Reviewed, UniProtKB/Swiss-Prot Q920N2 (BPL1_MOUSE)

Names and origin

Protein names

Recommended name:
    Biotin--protein ligase
    EC=6.3.4.-
Alternative name(s):
    Biotin apo-protein ligase
Including the following 4 domains:
    1- Recommended name:
            Biotin--[methylmalonyl-CoA-carboxytransferase] ligase
              EC=6.3.4.9
    2- Recommended name:
            Biotin--[propionyl-CoA-carboxylase [ATP-hydrolyzing]] ligase
              EC=6.3.4.10
        Alternative name(s):
            Holocarboxylase synthetase
              Short name=HCS
    3- Recommended name:
            Biotin--[methylcrotonoyl-CoA-carboxylase] ligase
              EC=6.3.4.11
    4- Recommended name:
            Biotin--[acetyl-CoA-carboxylase] ligase
              EC=6.3.4.15

Gene names

Name:

Hlcs

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	722 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Post-translational modification of specific protein by attachment of biotin. Acts on various carboxylases such as acetyl-CoA-carboxylase, pyruvate carboxylase, propionyl CoA carboxylase, and 3-methylcrotonyl CoA carboxylase By similarity.
Catalytic activity	ATP + biotin + apo-[methylmalonyl-CoA:pyruvate carboxytransferase] = AMP + diphosphate + [methylmalonyl-CoA:pyruvate carboxytransferase]. ATP + biotin + apo-[propionyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [propionyl-CoA:carbon-dioxide ligase (ADP-forming)]. ATP + biotin + apo-[3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [3-methylcrotonoyl-CoA:carbon-dioxide ligase (ADP-forming)]. ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)].
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm By similarity. Mitochondrion By similarity.
Sequence similarities	Belongs to the biotin--protein ligase family.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	protein modification process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW biotin-[acetyl-CoA-carboxylase] ligase activity Inferred from electronic annotation. Source: EC biotin-[methylcrotonoyl-CoA-carboxylase] ligase activity Inferred from electronic annotation. Source: EC biotin-[methylmalonyl-CoA-carboxytransferase] ligase activity Inferred from electronic annotation. Source: EC biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 722	722	Biotin--protein ligase		PRO_0000064980
Amino acid modifications
	Modified residue	122	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q920N2-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 93FD61FF31AA7A65	FASTA	722	78,516
	10 20 30 40 50 60 MEDRLQMDNG LIAQKIVSVH LKDPALKELG KASDKQVQGP PPGPEASPEA QPAQGVMEHA 70 80 90 100 110 120 GQGDCKAAGE GPSPRRRGCA PESEPAADGD PGLSSPELCQ LHLSICHECL ELENSTIDSV 130 140 150 160 170 180 RSASAENIPD LPCDHSGVEG AAGELCPERK GKRVNISGKA PNILLYVGSG SEEALGRLQQ 190 200 210 220 230 240 VRSVLTDCVD TDSYTLYHLL EDSALRDPWS DNCLLLVIAS RDPIPKDIQH KFMAYLSQGG 250 260 270 280 290 300 KVLGLSSPFT LGGFRVTRRD VLRNTVQNLV FSKADGTEVR LSVLSSGYVY EEGPSLGRLQ 310 320 330 340 350 360 GHLENEDKDK MIVHVPFGTL GGEAVLCQVH LELPPGASLV QTADDFNVLK SSNVRRHEVL 370 380 390 400 410 420 KEILTALGLS CDAPQVPALT PLYLLLAAEE TQDPFMQWLG RHTDPEGIIK SSKLSLQFVS 430 440 450 460 470 480 SYTSEAEITP SSMPVVTDPE AFSSEHFSLE TYRQNLQTTR LGKVILFAEV TSTTMSLLDG 490 500 510 520 530 540 LMFEMPQEMG LIAIAVRQTQ GKGRGPNAWL SPVGCALSTL LVFIPLRSQL GQRIPFVQHL 550 560 570 580 590 600 MSLAVVEAVR SIPGYEDINL RVKWPNDIYY SDLMKIGGVL VNSTLMGETF YILIGCGFNV 610 620 630 640 650 660 TNSNPTICIN DLIEEHNKQH GAGLKPLRAD CLIARAVTVL EKLIDRFQDQ GPDGVLPLYY 670 680 690 700 710 720 KYWVHGGQQV RLGSTEGPQA SIVGLDDSGF LQVHQEDGGV VTVHPDGNSF DMLRNLIVPK RQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Hattori M., Ishii K., Toyoda A., Taylor T.D., Hong-Seog P., Fujiyama A., Yada T., Totoki Y., Watanabe H., Sakaki Y. Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Testis.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo.
[3]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB066227 mRNA. Translation: BAB68213.1. BC050090 mRNA. Translation: AAH50090.1.
IPI	IPI00120795.
RefSeq	NP_631884.1.
UniGene	Mm.30921
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q920N2.
PTM databases
PhosphoSite	Q920N2.
Proteomic databases
PRIDE	Q920N2.
Genome annotation databases
Ensembl	ENSMUST00000099512; ENSMUSP00000097112; ENSMUSG00000040820; Mus musculus. [Genome view]
GeneID	110948.
KEGG	mmu:110948.
UCSC	uc008aag.1. mouse.
Organism-specific databases
CTD	110948.
MGI	MGI:894646. Hlcs.
Phylogenomic databases
HOGENOM	Q920N2.
HOVERGEN	Q920N2.
OMA	YWVHSGQ.
Enzyme and pathway databases
BRENDA	6.3.4.10. 244. 6.3.4.11. 244. 6.3.4.15. 244. 6.3.4.9. 244.
Gene expression databases
ArrayExpress	Q920N2.
Bgee	Q920N2.
Genevestigator	Q920N2.
GermOnline	ENSMUSG00000040820. Mus musculus.
Family and domain databases
InterPro	IPR004408. Biotin_CoA_COase_ligase. IPR003142. BPL_C. IPR004143. BPL_LipA_LipB. [Graphical view]
PANTHER	PTHR12835. BirA_ligase. 1 hit.
Pfam	PF02237. BPL_C. 1 hit. PF03099. BPL_LipA_LipB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00121. birA_ligase. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	364997.
SOURCE	Search...

Entry information

Entry name

BPL1_MOUSE

Accession

Primary (citable) accession number: Q920N2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 10, 2002
Last sequence update:	December 1, 2001
Last modified:	November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)