Q99M04 (LIAS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lipoyl synthase, mitochondrial
EC=2.8.1.8

Alternative name(s):
Lipoate synthase
Short name=LS
Short name=Lip-syn
Short name=mLIP1
Lipoic acid synthase

Gene names

Name:	Lias
Synonyms:	Lip1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	373 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives Probable. HAMAP-Rule MF_03123
Catalytic activity	Protein N(6)-(octanoyl)lysine + 2 sulfur + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 L-methionine + 2 5'-deoxyadenosine. HAMAP-Rule MF_03123
Cofactor	Binds 2 4Fe-4S clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine By similarity.
Pathway	Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2. HAMAP-Rule MF_03123
Subcellular location	Mitochondrion Ref.1.
Tissue specificity	Expressed predominantly in heart, testis, and liver. Ref.1
Sequence similarities	Belongs to the radical SAM superfamily. Lipoyl synthase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding S-adenosyl-L-methionine
Molecular function	Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	inflammatory response Inferred from mutant phenotype PubMed 18845616. Source: MGI neural tube closure Inferred from mutant phenotype PubMed 15755804. Source: MGI protein lipoylation Inferred from electronic annotation. Source: HAMAP response to lipopolysaccharide Inferred from mutant phenotype PubMed 18845616. Source: MGI response to oxidative stress Inferred from mutant phenotype PubMed 18845616. Source: MGI
Cellular_component	mitochondrion Inferred from direct assay Ref.1PubMed 14651853PubMed 18614015. Source: MGI
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: HAMAP lipoate synthase activity Inferred from genetic interaction Ref.1. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 26	26	Mitochondrion Potential
	Chain	27 – 373	347	Lipoyl synthase, mitochondrial HAMAP-Rule MF_03123		PRO_0000017724
Sites
	Metal binding	105	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	110	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	116	1	Iron-sulfur 1 (4Fe-4S) By similarity
	Metal binding	136	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	140	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity
	Metal binding	143	1	Iron-sulfur 2 (4Fe-4S-S-AdoMet) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q99M04 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 6796340A54BC5B8E	FASTA	373	41,879
	10 20 30 40 50 60 MALRCWDTAR SLGSRIFGRY AFTVRALSSL PDKKKEFLHN GPDLQDFVSG DLADKSTWDE 70 80 90 100 110 120 YKGNLKRQKG ERLRLPPWLK TKIPMGKNYN KLKNTLRNLS LHTVCEEARC PNIGECWGGG 130 140 150 160 170 180 EYATATATIM LMGDTCTRGC RFCSVKTARN PPPLDANEPD NTAKAIAEWG LDYVVLTSVD 190 200 210 220 230 240 RDDVADGGAE HIAKTVSCLK ERNPKILVEC LTPDFRGDLR AVEKVALSGL DVYAHNVETV 250 260 270 280 290 300 PELQRKVRDP RANFDQSLRV LRHAKEVQPD VVSKTSIMLG LGETDEQVYA TLKALRAADV 310 320 330 340 350 360 DCLTLGQYMQ PTKRHLKVEE YVTPEKFKYW EKVGNELGFL YTASGPLVRS SYKAGEFFLK 370 NLVARRKTKA SKV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria." Morikawa T., Yasuno R., Wada H. FEBS Lett. 498:16-21(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Heart.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Cerebellum and Testis.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB057731 mRNA. Translation: BAB62009.1. AK048744 mRNA. Translation: BAC33443.1. AK049548 mRNA. Translation: BAC33804.1. AK077192 mRNA. Translation: BAC36672.1. BC002141 mRNA. Translation: AAH02141.1.
IPI	IPI00117104.
RefSeq	NP_077791.1. NM_024471.4.
UniGene	Mm.195776.
3D structure databases
ProteinModelPortal	Q99M04.
SMR	Q99M04. Positions 127-309.
ModBase	Search...
Proteomic databases
PaxDb	Q99M04.
PRIDE	Q99M04.
Protocols and materials databases
DNASU	79464.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000031101; ENSMUSP00000031101; ENSMUSG00000029199.
GeneID	79464.
KEGG	mmu:79464.
UCSC	uc008xnq.1. mouse.
Organism-specific databases
CTD	11019.
MGI	MGI:1934604. Lias.
Phylogenomic databases
eggNOG	COG0320.
GeneTree	ENSGT00390000006234.
HOGENOM	HOG000235998.
HOVERGEN	HBG023328.
InParanoid	Q99M04.
KO	K03644.
OMA	EEYVTPE.
OrthoDB	EOG4T1HMX.
Enzyme and pathway databases
UniPathway	UPA00538; UER00593.
Gene expression databases
ArrayExpress	Q99M04.
Bgee	Q99M04.
CleanEx	MM_LIAS.
Genevestigator	Q99M04.
GermOnline	ENSMUSG00000029199. Mus musculus.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
HAMAP	MF_00206. Lipoyl_synth.
InterPro	IPR013785. Aldolase_TIM. IPR006638. Elp3/MiaB/NifB. IPR003698. Lipoyl_synth. IPR007197. rSAM. [Graphical view]
PANTHER	PTHR10949. PTHR10949. 1 hit.
Pfam	PF04055. Radical_SAM. 1 hit. [Graphical view]
PIRSF	PIRSF005963. Lipoyl_synth. 1 hit.
SMART	SM00729. Elp3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00510. lipA. 1 hit.
ProtoNet	Search...
Other
NextBio	349935.
SOURCE	Search...

Entry information

Entry name

LIAS_MOUSE

Accession

Primary (citable) accession number: Q99M04
Secondary accession number(s): Q543M1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	June 1, 2001
Last modified:	April 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program