HACD3_CHICK
ID HACD3_CHICK Reviewed; 362 AA.
AC Q5ZM57;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase {ECO:0000305};
DE EC=4.2.1.134 {ECO:0000250|UniProtKB:Q9P035};
DE AltName: Full=3-hydroxyacyl-CoA dehydratase {ECO:0000305};
DE Short=HACD {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};
GN ORFNames=RCJMB04_3b6 {ECO:0000312|EMBL:CAG31186.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 {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 -!- 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; AJ719527; CAG31186.1; -; mRNA.
DR RefSeq; NP_001007829.1; NM_001007828.1.
DR AlphaFoldDB; Q5ZM57; -.
DR STRING; 9031.ENSGALP00000012079; -.
DR PaxDb; Q5ZM57; -.
DR Ensembl; ENSGALT00000012093; ENSGALP00000012079; ENSGALG00000007481.
DR GeneID; 415539; -.
DR KEGG; gga:415539; -.
DR CTD; 51495; -.
DR VEuPathDB; HostDB:geneid_415539; -.
DR eggNOG; KOG3187; Eukaryota.
DR GeneTree; ENSGT00530000062962; -.
DR HOGENOM; CLU_046712_0_0_1; -.
DR InParanoid; Q5ZM57; -.
DR OMA; SYLVMSH; -.
DR OrthoDB; 1458293at2759; -.
DR PhylomeDB; Q5ZM57; -.
DR UniPathway; UPA00094; -.
DR PRO; PR:Q5ZM57; -.
DR Proteomes; UP000000539; Chromosome 10.
DR Bgee; ENSGALG00000007481; Expressed in liver and 13 other tissues.
DR ExpressionAtlas; Q5ZM57; baseline and differential.
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: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: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; 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 Coiled coil; Endoplasmic reticulum; Fatty acid biosynthesis;
KW Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Lyase;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..362
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase"
FT /id="PRO_0000313727"
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..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..319
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..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..135
FT /evidence="ECO:0000255"
FT ACT_SITE 286
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 293
FT /evidence="ECO:0000250|UniProtKB:P40857"
SQ SEQUENCE 362 AA; 42835 MW; 933F385AD50147AF CRC64;
MADCSLRPHV HWAQRHRELY LRVELSDVKN PDVSIADNVL RFRAQGHGAK GDNIYEFQIE
FLEPVEPKPV CRVTQRQLNI TVQKKESSWW ERLTKQEKRP LFLAPDFDRW LDESDAEMEL
KEKEEEKINK MKIESRVPKD PFKHLKKGYL IMYNLVQFLG FSWIFVNMTV RLFILGKDSF
YDTFHTIADM MYFCQTLALM EILNSLIGLV RSPLIPAVIQ VFGRNFILFV VLGSLEEMQS
KAVVFFLFYF WSIIELFRYP YYMLSCMGIE WKPLTWLRYT SWIPLYPLGG LAEAVCLIQS
IPIFSETGKF SLGLPNPLNV TIQFSFLLQM YLIALFLGLF VNFRYLYKQR KQHLGPKKRK
MK
