ID   J3KS69_HUMAN            Unreviewed;       174 AA.
AC   J3KS69;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 57.
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:ENSP00000462336.1};
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:ENSP00000462336.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000462336.1, 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:ENSP00000462336.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) 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|RuleBase:RU363109}; Multi-pass membrane protein
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}.
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DR   EMBL; AC069542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   MassIVE; J3KS69; -.
DR   PeptideAtlas; J3KS69; -.
DR   Antibodypedia; 57457; 74 antibodies from 14 providers.
DR   Ensembl; ENST00000466335.1; ENSP00000462336.1; ENSG00000165996.14.
DR   UCSC; uc057sbo.1; human.
DR   HGNC; HGNC:9639; HACD1.
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 right ventricle and 180 other cell types or tissues.
DR   ExpressionAtlas; J3KS69; baseline and differential.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0102158; F:very-long-chain (3R)-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; VERY-LONG-CHAIN (3R)-3-HYDROXYACYL-COA DEHYDRATASE; 1.
DR   PANTHER; PTHR11035:SF22; VERY-LONG-CHAIN (3R)-3-HYDROXYACYL-COA DEHYDRATASE 1; 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|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU363109};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|RuleBase:RU363109};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU363109};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU363109};
KW   Proteomics identification {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:ENSP00000462336.1"
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
//