LIPT2_MOUSE
ID LIPT2_MOUSE Reviewed; 231 AA.
AC Q9D009; Q14C29; Q9CVA5;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Putative lipoyltransferase 2, mitochondrial;
DE EC=2.3.1.181;
DE AltName: Full=Lipoate-protein ligase B;
DE AltName: Full=Lipoyl/octanoyl transferase;
DE AltName: Full=Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase;
DE Flags: Precursor;
GN Name=Lipt2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Stomach;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-43, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid
CC from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-
CC dependent enzymes, which catalyze essential redox reactions (By
CC similarity). Lipoyl-ACP can also act as a substrate although octanoyl-
CC ACP is likely to be the physiological substrate (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:A6NK58}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-
CC octanoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:17665, Rhea:RHEA-
CC COMP:9636, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:9928, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:64479,
CC ChEBI:CHEBI:78463, ChEBI:CHEBI:78809; EC=2.3.1.181;
CC -!- PATHWAY: Protein modification; protein lipoylation via endogenous
CC pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-
CC protein]: step 1/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:A6NK58}.
CC -!- MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic
CC acid is attached via an amide linkage to the epsilon-amino group of a
CC specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LipB family. {ECO:0000305}.
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; AK008917; BAB25967.1; -; mRNA.
DR EMBL; AK011925; BAB27920.1; -; mRNA.
DR EMBL; BC115472; AAI15473.1; -; mRNA.
DR EMBL; BC115473; AAI15474.1; -; mRNA.
DR CCDS; CCDS21494.1; -.
DR RefSeq; NP_080286.2; NM_026010.2.
DR AlphaFoldDB; Q9D009; -.
DR SMR; Q9D009; -.
DR BioGRID; 211989; 3.
DR STRING; 10090.ENSMUSP00000032967; -.
DR iPTMnet; Q9D009; -.
DR PhosphoSitePlus; Q9D009; -.
DR SwissPalm; Q9D009; -.
DR EPD; Q9D009; -.
DR MaxQB; Q9D009; -.
DR PaxDb; Q9D009; -.
DR PeptideAtlas; Q9D009; -.
DR PRIDE; Q9D009; -.
DR ProteomicsDB; 292099; -.
DR Antibodypedia; 48064; 86 antibodies from 16 providers.
DR DNASU; 67164; -.
DR Ensembl; ENSMUST00000032967; ENSMUSP00000032967; ENSMUSG00000030725.
DR GeneID; 67164; -.
DR KEGG; mmu:67164; -.
DR UCSC; uc009iml.2; mouse.
DR CTD; 387787; -.
DR MGI; MGI:1914414; Lipt2.
DR VEuPathDB; HostDB:ENSMUSG00000030725; -.
DR eggNOG; KOG0325; Eukaryota.
DR GeneTree; ENSGT00390000006450; -.
DR HOGENOM; CLU_035168_1_2_1; -.
DR InParanoid; Q9D009; -.
DR OMA; GEVTYHC; -.
DR OrthoDB; 1491838at2759; -.
DR PhylomeDB; Q9D009; -.
DR TreeFam; TF314262; -.
DR BRENDA; 2.3.1.181; 3474.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR UniPathway; UPA00538; UER00592.
DR BioGRID-ORCS; 67164; 22 hits in 73 CRISPR screens.
DR ChiTaRS; Lipt2; mouse.
DR PRO; PR:Q9D009; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9D009; protein.
DR Bgee; ENSMUSG00000030725; Expressed in epithelium of lens and 180 other tissues.
DR ExpressionAtlas; Q9D009; baseline and differential.
DR Genevisible; Q9D009; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0033819; F:lipoyl(octanoyl) transferase activity; IEA:UniProtKB-EC.
DR GO; GO:2000376; P:positive regulation of oxygen metabolic process; ISS:UniProtKB.
DR GO; GO:0009249; P:protein lipoylation; ISS:UniProtKB.
DR CDD; cd16444; LipB; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR000544; Octanoyltransferase.
DR PIRSF; PIRSF016262; LPLase; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00214; lipB; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Ligase; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..231
FT /note="Putative lipoyltransferase 2, mitochondrial"
FT /id="PRO_0000332306"
FT DOMAIN 41..224
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT ACT_SITE 185
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000250"
FT BINDING 85..92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 154..156
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 167..169
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 151
FT /note="Lowers pKa of active site Cys"
FT /evidence="ECO:0000250"
FT MOD_RES 43
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CONFLICT 190
FT /note="T -> A (in Ref. 1; BAB27920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 231 AA; 24955 MW; 57D192456112911B CRC64;
MSLPVVRLVW LGRVHYSELL ALQEHWLRRL QADPRPGTLS GTKAGVLLVC EPAGPVYTGG
LRGGLTPEET TRLRALGAEV RATGRGGLAT FHGPGQLLCH PVLDLRLLGL RLRTHVAALE
ACAVRLCELR GLQGARARPP PYTGVWLGER KICAIGVRCG RHITSHGLAL NCSTDLTWFE
HIVPCGLVGT GVTSLSEALQ RLVTVDEVMP SFLVAFKETF KCTLISEDSP S
