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Q5R668

- ACSL3_PONAB

UniProt

Q5R668 - ACSL3_PONAB

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Protein

Long-chain-fatty-acid--CoA ligase 3

Gene

ACSL3

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. ACSL3 has mainly an anabolic role in energy metabolism (By similarity). Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) (By similarity). Mediates hepatic lipogenesis (By similarity). Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates (By similarity).By similarity

Catalytic activityi

ATP + a long-chain fatty acid + CoA = AMP + diphosphate + an acyl-CoA.

Cofactori

Magnesium.By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. long-chain fatty acid-CoA ligase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

ATP-binding, Magnesium, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Long-chain-fatty-acid--CoA ligase 3 (EC:6.2.1.3)
Alternative name(s):
Long-chain acyl-CoA synthetase 3
Short name:
LACS 3
Gene namesi
Name:ACSL3
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. mitochondrial outer membrane Source: UniProtKB-KW
  4. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Mitochondrion outer membrane, Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 720720Long-chain-fatty-acid--CoA ligase 3PRO_0000240276Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei683 – 6831PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ5R668.

Structurei

3D structure databases

ProteinModelPortaliQ5R668.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 720679CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei21 – 4121Helical; Signal-anchor for type III membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG106947.
InParanoidiQ5R668.
KOiK01897.

Family and domain databases

InterProiIPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q5R668-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNNHVSSKPS TMKLKHTINP ILLYFIHFLI SLYTILTYIP FYFFSESRQE
60 70 80 90 100
KSNRIKAKPV NSKPDSAYRS VNSLDGLASV LYPGCDTLDK VFTYAKNKFK
110 120 130 140 150
NKRLLGTREV LNEEDEVQPN GKIFKKVILG QYNWLSYEDV FVRAFNFGNG
160 170 180 190 200
LQMLGQKPKT NIAIFCETRA EWMIAAQACF MYNFQLVTLY ATLGGPAIVH
210 220 230 240 250
ALNETEVTNI ITSKELLQTK LKDIVSLVPR LRHIITVDGK PPTWSEFPKG
260 270 280 290 300
IIVHTMAAVE ALGAKASMEN QPHSKPLPSD IAVIMYTSGS TGLPKGVMIS
310 320 330 340 350
HSNIIAGITG MAERIPELGE EDVYIGYLPL AHVLELSAEL VCLSHGCRIG
360 370 380 390 400
YSSPQTLADQ SSKIKKGSKG DTSMLKPTLM AAVPEIMDRI YKNVMNKVSE
410 420 430 440 450
MSSFQRNLFI LAYNYKMEQI SKGRNTPLCN SFVFRKVRSL LGGNIRLLLC
460 470 480 490 500
GGAPLSATTQ RFMNICFCCP VGQGYGLTES AGAGTISEVW DYNTGRVGAP
510 520 530 540 550
LVCCEIKLKN WEEGGYFNTD KPHPRGEILI GGQIVTMGYY KNEAKTKADF
560 570 580 590 600
FEDENGQRWL CTGDIGEFEP DGCLKIIDRK KDLVKLQAGE YVSLGKVEAA
610 620 630 640 650
LKNLPLVDNI CAYANSYHSY VIGFVVPNQK ELTELARKKG LKGTWEELCN
660 670 680 690 700
SCEMENEVLK VLSEAAISAS LEKFEIPVKI RLSPEPWTPE TGLVTDAFKL
710 720
KRKELKTHYQ ADIERMYGRK
Length:720
Mass (Da):80,445
Last modified:June 13, 2006 - v2
Checksum:iC5E83CFBD6904101
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041L → P in CAH91520. 1 PublicationCurated
Sequence conflicti112 – 1121N → S in CAH93302. 1 PublicationCurated
Sequence conflicti117 – 1171V → I in CAH93302. 1 PublicationCurated
Sequence conflicti210 – 2101I → T in CAH91520. 1 PublicationCurated
Sequence conflicti270 – 2701N → D in CAH93302. 1 PublicationCurated
Sequence conflicti386 – 3861I → T in CAH92748. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859345 mRNA. Translation: CAH91520.1.
CR860628 mRNA. Translation: CAH92748.1.
CR861232 mRNA. Translation: CAH93302.1.
RefSeqiNP_001127581.1. NM_001134109.1.
NP_001128901.1. NM_001135429.1.
UniGeneiPab.19655.

Genome annotation databases

GeneIDi100174659.
100189843.
KEGGipon:100174659.
pon:100189843.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR859345 mRNA. Translation: CAH91520.1 .
CR860628 mRNA. Translation: CAH92748.1 .
CR861232 mRNA. Translation: CAH93302.1 .
RefSeqi NP_001127581.1. NM_001134109.1.
NP_001128901.1. NM_001135429.1.
UniGenei Pab.19655.

3D structure databases

ProteinModelPortali Q5R668.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi Q5R668.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100174659.
100189843.
KEGGi pon:100174659.
pon:100189843.

Organism-specific databases

CTDi 2181.

Phylogenomic databases

HOVERGENi HBG106947.
InParanoidi Q5R668.
KOi K01897.

Family and domain databases

InterProi IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view ]
Pfami PF00501. AMP-binding. 1 hit.
[Graphical view ]
PROSITEi PS00455. AMP_BINDING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. The German cDNA consortium
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain cortex.

Entry informationi

Entry nameiACSL3_PONAB
AccessioniPrimary (citable) accession number: Q5R668
Secondary accession number(s): Q5R4L4, Q5R9P0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: June 13, 2006
Last modified: October 29, 2014
This is version 60 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3