ACBG1_HUMAN
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 03-AUG-2022, entry version 158.
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}; 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; 1.
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; Q96GR2; -.
DR PeptideAtlas; Q96GR2; -.
DR PRIDE; Q96GR2; -.
DR ProteomicsDB; 76656; -.
DR Antibodypedia; 27568; 170 antibodies from 22 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 CTD; 23205; -.
DR DisGeNET; 23205; -.
DR GeneCards; ACSBG1; -.
DR HGNC; HGNC:29567; ACSBG1.
DR HPA; ENSG00000103740; Tissue enriched (brain).
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; RGMRKYD; -.
DR OrthoDB; 806831at2759; -.
DR PhylomeDB; Q96GR2; -.
DR TreeFam; TF354286; -.
DR BioCyc; MetaCyc:HS02532-MON; -.
DR PathwayCommons; Q96GR2; -.
DR Reactome; R-HSA-75876; Synthesis of very long-chain fatty acyl-CoAs.
DR SignaLink; Q96GR2; -.
DR BioGRID-ORCS; 23205; 11 hits in 1071 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 128 other tissues.
DR ExpressionAtlas; Q96GR2; baseline and differential.
DR Genevisible; Q96GR2; HS.
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:0016405; F:CoA-ligase activity; IBA:GO_Central.
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:0001552; P:ovarian follicle atresia; IEA:Ensembl.
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 Gene3D; 3.40.50.12780; -; 2.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
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
