. Source: InterPro very-long-chain-acyl-CoA dehydrogenase activity Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q709F0-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q709F0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     564-667: Missing.

Isoform 3 (identifier: Q709F0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-120: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 780

780

Acyl-CoA dehydrogenase family member 11

PRO_0000254145

Regions

Nucleotide binding

504 – 514

11

FAD

Nucleotide binding

504 – 507

4

FAD

Nucleotide binding

512 – 514

3

FAD

Nucleotide binding

538 – 540

3

FAD

Nucleotide binding

727 – 731

5

FAD; shared with dimeric partner

Nucleotide binding

756 – 758

3

FAD

Region

629 – 632

4

Substrate binging By similarity

Sites

Binding site

514

1

Substrate; via carbonyl oxygen By similarity

Binding site

657

1

FAD

Binding site

657

1

FAD; shared with dimeric partner

Binding site

727

1

FAD

Binding site

755

1

Substrate; via amide nitrogen

Amino acid modifications

Modified residue

324

1

Phosphotyrosine Ref.5

Natural variations

Alternative sequence

1 – 120

120

Missing in isoform 3.

VSP_021187

Alternative sequence

564 – 667

104

Missing in isoform 2.

VSP_021188

Natural variant

157

1

R → H. Ref.1 Ref.2 Ref.3 Ref.4
Corresponds to variant rs821572 [ dbSNP | Ensembl ].

VAR_028825

Natural variant

362

1

V → L.
Corresponds to variant rs6776576 [ dbSNP | Ensembl ].

VAR_028826

Experimental info

Sequence conflict

414

1

K → T in CAH56354. Ref.2

Sequence conflict

549

1

I → V in CAE55233. Ref.1

Sequence conflict

549

1

I → V in BAB14158. Ref.3

Sequence conflict

562

1

S → SRLT in CAH56228. Ref.2

Secondary structure

1

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780

Helix Strand Turn

Details...

Helix

381 – 392

12

Helix

394 – 402

9

Helix

419 – 430

12

Turn

439 – 441

3

Helix

446 – 455

10

Helix

462 – 465

4

Turn

470 – 472

3

Helix

476 – 481

6

Helix

485 – 490

6

Helix

492 – 496

5

Beta strand

501 – 505

5

Helix

516 – 518

3

Beta strand

522 – 526

5

Beta strand

529 – 533

5

Beta strand

536 – 539

4

Beta strand

547 – 552

6

Helix

563 – 565

3

Beta strand

570 – 573

4

Beta strand

580 – 584

5

Beta strand

599 – 602

4

Beta strand

605 – 609

5

Helix

610 – 612

3

Turn

622 – 624

3

Helix

633 – 639

7

Helix

643 – 656

14

Helix

664 – 666

3

Helix

668 – 697

30

Helix

704 – 728

25

Helix

740 – 750

11

Helix

757 – 776

20

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: 407DAE4DC6563070	FASTA	780	87,283
	10 20 30 40 50 60 MKPGATGESD LAEVLPQHKF DSKSLEAYLN QHLSGFGAER EATLTIAQYR AGKSNPTFYL 70 80 90 100 110 120 QKGFQTYVLR KKPPGSLLPK AHQIDREFKV QKALFSIGFP VPKPILYCSD TSVIGTEFYV 130 140 150 160 170 180 MEHVQGRIFR DLTIPGLSPA ERSAIYVATV ETLAQLRSLN IQSLQLEGYG IGAGYCKRQV 190 200 210 220 230 240 STWTKQYQAA AHQDIPAMQQ LSEWLMKNLP DNDNEENLIH GDFRLDNIVF HPKECRVIAV 250 260 270 280 290 300 LDWELSTIGH PLSDLAHFSL FYFWPRTVPM INQGSYSENS GIPSMEELIS IYCRCRGINS 310 320 330 340 350 360 ILPNWNFFLA LSYFKMAGIA QGVYSRYLLG NNSSEDSFLF ANIVQPLAET GLQLSKRTFS 370 380 390 400 410 420 TVLPQIDTTG QLFVQTRKGQ EVLIKVKHFM KQHILPAEKE VTEFYVQNEN SVDKWGKPLV 430 440 450 460 470 480 IDKLKEMAKV EGLWNLFLPA VSGLSHVDYA LIAEETGKCF FAPDVFNCQA PDTGNMEVLH 490 500 510 520 530 540 LYGSEEQKKQ WLEPLLQGNI TSCFCMTEPD VASSDATNIE CSIQRDEDSY VINGKKWWSS 550 560 570 580 590 600 GAGNPKCKIA IVLGRTQNTS LSRHKQHSMI LVPMNTPGVK IIRPLSVFGY TDNFHGGHFE 610 620 630 640 650 660 IHFNQVRVPA TNLILGEGRG FEISQGRLGP GRIHHCMRTV GLAERALQIM CERATQRIAF 670 680 690 700 710 720 KKKLYAHEVV AHWIAESRIA IEKIRLLTLK AAHSMDTLGS AGAKKEIAMI KVAAPRAVSK 730 740 750 760 770 780 IVDWAIQVCG GAGVSQDYPL ANMYAITRVL RLADGPDEVH LSAIATMELR DQAKRLTAKI
	Isoform 2 [UniParc]. Checksum: 7014E38FD5C21E8E	FASTA	676	75,517
	10 20 30 40 50 60 MKPGATGESD LAEVLPQHKF DSKSLEAYLN QHLSGFGAER EATLTIAQYR AGKSNPTFYL 70 80 90 100 110 120 QKGFQTYVLR KKPPGSLLPK AHQIDREFKV QKALFSIGFP VPKPILYCSD TSVIGTEFYV 130 140 150 160 170 180 MEHVQGRIFR DLTIPGLSPA ERSAIYVATV ETLAQLRSLN IQSLQLEGYG IGAGYCKRQV 190 200 210 220 230 240 STWTKQYQAA AHQDIPAMQQ LSEWLMKNLP DNDNEENLIH GDFRLDNIVF HPKECRVIAV 250 260 270 280 290 300 LDWELSTIGH PLSDLAHFSL FYFWPRTVPM INQGSYSENS GIPSMEELIS IYCRCRGINS 310 320 330 340 350 360 ILPNWNFFLA LSYFKMAGIA QGVYSRYLLG NNSSEDSFLF ANIVQPLAET GLQLSKRTFS 370 380 390 400 410 420 TVLPQIDTTG QLFVQTRKGQ EVLIKVKHFM KQHILPAEKE VTEFYVQNEN SVDKWGKPLV 430 440 450 460 470 480 IDKLKEMAKV EGLWNLFLPA VSGLSHVDYA LIAEETGKCF FAPDVFNCQA PDTGNMEVLH 490 500 510 520 530 540 LYGSEEQKKQ WLEPLLQGNI TSCFCMTEPD VASSDATNIE CSIQRDEDSY VINGKKWWSS 550 560 570 580 590 600 GAGNPKCKIA IVLGRTQNTS LSREVVAHWI AESRIAIEKI RLLTLKAAHS MDTLGSAGAK 610 620 630 640 650 660 KEIAMIKVAA PRAVSKIVDW AIQVCGGAGV SQDYPLANMY AITRVLRLAD GPDEVHLSAI 670 ATMELRDQAK RLTAKI
	Isoform 3 [UniParc]. Checksum: 46963EAAC8967AF6	FASTA	660	73,920
	10 20 30 40 50 60 MEHVQGRIFR DLTIPGLSPA ERSAIYVATV ETLAQLRSLN IQSLQLEGYG IGAGYCKRQV 70 80 90 100 110 120 STWTKQYQAA AHQDIPAMQQ LSEWLMKNLP DNDNEENLIH GDFRLDNIVF HPKECRVIAV 130 140 150 160 170 180 LDWELSTIGH PLSDLAHFSL FYFWPRTVPM INQGSYSENS GIPSMEELIS IYCRCRGINS 190 200 210 220 230 240 ILPNWNFFLA LSYFKMAGIA QGVYSRYLLG NNSSEDSFLF ANIVQPLAET GLQLSKRTFS 250 260 270 280 290 300 TVLPQIDTTG QLFVQTRKGQ EVLIKVKHFM KQHILPAEKE VTEFYVQNEN SVDKWGKPLV 310 320 330 340 350 360 IDKLKEMAKV EGLWNLFLPA VSGLSHVDYA LIAEETGKCF FAPDVFNCQA PDTGNMEVLH 370 380 390 400 410 420 LYGSEEQKKQ WLEPLLQGNI TSCFCMTEPD VASSDATNIE CSIQRDEDSY VINGKKWWSS 430 440 450 460 470 480 GAGNPKCKIA IVLGRTQNTS LSRHKQHSMI LVPMNTPGVK IIRPLSVFGY TDNFHGGHFE 490 500 510 520 530 540 IHFNQVRVPA TNLILGEGRG FEISQGRLGP GRIHHCMRTV GLAERALQIM CERATQRIAF 550 560 570 580 590 600 KKKLYAHEVV AHWIAESRIA IEKIRLLTLK AAHSMDTLGS AGAKKEIAMI KVAAPRAVSK 610 620 630 640 650 660 IVDWAIQVCG GAGVSQDYPL ANMYAITRVL RLADGPDEVH LSAIATMELR DQAKRLTAKI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Presence of an acyl-CoA dehydrogenase in mammalian peroxisomes ?" Mahieu V., Van Veldhoven P.P. Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT HIS-157.
[2]	"The full-ORF clone resource of the German cDNA consortium." 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. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-780 (ISOFORM 1), VARIANT HIS-157. Tissue: Lymph node and Stomach.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-563 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 343-780 (ISOFORM 1), VARIANT HIS-157. Tissue: Tongue.
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT HIS-157. Tissue: Cervix.
[5]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-324, MASS SPECTROMETRY.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"Identification and characterization of new long chain acyl-CoA dehydrogenases." He M., Pei Z., Mohsen A.W., Watkins P., Murdoch G., Van Veldhoven P.P., Ensenauer R., Vockley J. Mol. Genet. Metab. 102:418-429(2011) [PubMed: 21237683] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[8]	"Crystal structure of human acyl-CoA dehydrogenase 11." Structural genomics consortium (SGC) Submitted (MAY-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 355-780 IN COMPLEX WITH FAD, COFACTOR, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ608287 mRNA. Translation: CAE55233.1.
AL833721 mRNA. Translation: CAH56228.1.
AL832873 mRNA. Translation: CAH56354.1.
AK022654 mRNA. Translation: BAB14158.1. Different initiation.
AK131265 mRNA. Translation: BAD18443.1.
BC019607 mRNA. Translation: AAH19607.2.
BC125204 mRNA. Translation: AAI25205.1.

IPI

IPI00420065.
IPI00795974.
IPI00796584.

RefSeq

NP_115545.3. NM_032169.4.

UniGene

Hs.441378.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2WBI	X-ray	2.80	A/B	355-780	[»]

ProteinModelPortal

Q709F0.

SMR

Q709F0. Positions 19-358, 374-776.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q709F0. 2 interactions.

PTM databases

PhosphoSite

Q709F0.

Polymorphism databases

DMDM

117949774.

Proteomic databases

PRIDE

Q709F0.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264990; ENSP00000264990; ENSG00000240303.

GeneID

84129.

KEGG

hsa:84129.

NMPDR

fig|9606.3.peg.23204.

UCSC

uc003eov.2. human.

Organism-specific databases

CTD

84129.

GeneCards

GC03M132276.

HGNC

HGNC:30211. ACAD11.

MIM

614288. gene.

neXtProt

NX_Q709F0.

PharmGKB

PA142672658.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00590000082906.

HOVERGEN

HBG057142.

OMA

DNIVFHP.

OrthoDB

EOG42RD6H.

PhylomeDB

Q709F0.

Gene expression databases

ArrayExpress

Q709F0.

Bgee

Q709F0.

CleanEx

HS_ACAD11.

Genevestigator

Q709F0.

GermOnline

ENSG00000113971. Homo sapiens.

Family and domain databases

InterPro

IPR006092. Acyl-CoA_DH_N.
IPR006090. Acyl-CoA_Oxase/DH_1.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase.
IPR002575. Aminoglycoside_PTrfase.
IPR011009. Kinase-like_dom.
[Graphical view]

Gene3D

G3DSA:2.40.110.10. Acyl_CoA_DH/ox_M. 1 hit.
G3DSA:1.10.540.10. AcylCoA_DH/ox_N. 1 hit.
G3DSA:1.20.140.10. AcylCoA_DH_1/2_C. 1 hit.

KO

K11730.

Pfam

PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
PF01636. APH. 1 hit.
[Graphical view]

SUPFAM

SSF56645. AcylCoA_dehyd_NM. 1 hit.
SSF47203. AcylCoADH_C_like. 1 hit.
SSF56112. Kinase_like. 1 hit.

ProtoNet

Search...

Other

NextBio

73411.

SOURCE

Search...

Entry information

Entry name

ACD11_HUMAN

Accession

Primary (citable) accession number: Q709F0
Secondary accession number(s): Q08AF0 , Q658N9, Q658Y2, Q6ZND2, Q8WUT6, Q9H9R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	January 25, 2012
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.