HACD3_PONAB
ID HACD3_PONAB Reviewed; 364 AA.
AC Q5NVQ2; Q5R6L7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 77.
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 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=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 {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. {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; CR860471; CAH92593.1; -; mRNA.
DR EMBL; CR925958; CAI29611.1; -; mRNA.
DR RefSeq; NP_001127566.1; NM_001134094.1.
DR AlphaFoldDB; Q5NVQ2; -.
DR SMR; Q5NVQ2; -.
DR STRING; 9601.ENSPPYP00000007450; -.
DR GeneID; 100174644; -.
DR KEGG; pon:100174644; -.
DR CTD; 51495; -.
DR eggNOG; KOG3187; Eukaryota.
DR HOGENOM; CLU_046712_0_0_1; -.
DR InParanoid; Q5NVQ2; -.
DR OrthoDB; 1458293at2759; -.
DR TreeFam; TF313326; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001595; 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: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; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..364
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT 3"
FT /id="PRO_0000313726"
FT TOPO_DOM 1..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..191
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 213..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..244
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..324
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 7..96
FT /note="CS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00547"
FT COILED 113..138
FT /evidence="ECO:0000255"
FT ACT_SITE 288
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 295
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P035"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P035"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P035"
FT CONFLICT 37
FT /note="T -> I (in Ref. 1; CAH92593)"
FT /evidence="ECO:0000305"
FT CONFLICT 274
FT /note="E -> K (in Ref. 1; CAH92593)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="V -> I (in Ref. 1; CAH92593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 43337 MW; 383BC2F70641C5D7 CRC64;
MAMENQVLTP HVYWAQRHRE LYLRVELSDV QNPAISTTEN VLHFKAQGHG AKGDNVYEFH
LEFLDLVKPE PVYKLTQRQV NITVQKKVSQ WWERLTKQEK RPLFLAPDFD RWLDESDAEM
ELRAKEEERL NKLRLESEGS PETLTNLRKG YLFMYNLVQF LGFSWIFVNL TVRFCILGKE
SFYDTFHTVA DMMYFCQMLA VVETINAAIG VTTSPVLPSL IQLLGRNFIL FIIFGTMEEM
QNKAVVFFVF YLWSAIEIFR YSFYMLTCID MDWEVLTWLR YTLWIPLYPL GCLAEAVSVV
QSIPIFNETG RFSFTLPYPV KIKVRFSFFL QIYLIMIFLG LYINFRHLYK QRRRRYGQKK
KKIH
