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Database: UniProt
Entry: F7H718_MACMU
LinkDB: F7H718_MACMU
Original site: F7H718_MACMU 
ID   F7H718_MACMU            Unreviewed;       758 AA.
AC   F7H718;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase ACSBG1 {ECO:0000256|ARBA:ARBA00040478};
DE            EC=6.2.1.3 {ECO:0000256|ARBA:ARBA00026121};
DE   AltName: Full=Acyl-CoA synthetase bubblegum family member 1 {ECO:0000256|ARBA:ARBA00043191};
GN   Name=ACSBG1 {ECO:0000313|Ensembl:ENSMMUP00000015536.4,
GN   ECO:0000313|VGNC:VGNC:69547};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000015536.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000015536.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000015536.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036716};
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:0000256|ARBA:ARBA00036355};
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:0000256|ARBA:ARBA00036813};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC       Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00004541}. Endoplasmic
CC       reticulum {ECO:0000256|ARBA:ARBA00004240}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004370}. Microsome
CC       {ECO:0000256|ARBA:ARBA00004144}. Vesicle
CC       {ECO:0000256|ARBA:ARBA00004373}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       Bubblegum subfamily. {ECO:0000256|ARBA:ARBA00038034}.
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DR   AlphaFoldDB; F7H718; -.
DR   SMR; F7H718; -.
DR   STRING; 9544.ENSMMUP00000015536; -.
DR   Ensembl; ENSMMUT00000016586.4; ENSMMUP00000015536.4; ENSMMUG00000011839.4.
DR   VEuPathDB; HostDB:ENSMMUG00000011839; -.
DR   VGNC; VGNC:69547; ACSBG1.
DR   GeneTree; ENSGT00940000160380; -.
DR   HOGENOM; CLU_000022_45_5_1; -.
DR   InParanoid; F7H718; -.
DR   OMA; ETCAYVC; -.
DR   OrthoDB; 443463at2759; -.
DR   TreeFam; TF354286; -.
DR   Proteomes; UP000006718; Chromosome 7.
DR   Bgee; ENSMMUG00000011839; Expressed in Ammon's horn and 16 other cell types or tissues.
DR   ExpressionAtlas; F7H718; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IBA:GO_Central.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0031957; F:very long-chain fatty acid-CoA ligase activity; IEA:Ensembl.
DR   GO; GO:0042759; P:long-chain fatty acid biosynthetic process; IBA:GO_Central.
DR   GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR   GO; GO:0000038; P:very long-chain fatty acid metabolic process; IEA:Ensembl.
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.
PE   3: Inferred from homology;
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022848};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Microsome {ECO:0000256|ARBA:ARBA00022848};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718}.
FT   DOMAIN          146..565
FT                   /note="AMP-dependent synthetase/ligase"
FT                   /evidence="ECO:0000259|Pfam:PF00501"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   758 AA;  84869 MW;  D641B0C0F3FA314A CRC64;
     MPRNSGAGYG CPHGDPSMLD SRETPQESRQ DMTVGTTQEK LKTRFLNRLL PGGPGCVHKL
     SFVRNLQCRQ GVRLNVRSSS LTDRQPLSKE SLNHALKLSV PEKVNNAQWD APEEALWTTR
     ADGRVRLRID PSCPQLPYTV HRMFYEALDK YGDFSALGFK CQDKWEHISY SQYYLLARRA
     AKGFLKLGLE RAHSVAILGF NSPEWFFSAV GTVFAGGIVT GIYTTSSPEA CQYIAYDCCA
     NVIMVDTQKQ LEKILKVWKQ LPHLKAVVIY KEPPPNKMAN VYTMEEFMEL GNEVPEEALD
     AIIDTQQPNQ CCVLVYTSGT TGNPKGVMLS QDNITWTARY GSQAGDIRPA EVQQEVVVSY
     LPLSHIAAQI YDLWTGIQWG AQVCFAEPDA LKGSLVNTLR EVEPTSHMGV PRVWEKIMER
     IQEVAAQSGF IRRKMLLWAM SVTLEQNLTC PGSDLKPFTT RLADYLVLAK VRQALGFAKC
     QKNFYGAAPM TAETQHFFLG LNIRLYAGYG LSETSGPHFM SSPCNYRLYS SGKLVPGCRV
     KLVNQDTEGI GKICLWGRTI FMGYLNMEDK TCEAIDEEGW LHTGDAGRLD ADGFLYITGR
     LKELIITAGG ENVPPVPIEE AVKMELPIIS NAMLIGDQRK FLSMLLTLKC TLDPDTSDPT
     DNLTEQAVEF CQRVGSRATT VSEIVGKDEA VYQAIEEGIR RVNMNAAARP YHIQKWAILE
     RDFSISGGEL GPTMKLKRLT VLEKYKDIID SFYREQKM
//
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