B2LA1_MOUSE
ID B2LA1_MOUSE Reviewed; 172 AA.
AC Q07440;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Bcl-2-related protein A1;
DE AltName: Full=A1-A;
DE AltName: Full=Hemopoietic-specific early response protein;
DE AltName: Full=Protein BFL-1;
GN Name=Bcl2a1; Synonyms=A1, Bcl2a1a, Bfl1;
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=CBA/J; TISSUE=Bone marrow;
RX PubMed=8345191;
RA Lin E.Y., Orlofsky A., Berger M.S., Prystowsky M.B.;
RT "Characterization of A1, a novel hemopoietic-specific early-response gene
RT with sequence similarity to bcl-2.";
RL J. Immunol. 151:1979-1988(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Liver;
RX PubMed=9645611; DOI=10.1093/intimm/10.5.631;
RA Hatakeyama S., Hamasaki A., Negishi I., Loh D.Y., Sendo F., Nakayama K.,
RA Nakayama K.;
RT "Multiple gene duplication and expression of mouse bcl-2-related genes,
RT A1.";
RL Int. Immunol. 10:631-637(1998).
RN [3]
RP FUNCTION, AND INTERACTION WITH ING4.
RX PubMed=11888890;
RA Ha S., Lee S., Chung M., Choi Y.;
RT "Mouse ING1 homologue, a protein interacting with A1, enhances cell death
RT and is inhibited by A1 in mammary epithelial cells.";
RL Cancer Res. 62:1275-1278(2002).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-152 IN COMPLEXES WITH BAK1; BID;
RP BMF AND BBC3.
RX PubMed=18462686; DOI=10.1016/j.str.2008.02.009;
RA Smits C., Czabotar P.E., Hinds M.G., Day C.L.;
RT "Structural plasticity underpins promiscuous binding of the prosurvival
RT protein A1.";
RL Structure 16:818-829(2008).
CC -!- FUNCTION: Retards apoptosis induced by IL-3 deprivation. May function
CC in the response of hemopoietic cells to external signals and in
CC maintaining endothelial survival during infection. Can inhibit
CC apoptosis induced by serum starvation in the mammary epithelial cell
CC line HC11 (PubMed:11888890). {ECO:0000269|PubMed:11888890}.
CC -!- SUBUNIT: Interacts directly with BCL2L11/BIM and PMAIP1 (By
CC similarity). Interacts directly with BAK1, BID, BMF and BBC3. Interacts
CC with BOP (By similarity). Interacts with isoform 3, isoform 4 and
CC isoform 5 of ING4. Interacts with UBQLN4 (By similarity).
CC {ECO:0000250|UniProtKB:Q16548, ECO:0000269|PubMed:11888890}.
CC -!- INTERACTION:
CC Q07440; O08734: Bak1; NbExp=2; IntAct=EBI-707754, EBI-822441;
CC Q07440; Q99ML1: Bbc3; NbExp=2; IntAct=EBI-707754, EBI-727801;
CC Q07440; P70444: Bid; NbExp=2; IntAct=EBI-707754, EBI-783400;
CC Q07440; Q91ZE9: Bmf; NbExp=2; IntAct=EBI-707754, EBI-708032;
CC Q07440; O43521: BCL2L11; Xeno; NbExp=2; IntAct=EBI-707754, EBI-526406;
CC Q07440; P55957: BID; Xeno; NbExp=3; IntAct=EBI-707754, EBI-519672;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16548}.
CC -!- TISSUE SPECIFICITY: Expressed in hemopoietic tissues, including bone
CC marrow, spleen and thymus.
CC -!- INDUCTION: By granulocyte-macrophage colony-stimulating factor and LPS
CC in macrophages.
CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}.
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DR EMBL; L16462; AAA16886.1; -; mRNA.
DR EMBL; U23774; AAB97953.1; -; Genomic_DNA.
DR EMBL; U23773; AAB97953.1; JOINED; Genomic_DNA.
DR CCDS; CCDS23391.1; -.
DR PIR; I49449; I49449.
DR RefSeq; NP_033872.1; NM_009742.3.
DR PDB; 2VOF; X-ray; 1.80 A; A/C=1-152.
DR PDB; 2VOG; X-ray; 1.90 A; A=1-152.
DR PDB; 2VOH; X-ray; 1.90 A; A=1-152.
DR PDB; 2VOI; X-ray; 2.10 A; A=1-152.
DR PDBsum; 2VOF; -.
DR PDBsum; 2VOG; -.
DR PDBsum; 2VOH; -.
DR PDBsum; 2VOI; -.
DR AlphaFoldDB; Q07440; -.
DR SMR; Q07440; -.
DR BioGRID; 198319; 1.
DR DIP; DIP-29804N; -.
DR ELM; Q07440; -.
DR IntAct; Q07440; 11.
DR STRING; 10090.ENSMUSP00000096086; -.
DR BindingDB; Q07440; -.
DR ChEMBL; CHEMBL1293239; -.
DR PhosphoSitePlus; Q07440; -.
DR PaxDb; Q07440; -.
DR PRIDE; Q07440; -.
DR ProteomicsDB; 273645; -.
DR DNASU; 12044; -.
DR Ensembl; ENSMUST00000098485; ENSMUSP00000096086; ENSMUSG00000102037.
DR GeneID; 12044; -.
DR KEGG; mmu:12044; -.
DR UCSC; uc009qzh.1; mouse.
DR CTD; 12044; -.
DR MGI; MGI:102687; Bcl2a1a.
DR VEuPathDB; HostDB:ENSMUSG00000102037; -.
DR eggNOG; KOG4728; Eukaryota.
DR GeneTree; ENSGT01050000244872; -.
DR HOGENOM; CLU_1554763_0_0_1; -.
DR InParanoid; Q07440; -.
DR OMA; SELMHIH; -.
DR OrthoDB; 1218929at2759; -.
DR PhylomeDB; Q07440; -.
DR TreeFam; TF315834; -.
DR BioGRID-ORCS; 12044; 5 hits in 38 CRISPR screens.
DR EvolutionaryTrace; Q07440; -.
DR PRO; PR:Q07440; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q07440; protein.
DR Bgee; ENSMUSG00000102037; Expressed in dermatocranium and 65 other tissues.
DR Genevisible; Q07440; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0001783; P:B cell apoptotic process; IDA:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IDA:MGI.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IDA:MGI.
DR CDD; cd06845; Bcl-2_like; 1.
DR Gene3D; 1.10.437.10; -; 1.
DR InterPro; IPR036834; Bcl-2-like_sf.
DR InterPro; IPR046371; Bcl-2_BH1-3.
DR InterPro; IPR026298; Bcl-2_fam.
DR InterPro; IPR002475; Bcl2-like.
DR InterPro; IPR020717; Bcl2_BH1_motif_CS.
DR InterPro; IPR020726; Bcl2_BH2_motif_CS.
DR InterPro; IPR013282; Bcl2A1.
DR PANTHER; PTHR11256; PTHR11256; 1.
DR PANTHER; PTHR11256:SF10; PTHR11256:SF10; 1.
DR Pfam; PF00452; Bcl-2; 1.
DR PRINTS; PR01862; BCL2FAMILY.
DR PRINTS; PR01867; BCL2RLATEDA1.
DR SMART; SM00337; BCL; 1.
DR SUPFAM; SSF56854; SSF56854; 1.
DR PROSITE; PS50062; BCL2_FAMILY; 1.
DR PROSITE; PS01080; BH1; 1.
DR PROSITE; PS01258; BH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Cytoplasm; Reference proteome.
FT CHAIN 1..172
FT /note="Bcl-2-related protein A1"
FT /id="PRO_0000143095"
FT MOTIF 77..97
FT /note="BH1"
FT MOTIF 132..147
FT /note="BH2"
FT HELIX 1..21
FT /evidence="ECO:0007829|PDB:2VOF"
FT HELIX 32..51
FT /evidence="ECO:0007829|PDB:2VOF"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:2VOF"
FT HELIX 64..79
FT /evidence="ECO:0007829|PDB:2VOF"
FT HELIX 86..105
FT /evidence="ECO:0007829|PDB:2VOF"
FT HELIX 114..136
FT /evidence="ECO:0007829|PDB:2VOF"
FT TURN 137..142
FT /evidence="ECO:0007829|PDB:2VOF"
FT HELIX 143..147
FT /evidence="ECO:0007829|PDB:2VOF"
SQ SEQUENCE 172 AA; 19914 MW; 37AD35818E756488 CRC64;
MAESELMHIH SLAEHYLQYV LQVPAFESAP SQACRVLQRV AFSVQKEVEK NLKSYLDDFH
VESIDTARII FNQVMEKEFE DGIINWGRIV TIFAFGGVLL KKLPQEQIAL DVCAYKQVSS
FVAEFIMNNT GEWIRQNGGW EDGFIKKFEP KSGWLTFLQM TGQIWEMLFL LK
