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Protein

Long-chain-fatty-acid--CoA ligase 1

Gene

ACSL1

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Preferentially uses palmitoleate, oleate and linoleate (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity

GO - Molecular functioni

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 1 (EC:6.2.1.3)
Alternative name(s):
Long-chain acyl-CoA synthetase 1
Short name:
LACS 1
Palmitoyl-CoA ligase
Gene namesi
Name:ACSL1
Synonyms:FACL1, LACS1
OrganismiCavia porcellus (Guinea pig)
Taxonomic identifieri10141 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaHystricognathiCaviidaeCavia
Proteomesi
  • UP000005447 Componenti: Unassembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001931031 – 698Long-chain-fatty-acid--CoA ligase 1Add BLAST698

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei9Nitrated tyrosineBy similarity1
Modified residuei84PhosphotyrosineBy similarity1
Glycosylationi135O-linked (GlcNAc)By similarity1
Modified residuei356N6-acetyllysineBy similarity1
Modified residuei386N6-acetyllysineBy similarity1
Modified residuei620PhosphoserineBy similarity1
Modified residuei632N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Glycoprotein, Nitration, Phosphoprotein

Proteomic databases

PRIDEiQ9JID6.

Interactioni

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000002483.

Structurei

3D structure databases

ProteinModelPortaliQ9JID6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1256. Eukaryota.
COG1022. LUCA.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiQ9JID6.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JID6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAHELLQYF RLPELVDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA
60 70 80 90 100
LKPPCDLSMQ SVEVAGSDGA RRSTLLDSDE PLVYFYDDVR TLYDVFQRGI
110 120 130 140 150
QVSNNGPCLG SRKPDQPYEW LSYKQVEDLS ECIGSALLQK GFQASPDQFI
160 170 180 190 200
GIFAQNRPEW VIIEQACFAY SMVVVPLYDT LGADAITYIV NKAELSVIFA
210 220 230 240 250
DKPEKARILL ESVENKLTPG LKIIVVMDSY GSELVEQGKK CGVEVISLKA
260 270 280 290 300
MEGLGRANRR KPKPPEPDDL AVICFTSGTT GNPKGAMITH KNVVSDCSAF
310 320 330 340 350
VKATEKALVL NASDIHISFL PLAHMYEQLL QCVMLCHGAK IGFFQGDIRL
360 370 380 390 400
LMDDLKALQP TIFPVVPRLL NRMFDRIFAQ ANTTVKRWLL DFASKRKEAE
410 420 430 440 450
LRSGIIRNNS VWDKLIFHKI QSSLGGKVRL MVTGAAPVSA TVLTFLRAAL
460 470 480 490 500
GCQFYEGYGQ TECTAGCSLS VPGDWTAGHV GAPMPCNFIK LVDVEEMNYM
510 520 530 540 550
AAMGEGEVCV KGPNVFKGYL KDPAKTAEAL DKDGWLHTGD IGKWLPNGTL
560 570 580 590 600
KIIDRKKHIF KLAQGEYIAP EKIENIYVRS EPVAQVFVHG ESLQAFLIAI
610 620 630 640 650
VVPDAESLAS WARKRGFEGS FEELCRNKDV KKAILEDMVR IGKDSGLKSF
660 670 680 690
EQVRGIALHP ELFSVDNGLL TPTMKAKRPE LRNYFRSQID ELYSTIKV
Length:698
Mass (Da):77,698
Last modified:October 1, 2000 - v1
Checksum:iCF8CB413209476AD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF236818 mRNA. Translation: AAF91295.1.
RefSeqiNP_001166379.1. NM_001172908.1.

Genome annotation databases

EnsembliENSCPOT00000002769; ENSCPOP00000002484; ENSCPOG00000002734.
GeneIDi100135469.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF236818 mRNA. Translation: AAF91295.1.
RefSeqiNP_001166379.1. NM_001172908.1.

3D structure databases

ProteinModelPortaliQ9JID6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10141.ENSCPOP00000002483.

Proteomic databases

PRIDEiQ9JID6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSCPOT00000002769; ENSCPOP00000002484; ENSCPOG00000002734.
GeneIDi100135469.

Organism-specific databases

CTDi2180.

Phylogenomic databases

eggNOGiKOG1256. Eukaryota.
COG1022. LUCA.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiQ9JID6.

Family and domain databases

InterProiIPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
[Graphical view]
PROSITEiPS00455. AMP_BINDING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACSL1_CAVPO
AccessioniPrimary (citable) accession number: Q9JID6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: October 5, 2016
This is version 88 of the entry and version 1 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

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.