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Protein

Lipoyl synthase, mitochondrial

Gene

Lias

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.Curated

Catalytic activityi

Protein N(6)-(octanoyl)lysine + 2 sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = protein N(6)-(lipoyl)lysine + 2 (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine.

Cofactori

[4Fe-4S] clusterUniRule annotationNote: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi105 – 1051Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi110 – 1101Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi116 – 1161Iron-sulfur 1 (4Fe-4S)UniRule annotation
Metal bindingi136 – 1361Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi140 – 1401Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation
Metal bindingi143 – 1431Iron-sulfur 2 (4Fe-4S-S-AdoMet)UniRule annotation

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
  2. lipoate synthase activity Source: MGI
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. inflammatory response Source: MGI
  2. lipoate biosynthetic process Source: MGI
  3. neural tube closure Source: MGI
  4. protein lipoylation Source: UniProtKB-HAMAP
  5. response to lipopolysaccharide Source: MGI
  6. response to oxidative stress Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Names & Taxonomyi

Protein namesi
Recommended name:
Lipoyl synthase, mitochondrialUniRule annotation (EC:2.8.1.8UniRule annotation)
Alternative name(s):
Lipoate synthaseUniRule annotation
Short name:
LSUniRule annotation
Short name:
Lip-synUniRule annotation
Short name:
mLIP1
Lipoic acid synthaseUniRule annotation
Gene namesi
Name:Lias
Synonyms:Lip1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1934604. Lias.

Subcellular locationi

Mitochondrion 1 PublicationUniRule annotation

GO - Cellular componenti

  1. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626MitochondrionUniRule annotationAdd
BLAST
Chaini27 – 373347Lipoyl synthase, mitochondrialPRO_0000017724Add
BLAST

Proteomic databases

MaxQBiQ99M04.
PaxDbiQ99M04.
PRIDEiQ99M04.

Expressioni

Tissue specificityi

Expressed predominantly in heart, testis, and liver.1 Publication

Gene expression databases

BgeeiQ99M04.
CleanExiMM_LIAS.
ExpressionAtlasiQ99M04. baseline and differential.
GenevestigatoriQ99M04.

Structurei

3D structure databases

ProteinModelPortaliQ99M04.
SMRiQ99M04. Positions 76-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the radical SAM superfamily. Lipoyl synthase family.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0320.
GeneTreeiENSGT00390000006234.
HOGENOMiHOG000235998.
HOVERGENiHBG023328.
InParanoidiQ99M04.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG7P2XS7.
PhylomeDBiQ99M04.
TreeFamiTF300817.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99M04-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MALRCWDTAR SLGSRIFGRY AFTVRALSSL PDKKKEFLHN GPDLQDFVSG
60 70 80 90 100
DLADKSTWDE YKGNLKRQKG ERLRLPPWLK TKIPMGKNYN KLKNTLRNLS
110 120 130 140 150
LHTVCEEARC PNIGECWGGG EYATATATIM LMGDTCTRGC RFCSVKTARN
160 170 180 190 200
PPPLDANEPD NTAKAIAEWG LDYVVLTSVD RDDVADGGAE HIAKTVSCLK
210 220 230 240 250
ERNPKILVEC LTPDFRGDLR AVEKVALSGL DVYAHNVETV PELQRKVRDP
260 270 280 290 300
RANFDQSLRV LRHAKEVQPD VVSKTSIMLG LGETDEQVYA TLKALRAADV
310 320 330 340 350
DCLTLGQYMQ PTKRHLKVEE YVTPEKFKYW EKVGNELGFL YTASGPLVRS
360 370
SYKAGEFFLK NLVARRKTKA SKV
Length:373
Mass (Da):41,879
Last modified:June 1, 2001 - v1
Checksum:i6796340A54BC5B8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19307.1.
RefSeqiNP_077791.1. NM_024471.4.
UniGeneiMm.195776.

Genome annotation databases

EnsembliENSMUST00000031101; ENSMUSP00000031101; ENSMUSG00000029199.
GeneIDi79464.
KEGGimmu:79464.
UCSCiuc008xnq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS19307.1.
RefSeqiNP_077791.1. NM_024471.4.
UniGeneiMm.195776.

3D structure databases

ProteinModelPortaliQ99M04.
SMRiQ99M04. Positions 76-356.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

MaxQBiQ99M04.
PaxDbiQ99M04.
PRIDEiQ99M04.

Protocols and materials databases

DNASUi79464.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031101; ENSMUSP00000031101; ENSMUSG00000029199.
GeneIDi79464.
KEGGimmu:79464.
UCSCiuc008xnq.1. mouse.

Organism-specific databases

CTDi11019.
MGIiMGI:1934604. Lias.

Phylogenomic databases

eggNOGiCOG0320.
GeneTreeiENSGT00390000006234.
HOGENOMiHOG000235998.
HOVERGENiHBG023328.
InParanoidiQ99M04.
KOiK03644.
OMAiEEYVTPE.
OrthoDBiEOG7P2XS7.
PhylomeDBiQ99M04.
TreeFamiTF300817.

Enzyme and pathway databases

UniPathwayiUPA00538; UER00593.

Miscellaneous databases

NextBioi349935.
PROiQ99M04.
SOURCEiSearch...

Gene expression databases

BgeeiQ99M04.
CleanExiMM_LIAS.
ExpressionAtlasiQ99M04. baseline and differential.
GenevestigatoriQ99M04.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
HAMAPiMF_00206. Lipoyl_synth.
InterProiIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR003698. Lipoyl_synth.
IPR007197. rSAM.
[Graphical view]
PANTHERiPTHR10949. PTHR10949. 1 hit.
PfamiPF04055. Radical_SAM. 1 hit.
[Graphical view]
PIRSFiPIRSF005963. Lipoyl_synth. 1 hit.
SMARTiSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00510. lipA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].

Entry informationi

Entry nameiLIAS_MOUSE
AccessioniPrimary (citable) accession number: Q99M04
Secondary accession number(s): Q543M1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2001
Last modified: January 7, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.