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Protein

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

Gene

Hacd3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. Involved in Rac1-signaling pathways leading to the modulation of gene expression. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (By similarity).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 sitei286 – 2861By similarity
Active sitei293 – 2931By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

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 3Curated (EC:4.2.1.134By similarity)
Alternative name(s):
3-hydroxyacyl-CoA dehydratase 3Curated
Short name:
HACD3Curated
Butyrate-induced protein 11 Publication
Short name:
B-ind11 Publication
Protein-tyrosine phosphatase-like A domain-containing protein 1Imported
Gene namesi
Name:Hacd3Imported
Synonyms:Ptplad1Curated
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1889341. Hacd3.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 149149CytoplasmicSequence analysisAdd
BLAST
Transmembranei150 – 17021HelicalSequence analysisAdd
BLAST
Topological domaini171 – 18919LumenalSequence analysisAdd
BLAST
Transmembranei190 – 21021HelicalSequence analysisAdd
BLAST
Topological domaini211 – 2122CytoplasmicSequence analysis
Transmembranei213 – 23321HelicalSequence analysisAdd
BLAST
Topological domaini234 – 2429LumenalSequence analysis
Transmembranei243 – 26321HelicalSequence analysisAdd
BLAST
Topological domaini264 – 28017CytoplasmicSequence analysisAdd
BLAST
Transmembranei281 – 30121HelicalSequence analysisAdd
BLAST
Topological domaini302 – 32221LumenalSequence analysisAdd
BLAST
Transmembranei323 – 34321HelicalSequence analysisAdd
BLAST
Topological domaini344 – 36219CytoplasmicSequence 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 – 362362Very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase 3PRO_0000313725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei114 – 1141PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8K2C9.
MaxQBiQ8K2C9.
PaxDbiQ8K2C9.
PRIDEiQ8K2C9.

PTM databases

iPTMnetiQ8K2C9.
PhosphoSiteiQ8K2C9.
SwissPalmiQ8K2C9.

Expressioni

Gene expression databases

BgeeiQ8K2C9.
GenevisibleiQ8K2C9. MM.

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. Interacts with RAC1. Associates with internalized insulin receptor/INSR complexes on Golgi/endosomal membranes; HACD3/PTPLAD1 together with ATIC and PRKAA2/AMPK2 is proposed to be part of a signaling network regulating INSR autophosphorylation and endocytosis (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMD2Q132002EBI-8329978,EBI-357648From a different organism.

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ8K2C9. 91 interactions.
MINTiMINT-1858563.
STRINGi10090.ENSMUSP00000044955.

Structurei

3D structure databases

ProteinModelPortaliQ8K2C9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 9490CSPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili111 – 13828Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi350 – 3534Poly-Arg
Compositional biasi357 – 3604Poly-Lys

Sequence similaritiesi

Contains 1 CS domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3187. Eukaryota.
COG5198. LUCA.
GeneTreeiENSGT00530000062962.
HOGENOMiHOG000008043.
HOVERGENiHBG108301.
InParanoidiQ8K2C9.
KOiK10703.
OMAiYMLSCID.
OrthoDBiEOG7BP82H.
PhylomeDBiQ8K2C9.
TreeFamiTF313326.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERiPTHR11035. PTHR11035. 1 hit.
PfamiPF04387. PTPLA. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K2C9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METQVLTPHV YWAQRHRELY LRVELSDVQN PAISITDNVL HFKAQGHGAK
60 70 80 90 100
GDNVYEFHLE FLDLVKPEPA YRLTQRQVNI TVQKKGSHWW ERLTKQEKRP
110 120 130 140 150
LFLAPDFDRW LDESDAEMEL RAKEEERLNK LRLEREGSPE TLTNLKKGYL
160 170 180 190 200
FMYNLVQLLG FSWIFVNLTV RFFILGKESF YDTFHNVADM MYFCQMLALV
210 220 230 240 250
ETLNAAIGVT STPVLPALIQ FLGRNFILFL VFGTMEEMQN KAVVFFVFYS
260 270 280 290 300
WSAIEIFRYP FYMLSCIDMD WKVLTWLRYT MWIPLYPLGC LSEAVAVIQS
310 320 330 340 350
IPVFNESGRF SFTLPYPVKM KVRFSFFLQV YLVMLFLGLY INFRHLYKQR
360
RRRYGQKKKK LH
Length:362
Mass (Da):43,131
Last modified:January 15, 2008 - v2
Checksum:i85716941EF7008F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321A → P in AAH57023 (PubMed:15489334).Curated
Sequence conflicti63 – 631D → E in AAH31755 (PubMed:15489334).Curated
Sequence conflicti146 – 1461K → R in CAB10097 (PubMed:10747961).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK051735 mRNA. Translation: BAC34744.1.
AK052865 mRNA. Translation: BAC35179.1.
AK050556 mRNA. Translation: BAE20677.1.
AK159494 mRNA. Translation: BAE35128.1.
BC031755 mRNA. Translation: AAH31755.1.
BC057023 mRNA. Translation: AAH57023.1.
Z97207 mRNA. Translation: CAB10097.2.
CCDSiCCDS23284.1.
RefSeqiNP_067320.2. NM_021345.2.
UniGeneiMm.308180.

Genome annotation databases

EnsembliENSMUST00000036615; ENSMUSP00000044955; ENSMUSG00000033629.
GeneIDi57874.
KEGGimmu:57874.
UCSCiuc009qcp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK051735 mRNA. Translation: BAC34744.1.
AK052865 mRNA. Translation: BAC35179.1.
AK050556 mRNA. Translation: BAE20677.1.
AK159494 mRNA. Translation: BAE35128.1.
BC031755 mRNA. Translation: AAH31755.1.
BC057023 mRNA. Translation: AAH57023.1.
Z97207 mRNA. Translation: CAB10097.2.
CCDSiCCDS23284.1.
RefSeqiNP_067320.2. NM_021345.2.
UniGeneiMm.308180.

3D structure databases

ProteinModelPortaliQ8K2C9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8K2C9. 91 interactions.
MINTiMINT-1858563.
STRINGi10090.ENSMUSP00000044955.

PTM databases

iPTMnetiQ8K2C9.
PhosphoSiteiQ8K2C9.
SwissPalmiQ8K2C9.

Proteomic databases

EPDiQ8K2C9.
MaxQBiQ8K2C9.
PaxDbiQ8K2C9.
PRIDEiQ8K2C9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036615; ENSMUSP00000044955; ENSMUSG00000033629.
GeneIDi57874.
KEGGimmu:57874.
UCSCiuc009qcp.2. mouse.

Organism-specific databases

CTDi51495.
MGIiMGI:1889341. Hacd3.

Phylogenomic databases

eggNOGiKOG3187. Eukaryota.
COG5198. LUCA.
GeneTreeiENSGT00530000062962.
HOGENOMiHOG000008043.
HOVERGENiHBG108301.
InParanoidiQ8K2C9.
KOiK10703.
OMAiYMLSCID.
OrthoDBiEOG7BP82H.
PhylomeDBiQ8K2C9.
TreeFamiTF313326.

Enzyme and pathway databases

UniPathwayiUPA00094.

Miscellaneous databases

ChiTaRSiPtplad1. mouse.
NextBioi314029.
PROiQ8K2C9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8K2C9.
GenevisibleiQ8K2C9. MM.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
IPR007482. Tyr_Pase-like_PTPLA.
[Graphical view]
PANTHERiPTHR11035. PTHR11035. 1 hit.
PfamiPF04387. PTPLA. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Heart, Pancreas and Spinal ganglion.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain.
  3. "B-ind1, a novel mediator of Rac1 signaling cloned from sodium butyrate-treated fibroblasts."
    Courilleau D., Chastre E., Sabbah M., Redeuilh G., Atfi A., Mester J.
    J. Biol. Chem. 275:17344-17348(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-190.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  5. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiHACD3_MOUSE
AccessioniPrimary (citable) accession number: Q8K2C9
Secondary accession number(s): O09003, Q6PGH3, Q8BGM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: May 11, 2016
This is version 102 of the entry and version 2 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.