ID   ACSL5_MOUSE             Reviewed;         683 AA.
AC   Q8JZR0;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Long-chain-fatty-acid--CoA ligase 5;
DE            EC=6.2.1.3;
DE   AltName: Full=Long-chain acyl-CoA synthetase 5;
DE            Short=LACS 5;
GN   Name=Acsl5; Synonyms=Facl5;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Activation of long-chain fatty acids for both synthesis
CC       of cellular lipids, and degradation via beta-oxidation. Utilizes a
CC       wide range of saturated fatty acids with a preference for C16-C18
CC       unsaturated fatty acids (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a long-chain carboxylic acid + CoA = AMP
CC       + diphosphate + an acyl-CoA.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC       type III membrane protein (By similarity). Peroxisome membrane;
CC       Single-pass type III membrane protein (By similarity). Microsome
CC       membrane; Single-pass type III membrane protein (By similarity).
CC       Endoplasmic reticulum membrane; Single-pass type III membrane
CC       protein (By similarity).
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
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DR   EMBL; BC031544; AAH31544.1; -; mRNA.
DR   IPI; IPI00170363; -.
DR   PIR; S49487; S49487.
DR   RefSeq; NP_082252.1; -.
DR   UniGene; Mm.292056; -.
DR   HSSP; P08659; 1LCI.
DR   PhosphoSite; Q8JZR0; -.
DR   PRIDE; Q8JZR0; -.
DR   Ensembl; ENSMUSG00000024981; Mus musculus.
DR   GeneID; 433256; -.
DR   KEGG; mmu:433256; -.
DR   NMPDR; fig|10090.3.peg.5260; -.
DR   MGI; MGI:1919129; Acsl5.
DR   HOGENOM; Q8JZR0; -.
DR   HOVERGEN; Q8JZR0; -.
DR   OMA; Q8JZR0; XWVISEL.
DR   BRENDA; 6.2.1.3; 244.
DR   NextBio; 408505; -.
DR   ArrayExpress; Q8JZR0; -.
DR   Bgee; Q8JZR0; -.
DR   CleanEx; MM_ACSL5; -.
DR   GermOnline; ENSMUSG00000024981; Mus musculus.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004467; F:long-chain-fatty-acid-CoA ligase activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   Pfam; PF00501; AMP-binding; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Endoplasmic reticulum; Fatty acid metabolism; Ligase;
KW   Lipid metabolism; Magnesium; Membrane; Microsome; Mitochondrion;
KW   Mitochondrion outer membrane; Nucleotide-binding; Peroxisome;
KW   Signal-anchor; Transmembrane.
FT   CHAIN         1    683       Long-chain-fatty-acid--CoA ligase 5.
FT                                /FTId=PRO_0000193113.
FT   TRANSMEM     12     32       Signal-anchor for type III membrane
FT                                protein (Potential).
FT   TOPO_DOM     33    683       Cytoplasmic (Potential).
SQ   SEQUENCE   683 AA;  76206 MW;  734A1A5878741D70 CRC64;
     MLFIFNFLFS PLPTPALICL LTFGTAIFLW LINRPQPVLP LIDLDNQSVG IEGGARRGAF
     QKNNDLILYY FSDAKTLYEN FQRGLAVSDN GPCLGYRKPN QPYKWISYKQ VSDRAEYLGS
     CLLHKGYKSS QDQFVGIFAQ NRPEWVISEL ACYTYSMVAV PLYDTLGTEA IIFVINRADI
     PVVICDTPQK ATMLVENVEK GLTPGLKTII LMDPFDDDLM KRGEKCGVEM LSLHDAENIG
     KENFKKPVPP KPEDLSVICF TSGTTGDPKG AMLTHENVVS NMAAFLKFLE PIFQPTSDDV
     TISYLPLAHM FERLVQGILF SCGGKIGFFQ GDIRLLPDDM KALKPTVFPT VPRLLNRVYD
     KVQNEAKTPL KKFLLNLAII SKFNEVKNGI IRRDSLWDKL VFSKIQGSLG GKVRLMITGA
     APISTPVLTF FRAAMGCWVF EAYGQTECTG GCSITSPGDW TAGHVGTPVA CNFVKLEDVA
     DMNYFSVNNE GEICIKGNNV FKGYLKDPEK TQEVLDKDGW LHTGDIGRWL PNGTLKIVDR
     KKNIFKLAQG EYIAPEKIEN VYSRSRPVLQ VFVHGESLRS FLIGVVVPDP DSLPSFAAKI
     GVKGSFEELC KNQCVKEAIL EDLQKIGKEG GLKSFEQVKS IFVHPEPFTI ENGLLTPTLK
     AKRVELAKFF QTQIKSLYES IEE
//