[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=CBA/J; TISSUE=Bone marrow; PubMed=8345191 [NCBI, ExPASy, EBI, Israel, Japan] Lin E.Y., Orlofsky A., Berger M.S., Prystowsky M.B.; "Characterization of A1, a novel hemopoietic-specific early-response gene with sequence similarity to bcl-2."; J. Immunol. 151:1979-1988(1993).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=129/Sv; TISSUE=Liver; DOI=10.1093/intimm/10.5.631; PubMed=9645611 [NCBI, ExPASy, EBI, Israel, Japan] Hatakeyama S., Hamasaki A., Negishi I., Loh D.Y., Sendo F., Nakayama K., Nakayama K.; "Multiple gene duplication and expression of mouse bcl-2-related genes, A1."; Int. Immunol. 10:631-637(1998).
[3]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-152 IN COMPLEXES WITH BAK1; BID; BMF AND BBC3. DOI=10.1016/j.str.2008.02.009; PubMed=18462686 [NCBI, ExPASy, EBI, Israel, Japan] Smits C., Czabotar P.E., Hinds M.G., Day C.L.; "Structural plasticity underpins promiscuous binding of the prosurvival protein A1."; Structure 16:818-829(2008).

Comments

FUNCTION: Retards apoptosis induced by IL-3 deprivation. May function in the response of hemopoietic cells to external signals and in maintaining endothelial survival during infection.
SUBUNIT: Interacts directly with BCL2L11/BIM (By similarity). Interacts directly with BAK1, BID, BMF and BBC3.
INTERACTION:
Q9BXH1:BBC3 (xeno); NbExp=1; IntAct=EBI-707754, EBI-519884;
O43521:BCL2L11 (xeno); NbExp=1; IntAct=EBI-707754, EBI-526406;
O54918:Bcl2l11; NbExp=1; IntAct=EBI-707754, EBI-526067;
P55957:BID (xeno); NbExp=1; IntAct=EBI-707754, EBI-519672;
Q13323:BIK (xeno); NbExp=1; IntAct=EBI-707754, EBI-700794;
O00198:HRK (xeno); NbExp=1; IntAct=EBI-707754, EBI-701322;
Q13794:PMAIP1 (xeno); NbExp=1; IntAct=EBI-707754, EBI-707392;
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Expressed in hemopoietic tissues, including bone marrow, spleen and thymus.
INDUCTION: By granulocyte-macrophage colony-stimulating factor and LPS in macrophages.
SIMILARITY: Belongs to the Bcl-2 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L16462; AAA16886.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U23774; AAB97953.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U23773; AAB97953.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

I49449; I49449.

NP_033872.1; -.

3D structure databases

PDB

2VOF; X-ray; 1.80 A; A/C=1-152.	[ExPASy / RCSB / EBI]
2VOG; X-ray; 1.90 A; A=1-152.	[ExPASy / RCSB / EBI]
2VOH; X-ray; 1.90 A; A=1-152.	[ExPASy / RCSB / EBI]
2VOI; X-ray; 2.10 A; A=1-152.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

2VOF; -.
2VOG; -.
2VOH; -.
2VOI; -.

ModBase

Q07440.

Protein-protein interaction databases

IntAct

Q07440; -.

Organism-specific databases

MGI

MGI:102687; Bcl2a1a.

Gene expression databases

CleanEx

MM_BCL2A1A; -.

GermOnline

ENSMUSG00000074147; Mus musculus.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0001782;	Biological process: B cell homeostasis (inferred from direct assay from MGI).
GO:0043066;	Biological process: negative regulation of apoptosis (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR013282; Apop_reg_Bcl2Rel.
IPR002475; BCL2_apoptsis.
IPR000712; Bcl2_BH.
Graphical view of domain structure.

Pfam

PF00452; Bcl-2; 1.
Pfam graphical view of domain structure.

PRINTS

PR01862; BCL2FAMILY.
PR01867; BCL2RLATEDA1.

SMART

SM00337; BCL; 1.
SMART graphical view of domain structure.

PROSITE

PS50062; BCL2_FAMILY; 1.
PS01080; BH1; 1.
PS01258; BH2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q07440.

Genome annotation databases

Ensembl

ENSMUSG00000074147; Mus musculus. [Contig view]

GeneID

12044; -.

KEGG

mmu:12044; -.

Phylogenomic databases

HOVERGEN

Q07440; -.

Other

SOURCE

Bcl2a1; Mus musculus.

ProtoNet

Q07440.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Apoptosis; Cytoplasm.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 172`	`172`	`Bcl-2-related protein A1.`	`PRO_0000143095`
`MOTIF`	`77 97`	`21`	`BH1.`
`MOTIF`	`132 147`	`16`	`BH2.`
`COMPBIAS`	`24 33`	`10`	`Ala/Pro-rich.`
`HELIX`	`1 21`	`21`
`HELIX`	`32 51`	`20`
`HELIX`	`53 56`	`4`
`HELIX`	`64 79`	`16`
`HELIX`	`86 105`	`20`
`HELIX`	`114 136`	`23`
`TURN`	`137 142`	`6`
`HELIX`	`143 147`	`5`

Sequence information

Length: 172 AA [This is the length of the unprocessed precursor]

Molecular weight: 19914 Da [This is the MW of the unprocessed precursor]

CRC64: 37AD35818E756488 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAESELMHIH SLAEHYLQYV LQVPAFESAP SQACRVLQRV AFSVQKEVEK NLKSYLDDFH 

        70         80         90        100        110        120 
VESIDTARII FNQVMEKEFE DGIINWGRIV TIFAFGGVLL KKLPQEQIAL DVCAYKQVSS 

       130        140        150        160        170 
FVAEFIMNNT GEWIRQNGGW EDGFIKKFEP KSGWLTFLQM TGQIWEMLFL LK

Q07440 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools