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Protein

Acyl-CoA dehydrogenase family member 11

Gene

ACAD11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acyl-CoA dehydrogenase, that exhibits maximal activity towards saturated C22-CoA.1 Publication

Catalytic activityi

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

Cofactori

FAD1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei514Substrate; via carbonyl oxygenBy similarity1
Binding sitei657FAD1 Publication1
Binding sitei657FAD; shared with dimeric partner1 Publication1
Binding sitei727FAD1 Publication1
Binding sitei755Substrate; via amide nitrogen1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi504 – 514FAD1 PublicationAdd BLAST11
Nucleotide bindingi538 – 540FAD1 Publication3
Nucleotide bindingi727 – 731FAD; shared with dimeric partner1 Publication5
Nucleotide bindingi756 – 758FAD1 Publication3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

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

Chemistry databases

SwissLipidsiSLP:000001326.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyl-CoA dehydrogenase family member 11 (EC:1.3.99.-)
Short name:
ACAD-11
Gene namesi
Name:ACAD11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:30211. ACAD11.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial inner membrane Source: Reactome
  • mitochondrial membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • peroxisome Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142672658.

Polymorphism and mutation databases

BioMutaiACAD11.
DMDMi117949774.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002541451 – 780Acyl-CoA dehydrogenase family member 11Add BLAST780

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei177N6-acetyllysineBy similarity1
Modified residuei324PhosphotyrosineBy similarity1
Modified residuei391N6-succinyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ709F0.
MaxQBiQ709F0.
PaxDbiQ709F0.
PeptideAtlasiQ709F0.
PRIDEiQ709F0.

PTM databases

iPTMnetiQ709F0.
PhosphoSitePlusiQ709F0.

Expressioni

Tissue specificityi

Widely expressed with highest levels in brain followed by liver, heart and kidney.1 Publication

Gene expression databases

BgeeiENSG00000240303.
CleanExiHS_ACAD11.
ExpressionAtlasiQ709F0. baseline and differential.
GenevisibleiQ709F0. HS.

Organism-specific databases

HPAiHPA048317.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi123902. 44 interactors.
IntActiQ709F0. 11 interactors.
STRINGi9606.ENSP00000264990.

Structurei

Secondary structure

1780
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi377 – 392Combined sources16
Helixi394 – 402Combined sources9
Helixi404 – 408Combined sources5
Helixi419 – 430Combined sources12
Helixi439 – 442Combined sources4
Helixi446 – 456Combined sources11
Helixi462 – 465Combined sources4
Helixi472 – 482Combined sources11
Helixi485 – 490Combined sources6
Helixi492 – 497Combined sources6
Beta strandi499 – 505Combined sources7
Helixi516 – 518Combined sources3
Beta strandi522 – 526Combined sources5
Beta strandi529 – 540Combined sources12
Turni541 – 543Combined sources3
Beta strandi547 – 555Combined sources9
Helixi563 – 565Combined sources3
Beta strandi567 – 573Combined sources7
Beta strandi579 – 584Combined sources6
Helixi593 – 595Combined sources3
Beta strandi598 – 609Combined sources12
Helixi610 – 612Combined sources3
Helixi620 – 656Combined sources37
Helixi664 – 666Combined sources3
Helixi668 – 702Combined sources35
Helixi704 – 728Combined sources25
Helixi730 – 734Combined sources5
Helixi740 – 750Combined sources11
Turni751 – 754Combined sources4
Helixi757 – 776Combined sources20

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WBIX-ray2.80A/B355-780[»]
ProteinModelPortaliQ709F0.
SMRiQ709F0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ709F0.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni629 – 632Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG410IIP9. Eukaryota.
COG3173. LUCA.
HOVERGENiHBG057142.
InParanoidiQ709F0.
KOiK11730.
OrthoDBiEOG091G03B8.
PhylomeDBiQ709F0.
TreeFamiTF333953.

Family and domain databases

Gene3Di1.10.540.10. 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.
IPR011009. Kinase-like_dom.
[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.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF56645. SSF56645. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q709F0-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MKPGATGESD LAEVLPQHKF DSKSLEAYLN QHLSGFGAER EATLTIAQYR
60 70 80 90 100
AGKSNPTFYL QKGFQTYVLR KKPPGSLLPK AHQIDREFKV QKALFSIGFP
110 120 130 140 150
VPKPILYCSD TSVIGTEFYV MEHVQGRIFR DLTIPGLSPA ERSAIYVATV
160 170 180 190 200
ETLAQLRSLN IQSLQLEGYG IGAGYCKRQV STWTKQYQAA AHQDIPAMQQ
210 220 230 240 250
LSEWLMKNLP DNDNEENLIH GDFRLDNIVF HPKECRVIAV LDWELSTIGH
260 270 280 290 300
PLSDLAHFSL FYFWPRTVPM INQGSYSENS GIPSMEELIS IYCRCRGINS
310 320 330 340 350
ILPNWNFFLA LSYFKMAGIA QGVYSRYLLG NNSSEDSFLF ANIVQPLAET
360 370 380 390 400
GLQLSKRTFS TVLPQIDTTG QLFVQTRKGQ EVLIKVKHFM KQHILPAEKE
410 420 430 440 450
VTEFYVQNEN SVDKWGKPLV IDKLKEMAKV EGLWNLFLPA VSGLSHVDYA
460 470 480 490 500
LIAEETGKCF FAPDVFNCQA PDTGNMEVLH LYGSEEQKKQ WLEPLLQGNI
510 520 530 540 550
TSCFCMTEPD VASSDATNIE CSIQRDEDSY VINGKKWWSS GAGNPKCKIA
560 570 580 590 600
IVLGRTQNTS LSRHKQHSMI LVPMNTPGVK IIRPLSVFGY TDNFHGGHFE
610 620 630 640 650
IHFNQVRVPA TNLILGEGRG FEISQGRLGP GRIHHCMRTV GLAERALQIM
660 670 680 690 700
CERATQRIAF KKKLYAHEVV AHWIAESRIA IEKIRLLTLK AAHSMDTLGS
710 720 730 740 750
AGAKKEIAMI KVAAPRAVSK IVDWAIQVCG GAGVSQDYPL ANMYAITRVL
760 770 780
RLADGPDEVH LSAIATMELR DQAKRLTAKI
Length:780
Mass (Da):87,283
Last modified:October 31, 2006 - v2
Checksum:i407DAE4DC6563070
GO
Isoform 2 (identifier: Q709F0-2) [UniParc]FASTAAdd to basket

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

Show »
Length:676
Mass (Da):75,517
Checksum:i7014E38FD5C21E8E
GO
Isoform 3 (identifier: Q709F0-3) [UniParc]FASTAAdd to basket

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

Show »
Length:660
Mass (Da):73,920
Checksum:i46963EAAC8967AF6
GO

Sequence cautioni

The sequence BAB14158 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti414K → T in CAH56354 (PubMed:17974005).Curated1
Sequence conflicti549I → V in CAE55233 (Ref. 1) Curated1
Sequence conflicti549I → V in BAB14158 (PubMed:14702039).Curated1
Sequence conflicti562S → SRLT in CAH56228 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_028825157R → H.4 PublicationsCorresponds to variant rs821572dbSNPEnsembl.1
Natural variantiVAR_028826362V → L.Corresponds to variant rs6776576dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0211871 – 120Missing in isoform 3. 1 PublicationAdd BLAST120
Alternative sequenceiVSP_021188564 – 667Missing in isoform 2. 1 PublicationAdd BLAST104

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3074.1. [Q709F0-1]
RefSeqiNP_115545.3. NM_032169.4.
UniGeneiHs.441378.

Genome annotation databases

EnsembliENST00000264990; ENSP00000264990; ENSG00000240303.
GeneIDi84129.
KEGGihsa:84129.
UCSCiuc003eov.5. human. [Q709F0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS3074.1. [Q709F0-1]
RefSeqiNP_115545.3. NM_032169.4.
UniGeneiHs.441378.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2WBIX-ray2.80A/B355-780[»]
ProteinModelPortaliQ709F0.
SMRiQ709F0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123902. 44 interactors.
IntActiQ709F0. 11 interactors.
STRINGi9606.ENSP00000264990.

Chemistry databases

SwissLipidsiSLP:000001326.

PTM databases

iPTMnetiQ709F0.
PhosphoSitePlusiQ709F0.

Polymorphism and mutation databases

BioMutaiACAD11.
DMDMi117949774.

Proteomic databases

EPDiQ709F0.
MaxQBiQ709F0.
PaxDbiQ709F0.
PeptideAtlasiQ709F0.
PRIDEiQ709F0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264990; ENSP00000264990; ENSG00000240303.
GeneIDi84129.
KEGGihsa:84129.
UCSCiuc003eov.5. human. [Q709F0-1]

Organism-specific databases

CTDi84129.
GeneCardsiACAD11.
HGNCiHGNC:30211. ACAD11.
HPAiHPA048317.
MIMi614288. gene.
neXtProtiNX_Q709F0.
PharmGKBiPA142672658.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIP9. Eukaryota.
COG3173. LUCA.
HOVERGENiHBG057142.
InParanoidiQ709F0.
KOiK11730.
OrthoDBiEOG091G03B8.
PhylomeDBiQ709F0.
TreeFamiTF333953.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiACAD11. human.
EvolutionaryTraceiQ709F0.
GenomeRNAii84129.
PROiQ709F0.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000240303.
CleanExiHS_ACAD11.
ExpressionAtlasiQ709F0. baseline and differential.
GenevisibleiQ709F0. HS.

Family and domain databases

Gene3Di1.10.540.10. 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.
IPR011009. Kinase-like_dom.
[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.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56112. SSF56112. 1 hit.
SSF56645. SSF56645. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiACD11_HUMAN
AccessioniPrimary (citable) accession number: Q709F0
Secondary accession number(s): Q08AF0
, Q658N9, Q658Y2, Q6ZND2, Q8WUT6, Q9H9R3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: November 30, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.