HACD1_MOUSE
ID HACD1_MOUSE Reviewed; 281 AA.
AC Q9QY80; Q9D6P7;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
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:0000312|MGI:MGI:1353592};
GN Name=Hacd1 {ECO:0000312|MGI:MGI:1353592}; Synonyms=Ptpla;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP EXPRESSION.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-281.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=12466851; DOI=10.1038/nature01266;
RA Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S.,
RA Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H.,
RA Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T.,
RA Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J., Schriml L.M.,
RA Kanapin A., Matsuda H., Batalov S., Beisel K.W., Blake J.A., Bradt D.,
RA Brusic V., Chothia C., Corbani L.E., Cousins S., Dalla E., Dragani T.A.,
RA Fletcher C.F., Forrest A., Frazer K.S., Gaasterland T., Gariboldi M.,
RA Gissi C., Godzik A., Gough J., Grimmond S., Gustincich S., Hirokawa N.,
RA Jackson I.J., Jarvis E.D., Kanai A., Kawaji H., Kawasawa Y.,
RA Kedzierski R.M., King B.L., Konagaya A., Kurochkin I.V., Lee Y.,
RA Lenhard B., Lyons P.A., Maglott D.R., Maltais L., Marchionni L.,
RA McKenzie L., Miki H., Nagashima T., Numata K., Okido T., Pavan W.J.,
RA Pertea G., Pesole G., Petrovsky N., Pillai R., Pontius J.U., Qi D.,
RA Ramachandran S., Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z.,
RA Ringwald M., Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K.,
RA Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M., Verardo R.,
RA Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C., Wilming L.G.,
RA Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L., Yuan Z., Zavolan M.,
RA Zhu Y., Zimmer A., Carninci P., Hayatsu N., Hirozane-Kishikawa T.,
RA Konno H., Nakamura M., Sakazume N., Sato K., Shiraki T., Waki K., Kawai J.,
RA Aizawa K., Arakawa T., Fukuda S., Hara A., Hashizume W., Imotani K.,
RA Ishii Y., Itoh M., Kagawa I., Miyazaki A., Sakai K., Sasaki D., Shibata K.,
RA Shinagawa A., Yasunishi A., Yoshino M., Waterston R., Lander E.S.,
RA Rogers J., Birney E., Hayashizaki Y.;
RT "Analysis of the mouse transcriptome based on functional annotation of
RT 60,770 full-length cDNAs.";
RL Nature 420:563-573(2002).
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 at high levels in heart, skeletal muscle
CC and testis, weak expression in kidney and liver.
CC {ECO:0000269|PubMed:10644438}.
CC -!- DEVELOPMENTAL STAGE: Differentially expressed during embryogenesis.
CC First detected throughout the somites at 8.5 dpc and in the myotome at
CC 11.5 dpc. Expression was observed in muscles ventral to the developing
CC vertebral column of the neck, thorax, abdomen and tail. Expression was
CC maintained in skeletal muscle types well after the terminal
CC differentiation of muscle fibers. During cardiac development,
CC expression was restricted to the myocytes of the primitive heart tube,
CC and by 10.5 dpc, it was expressed in the muscles throughout all the
CC cardiac chambers. At this last stage it is also detected in the hepatic
CC primordia, and later in embryonic liver. By 15.5 expression was also
CC observed in the smooth muscle surrounding the digestive, respiratory
CC and urogenital tracts.
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; AF114493; AAF21975.1; -; mRNA.
DR EMBL; AL844560; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK010119; BAB26713.1; -; mRNA.
DR RefSeq; NP_038963.3; NM_013935.3.
DR AlphaFoldDB; Q9QY80; -.
DR IntAct; Q9QY80; 1.
DR STRING; 10090.ENSMUSP00000110401; -.
DR GlyGen; Q9QY80; 1 site.
DR iPTMnet; Q9QY80; -.
DR PhosphoSitePlus; Q9QY80; -.
DR MaxQB; Q9QY80; -.
DR PaxDb; Q9QY80; -.
DR PRIDE; Q9QY80; -.
DR ProteomicsDB; 270930; -.
DR DNASU; 30963; -.
DR GeneID; 30963; -.
DR KEGG; mmu:30963; -.
DR UCSC; uc008ikd.1; mouse.
DR CTD; 9200; -.
DR MGI; MGI:1353592; Hacd1.
DR eggNOG; KOG3187; Eukaryota.
DR InParanoid; Q9QY80; -.
DR OrthoDB; 1458293at2759; -.
DR Reactome; R-MMU-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR UniPathway; UPA00094; -.
DR BioGRID-ORCS; 30963; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Hacd1; mouse.
DR PRO; PR:Q9QY80; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QY80; protein.
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:0080023; F:3R-hydroxyacyl-CoA dehydratase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISS:UniProtKB.
DR GO; GO:0046848; F:hydroxyapatite binding; ISO:MGI.
DR GO; GO:0102158; F:very-long-chain 3-hydroxyacyl-CoA dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0071529; P:cementum mineralization; ISO:MGI.
DR GO; GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
DR GO; GO:0014902; P:myotube differentiation; IGI:MGI.
DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISO:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IMP:MGI.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:MGI.
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..281
FT /note="Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase
FT 1"
FT /id="PRO_0000349316"
FT TOPO_DOM 1..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 89..107
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 125..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..152
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 153..158
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..244
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 203
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT ACT_SITE 210
FT /evidence="ECO:0000250|UniProtKB:P40857"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 281 AA; 32327 MW; 24D64726C427BB08 CRC64;
MGKGDWRQGR VEMPCAHVSR LHKTCVQVRV RVTMASSEED GTNGASEASD EKEAAGKRRR
LGLLATAWLT FYNIAMTAGW LVLAIAMVRF YMEKGTHRGL YKSIQKTLKF FQTFALLEVV
HCLIGIVPTS VLVTGVQVSS RIFMVWLITH SIKPIQNEES VVLFLVSWTV TEITRYSFYT
FSLLDHLPHF IKWARYNLFI ILYPVGVAGE LLTIYAALPY VKKSGMFSVR LPNKYNVSFD
YYYFLLITMA SYIPLFPQLY FHMLRQRRKV LHGEVIAEKD D
