BPL1_MOUSE
ID BPL1_MOUSE Reviewed; 722 AA.
AC Q920N2;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Biotin--protein ligase;
DE EC=6.3.4.- {ECO:0000250|UniProtKB:P50747};
DE AltName: Full=Biotin apo-protein ligase;
DE Includes:
DE RecName: Full=Biotin--[methylmalonyl-CoA-carboxytransferase] ligase;
DE EC=6.3.4.9 {ECO:0000250|UniProtKB:P50747};
DE Includes:
DE RecName: Full=Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase;
DE EC=6.3.4.10 {ECO:0000250|UniProtKB:P50747};
DE AltName: Full=Holocarboxylase synthetase;
DE Short=HCS;
DE Includes:
DE RecName: Full=Biotin--[methylcrotonoyl-CoA-carboxylase] ligase;
DE EC=6.3.4.11 {ECO:0000250|UniProtKB:P50747};
DE Includes:
DE RecName: Full=Biotin--[acetyl-CoA-carboxylase] ligase;
DE EC=6.3.4.15 {ECO:0000250|UniProtKB:P50747};
GN Name=Hlcs {ECO:0000312|MGI:MGI:894646};
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RA Hattori M., Ishii K., Toyoda A., Taylor T.D., Hong-Seog P., Fujiyama A.,
RA Yada T., Totoki Y., Watanabe H., Sakaki Y.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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, 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).
CC -!- FUNCTION: Biotin--protein ligase catalyzing the biotinylation of the 4
CC biotin-dependent carboxylases acetyl-CoA-carboxylase, pyruvate
CC carboxylase, propionyl-CoA carboxylase, and methylcrotonyl-CoA
CC carboxylase. {ECO:0000250|UniProtKB:P50747}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[methylmalonyl-CoA:pyruvate carboxytransferase] + ATP +
CC biotin = AMP + diphosphate + H(+) + holo-[methylmalonyl-CoA:pyruvate
CC carboxytransferase]; Xref=Rhea:RHEA:23668, Rhea:RHEA-COMP:10508,
CC Rhea:RHEA-COMP:10509, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57586,
CC ChEBI:CHEBI:83144, ChEBI:CHEBI:456215; EC=6.3.4.9;
CC Evidence={ECO:0000250|UniProtKB:P50747};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23669;
CC Evidence={ECO:0000250|UniProtKB:P50747};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] + ATP
CC + biotin = AMP + diphosphate + H(+) + holo-[propionyl-CoA:carbon-
CC dioxide ligase (ADP-forming)]; Xref=Rhea:RHEA:11204, Rhea:RHEA-
CC COMP:10511, Rhea:RHEA-COMP:10512, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215;
CC EC=6.3.4.10; Evidence={ECO:0000250|UniProtKB:P50747};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11205;
CC Evidence={ECO:0000250|UniProtKB:P50747};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-
CC forming)] + ATP + biotin = AMP + diphosphate + H(+) + holo-[3-
CC methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)];
CC Xref=Rhea:RHEA:24376, Rhea:RHEA-COMP:10514, Rhea:RHEA-COMP:10515,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57586, ChEBI:CHEBI:83144,
CC ChEBI:CHEBI:456215; EC=6.3.4.11;
CC Evidence={ECO:0000250|UniProtKB:P50747};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24377;
CC Evidence={ECO:0000250|UniProtKB:P50747};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + biotin + L-lysyl-[protein] = AMP + diphosphate + H(+) +
CC N(6)-biotinyl-L-lysyl-[protein]; Xref=Rhea:RHEA:11756, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:10505, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57586, ChEBI:CHEBI:83144, ChEBI:CHEBI:456215;
CC EC=6.3.4.15; Evidence={ECO:0000250|UniProtKB:P50747};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11757;
CC Evidence={ECO:0000250|UniProtKB:P50747};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P50747}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50747}.
CC Mitochondrion {ECO:0000250|UniProtKB:P50747}.
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000305}.
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DR EMBL; AB066227; BAB68213.1; -; mRNA.
DR EMBL; BC050090; AAH50090.1; -; mRNA.
DR CCDS; CCDS28346.1; -.
DR RefSeq; NP_631884.1; NM_139145.4.
DR RefSeq; XP_006522918.1; XM_006522855.2.
DR RefSeq; XP_006522919.1; XM_006522856.2.
DR AlphaFoldDB; Q920N2; -.
DR SMR; Q920N2; -.
DR BioGRID; 226044; 1.
DR STRING; 10090.ENSMUSP00000130981; -.
DR iPTMnet; Q920N2; -.
DR PhosphoSitePlus; Q920N2; -.
DR MaxQB; Q920N2; -.
DR PaxDb; Q920N2; -.
DR PRIDE; Q920N2; -.
DR ProteomicsDB; 265457; -.
DR Antibodypedia; 8381; 162 antibodies from 23 providers.
DR DNASU; 110948; -.
DR Ensembl; ENSMUST00000099512; ENSMUSP00000097112; ENSMUSG00000040820.
DR Ensembl; ENSMUST00000163193; ENSMUSP00000130981; ENSMUSG00000040820.
DR GeneID; 110948; -.
DR KEGG; mmu:110948; -.
DR UCSC; uc008aag.1; mouse.
DR CTD; 3141; -.
DR MGI; MGI:894646; Hlcs.
DR VEuPathDB; HostDB:ENSMUSG00000040820; -.
DR eggNOG; KOG1536; Eukaryota.
DR GeneTree; ENSGT00390000002960; -.
DR HOGENOM; CLU_006150_2_0_1; -.
DR InParanoid; Q920N2; -.
DR OrthoDB; 1392751at2759; -.
DR PhylomeDB; Q920N2; -.
DR TreeFam; TF105860; -.
DR Reactome; R-MMU-196780; Biotin transport and metabolism.
DR BioGRID-ORCS; 110948; 11 hits in 80 CRISPR screens.
DR PRO; PR:Q920N2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q920N2; protein.
DR Bgee; ENSMUSG00000040820; Expressed in granulocyte and 176 other tissues.
DR ExpressionAtlas; Q920N2; baseline and differential.
DR Genevisible; Q920N2; MM.
DR GO; GO:0000785; C:chromatin; ISS:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005652; C:nuclear lamina; ISS:BHF-UCL.
DR GO; GO:0016363; C:nuclear matrix; ISS:BHF-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0009374; F:biotin binding; ISS:BHF-UCL.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IBA:GO_Central.
DR GO; GO:0004078; F:biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004079; F:biotin-[methylmalonyl-CoA-carboxytransferase] ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0004080; F:biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity; ISS:BHF-UCL.
DR GO; GO:0018271; F:biotin-protein ligase activity; ISS:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
DR GO; GO:0016570; P:histone modification; ISO:MGI.
DR GO; GO:0070781; P:response to biotin; ISS:BHF-UCL.
DR CDD; cd16442; BPL; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR019197; Biotin-prot_ligase_N.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR003142; BPL_C.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR Pfam; PF09825; BPL_N; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00121; birA_ligase; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Ligase; Mitochondrion; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..722
FT /note="Biotin--protein ligase"
FT /id="PRO_0000064980"
FT DOMAIN 459..648
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01067"
FT REGION 27..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50747"
SQ SEQUENCE 722 AA; 78516 MW; 93FD61FF31AA7A65 CRC64;
MEDRLQMDNG LIAQKIVSVH LKDPALKELG KASDKQVQGP PPGPEASPEA QPAQGVMEHA
GQGDCKAAGE GPSPRRRGCA PESEPAADGD PGLSSPELCQ LHLSICHECL ELENSTIDSV
RSASAENIPD LPCDHSGVEG AAGELCPERK GKRVNISGKA PNILLYVGSG SEEALGRLQQ
VRSVLTDCVD TDSYTLYHLL EDSALRDPWS DNCLLLVIAS RDPIPKDIQH KFMAYLSQGG
KVLGLSSPFT LGGFRVTRRD VLRNTVQNLV FSKADGTEVR LSVLSSGYVY EEGPSLGRLQ
GHLENEDKDK MIVHVPFGTL GGEAVLCQVH LELPPGASLV QTADDFNVLK SSNVRRHEVL
KEILTALGLS CDAPQVPALT PLYLLLAAEE TQDPFMQWLG RHTDPEGIIK SSKLSLQFVS
SYTSEAEITP SSMPVVTDPE AFSSEHFSLE TYRQNLQTTR LGKVILFAEV TSTTMSLLDG
LMFEMPQEMG LIAIAVRQTQ GKGRGPNAWL SPVGCALSTL LVFIPLRSQL GQRIPFVQHL
MSLAVVEAVR SIPGYEDINL RVKWPNDIYY SDLMKIGGVL VNSTLMGETF YILIGCGFNV
TNSNPTICIN DLIEEHNKQH GAGLKPLRAD CLIARAVTVL EKLIDRFQDQ GPDGVLPLYY
KYWVHGGQQV RLGSTEGPQA SIVGLDDSGF LQVHQEDGGV VTVHPDGNSF DMLRNLIVPK
RQ
