Bcl-2-like protein 1 - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot Q64373 (B2CL1_MOUSE)

Last modified June 16, 2009. Version 93. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Bcl-2-like protein 1
      Short name=Bcl2-L-1
Alternative name(s):
    Apoptosis regulator Bcl-X

Gene names

Name:	Bcl2l1
Synonyms:	Bcl2l, Bclx

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

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Protein attributes

Sequence length	233 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Potent inhibitor of cell death. Isoform Bcl-X(L) anti-apoptotic activity is inhibited by association with SIVA isoform 1. Inhibits activation of caspases By similarity. Appears to regulate cell death by binding and blocking the voltage-dependent anion channnel (VDAC), thus preventing the release of the caspase activator, cytochrome c, from the mitochondrial membrane. The Bcl-X(S) isoform promotes apoptosis.
Subunit structure	Bcl-X(L) forms heterodimers with BAX, BAK and BCL2 By similarity. Heterodimerization with BAX does not seem to be required for anti-apoptotic activity By similarity. Also interacts with BBC3 By similarity. Isoform Bcl-X(L) binds to binds to Siva isoform 1. Interacts with BECN1 and PGAM5 By similarity. Interacts with BCL2L11.
Subcellular location	Isoform Bcl-X(L): Mitochondrion membrane. Note: Mitochondrial membranes and perinuclear envelope for Bcl-X(L). Isoform Bcl-X(delta-TM): Cytoplasm.
Tissue specificity	Widely expressed, with highest levels in the brain, thymus, bone marrow, and kidney. Bcl-X(L) and Bcl-X(delta-TM) expression is enhanced in B- and T-lymphocytes that have been activated.
Developmental stage	Bcl-X(beta) is expressed in both embryonal and postnatal tissues, whereas Bcl-X(L) is predominantly found in postnatal tissues.
Domain	The BH4 motif is required for anti-apoptotic activity. The BH1 and BH2 motifs are required for both heterodimerization with other Bcl-2 family members and for repression of cell death.
Post-translational modification	Proteolytically cleaved by caspases during apoptosis By similarity. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity By similarity.
Sequence similarities	Belongs to the Bcl-2 family.

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Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cytoplasm Membrane Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transmembrane
Technical term	3D-structure
Gene Ontology (GO)
Biological process	anti-apoptosis Ref.2 Inferred from direct assay. Source: MGI cell proliferation Inferred from direct assay. Source: MGI fertilization Inferred from genetic interaction. Source: MGI germ cell development Inferred from genetic interaction. Source: MGI growth Inferred from mutant phenotype. Source: MGI in utero embryonic development Inferred from mutant phenotype. Source: MGI male gonad development Inferred from mutant phenotype. Source: MGI negative regulation of neuron apoptosis Inferred from direct assay. Source: MGI ovarian follicle development Inferred from genetic interaction. Source: MGI positive regulation of anti-apoptosis Inferred from direct assay. Source: MGI positive regulation of apoptosis Inferred from direct assay. Source: MGI positive regulation of cell proliferation Inferred from direct assay. Source: MGI release of cytochrome c from mitochondria Inferred from genetic interaction. Source: MGI response to cycloheximide Inferred from direct assay. Source: MGI response to protein stimulus Inferred from direct assay. Source: MGI response to radiation Inferred from mutant phenotype. Source: MGI spermatogenesis Inferred from genetic interaction. Source: MGI
Cellular component	cytosol Inferred from direct assay. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from Experiment. Source: Reactome
Molecular function	protein heterodimerization activity Inferred from physical interaction. Source: MGI
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
BCL2L1	Q07817-1	1	EBI-526380,EBI-287195	From a different organism.
Bcl2l11	O54918	1	EBI-526361,EBI-526067
Ppp1cc	P63087-1	1	EBI-526361,EBI-450267
Siva1	O54926	1	EBI-526380,EBI-1393169

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Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform Bcl-X(L) (identifier: Q64373-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Mitochondrial membranes and perinuclear envelope for Bcl-X(L).

Isoform Bcl-X(S) (identifier: Q64373-2) The sequence of this isoform differs from the canonical sequence as follows: 126-188: Missing.

Isoform Bcl-X(beta) (identifier: Q64373-3) The sequence of this isoform differs from the canonical sequence as follows: 189-233: DTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK → VRTTPLVCPPLACVSLLCEHP

Isoform Bcl-X(delta-TM) (identifier: Q64373-4) The sequence of this isoform differs from the canonical sequence as follows: 194-233: LYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK → GHDCGWCGSAGLTLQSEVTRH

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 233

233

Bcl-2-like protein 1

PRO_0000143063

Regions

Transmembrane

210 – 226

Potential

Motif

4 – 24

BH4

Motif

86 – 100

BH3

Motif

129 – 148

BH1

Motif

180 – 195

BH2

Natural variations

Alternative sequence

126 – 188

Missing in isoform Bcl-X(S).

VSP_000517

Alternative sequence

189 – 233

DTFVD…LFSRK → VRTTPLVCPPLACVSLLCEH P in isoform Bcl-X(beta).

VSP_000518

Alternative sequence

194 – 233

LYGNN…LFSRK → GHDCGWCGSAGLTLQSEVTR H in isoform Bcl-X(delta-TM).

VSP_000519

Experimental info

Sequence conflict

207 – 209

QER → KEG in AAC53459. Ref.4

Secondary structure

233

Helix Strand Turn

Details...

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Sequences

Sequence		Length	Mass (Da)
Isoform Bcl-X(L) [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 24D2AC79887E072E Show »	FASTA	233	26,132
10 20 30 40 50 60 MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEAERETPSA INGNPSWHLA 70 80 90 100 110 120 DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY 130 140 150 160 170 180 QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIASWM ATYLNDHLEP 190 200 210 220 230 WIQENGGWDT FVDLYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK « Hide
Isoform Bcl-X(S). Checksum: 2C12D8EC7F735D52 Show »	FASTA	170	18,961
10 20 30 40 50 60 MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEAERETPSA INGNPSWHLA 70 80 90 100 110 120 DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY 130 140 150 160 170 QSFEQDTFVD LYGNNAAAES RKGQERFNRW FLTGMTVAGV VLLGSLFSRK « Hide
Isoform Bcl-X(beta). Checksum: DC53895D8014B5DD Show »	FASTA	209	23,357
10 20 30 40 50 60 MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEAERETPSA INGNPSWHLA 70 80 90 100 110 120 DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY 130 140 150 160 170 180 QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIASWM ATYLNDHLEP 190 200 WIQENGGWVR TTPLVCPPLA CVSLLCEHP « Hide
Isoform Bcl-X(delta-TM). Checksum: 4FAECDC42B064B4A Show »	FASTA	214	23,900
10 20 30 40 50 60 MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEAERETPSA INGNPSWHLA 70 80 90 100 110 120 DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY 130 140 150 160 170 180 QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIASWM ATYLNDHLEP 190 200 210 WIQENGGWDT FVDGHDCGWC GSAGLTLQSE VTRH « Hide

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References

[1]	Kamesaki H., Michaud G.Y., Takatsu K., Okuma M. Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE (ISOFORM BCL-X(L)). Strain: 2A4B.
[2]	"bcl-XL is the major bcl-x mRNA form expressed during murine development and its product localizes to mitochondria." Gonzalez-Garcia M., Perez-Ballestero R., Ding L., Duan L., Boise L.H., Thompson C.B., Nunez G. Development 120:3033-3042(1994) [PubMed: 7607090] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS BCL-X(L) AND BCL-X(BETA)). Strain: C57BL/6. Tissue: Brain.
[3]	"Cloning and molecular characterization of mouse bcl-x in B and T lymphocytes." Fang W., Rivard J.J., Mueller D.L., Behrens T.W. J. Immunol. 153:4388-4398(1994) [PubMed: 7963517] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L); BCL-X(S) AND BCL-X(DELTA-TM)). Tissue: Pre-B cell.
[4]	"A novel Bcl-x isoform connected to the T cell receptor regulates apoptosis in T cells." Yang X.-F., Weber G.F., Cantor H. Immunity 7:629-639(1997) [PubMed: 9390687] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(BETA)). Strain: C57BL/6 X CBA. Tissue: Thymus.
[5]	"Genomic organization, promoter region analysis, and chromosome localization of the mouse bcl-x gene." Grillot D.A., Gonzalez-Garcia M., Ekhterae D., Duan L., Inohara N., Ohta S., Seldin M.F., Nunez G. J. Immunol. 158:4750-4757(1997) [PubMed: 9144489] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"The structure of a Bcl-xL/Bim fragment complex: implications for Bim function." Liu X., Dai S., Zhu Y., Marrack P., Kappler J.W. Immunity 19:341-352(2003) [PubMed: 14499110] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-196 IN COMPLEX WITH BCL2L11.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X83574 mRNA. Translation: CAA58557.1.
L35049 mRNA. Translation: AAA51039.1.
L35048 mRNA. Translation: AAA51040.1.
U10102 mRNA. Translation: AAA82174.1.
U10101 mRNA. Translation: AAA82173.1.
U10100 mRNA. Translation: AAA82172.1.
U51278 mRNA. Translation: AAC53459.1.
U51279 mRNA. Translation: AAC53460.1.
U78031, U78030 Genomic DNA. Translation: AAB96881.1.

IPI

IPI00133454.
IPI00227922.
IPI00227924.
IPI00406354.

PIR

I49055.
I49056.
I49057.

RefSeq

NP_033873.3.

UniGene

Mm.238213

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1PQ0	X-ray	2.20	A	1-196	[»]
1PQ1	X-ray	1.65	A	1-196	[»]
2BZW	X-ray	2.30	A	1-211	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q64373. 9 interactions.

PTM databases

PhosphoSite

Q64373.

Genome annotation databases

Ensembl

ENSMUSG00000007659. Mus musculus. [Contig view]

GeneID

12048.

KEGG

mmu:12048.

Organism-specific databases

MGI

MGI:88139. Bcl2l1.

Phylogenomic databases

HOVERGEN

Q64373.

OMA

Q64373. RTEASEG.

Gene expression databases

ArrayExpress

Q64373.

Bgee

Q64373.

CleanEx

MM_BCL2L1.

GermOnline

ENSMUSG00000007659. Mus musculus.

Family and domain databases

InterPro

IPR013279. Apop_reg_BclX.
IPR002475. BCL2_apoptsis.
IPR000712. Bcl2_BH.
IPR003093. Bcl2_BH4.
IPR004725. Bcl2_reg.
[Graphical view]

Pfam

PF00452. Bcl-2. 1 hit.
PF02180. BH4. 1 hit.
[Graphical view]

PRINTS

PR01864. APOPREGBCLX.
PR01862. BCL2FAMILY.

SMART

SM00337. BCL. 1 hit.
SM00265. BH4. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00865. bcl-2. 1 hit.

PROSITE

PS50062. BCL2_FAMILY. 1 hit.
PS01080. BH1. 1 hit.
PS01258. BH2. 1 hit.
PS01259. BH3. 1 hit.
PS01260. BH4_1. 1 hit.
PS50063. BH4_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

280335.

PMAP-CutDB

Q64373.

SOURCE

Search...

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Entry information

Entry name

B2CL1_MOUSE

Accession

Primary (citable) accession number: Q64373
Secondary accession number(s): O35844

Q61338

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 93 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents