HACD3_BOVIN
ID HACD3_BOVIN Reviewed; 362 AA.
AC A7YY55;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3 {ECO:0000305};
DE EC=4.2.1.134 {ECO:0000250|UniProtKB:Q9P035};
DE AltName: Full=3-hydroxyacyl-CoA dehydratase 3 {ECO:0000305};
DE Short=HACD3 {ECO:0000305};
DE AltName: Full=Protein-tyrosine phosphatase-like A domain-containing protein 1 {ECO:0000305};
GN Name=HACD3 {ECO:0000305}; Synonyms=PTPLAD1 {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=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) 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. Involved in Rac1-
CC signaling pathways leading to the modulation of gene expression.
CC Promotes insulin receptor/INSR autophosphorylation and is involved in
CC INSR internalization (By similarity). {ECO:0000250|UniProtKB:Q9P035}.
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:Q9P035};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45813;
CC Evidence={ECO:0000250|UniProtKB:Q9P035};
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:Q9P035};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39160;
CC Evidence={ECO:0000250|UniProtKB:Q9P035};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000250|UniProtKB:Q9P035}.
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 RAC1. Associates with internalized insulin receptor/INSR
CC complexes on Golgi/endosomal membranes; HACD3/PTPLAD1 together with
CC ATIC and PRKAA2/AMPK2 is proposed to be part of a signaling network
CC regulating INSR autophosphorylation and endocytosis (By similarity).
CC {ECO:0000250|UniProtKB:Q9P035}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9P035}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9P035}.
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:Q9P035}.
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DR EMBL; BC151339; AAI51340.1; -; mRNA.
DR RefSeq; NP_001096786.1; NM_001103316.1.
DR AlphaFoldDB; A7YY55; -.
DR SMR; A7YY55; -.
DR STRING; 9913.ENSBTAP00000036401; -.
DR PaxDb; A7YY55; -.
DR PRIDE; A7YY55; -.
DR Ensembl; ENSBTAT00000036544; ENSBTAP00000036401; ENSBTAG00000015155.
DR GeneID; 100125237; -.
DR KEGG; bta:100125237; -.
DR CTD; 51495; -.
DR VEuPathDB; HostDB:ENSBTAG00000015155; -.
DR VGNC; VGNC:29738; HACD3.
DR eggNOG; KOG3187; Eukaryota.
DR GeneTree; ENSGT00530000062962; -.
DR HOGENOM; CLU_046712_0_0_1; -.
DR InParanoid; A7YY55; -.
DR OMA; SYLVMSH; -.
DR OrthoDB; 1458293at2759; -.
DR TreeFam; TF313326; -.
DR Reactome; R-BTA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000009136; Chromosome 10.
DR Bgee; ENSBTAG00000015155; Expressed in corpus epididymis and 106 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
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:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0007254; P:JNK cascade; IEA:Ensembl.
DR GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; IEA:Ensembl.
DR GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl.
DR GO; GO:0030148; P:sphingolipid biosynthetic process; IBA:GO_Central.
DR GO; GO:0042761; P:very long-chain fatty acid biosynthetic process; ISS:UniProtKB.
DR Gene3D; 2.60.40.790; -; 1.
DR InterPro; IPR007052; CS_dom.
DR InterPro; IPR008978; HSP20-like_chaperone.
DR InterPro; IPR007482; Tyr_Pase-like_PTPLA.
DR PANTHER; PTHR11035; PTHR11035; 1.
DR Pfam; PF04387; PTPLA; 1.
DR SUPFAM; SSF49764; SSF49764; 1.
DR PROSITE; PS51203; CS; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Lyase;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..362
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT 3"
FT /id="PRO_0000313723"
FT TOPO_DOM 1..149
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..189
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..212
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..242
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..280
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..325
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 5..94
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT COILED 111..136
FT /evidence="ECO:0000255"
FT ACT_SITE 286
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 293
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9P035"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P035"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P035"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P035"
SQ SEQUENCE 362 AA; 43133 MW; D6335E5242A2E344 CRC64;
MENQVLTPHV YWAQRHHELY LRVELSDVQN PAISITENVL HFKAQGHGAK GDNVYEFHLE
FLDLVKPEPV YKLTQRQVNI TVQKKESQWW ERLTKQEKRP LFLAPDFDRW LDESDAEMEL
RAKEEEQLNK LRLESQGSPE TLTSLKKGYL FMYNLVQFLG FSWIFVNMTV RFFILGKESF
YDTFHTVADM MYFCQMLAAV ESINAAIGVT KSPVVPSLFQ LLGRNFILFI IFGTMEEMQN
KAVVFFVFYI WSTVEIFRYP FYMLSCIDMD WKVLTWLRYT VWIPLYPMGC LAEAVSVIQS
IPVFNETGRF SFTLPYPVKI KVRFSFFLQI YLILLFLGLY VNFRYLYKQR RRRFGQKKKK
IH
