HACD1_SHEEP
ID HACD1_SHEEP Reviewed; 288 AA.
AC Q9N1R5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 72.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1 {ECO:0000305};
DE EC=4.2.1.134 {ECO:0000250|UniProtKB:B0YJ81};
DE AltName: Full=3-hydroxyacyl-CoA dehydratase 1 {ECO:0000305};
DE Short=HACD1 {ECO:0000305};
DE AltName: Full=Protein-tyrosine phosphatase-like member A {ECO:0000305};
GN Name=HACD1; Synonyms=PTPLA {ECO:0000305};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10644438; DOI=10.1006/geno.1999.5950;
RA Uwanogho D.A., Hardcastle Z., Balogh P., Mirza G., Thornburg K.L.,
RA Ragoussis J., Sharpe P.T.;
RT "Molecular cloning, chromosomal mapping, and developmental expression of a
RT novel protein tyrosine phosphatase-like gene.";
RL Genomics 62:406-416(1999).
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:B0YJ81}.
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:B0YJ81};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45813;
CC Evidence={ECO:0000250|UniProtKB:B0YJ81};
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:B0YJ81};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39160;
CC Evidence={ECO:0000250|UniProtKB:B0YJ81};
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:B0YJ81};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39156;
CC Evidence={ECO:0000250|UniProtKB:B0YJ81};
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:B0YJ81};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39176;
CC Evidence={ECO:0000250|UniProtKB:B0YJ81};
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:B0YJ81};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39188;
CC Evidence={ECO:0000250|UniProtKB:B0YJ81};
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:B0YJ81};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39200;
CC Evidence={ECO:0000250|UniProtKB:B0YJ81};
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:B0YJ81};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39212;
CC Evidence={ECO:0000250|UniProtKB:B0YJ81};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:B0YJ81}.
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:B0YJ81}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:B0YJ81}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:B0YJ81}.
CC -!- TISSUE SPECIFICITY: Expressed in heart. {ECO:0000269|PubMed:10644438}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:B0YJ81}.
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:B0YJ81}.
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DR EMBL; AF162707; AAF29469.1; -; mRNA.
DR RefSeq; NP_001009443.1; NM_001009443.1.
DR AlphaFoldDB; Q9N1R5; -.
DR STRING; 9940.ENSOARP00000012420; -.
DR GeneID; 443484; -.
DR KEGG; oas:443484; -.
DR CTD; 9200; -.
DR eggNOG; KOG3187; Eukaryota.
DR OrthoDB; 1458293at2759; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000002356; 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 Developmental protein; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..288
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT 1"
FT /id="PRO_0000349317"
FT TOPO_DOM 1..75
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..114
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 115..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..165
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..251
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 210
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 217
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 288 AA; 32152 MW; 63B0D84D7B79EF7A CRC64;
MGRLTEAAAA GGGASAARSA GPPPAPLPLS STSPGCAAAM ASSEEDGTNG GASEASDERE
AVGKRRRLGL LATIWLTFYN IAMTAGWLVL AIAMVRFYME KGTHKGLYKS IQKTLKFFQT
FALLEIVHCL IGIVPTSVLV AGVQVSSRIF MVWLVTHSIK PIQNEESVVL FLVAWTVTEI
TRYSFYTFSL LDHLPYFIKW ARYNFFIILY PVGVAGELLT IYAALPYVKK TGMFSIRLPN
KYNVSFDYYY FLLITMASYI PLFPQLYFHM LRQRRKVLHG EVIVEKDD
