ID   HACD4_BOVIN             Reviewed;         231 AA.
AC   Q0P5C7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 4 {ECO:0000305};
DE            EC=4.2.1.134 {ECO:0000250|UniProtKB:Q9P035};
DE   AltName: Full=3-hydroxyacyl-CoA dehydratase 4 {ECO:0000305};
DE            Short=HACD4 {ECO:0000305};
DE   AltName: Full=Protein-tyrosine phosphatase-like A domain-containing protein 2 {ECO:0000305};
GN   Name=HACD4 {ECO:0000305}; Synonyms=PTPLAD2 {ECO:0000305};
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) 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   -!- SUBUNIT: May interact with enzymes of the ELO family (including
CC       ELOVL1); with those enzymes that mediate condensation, the first of the
CC       four steps of the reaction cycle responsible for fatty acids
CC       elongation, may be part of a larger fatty acids elongase complex.
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; BC120231; AAI20232.1; -; mRNA.
DR   RefSeq; NP_001069990.1; NM_001076522.2.
DR   AlphaFoldDB; Q0P5C7; -.
DR   STRING; 9913.ENSBTAP00000023587; -.
DR   PaxDb; Q0P5C7; -.
DR   GeneID; 618814; -.
DR   KEGG; bta:618814; -.
DR   CTD; 401494; -.
DR   eggNOG; KOG3187; Eukaryota.
DR   InParanoid; Q0P5C7; -.
DR   OrthoDB; 1458293at2759; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000009136; Unplaced.
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..231
FT                   /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT                   4"
FT                   /id="PRO_0000313729"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..56
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        78..112
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        134..135
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..189
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        211..231
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        156
FT                   /evidence="ECO:0000250|UniProtKB:P40857"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000250|UniProtKB:P40857"
SQ   SEQUENCE   231 AA;  27559 MW;  4180FB22472AACEB CRC64;
     MGPVALPTWL QPRYRKNAYL FIYYLIQFCG HSWIFTNMTV RFFSFGKDSM VDTFYAIGLV
     MQLCQSISLL ELLHIYVGIE SNHLLPRILQ LTERIIVLFM VITSQEEVQE KYVVCVLFIF
     RNLLDMVRYT YSMLSVIGIS YAVLTWFSQT LWMPIYPLCV LAEAFTIYQS LPYFESFGTY
     STKLPFDLSF YFPYVLKIYL MMLFVGMYFT YNHLYSERRD ILRVFPNKKK M