ID J3KS69_HUMAN Unreviewed; 174 AA. AC J3KS69; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 19-JAN-2022, entry version 48. DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase {ECO:0000256|ARBA:ARBA00013122, ECO:0000256|RuleBase:RU363109}; DE EC=4.2.1.134 {ECO:0000256|ARBA:ARBA00013122, 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC 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., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R., Hubbard T., 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-chain CC fatty acids elongation cycle. This endoplasmic reticulum-bound CC enzymatic process, allows the addition of two carbons to the chain of CC long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme CC catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into CC trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. CC Thereby, it participates to the production of VLCFAs of different chain CC lengths that are involved in multiple biological processes as CC precursors of membrane lipids and lipid mediators. CC {ECO:0000256|RuleBase:RU363109}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(3R)-hydroxyhexadecanoyl-CoA = (2E)-hexadecenoyl-CoA + H2O; CC Xref=Rhea:RHEA:39159, ChEBI:CHEBI:15377, ChEBI:CHEBI:61526, CC ChEBI:CHEBI:74278; Evidence={ECO:0000256|ARBA:ARBA00023688}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39160; CC Evidence={ECO:0000256|ARBA:ARBA00023688}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain CC (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:45812, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:83728, ChEBI:CHEBI:85440; EC=4.2.1.134; CC Evidence={ECO:0000256|ARBA:ARBA00023727}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45813; CC Evidence={ECO:0000256|ARBA:ARBA00023727}; CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. CC {ECO:0000256|ARBA:ARBA00005194, ECO:0000256|RuleBase:RU363109}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363109}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477, CC ECO:0000256|RuleBase:RU363109}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD CC family. {ECO:0000256|ARBA:ARBA00007811, ECO:0000256|RuleBase:RU363109}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC 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 Antibodypedia; 57457; 63 antibodies from 14 providers. DR Ensembl; ENST00000466335; ENSP00000462336; ENSG00000165996. DR UCSC; uc057sbo.1; human. DR HGNC; HGNC:9639; HACD1. DR OpenTargets; ENSG00000165996; -. DR VEuPathDB; HostDB:ENSG00000165996; -. DR GeneTree; ENSGT00530000062962; -. DR HOGENOM; CLU_034302_2_1_1; -. DR UniPathway; UPA00094; -. DR ChiTaRS; HACD1; human. DR Proteomes; UP000005640; Chromosome 10. DR Bgee; ENSG00000165996; Expressed in heart and 211 other tissues. 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 1: Evidence at protein level; 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|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363109}; KW Proteomics identification {ECO:0007829|PeptideAtlas:J3KS69, KW ECO:0007829|ProteomicsDB:J3KS69}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU363109}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU363109}. FT TRANSMEM 42..65 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363109" FT TRANSMEM 86..106 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU363109" FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="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 //