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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 to 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei203 – 2031By similarity
Active sitei210 – 2101By similarity

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
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Lyase

Keywords - Biological processi

Fatty 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1353592. Hacd1.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6868CytoplasmicSequence analysisAdd
BLAST
Transmembranei69 – 8820HelicalSequence analysisAdd
BLAST
Topological domaini89 – 10719LumenalSequence analysisAdd
BLAST
Transmembranei108 – 12417HelicalSequence analysisAdd
BLAST
Topological domaini125 – 13410CytoplasmicSequence analysis
Transmembranei135 – 15218HelicalSequence analysisAdd
BLAST
Topological domaini153 – 1586LumenalSequence analysis
Transmembranei159 – 17315HelicalSequence analysisAdd
BLAST
Topological domaini174 – 19623CytoplasmicSequence analysisAdd
BLAST
Transmembranei197 – 21418HelicalSequence analysisAdd
BLAST
Topological domaini215 – 24430LumenalSequence analysisAdd
BLAST
Transmembranei245 – 26218HelicalSequence analysisAdd
BLAST
Topological domaini263 – 28119CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 281281Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 1PRO_0000349316Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ9QY80.
PaxDbiQ9QY80.
PRIDEiQ9QY80.

PTM databases

iPTMnetiQ9QY80.
PhosphoSiteiQ9QY80.

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.

Gene expression databases

BgeeiQ9QY80.

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.

Family and domain databases

InterProiIPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERiPTHR11035. PTHR11035. 1 hit.
PfamiPF04387. PTPLA. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000074397.

PTM databases

iPTMnetiQ9QY80.
PhosphoSiteiQ9QY80.

Proteomic databases

MaxQBiQ9QY80.
PaxDbiQ9QY80.
PRIDEiQ9QY80.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi9200.
MGIiMGI:1353592. Hacd1.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

PROiQ9QY80.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QY80.

Family and domain databases

InterProiIPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERiPTHR11035. PTHR11035. 1 hit.
PfamiPF04387. PTPLA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, chromosomal mapping, and developmental expression of a novel protein tyrosine phosphatase-like gene."
    Uwanogho D.A., Hardcastle Z., Balogh P., Mirza G., Thornburg K.L., Ragoussis J., Sharpe P.T.
    Genomics 62:406-416(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL EXPRESSION.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs."
    Okazaki Y., Furuno M., Kasukawa T., Adachi J., Bono H., Kondo S., Nikaido I., Osato N., Saito R., Suzuki H., Yamanaka I., Kiyosawa H., Yagi K., Tomaru Y., Hasegawa Y., Nogami A., Schonbach C., Gojobori T.
    , Baldarelli R., Hill D.P., Bult C., Hume D.A., Quackenbush J., Schriml L.M., Kanapin A., Matsuda H., Batalov S., Beisel K.W., Blake J.A., Bradt D., Brusic V., Chothia C., Corbani L.E., Cousins S., Dalla E., Dragani T.A., Fletcher C.F., Forrest A., Frazer K.S., Gaasterland T., Gariboldi M., Gissi C., Godzik A., Gough J., Grimmond S., Gustincich S., Hirokawa N., Jackson I.J., Jarvis E.D., Kanai A., Kawaji H., Kawasawa Y., Kedzierski R.M., King B.L., Konagaya A., Kurochkin I.V., Lee Y., Lenhard B., Lyons P.A., Maglott D.R., Maltais L., Marchionni L., McKenzie L., Miki H., Nagashima T., Numata K., Okido T., Pavan W.J., Pertea G., Pesole G., Petrovsky N., Pillai R., Pontius J.U., Qi D., Ramachandran S., Ravasi T., Reed J.C., Reed D.J., Reid J., Ring B.Z., Ringwald M., Sandelin A., Schneider C., Semple C.A., Setou M., Shimada K., Sultana R., Takenaka Y., Taylor M.S., Teasdale R.D., Tomita M., Verardo R., Wagner L., Wahlestedt C., Wang Y., Watanabe Y., Wells C., Wilming L.G., Wynshaw-Boris A., Yanagisawa M., Yang I., Yang L., Yuan Z., Zavolan M., Zhu Y., Zimmer A., Carninci P., Hayatsu N., Hirozane-Kishikawa T., Konno H., Nakamura M., Sakazume N., Sato K., Shiraki T., Waki K., Kawai J., Aizawa K., Arakawa T., Fukuda S., Hara A., Hashizume W., Imotani K., Ishii Y., Itoh M., Kagawa I., Miyazaki A., Sakai K., Sasaki D., Shibata K., Shinagawa A., Yasunishi A., Yoshino M., Waterston R., Lander E.S., Rogers J., Birney E., Hayashizaki Y.
    Nature 420:563-573(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 34-281.
    Strain: C57BL/6J.
    Tissue: Tongue.

Entry informationi

Entry nameiHACD1_MOUSE
AccessioniPrimary (citable) accession number: Q9QY80
Secondary accession number(s): Q9D6P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 80 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.