ID J3KS69_HUMAN Unreviewed; 174 AA. AC J3KS69; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 08-MAY-2019, entry version 36. DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase {ECO:0000256|RuleBase:RU363109}; DE EC=4.2.1.134 {ECO:0000256|RuleBase:RU363109}; DE Flags: Fragment; GN Name=HACD1 {ECO:0000313|Ensembl:ENSP00000462336}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000462336, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000462336, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [2] {ECO:0000313|Ensembl:ENSP00000462336} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2012) to UniProtKB. CC -!- FUNCTION: Catalyzes the third of the four reactions of the long- CC chain fatty acids elongation cycle. This endoplasmic reticulum- CC bound enzymatic process, allows the addition of two carbons to the CC chain of long- and very long-chain fatty acids/VLCFAs per cycle. CC This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA CC intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty CC acid elongation. Thereby, it participates to the production of CC VLCFAs of different chain lengths that are involved in multiple CC biological processes as precursors of membrane lipids and lipid CC mediators. {ECO:0000256|RuleBase:RU363109}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a very-long-chain (3R)-hydroxyacyl-CoA = a very-long- CC chain (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:45812, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:83728, ChEBI:CHEBI:85440; CC EC=4.2.1.134; Evidence={ECO:0000256|RuleBase:RU363109}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000256|RuleBase:RU363109}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|RuleBase:RU363109}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU363109}. CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase CC HACD family. {ECO:0000256|RuleBase:RU363109}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|RuleBase:RU363109}. 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; AC069542; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PeptideAtlas; J3KS69; -. DR PRIDE; J3KS69; -. DR Ensembl; ENST00000466335; ENSP00000462336; ENSG00000165996. DR UCSC; uc057sbo.1; human. DR HGNC; HGNC:9639; HACD1. DR OpenTargets; ENSG00000165996; -. DR eggNOG; KOG3187; Eukaryota. DR eggNOG; COG5198; LUCA. DR GeneTree; ENSGT00530000062962; -. DR UniPathway; UPA00094; -. DR ChiTaRS; HACD1; human. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000165996; Expressed in 199 organ(s), highest expression level in heart. DR ExpressionAtlas; J3KS69; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0102343; F:3-hydroxy-arachidoyl-CoA dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0102344; F:3-hydroxy-behenoyl-CoA dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0102345; F:3-hydroxy-lignoceroyl-CoA dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0102158; F:very-long-chain 3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR007482; Tyr_Pase-like_PTPLA. DR PANTHER; PTHR11035; PTHR11035; 1. DR Pfam; PF04387; PTPLA; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU363109}; KW Fatty acid biosynthesis {ECO:0000256|RuleBase:RU363109}; KW Fatty acid metabolism {ECO:0000256|RuleBase:RU363109}; KW Lipid biosynthesis {ECO:0000256|RuleBase:RU363109}; KW Lipid metabolism {ECO:0000256|RuleBase:RU363109}; KW Lyase {ECO:0000256|RuleBase:RU363109}; KW Membrane {ECO:0000256|RuleBase:RU363109}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|RuleBase:RU363109}; KW Transmembrane helix {ECO:0000256|RuleBase:RU363109}. FT TRANSMEM 42 65 Helical. {ECO:0000256|RuleBase:RU363109}. FT TRANSMEM 86 106 Helical. {ECO:0000256|RuleBase:RU363109}. FT NON_TER 1 1 {ECO:0000313|Ensembl:ENSP00000462336}. SQ SEQUENCE 174 AA; 19719 MW; 64B1506E9B193B80 CRC64; XCAATMASSD EDGTNGGASE AGEDREAPGE RRRLGVLATA WLTFYDIAMT AGWLVLAIAM VRFYMEKGTH RGLYKSIQKT LKFFQTFALL EIVHCLIGIV PTSVIVTGVQ VSSRIFMVWL ITHSIKPIQN EESVVLFLVA WTVTEITRYS FYTFSLLDHL PYFIKWARWR YLAV //