ACD11_CAEEL
ID ACD11_CAEEL Reviewed; 617 AA.
AC Q9XWZ2; Q3T978;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Acyl-CoA dehydrogenase family member 11 {ECO:0000312|WormBase:Y45F3A.3a};
DE EC=1.3.99.- {ECO:0000305};
GN Name=acdh-11 {ECO:0000312|WormBase:Y45F3A.3a};
GN ORFNames=Y45F3A.3 {ECO:0000312|WormBase:Y45F3A.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0007744|PDB:4Y9J, ECO:0007744|PDB:4Y9L}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 19-611 IN COMPLEX WITH
RP ACYL-COENZYME A, FUNCTION, SUBUNIT, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLU-91; SER-156; GLY-158; GLY-214; GLY-443 AND ARG-455.
RX PubMed=25981666; DOI=10.1016/j.cell.2015.04.026;
RA Ma D.K., Li Z., Lu A.Y., Sun F., Chen S., Rothe M., Menzel R., Sun F.,
RA Horvitz H.R.;
RT "Acyl-CoA dehydrogenase drives heat adaptation by sequestering fatty
RT acids.";
RL Cell 161:1152-1163(2015).
CC -!- FUNCTION: Promotes adaption to elevated temperatures by regulating
CC expression of the lipid desaturase, fat-7. Binds selectively and with
CC high affinity to fatty acids with chain lengths from C10 to C12 and
CC prevents them from activating fat-7 expression mediated by the nuclear
CC hormone receptor nhr-49, leading to low levels of membrane lipid
CC desaturation and membrane fluidity for adaption to heat.
CC {ECO:0000269|PubMed:25981666}.
CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000269|PubMed:25981666}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y45F3A.3a};
CC IsoId=Q9XWZ2-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y45F3A.3b};
CC IsoId=Q9XWZ2-2; Sequence=VSP_057934;
CC -!- INDUCTION: By heat. Two-fold induction at 25 degrees Celsius compared
CC with 15 degrees Celsius. {ECO:0000269|PubMed:25981666}.
CC -!- DISRUPTION PHENOTYPE: Temperature-sensitive mutants in which embryos
CC develop to adulthood at 15 and 20 degrees Celsius, but have a poor
CC survival incidence at 25 degrees Celsius. Mutants have increased
CC membrane fluidity and abnormal compositions of fatty acid species.
CC {ECO:0000269|PubMed:25981666}.
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000255|RuleBase:RU004309}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284603; CAA21490.1; -; Genomic_DNA.
DR EMBL; BX284603; CAJ30236.1; -; Genomic_DNA.
DR PIR; T26942; T26942.
DR RefSeq; NP_001033378.1; NM_001038289.3. [Q9XWZ2-1]
DR RefSeq; NP_001033379.1; NM_001038290.2.
DR PDB; 4Y9J; X-ray; 1.80 A; A/B=19-611.
DR PDB; 4Y9L; X-ray; 2.27 A; A/B=19-611.
DR PDBsum; 4Y9J; -.
DR PDBsum; 4Y9L; -.
DR AlphaFoldDB; Q9XWZ2; -.
DR SMR; Q9XWZ2; -.
DR STRING; 6239.Y45F3A.3a.2; -.
DR EPD; Q9XWZ2; -.
DR PaxDb; Q9XWZ2; -.
DR PeptideAtlas; Q9XWZ2; -.
DR EnsemblMetazoa; Y45F3A.3a.1; Y45F3A.3a.1; WBGene00012860. [Q9XWZ2-1]
DR EnsemblMetazoa; Y45F3A.3b.1; Y45F3A.3b.1; WBGene00012860. [Q9XWZ2-2]
DR GeneID; 176477; -.
DR KEGG; cel:CELE_Y45F3A.3; -.
DR UCSC; Y45F3A.3a.1; c. elegans.
DR CTD; 176477; -.
DR WormBase; Y45F3A.3a; CE19166; WBGene00012860; acdh-11. [Q9XWZ2-1]
DR WormBase; Y45F3A.3b; CE39116; WBGene00012860; acdh-11. [Q9XWZ2-2]
DR eggNOG; KOG0137; Eukaryota.
DR GeneTree; ENSGT00640000091701; -.
DR InParanoid; Q9XWZ2; -.
DR OMA; GNVQCLD; -.
DR OrthoDB; 1115216at2759; -.
DR PhylomeDB; Q9XWZ2; -.
DR PRO; PR:Q9XWZ2; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00012860; Expressed in embryo and 4 other tissues.
DR GO; GO:0005504; F:fatty acid binding; IMP:WormBase.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:1990845; P:adaptive thermogenesis; IMP:WormBase.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR CDD; cd01154; AidB; 1.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom.
DR InterPro; IPR034184; AidB.
DR InterPro; IPR041504; AidB_N.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF18158; AidB_N; 1.
DR SUPFAM; SSF47203; SSF47203; 1.
DR SUPFAM; SSF56645; SSF56645; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; FAD; Fatty acid metabolism;
KW Flavoprotein; Lipid metabolism; Nucleotide-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..617
FT /note="Acyl-CoA dehydrogenase family member 11"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434437"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 206..215
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0007744|PDB:4Y9J, ECO:0007744|PDB:4Y9L"
FT BINDING 215
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4Y9J"
FT BINDING 241..243
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0007744|PDB:4Y9J, ECO:0007744|PDB:4Y9L"
FT BINDING 267
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4Y9J"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0007744|PDB:4Y9J"
FT BINDING 359
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0007744|PDB:4Y9J, ECO:0007744|PDB:4Y9L"
FT BINDING 366..369
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0007744|PDB:4Y9J, ECO:0007744|PDB:4Y9L"
FT BINDING 437
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0007744|PDB:4Y9L"
FT BINDING 441
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0007744|PDB:4Y9J, ECO:0007744|PDB:4Y9L"
FT BINDING 464..466
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0007744|PDB:4Y9J, ECO:0007744|PDB:4Y9L"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057934"
FT MUTAGEN 91
FT /note="E->K: In n5655; suppresses the defects in egg-laying
FT and response to reoxygenation of paqr-2 mutants."
FT /evidence="ECO:0000269|PubMed:25981666"
FT MUTAGEN 156
FT /note="S->F: In n5657; suppresses the defects in egg-laying
FT and response to reoxygenation of paqr-2 mutants."
FT /evidence="ECO:0000269|PubMed:25981666"
FT MUTAGEN 158
FT /note="G->R: In n5661; suppresses the defects in egg-laying
FT and response to reoxygenation of paqr-2 mutants."
FT /evidence="ECO:0000269|PubMed:25981666"
FT MUTAGEN 214
FT /note="G->E: In n5879; suppresses the defects in egg-laying
FT and response to reoxygenation of paqr-2 mutants."
FT /evidence="ECO:0000269|PubMed:25981666"
FT MUTAGEN 443
FT /note="G->R: In n5877; suppresses the defects in egg-laying
FT and response to reoxygenation of paqr-2 mutants."
FT /evidence="ECO:0000269|PubMed:25981666"
FT MUTAGEN 455
FT /note="R->H: In n5876; suppresses the defects in egg-laying
FT and response to reoxygenation of paqr-2 mutants."
FT /evidence="ECO:0000269|PubMed:25981666"
FT HELIX 24..26
FT /evidence="ECO:0007829|PDB:4Y9J"
FT TURN 45..48
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 52..59
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 62..81
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:4Y9J"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:4Y9J"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:4Y9J"
FT TURN 126..129
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 139..153
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:4Y9J"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:4Y9J"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 184..193
FT /evidence="ECO:0007829|PDB:4Y9J"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:4Y9J"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:4Y9J"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:4Y9J"
FT STRAND 232..243
FT /evidence="ECO:0007829|PDB:4Y9J"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:4Y9J"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:4Y9J"
FT STRAND 284..292
FT /evidence="ECO:0007829|PDB:4Y9J"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:4Y9J"
FT STRAND 303..317
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 322..327
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 330..356
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 370..402
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 407..437
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 438..444
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 446..448
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 450..457
FT /evidence="ECO:0007829|PDB:4Y9J"
FT TURN 458..464
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 467..478
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 483..496
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 504..528
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 530..535
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 538..541
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 542..562
FT /evidence="ECO:0007829|PDB:4Y9J"
FT TURN 565..567
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 570..581
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 590..593
FT /evidence="ECO:0007829|PDB:4Y9J"
FT HELIX 595..605
FT /evidence="ECO:0007829|PDB:4Y9J"
FT TURN 606..608
FT /evidence="ECO:0007829|PDB:4Y9J"
SQ SEQUENCE 617 AA; 68292 MW; F77640C47829B6D2 CRC64;
MHRIGNAVRM ASSSSANATI TARHTQYSHA KTGGFSQTGP TLHNPYKDDP ILDRTLRRLL
PESEYMRVAA DLSKFGDRIT SEVEHLGRQA ELEQPRLEHQ DAWGKRVDKL IVCNEWHKLK
QICAEEGVIS IGYEDSVDPF VRRIHQVAKL FLFSPSAGLV SCPMAMTDGA VKTLTSLNLY
GKHKLATEAV DRLRSRDPSK AWTSGQWMTE KKGGSDVAGG CDTYAVQIDK DTYRLHGYKW
FSSAVDADVA LTLARIVDSD GNALEGSRGL SLFLLKIRDE SGNLNGIQMV RLKNKLGTKQ
LPTAELLLDG AIAERIGDQG RGVAGISNML NITRIHNAVA SLGYMRRIIS LARDYSTKRV
VFGQTQSKWP LHTTTLAKME VDTRGSMLLL FEAARLLGLS EAGKSSDVEA MMLRLITPVL
KLYAGKQAVP MVSEGIECFG GQGYMEDTGL PTLLRDAQVT PIWEGTTNVL SLDVLRVFSG
KENILLAFGK RVEQLLGNTK TEDEKLKKSK EAVESALKQL QKLLVKASDS AIQGETRIDS
VARHIAFTIA RIYSGALLID HASDSSVANQ SDIEVAYRYC CEQPLIDLRW EWFASERVKA
DREIVFDNFT ALEKSKI
