NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: Activation of long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation. Utilizes a wide range of saturated fatty acids with a preference for C16-C18 unsaturated fatty acids (By similarity).
CATALYTIC ACTIVITY: ATP + a long-chain carboxylic acid + CoA = AMP + diphosphate + an acyl-CoA.
SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass type III membrane protein (By similarity). Peroxisome membrane; Single-pass type III membrane protein (By similarity). Microsome membrane; Single-pass type III membrane protein (By similarity). Endoplasmic reticulum membrane; Single-pass type III membrane protein (By similarity).
SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BC031544; AAH31544.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

S49487; S49487.

NP_082252.1; -.

3D structure databases

HSSP

P08659; 1LCI. [HSSP ENTRY / PDB]

ModBase

Q8JZR0.

PTM databases

PhosphoSite

Q8JZR0; -.

Organism-specific databases

MGI

MGI:1919129; Acsl5.

Gene expression databases

ArrayExpress

Q8JZR0; -.

CleanEx

MM_ACSL5; -.

GermOnline

ENSMUSG00000024981; Mus musculus.

Ontologies

GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005792;	Cellular component: microsome (inferred from electronic annotation from UniProtKB-KW).
GO:0005743;	Cellular component: mitochondrial inner membrane (inferred from direct assay from MGI).
GO:0005741;	Cellular component: mitochondrial outer membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005778;	Cellular component: peroxisomal membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004467;	Molecular function: long-chain-fatty-acid-CoA ligase activity (inferred from electronic annotation from EC).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006631;	Biological process: fatty acid metabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000873; AMP-dep_Synth/Lig.
Graphical view of domain structure.

Pfam

PF00501; AMP-binding; 2.
Pfam graphical view of domain structure.

PRINTS

PR00154; AMPBINDING.

PROSITE

PS00455; AMP_BINDING; 1.

Proteomics databases

PRIDE

Q8JZR0; -.

Genome annotation databases

Ensembl

ENSMUSG00000024981; Mus musculus. [Contig view]

GeneID

433256; -.

KEGG

mmu:433256; -.

NMPDR

fig|10090.3.peg.5260; -.

Phylogenomic databases

HOGENOM

Q8JZR0; -.

HOVERGEN

Q8JZR0; -.

Other

408505; -.

Acsl5; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Endoplasmic reticulum; Fatty acid metabolism; Ligase; Lipid metabolism; Magnesium; Membrane; Microsome; Mitochondrion; Mitochondrion outer membrane; Peroxisome; Signal-anchor; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 683`	`683`	`Long-chain-fatty-acid--CoA ligase 5.`	`PRO_0000193113`
`TRANSMEM`	`12 32`	`21`	`Signal-anchor for type III membrane protein (Potential).`
`TOPO_DOM`	`33 683`	`651`	`Cytoplasmic (Potential).`

Sequence information

Length: 683 AA [This is the length of the unprocessed precursor]

Molecular weight: 76206 Da [This is the MW of the unprocessed precursor]

CRC64: 734A1A5878741D70 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLFIFNFLFS PLPTPALICL LTFGTAIFLW LINRPQPVLP LIDLDNQSVG IEGGARRGAF 

        70         80         90        100        110        120 
QKNNDLILYY FSDAKTLYEN FQRGLAVSDN GPCLGYRKPN QPYKWISYKQ VSDRAEYLGS 

       130        140        150        160        170        180 
CLLHKGYKSS QDQFVGIFAQ NRPEWVISEL ACYTYSMVAV PLYDTLGTEA IIFVINRADI 

       190        200        210        220        230        240 
PVVICDTPQK ATMLVENVEK GLTPGLKTII LMDPFDDDLM KRGEKCGVEM LSLHDAENIG 

       250        260        270        280        290        300 
KENFKKPVPP KPEDLSVICF TSGTTGDPKG AMLTHENVVS NMAAFLKFLE PIFQPTSDDV 

       310        320        330        340        350        360 
TISYLPLAHM FERLVQGILF SCGGKIGFFQ GDIRLLPDDM KALKPTVFPT VPRLLNRVYD 

       370        380        390        400        410        420 
KVQNEAKTPL KKFLLNLAII SKFNEVKNGI IRRDSLWDKL VFSKIQGSLG GKVRLMITGA 

       430        440        450        460        470        480 
APISTPVLTF FRAAMGCWVF EAYGQTECTG GCSITSPGDW TAGHVGTPVA CNFVKLEDVA 

       490        500        510        520        530        540 
DMNYFSVNNE GEICIKGNNV FKGYLKDPEK TQEVLDKDGW LHTGDIGRWL PNGTLKIVDR 

       550        560        570        580        590        600 
KKNIFKLAQG EYIAPEKIEN VYSRSRPVLQ VFVHGESLRS FLIGVVVPDP DSLPSFAAKI 

       610        620        630        640        650        660 
GVKGSFEELC KNQCVKEAIL EDLQKIGKEG GLKSFEQVKS IFVHPEPFTI ENGLLTPTLK 

       670        680 
AKRVELAKFF QTQIKSLYES IEE

Q8JZR0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools