ID ACBG1_HUMAN Reviewed; 724 AA. AC Q96GR2; B2RB61; O75126; Q76N27; Q9HC26; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 27-MAR-2024, entry version 167. DE RecName: Full=Long-chain-fatty-acid--CoA ligase ACSBG1 {ECO:0000305}; DE EC=6.2.1.3 {ECO:0000269|PubMed:10954726, ECO:0000269|PubMed:24269233}; DE AltName: Full=Acyl-CoA synthetase bubblegum family member 1; DE Short=hBG1; DE Short=hsBG; DE Short=hsBGM; DE AltName: Full=Lipidosin; GN Name=ACSBG1 {ECO:0000312|HGNC:HGNC:29567}; GN Synonyms=BGM, KIAA0631, LPD; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, FUNCTION, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=10954726; DOI=10.1074/jbc.m006403200; RA Steinberg S.J., Morgenthaler J., Heinzer A.K., Smith K.D., Watkins P.A.; RT "Very long-chain acyl-CoA synthetases. Human 'bubblegum' represents a new RT family of proteins capable of activating very long-chain fatty acids."; RL J. Biol. Chem. 275:35162-35169(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-633. RC TISSUE=Brain; RX PubMed=9734811; DOI=10.1093/dnares/5.3.169; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [3] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-633 AND VAL-673. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-633. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-633. RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=12975357; DOI=10.1074/jbc.m310075200; RA Pei Z., Oey N.A., Zuidervaart M.M., Jia Z., Li Y., Steinberg S.J., RA Smith K.D., Watkins P.A.; RT "The acyl-CoA synthetase 'bubblegum' (lipidosin): further characterization RT and role in neuronal fatty acid beta-oxidation."; RL J. Biol. Chem. 278:47070-47078(2003). RN [9] RP CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=24269233; DOI=10.1016/j.bbrc.2013.11.036; RA Ohkuni A., Ohno Y., Kihara A.; RT "Identification of acyl-CoA synthetases involved in the mammalian RT sphingosine 1-phosphate metabolic pathway."; RL Biochem. Biophys. Res. Commun. 442:195-201(2013). 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 CC (PubMed:12975357, PubMed:24269233, PubMed:10954726). Can activate CC diverse saturated, monosaturated and polyunsaturated fatty acids CC (PubMed:10954726). {ECO:0000269|PubMed:10954726, CC ECO:0000269|PubMed:12975357, ECO:0000269|PubMed:24269233}. 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:10954726, ECO:0000269|PubMed:24269233}; 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:0000269|PubMed:24269233}; 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:0000269|PubMed:24269233}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10954726}. CC Cytoplasmic vesicle {ECO:0000250}. Microsome {ECO:0000250}. Endoplasmic CC reticulum {ECO:0000269|PubMed:24269233}. Cell membrane CC {ECO:0000269|PubMed:24269233}. CC -!- TISSUE SPECIFICITY: Expressed primarily in brain. Expressed at lower CC level in testis and adrenal gland. Present in all regions of brain CC except pituitary. {ECO:0000269|PubMed:10954726, CC ECO:0000269|PubMed:12975357, ECO:0000269|PubMed:24269233}. CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family. CC Bubblegum subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA31606.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF179481; AAG09404.1; -; mRNA. DR EMBL; AB014531; BAA31606.2; ALT_INIT; mRNA. DR EMBL; AK314508; BAG37108.1; -; mRNA. DR EMBL; AC090260; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC090607; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471136; EAW99180.1; -; Genomic_DNA. DR EMBL; BC009289; AAH09289.1; -; mRNA. DR CCDS; CCDS10298.1; -. DR RefSeq; NP_001186306.1; NM_001199377.1. DR RefSeq; NP_055977.3; NM_015162.4. DR AlphaFoldDB; Q96GR2; -. DR SMR; Q96GR2; -. DR BioGRID; 116813; 8. DR IntAct; Q96GR2; 2. DR MINT; Q96GR2; -. DR STRING; 9606.ENSP00000258873; -. DR DrugBank; DB08326; 2-(6-HYDROXY-1,3-BENZOTHIAZOL-2-YL)-1,3-THIAZOL-4(5H)-ONE. DR SwissLipids; SLP:000000450; -. DR iPTMnet; Q96GR2; -. DR PhosphoSitePlus; Q96GR2; -. DR BioMuta; ACSBG1; -. DR DMDM; 296434385; -. DR MassIVE; Q96GR2; -. DR PaxDb; 9606-ENSP00000258873; -. DR PeptideAtlas; Q96GR2; -. DR ProteomicsDB; 76656; -. DR Antibodypedia; 27568; 188 antibodies from 23 providers. DR DNASU; 23205; -. DR Ensembl; ENST00000258873.9; ENSP00000258873.4; ENSG00000103740.10. DR GeneID; 23205; -. DR KEGG; hsa:23205; -. DR MANE-Select; ENST00000258873.9; ENSP00000258873.4; NM_015162.5; NP_055977.3. DR UCSC; uc002bdh.4; human. DR AGR; HGNC:29567; -. DR CTD; 23205; -. DR DisGeNET; 23205; -. DR GeneCards; ACSBG1; -. DR HGNC; HGNC:29567; ACSBG1. DR HPA; ENSG00000103740; Group enriched (brain, skin). DR MIM; 614362; gene. DR neXtProt; NX_Q96GR2; -. DR OpenTargets; ENSG00000103740; -. DR PharmGKB; PA142672648; -. DR VEuPathDB; HostDB:ENSG00000103740; -. DR eggNOG; KOG1256; Eukaryota. DR GeneTree; ENSGT00940000160380; -. DR InParanoid; Q96GR2; -. DR OMA; ETCAYVC; -. DR OrthoDB; 443463at2759; -. DR PhylomeDB; Q96GR2; -. DR TreeFam; TF354286; -. DR BioCyc; MetaCyc:HS02532-MONOMER; -. DR PathwayCommons; Q96GR2; -. DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs. DR SignaLink; Q96GR2; -. DR BioGRID-ORCS; 23205; 12 hits in 1151 CRISPR screens. DR ChiTaRS; ACSBG1; human. DR GeneWiki; ACSBG1; -. DR GenomeRNAi; 23205; -. DR Pharos; Q96GR2; Tbio. DR PRO; PR:Q96GR2; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q96GR2; Protein. DR Bgee; ENSG00000103740; Expressed in upper leg skin and 130 other cell types or tissues. DR ExpressionAtlas; Q96GR2; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL. DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:UniProtKB. DR GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IDA:HGNC-UCL. DR GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central. DR GO; GO:0001676; P:long-chain fatty acid metabolic process; IDA:UniProtKB. DR GO; GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome. DR GO; GO:0042552; P:myelination; NAS:HGNC-UCL. DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl. DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; IDA: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 Genevisible; Q96GR2; HS. 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..724 FT /note="Long-chain-fatty-acid--CoA ligase ACSBG1" FT /id="PRO_0000315808" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 282..290 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 472..477 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 550 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 565 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT BINDING 701 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250" FT MOD_RES 53 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q924N5" FT MOD_RES 56 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99PU5" FT MOD_RES 658 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q99PU5" FT VARIANT 194 FT /note="E -> V (in dbSNP:rs12899901)" FT /id="VAR_038314" FT VARIANT 633 FT /note="M -> V (in dbSNP:rs2304824)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9734811, FT ECO:0000269|Ref.6" FT /id="VAR_038315" FT VARIANT 673 FT /note="A -> V (in dbSNP:rs11072735)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_038316" SQ SEQUENCE 724 AA; 81290 MW; 2C27BA65CE95CE17 CRC64; MPRNSGAGYG CPHGDPSMLD SRETPQESRQ DMIVRTTQEK LKTSSLTDRQ PLSKESLNHA LELSVPEKVN NAQWDAPEEA LWTTRADGRV RLRIDPSCPQ LPYTVHRMFY EALDKYGDLI ALGFKRQDKW EHISYSQYYL LARRAAKGFL KLGLKQAHSV AILGFNSPEW FFSAVGTVFA GGIVTGIYTT SSPEACQYIA YDCCANVIMV DTQKQLEKIL KIWKQLPHLK AVVIYKEPPP NKMANVYTME EFMELGNEVP EEALDAIIDT QQPNQCCVLV YTSGTTGNPK GVMLSQDNIT WTARYGSQAG DIRPAEVQQE VVVSYLPLSH IAAQIYDLWT GIQWGAQVCF AEPDALKGSL VNTLREVEPT SHMGVPRVWE KIMERIQEVA AQSGFIRRKM LLWAMSVTLE QNLTCPGSDL KPFTTRLADY LVLAKVRQAL GFAKCQKNFY GAAPMMAETQ HFFLGLNIRL YAGYGLSETS GPHFMSSPYN YRLYSSGKLV PGCRVKLVNQ DAEGIGEICL WGRTIFMGYL NMEDKTCEAI DEEGWLHTGD AGRLDADGFL YITGRLKELI ITAGGENVPP VPIEEAVKME LPIISNAMLI GDQRKFLSML LTLKCTLDPD TSDQTDNLTE QAMEFCQRVG SRATTVSEII EKKDEAVYQA IEEGIRRVNM NAAARPYHIQ KWAILERDFS ISGGELGPTM KLKRLTVLEK YKGIIDSFYQ EQKM //