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Q9JID6

- ACSL1_CAVPO

UniProt

Q9JID6 - ACSL1_CAVPO

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Protein

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

Gene

ACSL1

Organism
Cavia porcellus (Guinea pig)
Status
Reviewed - 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

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 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
ProteomesiUP000005447: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB-KW
  2. mitochondrial outer membrane Source: UniProtKB-KW
  3. 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 – 698698Long-chain-fatty-acid--CoA ligase 1PRO_0000193103Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei9 – 91Nitrated tyrosineBy similarity
Modified residuei84 – 841PhosphotyrosineBy similarity
Glycosylationi135 – 1351O-linked (GlcNAc)By similarity
Modified residuei356 – 3561N6-acetyllysineBy similarity
Modified residuei386 – 3861N6-acetyllysineBy similarity
Modified residuei620 – 6201PhosphoserineBy similarity
Modified residuei632 – 6321N6-acetyllysineBy similarity

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

eggNOGiCOG1022.
GeneTreeiENSGT00690000101725.
HOGENOMiHOG000159459.
HOVERGENiHBG050452.
InParanoidiQ9JID6.
OrthoDBiEOG71CFKN.

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.

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF236818 mRNA. Translation: AAF91295.1 .
RefSeqi NP_001166379.1. NM_001172908.1.

3D structure databases

ProteinModelPortali Q9JID6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10141.ENSCPOP00000002483.

Proteomic databases

PRIDEi Q9JID6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSCPOT00000002769 ; ENSCPOP00000002484 ; ENSCPOG00000002734 .
GeneIDi 100135469.

Organism-specific databases

CTDi 2180.

Phylogenomic databases

eggNOGi COG1022.
GeneTreei ENSGT00690000101725.
HOGENOMi HOG000159459.
HOVERGENi HBG050452.
InParanoidi Q9JID6.
OrthoDBi EOG71CFKN.

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. "Molecular characterization and expression of guinea-pig acyl-CoA synthetase 1."
    Sevoz C., Benoit E., Buronfosse T.
    Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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 29, 2014
This is version 81 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

External Data

Dasty 3