Reviewed, UniProtKB/Swiss-Prot Q924N5 (ACBG1_RAT)

Names and origin

Protein names

Recommended name:
    Long-chain-fatty-acid--CoA ligase ACSBG1
    EC=6.2.1.3
Alternative name(s):
    Acyl-CoA synthetase bubblegum family member 1
    Gonadotropin-regulated long chain acyl CoA synthetase
      Short name=GR-LACS

Gene names

Name:	Acsbg1
Synonyms:	Grlacs

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	721 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Mediates activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Able to activate long-chain fatty acids. Can activate diverse saturated, monosaturated and polyunsaturated fatty acids. Ref.1
Catalytic activity	ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA. Ref.1
Subcellular location	Cytoplasm. Cytoplasmic vesicle By similarity. Microsome By similarity. Endoplasmic reticulum By similarity.
Tissue specificity	Present in testis, at a lower level in brain, and at a very low level in ovary. Not detected in other tissues. tested. Present in Leydig cells of the adult testis and to a lesser degree in the seminiferous tubules in spermatogonia and Sertoli cells (at protein level). Ref.1 Ref.2
Induction	Down-regulated by gonadotropin. Ref.1
Sequence similarities	Belongs to the ATP-dependent AMP-binding enzyme family. Bubblegum subfamily.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Cytoplasm Cytoplasmic vesicle Endoplasmic reticulum Microsome
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	long-chain fatty acid metabolic process Ref.1 Inferred from sequence or structural similarity. Source: HGNC ovarian follicle atresia Ref.2 Inferred from expression pattern. Source: RGD very-long-chain fatty acid metabolic process Inferred from sequence or structural similarity. Source: HGNC
Cellular component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell microsome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW long-chain-fatty-acid-CoA ligase activity Ref.1 Inferred from sequence or structural similarity. Source: HGNC very-long-chain-fatty-acid-CoA ligase activity Inferred from sequence or structural similarity. Source: HGNC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 721	721	Long-chain-fatty-acid--CoA ligase ACSBG1		PRO_0000315811
Regions
	Nucleotide binding	279 – 287	9	ATP By similarity
	Nucleotide binding	469 – 474	6	ATP By similarity
Sites
	Binding site	547	1	ATP By similarity
	Binding site	562	1	ATP By similarity
	Binding site	698	1	ATP By similarity
Amino acid modifications
	Modified residue	132	1	Phosphotyrosine By similarity
	Modified residue	135	1	Phosphotyrosine By similarity
	Modified residue	136	1	Phosphotyrosine By similarity
	Modified residue	655	1	Phosphotyrosine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q924N5-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 600DC8F87546DA32	FASTA	721	80,519
	10 20 30 40 50 60 MPRSSEAGYC CLSRDSNMPD SRDDQQQGAS MGTSPDNSQT SSLIDGRTLS KESPSHGLEL 70 80 90 100 110 120 SAPEKARAAS LDASEEALWT TRADGRVRLR LEPFCTQLPY TVHQMFYEAL DKYGNLSALG 130 140 150 160 170 180 FKRKDKWERI SYYQYYLIAR KVAKGFLKLG LERAHSVAIL GFNSPEWFFS AVGTVFAGGI 190 200 210 220 230 240 VTGIYTTSSP EACQYIAHDC RANVIVVDTQ KQLEKILKIW KDLPHLKAVV IYQEPPPKKM 250 260 270 280 290 300 ANVYTMEELI ELGQEVPEEA LDAIIDTQQP NQCCVLVYTS GTTGNPKGVM LSQDNITWTA 310 320 330 340 350 360 RYGSQAGDIQ PAEVQQEVVV SYLPLSHIAA QIYDLWTGIQ WGAQVCFADP DALKGTLVNT 370 380 390 400 410 420 LREVEPTSHM GVPRVWEKIM ERIQEVAAQS GFIRRKMLLW AMSVTLEQNL TCPSNDLKPF 430 440 450 460 470 480 TSRLADYLVL ARVRQALGFA KCQKNFYGAA PMTAETQRFF LGLNIRLYAG YGLSESTGPH 490 500 510 520 530 540 FMSSPYNYRL YSSGRVVPGC RVKLVNQDAD GIGEICLWGR TIFMGYLNME DKTHEAIDSE 550 560 570 580 590 600 GWLHTGDMGR LDDDGFLYIT GRLKELIITA GGENVPPVPI EEAVKMELPI ISSAMLIGDQ 610 620 630 640 650 660 RKFLSMLLTL KCTLNPETSE PTDNLTEQAV EFCQRVGSKA STVSEIVGQK DEAVYQAIHE 670 680 690 700 710 720 GIQRVNANAA ARPYHIQKWA ILERDFSISG GELGPTMKLK RLTVLEKYKD IIDSFYQEQK Q

References

[1]	"Cloning and characterization of a hormonally regulated rat long chain acyl-CoA synthetase." Tang P.-Z., Tsai-Morris C.-H., Dufau M.L. Proc. Natl. Acad. Sci. U.S.A. 98:6581-6586(2001) [PubMed: 11381125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
[2]	"Tissue-cell- and species-specific expression of gonadotropin-regulated long chain acyl-CoA synthetase (GR-LACS) in gonads, adrenal and brain. Identification of novel forms in the brain." Li J., Sheng Y., Tang P.-Z., Tsai-Morris C.-H., Dufau M.L. J. Steroid Biochem. Mol. Biol. 98:207-217(2006) [PubMed: 16469493] [Abstract] Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF208125 mRNA. Translation: AAG35729.1.
IPI	IPI00204896.
RefSeq	NP_599216.1.
UniGene	Rn.17672
3D structure databases
HSSP	HSSP built from PDB template 1LCI based on UniProtKB P08659.
ModBase	Search...
Protein-protein interaction databases
STRING	Q924N5.
PTM databases
PhosphoSite	Q924N5.
Proteomic databases
PRIDE	Q924N5.
Genome annotation databases
Ensembl	ENSRNOT00000016104; ENSRNOP00000016104; ENSRNOG00000011381; Rattus norvegicus. [Genome view]
GeneID	171410.
KEGG	rno:171410.
NMPDR	fig|10116.3.peg.28628.
UCSC	NM_134389. rat.
Organism-specific databases
CTD	171410.
RGD	708557. Acsbg1.
Phylogenomic databases
HOVERGEN	Q924N5.
OMA	HMGVPRV.
Gene expression databases
ArrayExpress	Q924N5.
Genevestigator	Q924N5.
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...
Other Resources
NextBio	622288.

Entry information

Entry name

ACBG1_RAT

Accession

Primary (citable) accession number: Q924N5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)