ID Q5ICG6_MOUSE Unreviewed; 722 AA. AC Q5ICG6; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 09-DEC-2015, entry version 54. DE SubName: Full=Long chain acyl-CoA synthetase 6 isoform 2 {ECO:0000313|EMBL:AAW33884.1}; GN Name=Acsl6 {ECO:0000313|MGI:MGI:894291}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAW33884.1}; RN [1] {ECO:0000313|EMBL:AAW33884.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=C57BL/6J {ECO:0000313|EMBL:AAW33884.1}; RX PubMed=15629433; DOI=10.1016/j.bbrc.2004.11.141; RA Lee E.J., Kim H.C., Cho Y.Y., Byun S.J., Lim J.M., Ryoo Z.Y.; RT "Alternative promotion of the mouse acyl-CoA synthetase 6 (mAcsl6) RT gene mediates the expression of multiple transcripts with 5'-end RT heterogeneity: genetic organization of mAcsl6 variants."; RL Biochem. Biophys. Res. Commun. 327:84-93(2005). 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; AY786361; AAW33884.1; -; mRNA. DR UniGene; Mm.267478; -. DR ProteinModelPortal; Q5ICG6; -. DR STRING; 10090.ENSMUSP00000104532; -. DR PaxDb; Q5ICG6; -. DR PRIDE; Q5ICG6; -. DR MGI; MGI:894291; Acsl6. DR eggNOG; COG1022; LUCA. DR eggNOG; KOG1256; Eukaryota. DR HOVERGEN; HBG050452; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; ISO:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0004467; F:long-chain fatty acid-CoA ligase activity; IDA:MGI. DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI. DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISO:MGI. DR GO; GO:0007405; P:neuroblast proliferation; IDA:MGI. DR InterPro; IPR020845; AMP-binding_CS. DR InterPro; IPR000873; AMP-dep_Synth/Lig. DR Pfam; PF00501; AMP-binding; 1. DR PROSITE; PS00455; AMP_BINDING; 1. PE 2: Evidence at transcript level; KW Membrane {ECO:0000256|SAM:Phobius}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 47 69 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 141 587 AMP-binding. {ECO:0000259|Pfam:PF00501}. SQ SEQUENCE 722 AA; 80776 MW; B7DD494A0468660B CRC64; MLTFFLVSGG SLWLFAEIAL SLLEKMQTQE ILRILRLPEL SDLGQFFRSL SATTLVSVGA LAAVLAYWLT HRPKALQPPC NLLKQSEEVE DGGGARRSVI GGCTQLLTHY YDDARTMYQV FRRGLSISGN GPCLGFRKPE QPYQWLSYQE VAKRAEFLGS GLLQHDCKVG TEQFVGVFAQ NRPEWIIAEL ACYTYSMVVV PLYDTLGPGS ISYIINTADI CTVIVDKPHK ATLLLEHVER KETPGLKLVI LMEPFEDALR ERGKKCGVDI KSMQAIEDCG RENHHAPVPP RPDDLSIVCF TSGTTGNPKG AMLTHGNVVA DFSGFLKVTE KVIFPRQDDV LISFLPLAHM FERVIQSVVY CHGGRVGFFQ GDIRLLSDDM KALRPTIFSV VPRLLNRMYD KIFHQADTSL KRWLLEFAAK RKQAEVRSGI IRNNSIWDEL FFNKIQASLG GHVRMIVTGA APASPTVLGF LRAALGCQVY EGYGQTECTA GCTFTTPGDW TSGHVGAPLP CNHIKLVDAE ELNYWTCKGE GEICVKGPNV FKGYLKDEDR TKEALDSDGW LHTGDIGKWL PEGTLKIIDR KKHIFKLAQG EYVAPEKIEN IYIRSEPVAQ IYVHGDSLKA FLVGIVVPDP EVMPSWAQKK GIEGTYQELC MKKELKKAIL DDMVMLGKES GLHSFEQVKA IYIHCDMFSV QNGLLTPTLK AKRPELREYF KKQIEELYLV SV //