ID   ACBG1_RAT               Reviewed;         721 AA.
AC   Q924N5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   24-JAN-2024, entry version 129.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase ACSBG1 {ECO:0000305};
DE            EC=6.2.1.3 {ECO:0000269|PubMed:11381125};
DE   AltName: Full=Acyl-CoA synthetase bubblegum family member 1;
DE   AltName: Full=Gonadotropin-regulated long chain acyl CoA synthetase;
DE            Short=GR-LACS;
GN   Name=Acsbg1 {ECO:0000312|RGD:708557}; Synonyms=Grlacs;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME ACTIVITY, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=11381125; DOI=10.1073/pnas.121046998;
RA   Tang P.-Z., Tsai-Morris C.-H., Dufau M.L.;
RT   "Cloning and characterization of a hormonally regulated rat long chain
RT   acyl-CoA synthetase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:6581-6586(2001).
RN   [2]
RP   TISSUE SPECIFICITY.
RX   PubMed=16469493; DOI=10.1016/j.jsbmb.2005.10.005;
RA   Li J., Sheng Y., Tang P.-Z., Tsai-Morris C.-H., Dufau M.L.;
RT   "Tissue-cell- and species-specific expression of gonadotropin-regulated
RT   long chain acyl-CoA synthetase (GR-LACS) in gonads, adrenal and brain.
RT   Identification of novel forms in the brain.";
RL   J. Steroid Biochem. Mol. Biol. 98:207-217(2006).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-50; SER-53 AND
RP   SER-70, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Catalyzes the conversion of fatty acids such as long-chain
CC       and very long-chain fatty acids to their active form acyl-CoAs for both
CC       synthesis of cellular lipids, and degradation via beta-oxidation. Can
CC       activate diverse saturated, monosaturated and polyunsaturated fatty
CC       acids. {ECO:0000269|PubMed:11381125}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-
CC         CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560,
CC         ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3;
CC         Evidence={ECO:0000269|PubMed:11381125};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP
CC         + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526,
CC         ChEBI:CHEBI:72745, ChEBI:CHEBI:456215;
CC         Evidence={ECO:0000250|UniProtKB:Q96GR2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-
CC         CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q96GR2};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11381125}.
CC       Cytoplasmic vesicle {ECO:0000250}. Microsome {ECO:0000250}. Endoplasmic
CC       reticulum {ECO:0000250|UniProtKB:Q96GR2}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q96GR2}.
CC   -!- TISSUE SPECIFICITY: Present in testis, at a lower level in brain, and
CC       at a very low level in ovary. Not detected in other tissues. tested.
CC       Present in Leydig cells of the adult testis and to a lesser degree in
CC       the seminiferous tubules in spermatogonia and Sertoli cells (at protein
CC       level). {ECO:0000269|PubMed:11381125, ECO:0000269|PubMed:16469493}.
CC   -!- INDUCTION: Down-regulated by gonadotropin.
CC       {ECO:0000269|PubMed:11381125}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       Bubblegum subfamily. {ECO:0000305}.
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DR   EMBL; AF208125; AAG35729.1; -; mRNA.
DR   RefSeq; NP_599216.1; NM_134389.1.
DR   AlphaFoldDB; Q924N5; -.
DR   SMR; Q924N5; -.
DR   BioGRID; 251236; 3.
DR   STRING; 10116.ENSRNOP00000074226; -.
DR   iPTMnet; Q924N5; -.
DR   PhosphoSitePlus; Q924N5; -.
DR   PaxDb; 10116-ENSRNOP00000016104; -.
DR   GeneID; 171410; -.
DR   KEGG; rno:171410; -.
DR   UCSC; RGD:708557; rat.
DR   AGR; RGD:708557; -.
DR   CTD; 23205; -.
DR   RGD; 708557; Acsbg1.
DR   VEuPathDB; HostDB:ENSRNOG00000011381; -.
DR   eggNOG; KOG1256; Eukaryota.
DR   InParanoid; Q924N5; -.
DR   OrthoDB; 443463at2759; -.
DR   PhylomeDB; Q924N5; -.
DR   TreeFam; TF354286; -.
DR   BRENDA; 6.2.1.3; 5301.
DR   Reactome; R-RNO-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR   PRO; PR:Q924N5; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000011381; Expressed in ovary and 13 other cell types or tissues.
DR   ExpressionAtlas; Q924N5; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; ISS:HGNC-UCL.
DR   GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; ISS:HGNC-UCL.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IDA:RGD.
DR   GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:HGNC-UCL.
DR   GO; GO:0001552; P:ovarian follicle atresia; IEP:RGD.
DR   GO; GO:0051384; P:response to glucocorticoid; ISO:RGD.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISS:HGNC-UCL.
DR   CDD; cd05933; ACSBG_like; 1.
DR   Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 2.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   PANTHER; PTHR43272:SF93; ACYL-COA SYNTHETASE BUBBLEGUM FAMILY MEMBER 1; 1.
DR   PANTHER; PTHR43272; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   World-2DPAGE; 0004:Q924N5; -.
DR   Genevisible; Q924N5; RN.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW   Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism;
KW   Membrane; Microsome; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..721
FT                   /note="Long-chain-fatty-acid--CoA ligase ACSBG1"
FT                   /id="PRO_0000315811"
FT   REGION          1..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         279..287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         469..474
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         547
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         562
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         698
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         34
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         53
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         655
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99PU5"
SQ   SEQUENCE   721 AA;  80519 MW;  600DC8F87546DA32 CRC64;
     MPRSSEAGYC CLSRDSNMPD SRDDQQQGAS MGTSPDNSQT SSLIDGRTLS KESPSHGLEL
     SAPEKARAAS LDASEEALWT TRADGRVRLR LEPFCTQLPY TVHQMFYEAL DKYGNLSALG
     FKRKDKWERI SYYQYYLIAR KVAKGFLKLG LERAHSVAIL GFNSPEWFFS AVGTVFAGGI
     VTGIYTTSSP EACQYIAHDC RANVIVVDTQ KQLEKILKIW KDLPHLKAVV IYQEPPPKKM
     ANVYTMEELI ELGQEVPEEA LDAIIDTQQP NQCCVLVYTS GTTGNPKGVM LSQDNITWTA
     RYGSQAGDIQ PAEVQQEVVV SYLPLSHIAA QIYDLWTGIQ WGAQVCFADP DALKGTLVNT
     LREVEPTSHM GVPRVWEKIM ERIQEVAAQS GFIRRKMLLW AMSVTLEQNL TCPSNDLKPF
     TSRLADYLVL ARVRQALGFA KCQKNFYGAA PMTAETQRFF LGLNIRLYAG YGLSESTGPH
     FMSSPYNYRL YSSGRVVPGC RVKLVNQDAD GIGEICLWGR TIFMGYLNME DKTHEAIDSE
     GWLHTGDMGR LDDDGFLYIT GRLKELIITA GGENVPPVPI EEAVKMELPI ISSAMLIGDQ
     RKFLSMLLTL KCTLNPETSE PTDNLTEQAV EFCQRVGSKA STVSEIVGQK DEAVYQAIHE
     GIQRVNANAA ARPYHIQKWA ILERDFSISG GELGPTMKLK RLTVLEKYKD IIDSFYQEQK
     Q
//