HACD2_PONAB
ID HACD2_PONAB Reviewed; 255 AA.
AC Q5RBK3;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 70.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR858641; CAH90857.1; -; mRNA.
DR RefSeq; NP_001125489.1; NM_001132017.1.
DR AlphaFoldDB; Q5RBK3; -.
DR STRING; 9601.ENSPPYP00000015068; -.
DR Ensembl; ENSPPYT00000046269; ENSPPYP00000044289; ENSPPYG00000037558.
DR GeneID; 100172398; -.
DR KEGG; pon:100172398; -.
DR CTD; 201562; -.
DR eggNOG; KOG3187; Eukaryota.
DR GeneTree; ENSGT00530000062962; -.
DR HOGENOM; CLU_034302_2_0_1; -.
DR InParanoid; Q5RBK3; -.
DR OMA; RADNGYG; -.
DR OrthoDB; 1458293at2759; -.
DR TreeFam; TF313326; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001595; Chromosome 3.
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 Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism;
KW Glycoprotein; Lipid biosynthesis; Lipid metabolism; Lyase; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..255
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT 2"
FT /id="PRO_0000349321"
FT TOPO_DOM 3..42
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..80
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..131
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 148..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..218
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..236
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 237..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 11..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 184
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 255 AA; 28411 MW; 6B345134C695AFB7 CRC64;
MAAAAAATAA AKGNGGGGGR AGAGDASGTR KKKGPGPLAT AYLVIYNVVM TAGWLVIAVG
LVRAYLAKGS YHSLYYSIEK PLKFFQTGAL LEILHCAIGI VPSSVVLTSF QVMSRVFLIW
AVTHSVKEVQ SEDSVLLFVI AWTITEIIRY SFYTFSLLNH LPYLIKWARY TLFIVLYPMG
VSGELLTIYA ALPFVRQAGL YSISLPNKYN FSFDYYAFLI LIMISYIPIF PQLYFHMIHQ
RRKILSHTEE HKKFE
