ID   HACD_CAEEL              Reviewed;         218 AA.
AC   O17040;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase hpo-8 {ECO:0000305};
DE            EC=4.2.1.134 {ECO:0000250|UniProtKB:P40857};
DE   AltName: Full=Probable 3-hydroxyacyl-CoA dehydratase {ECO:0000305};
GN   Name=hpo-8; ORFNames=T15B7.2;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
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).
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 in 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:0000250|UniProtKB:P40857}.
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:0000250|UniProtKB:P40857};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000250|UniProtKB:P40857}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD
CC       family. {ECO:0000305}.
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; FO080967; CCD68156.1; -; Genomic_DNA.
DR   PIR; T32252; T32252.
DR   RefSeq; NP_504740.2; NM_072339.5.
DR   AlphaFoldDB; O17040; -.
DR   BioGRID; 53176; 2.
DR   STRING; 6239.T15B7.2.2; -.
DR   EPD; O17040; -.
DR   PaxDb; O17040; -.
DR   PeptideAtlas; O17040; -.
DR   EnsemblMetazoa; T15B7.2.1; T15B7.2.1; WBGene00020517.
DR   GeneID; 188513; -.
DR   KEGG; cel:CELE_T15B7.2; -.
DR   UCSC; T15B7.2.1; c. elegans.
DR   CTD; 188513; -.
DR   WormBase; T15B7.2; CE33319; WBGene00020517; hpo-8.
DR   eggNOG; KOG3187; Eukaryota.
DR   GeneTree; ENSGT00530000062962; -.
DR   HOGENOM; CLU_034302_2_2_1; -.
DR   InParanoid; O17040; -.
DR   OMA; RADNGYG; -.
DR   OrthoDB; 1458293at2759; -.
DR   PhylomeDB; O17040; -.
DR   Reactome; R-CEL-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR   UniPathway; UPA00094; -.
DR   PRO; PR:O17040; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00020517; Expressed in larva and 4 other tissues.
DR   GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
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:0018812; F:3-hydroxyacyl-CoA dehydratase activity; IBA:GO_Central.
DR   GO; GO:0102158; F:very-long-chain 3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030497; P:fatty acid elongation; IBA:GO_Central.
DR   GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR   InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR   PANTHER; PTHR11035; PTHR11035; 1.
DR   Pfam; PF04387; PTPLA; 1.
PE   3: Inferred from homology;
KW   Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis;
KW   Lipid metabolism; Lyase; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..218
FT                   /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT                   hpo-8"
FT                   /id="PRO_0000421280"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        142
FT                   /evidence="ECO:0000250|UniProtKB:P40857"
FT   ACT_SITE        149
FT                   /evidence="ECO:0000250|UniProtKB:P40857"
SQ   SEQUENCE   218 AA;  24646 MW;  40BD907322CBBC0C CRC64;
     MSVQTYLVAY NVLQILGWSA ILVKTVLGLA NGLTWPQLYE SVEFELKIFQ TAAILEVIHA
     IVGLVRSPVG TTAMQVTSRV VLVWPILHLC STARFSIGVP LLLVAWSVTE VIRYSFYALS
     VLKQPIPYFL LYLRYTLFYV LYPMGVSGEL LTLFASLNEV DEKKILTLEM PNRLNMGISF
     WWVLIIAALS YIPGFPQLYF YMIGQRKKIL GGGSKKKQ