HACD2_BOVIN
ID HACD2_BOVIN Reviewed; 254 AA.
AC Q2KIP8;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 2 {ECO:0000305};
DE EC=4.2.1.134 {ECO:0000250|UniProtKB:Q6Y1H2};
DE AltName: Full=3-hydroxyacyl-CoA dehydratase 2 {ECO:0000305};
DE Short=HACD2 {ECO:0000305};
DE AltName: Full=Protein-tyrosine phosphatase-like member B {ECO:0000305};
GN Name=HACD2 {ECO:0000305}; Synonyms=PTPLB {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=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the third of the very long-chain fatty acids
CC (VLCFA) elongation four-step cycle (condensation, reduction,
CC dehydration, and reduction). This endoplasmic reticulum-elongation
CC process is characterized by the addition of two carbons to the lipid
CC chain through each cycle. This enzyme catalyzes the dehydration of the
CC 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each
CC cycle of elongation. Therefore, it participates in the production of
CC various VLCFAs involved in multiple biological processes as precursors
CC of membrane lipids and lipid mediators. {ECO:0000250|UniProtKB:Q6Y1H2}.
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:Q6Y1H2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45813;
CC Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
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:Q6Y1H2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39160;
CC Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyoctadecanoyl-CoA = (2E)-octadecenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39155, ChEBI:CHEBI:15377, ChEBI:CHEBI:71412,
CC ChEBI:CHEBI:76374; Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39156;
CC Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyeicosanoyl-CoA = (2E)-eicosenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39175, ChEBI:CHEBI:15377, ChEBI:CHEBI:74691,
CC ChEBI:CHEBI:76373; Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39176;
CC Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxydocosanoyl-CoA = (2E)-docosenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39187, ChEBI:CHEBI:15377, ChEBI:CHEBI:74692,
CC ChEBI:CHEBI:76375; Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39188;
CC Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxytetracosanoyl-CoA = (2E)-tetracosenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39199, ChEBI:CHEBI:15377, ChEBI:CHEBI:74693,
CC ChEBI:CHEBI:76377; Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39200;
CC Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(3R)-hydroxyhexacosanoyl-CoA = (2E)-hexacosenoyl-CoA + H2O;
CC Xref=Rhea:RHEA:39211, ChEBI:CHEBI:15377, ChEBI:CHEBI:74281,
CC ChEBI:CHEBI:76378; Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39212;
CC Evidence={ECO:0000250|UniProtKB:Q6Y1H2};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q6Y1H2}.
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 Interacts with BCAP31. {ECO:0000250|UniProtKB:Q6Y1H2}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q6Y1H2}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q6Y1H2}.
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:Q6Y1H2}.
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DR EMBL; BC112557; AAI12558.2; -; mRNA.
DR RefSeq; NP_001124229.1; NM_001130757.2.
DR AlphaFoldDB; Q2KIP8; -.
DR STRING; 9913.ENSBTAP00000032212; -.
DR PaxDb; Q2KIP8; -.
DR GeneID; 613886; -.
DR KEGG; bta:613886; -.
DR CTD; 201562; -.
DR eggNOG; KOG3187; Eukaryota.
DR InParanoid; Q2KIP8; -.
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:0030148; P:sphingolipid biosynthetic process; 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 Acetylation; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6Y1H2"
FT CHAIN 2..254
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT 2"
FT /id="PRO_0000349318"
FT TOPO_DOM 2..41
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..79
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..107
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..130
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 131..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 170..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..217
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 183
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6Y1H2"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 254 AA; 28422 MW; F86426F551F86115 CRC64;
MAAAAAIAAS KGNGGGGGRA GAGEASSSRR KKGPGPLTTA YLVIYNVVMT AGWLVIAVGL
VRAYLAKGSY HSLYYSIEKP LKFFQTGALL EILHCAIGIV PSSVVLTSIQ VMSRVFLIWA
VTHSVKEVQS EDSVLLFVIA WTITEIIRYS FYTFSLLNHL PYLIKWARYT LFIVLYPMGV
SGELLTIYAA LPFVRQAGLY SISLPNKYNF SFDYYAFLIL IMISYIPLFP QLYFHMIHQR
RKILSHTEEH KKFE
