HACD4_XENLA
ID HACD4_XENLA Reviewed; 218 AA.
AC Q6GNB5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase {ECO:0000305};
DE EC=4.2.1.134 {ECO:0000250|UniProtKB:Q9P035};
DE AltName: Full=3-hydroxyacyl-CoA dehydratase {ECO:0000305};
DE Short=HACD {ECO:0000305};
DE AltName: Full=Protein-tyrosine phosphatase-like A domain-containing protein 2 {ECO:0000305};
GN Name=hacd4 {ECO:0000305};
GN Synonyms=hacd {ECO:0000305}, ptplad2 {ECO:0000305};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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:Q5VWC8}.
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:Q5VWC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45813;
CC Evidence={ECO:0000250|UniProtKB:Q5VWC8};
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:0000250|UniProtKB:Q5VWC8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39160;
CC Evidence={ECO:0000250|UniProtKB:Q5VWC8};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q5VWC8}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q5VWC8}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q5VWC8}.
CC -!- SIMILARITY: Belongs to the very long-chain fatty acids dehydratase HACD
CC family. {ECO:0000305}.
CC -!- CAUTION: Shares some similarity with tyrosine phosphatase proteins but
CC it has probably no phosphatase activity.
CC {ECO:0000250|UniProtKB:Q5VWC8}.
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DR EMBL; BC073600; AAH73600.1; -; mRNA.
DR AlphaFoldDB; Q6GNB5; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
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:0018812; F:3-hydroxyacyl-CoA dehydratase activity; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR GO; GO:0102158; F:very-long-chain 3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; ISS:UniProtKB.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR11035; PTHR11035; 1.
DR Pfam; PF04387; PTPLA; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..218
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase"
FT /id="PRO_0000313732"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..38
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..96
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..178
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 202..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 141
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 148
FT /evidence="ECO:0000250|UniProtKB:P40857"
SQ SEQUENCE 218 AA; 25736 MW; CEA0D40DC6CD24CD CRC64;
MKTYLSIYYL IQFCGHSWIF TNMTTRFLFF GQDAFADTFY SIGLVMQGCQ LLSILELAHI
LLGVEQNGFL PMFLQVAERF IILFVVITSQ EEVQSKYIVC ALFFIWNLWD VIRYPYDMLA
AVDTDYSALT WLRHTWWIVA YPLSVLAEAY TIYESLPYFE SLGTYSFKMA LPVSLSFHFP
YILTLYLVLQ PVGMLYICSC LWSERKQYFQ RKLKLKKN
