LIPT_MOUSE
ID LIPT_MOUSE Reviewed; 373 AA.
AC Q8VCM4;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Lipoyltransferase 1, mitochondrial;
DE EC=2.3.1.-;
DE AltName: Full=Lipoate biosynthesis protein;
DE AltName: Full=Lipoate-protein ligase;
DE AltName: Full=Lipoyl ligase;
DE Flags: Precursor;
GN Name=Lipt1;
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 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, and Spleen;
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).
CC -!- FUNCTION: Catalyzes the transfer of the lipoyl group from lipoyl-AMP to
CC the specific lysine residue of lipoyl domains of lipoate-dependent
CC enzymes. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-lipoyl-5'-AMP + L-lysyl-[lipoyl-carrier protein] = (R)-
CC N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + 2 H(+);
CC Xref=Rhea:RHEA:20473, Rhea:RHEA-COMP:10500, Rhea:RHEA-COMP:10502,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:83091,
CC ChEBI:CHEBI:83099, ChEBI:CHEBI:456215;
CC -!- PATHWAY: Protein modification; protein lipoylation via exogenous
CC pathway; protein N(6)-(lipoyl)lysine from lipoate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LplA family. {ECO:0000305}.
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DR EMBL; BC019519; AAH19519.1; -; mRNA.
DR CCDS; CCDS14895.1; -.
DR RefSeq; NP_001033007.2; NM_001037918.3.
DR RefSeq; XP_006496237.1; XM_006496174.1.
DR RefSeq; XP_006496238.1; XM_006496175.3.
DR RefSeq; XP_006496239.1; XM_006496176.2.
DR RefSeq; XP_006496240.1; XM_006496177.2.
DR RefSeq; XP_006496241.1; XM_006496178.2.
DR AlphaFoldDB; Q8VCM4; -.
DR SMR; Q8VCM4; -.
DR STRING; 10090.ENSMUSP00000038739; -.
DR iPTMnet; Q8VCM4; -.
DR PhosphoSitePlus; Q8VCM4; -.
DR SwissPalm; Q8VCM4; -.
DR EPD; Q8VCM4; -.
DR MaxQB; Q8VCM4; -.
DR PaxDb; Q8VCM4; -.
DR PRIDE; Q8VCM4; -.
DR ProteomicsDB; 290037; -.
DR Antibodypedia; 32790; 46 antibodies from 18 providers.
DR DNASU; 623661; -.
DR Ensembl; ENSMUST00000041621; ENSMUSP00000038739; ENSMUSG00000037216.
DR GeneID; 623661; -.
DR KEGG; mmu:623661; -.
DR UCSC; uc007ash.2; mouse.
DR CTD; 51601; -.
DR MGI; MGI:3645211; Lipt1.
DR VEuPathDB; HostDB:ENSMUSG00000037216; -.
DR eggNOG; KOG3159; Eukaryota.
DR GeneTree; ENSGT00390000008846; -.
DR HOGENOM; CLU_022986_4_1_1; -.
DR InParanoid; Q8VCM4; -.
DR OMA; RTCPEDD; -.
DR OrthoDB; 1090038at2759; -.
DR PhylomeDB; Q8VCM4; -.
DR TreeFam; TF314085; -.
DR Reactome; R-MMU-389661; Glyoxylate metabolism and glycine degradation.
DR UniPathway; UPA00537; UER00595.
DR BioGRID-ORCS; 623661; 21 hits in 75 CRISPR screens.
DR ChiTaRS; Lipt1; mouse.
DR PRO; PR:Q8VCM4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8VCM4; protein.
DR Bgee; ENSMUSG00000037216; Expressed in animal zygote and 153 other tissues.
DR ExpressionAtlas; Q8VCM4; baseline and differential.
DR Genevisible; Q8VCM4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0017118; F:lipoyltransferase activity; IBA:GO_Central.
DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR004562; LipoylTrfase_LipoateP_Ligase.
DR PANTHER; PTHR12561; PTHR12561; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00545; lipoyltrans; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Mitochondrion; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..25
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 26..373
FT /note="Lipoyltransferase 1, mitochondrial"
FT /id="PRO_0000017857"
FT DOMAIN 57..243
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 373 AA; 42146 MW; 33517278E9346AAD CRC64;
MLIPLSMKNC FRLLCQHKVP AAGFKSPPTH GLILQSISND VYENLAFEDW IHDHIHLEGK
PILFLWRNSP SVVIGRHQNP WQECNLHLMR QEGIKLARRK SGGGAVYHDM GNINLTFFTT
KTKYDRMENL KLIVRALNAV QPQLDVQPTK KFDLLLDGQF KISGTASKIG RTAAYHHCTL
LCSTNRTALS SSLKSPYCGI KSNATPSIPS AVKNLLERDS TLTCEVLMSA VAAEYAAHHQ
VDGHVNLINP ADETMFPGIN RKVKELQSWE WVYGRTPKFT VDTTFHVPYE QAHLEIQVFM
DVKNGRIETC AIKAPDHWLP LEIGEKLNSS FIGSKFCPVE TTLLTNVLLR TCPGDHHLHS
KWYILCEKIR GIM
