Reviewed, UniProtKB/Swiss-Prot Q9JID6 (ACSL1_CAVPO)

Names and origin

Protein names

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 names

Name:	ACSL1
Synonyms:	FACL1, LACS1

Organism

Cavia porcellus (Guinea pig)

Taxonomic identifier

10141 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Hystricognathi › Caviidae › Cavia

Protein attributes

Sequence length	698 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	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.
Catalytic activity	ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
Cofactor	Magnesium By similarity.
Subcellular location	Microsome membrane; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein By similarity. Peroxisome membrane; Peripheral membrane protein By similarity. Endoplasmic reticulum membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Endoplasmic reticulum Membrane Microsome Mitochondrion Mitochondrion outer membrane Peroxisome
Ligand	ATP-binding Magnesium Nucleotide-binding
Molecular function	Ligase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-KW extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-KW peroxisome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain-fatty-acid-CoA ligase activity Inferred from electronic annotation. Source: EC magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 698	698	Long-chain-fatty-acid--CoA ligase 1		PRO_0000193103
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity
	Modified residue	84	1	Phosphotyrosine By similarity
	Modified residue	543	1	N6-acetyllysine By similarity
	Modified residue	632	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9JID6-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: CF8CB413209476AD	FASTA	698	77,698
	10 20 30 40 50 60 MQAHELLQYF RLPELVDIRQ YVRTLPTNTL MGFGAFAALT TFWYATRPKA LKPPCDLSMQ 70 80 90 100 110 120 SVEVAGSDGA RRSTLLDSDE PLVYFYDDVR TLYDVFQRGI QVSNNGPCLG SRKPDQPYEW 130 140 150 160 170 180 LSYKQVEDLS ECIGSALLQK GFQASPDQFI GIFAQNRPEW VIIEQACFAY SMVVVPLYDT 190 200 210 220 230 240 LGADAITYIV NKAELSVIFA DKPEKARILL ESVENKLTPG LKIIVVMDSY GSELVEQGKK 250 260 270 280 290 300 CGVEVISLKA MEGLGRANRR KPKPPEPDDL AVICFTSGTT GNPKGAMITH KNVVSDCSAF 310 320 330 340 350 360 VKATEKALVL NASDIHISFL PLAHMYEQLL QCVMLCHGAK IGFFQGDIRL LMDDLKALQP 370 380 390 400 410 420 TIFPVVPRLL NRMFDRIFAQ ANTTVKRWLL DFASKRKEAE LRSGIIRNNS VWDKLIFHKI 430 440 450 460 470 480 QSSLGGKVRL MVTGAAPVSA TVLTFLRAAL GCQFYEGYGQ TECTAGCSLS VPGDWTAGHV 490 500 510 520 530 540 GAPMPCNFIK LVDVEEMNYM AAMGEGEVCV KGPNVFKGYL KDPAKTAEAL DKDGWLHTGD 550 560 570 580 590 600 IGKWLPNGTL KIIDRKKHIF KLAQGEYIAP EKIENIYVRS EPVAQVFVHG ESLQAFLIAI 610 620 630 640 650 660 VVPDAESLAS WARKRGFEGS FEELCRNKDV KKAILEDMVR IGKDSGLKSF EQVRGIALHP 670 680 690 ELFSVDNGLL TPTMKAKRPE LRNYFRSQID ELYSTIKV

References

[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].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF236818 mRNA. Translation: AAF91295.1.
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Genome annotation databases
Ensembl	ENSCPOT00000002768; ENSCPOP00000002483; ENSCPOG00000002734; Cavia porcellus. [Genome view] ENSCPOT00000002769; ENSCPOP00000002484; ENSCPOG00000002734; Cavia porcellus. [Genome view]
Phylogenomic databases
HOVERGEN	Q9JID6.
Enzyme and pathway databases
BRENDA	6.2.1.3. 44.
Family and domain databases
InterPro	IPR000873. AMP-dep_Synth/Lig. [Graphical view]
Pfam	PF00501. AMP-binding. 1 hit. [Graphical view]
PROSITE	PS00455. AMP_BINDING. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ACSL1_CAVPO

Accession

Primary (citable) accession number: Q9JID6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	October 1, 2000
Last modified:	October 13, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)