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Protein

Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1

Gene

Hacd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.By similarity

Catalytic activityi

A very-long-chain (3R)-3-hydroxyacyl-CoA = a very-long-chain trans-2,3-dehydroacyl-CoA + H2O.By similarity

Pathwayi: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.By similarity
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei203By similarity1
Active sitei210By similarity1

GO - Molecular functioni

GO - Biological processi

  • cellular macromolecular complex assembly Source: MGI
  • cementum mineralization Source: MGI
  • fatty acid elongation Source: UniProtKB
  • myotube differentiation Source: MGI
  • positive regulation of cell-substrate adhesion Source: MGI
  • regulation of G1/S transition of mitotic cell cycle Source: MGI
  • regulation of G2/M transition of mitotic cell cycle Source: MGI
  • sphingolipid biosynthetic process Source: UniProtKB
  • very long-chain fatty acid biosynthetic process Source: UniProtKB

Keywordsi

Molecular functionDevelopmental protein, Lyase
Biological processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism

Enzyme and pathway databases

UniPathwayiUPA00094.

Names & Taxonomyi

Protein namesi
Recommended name:
Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1Curated (EC:4.2.1.134By similarity)
Alternative name(s):
3-hydroxyacyl-CoA dehydratase 1Curated
Short name:
HACD1Curated
Protein-tyrosine phosphatase-like member AImported
Gene namesi
Name:Hacd1Imported
Synonyms:Ptpla
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1353592. Hacd1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 68CytoplasmicSequence analysisAdd BLAST68
Transmembranei69 – 88HelicalSequence analysisAdd BLAST20
Topological domaini89 – 107LumenalSequence analysisAdd BLAST19
Transmembranei108 – 124HelicalSequence analysisAdd BLAST17
Topological domaini125 – 134CytoplasmicSequence analysis10
Transmembranei135 – 152HelicalSequence analysisAdd BLAST18
Topological domaini153 – 158LumenalSequence analysis6
Transmembranei159 – 173HelicalSequence analysisAdd BLAST15
Topological domaini174 – 196CytoplasmicSequence analysisAdd BLAST23
Transmembranei197 – 214HelicalSequence analysisAdd BLAST18
Topological domaini215 – 244LumenalSequence analysisAdd BLAST30
Transmembranei245 – 262HelicalSequence analysisAdd BLAST18
Topological domaini263 – 281CytoplasmicSequence analysisAdd BLAST19

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003493161 – 281Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1Add BLAST281

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi236N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9QY80.
PaxDbiQ9QY80.
PRIDEiQ9QY80.

PTM databases

iPTMnetiQ9QY80.
PhosphoSitePlusiQ9QY80.

Expressioni

Tissue specificityi

Expressed at high levels in heart, skeletal muscle and testis, weak expression in kidney and liver.1 Publication

Developmental stagei

Differentially expressed during embryogenesis. First detected throughout the somites at E8.5 and in the myotome at E11.5. Expression was observed in muscles ventral to the developing vertebral column of the neck, thorax, abdomen and tail. Expression was maintained in skeletal muscle types well after the terminal differentiation of muscle fibers. During cardiac development, expression was restricted to the myocytes of the primitive heart tube, and by E10.5, it was expressed in the muscles throughout all the cardiac chambers. At this last stage it is also detected in the hepatic primordia, and later in embryonic liver. By 15.5 expression was also observed in the smooth muscle surrounding the digestive, respiratory and urogenital tracts.

Interactioni

Subunit structurei

May interact with enzymes of the ELO family (including ELOVL1); with those enzymes that mediate condensation, the first of the four steps of the reaction cycle responsible for fatty acids elongation, may be part of a larger fatty acids elongase complex.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000074397.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3187. Eukaryota.
COG5198. LUCA.
HOGENOMiHOG000190538.
HOVERGENiHBG057518.
InParanoidiQ9QY80.
KOiK10703.

Family and domain databases

InterProiView protein in InterPro
IPR007482. Tyr_Pase-like_PTPLA.
PANTHERiPTHR11035. PTHR11035. 1 hit.
PfamiView protein in Pfam
PF04387. PTPLA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9QY80-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGDWRQGR VEMPCAHVSR LHKTCVQVRV RVTMASSEED GTNGASEASD
60 70 80 90 100
EKEAAGKRRR LGLLATAWLT FYNIAMTAGW LVLAIAMVRF YMEKGTHRGL
110 120 130 140 150
YKSIQKTLKF FQTFALLEVV HCLIGIVPTS VLVTGVQVSS RIFMVWLITH
160 170 180 190 200
SIKPIQNEES VVLFLVSWTV TEITRYSFYT FSLLDHLPHF IKWARYNLFI
210 220 230 240 250
ILYPVGVAGE LLTIYAALPY VKKSGMFSVR LPNKYNVSFD YYYFLLITMA
260 270 280
SYIPLFPQLY FHMLRQRRKV LHGEVIAEKD D
Length:281
Mass (Da):32,327
Last modified:May 1, 2000 - v1
Checksum:i24D64726C427BB08
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF114493 mRNA. Translation: AAF21975.1.
AL844560 Genomic DNA. Translation: CAM21321.1.
AK010119 mRNA. Translation: BAB26713.1.
RefSeqiNP_038963.3. NM_013935.3.
UniGeneiMm.241205.

Genome annotation databases

GeneIDi30963.
KEGGimmu:30963.
UCSCiuc008ikd.1. mouse.

Similar proteinsi

Entry informationi

Entry nameiHACD1_MOUSE
AccessioniPrimary (citable) accession number: Q9QY80
Secondary accession number(s): Q9D6P7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 1, 2000
Last modified: November 22, 2017
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Shares some similarity with tyrosine phosphatase proteins but it has probably no phosphatase activity.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families