Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Bcl-2-like protein 1

Gene

Bcl2l1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.
Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F1F0 activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release (By similarity).By similarity5 Publications
Isoform Bcl-X(S) promotes apoptosis.

GO - Molecular functioni

  • BH domain binding Source: RGD
  • clathrin binding Source: CAFA
  • cysteine-type endopeptidase inhibitor activity involved in apoptotic process Source: RGD
  • GTPase binding Source: CAFA
  • MDM2/MDM4 family protein binding Source: RGD
  • protein-containing complex binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: GO_Central
  • transcription factor binding Source: RGD

GO - Biological processi

  • aging Source: RGD
  • apoptotic process Source: RGD
  • cellular response to astaxanthin Source: RGD
  • cellular response to cAMP Source: RGD
  • cellular response to dexamethasone stimulus Source: RGD
  • cellular response to drug Source: RGD
  • cellular response to erythropoietin Source: RGD
  • cellular response to hypoxia Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to prolactin Source: RGD
  • cellular response to thapsigargin Source: RGD
  • cellular response to tumor necrosis factor Source: RGD
  • cerebral cortex development Source: RGD
  • endocytosis Source: UniProtKB-KW
  • extrinsic apoptotic signaling pathway in absence of ligand Source: GO_Central
  • intrinsic apoptotic signaling pathway in response to DNA damage Source: GO_Central
  • mitotic cell cycle checkpoint Source: UniProtKB
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of execution phase of apoptosis Source: UniProtKB
  • negative regulation of intrinsic apoptotic signaling pathway Source: GO_Central
  • ovarian follicle development Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of ATP biosynthetic process Source: CAFA
  • positive regulation of synaptic vesicle clustering Source: CAFA
  • positive regulation of synaptic vesicle endocytosis Source: CAFA
  • positive regulation of synaptic vesicle exocytosis Source: CAFA
  • regulation of apoptotic process Source: RGD
  • regulation of cytokinesis Source: UniProtKB
  • regulation of long term synaptic depression Source: CAFA
  • response to drug Source: RGD
  • response to electrical stimulus Source: RGD
  • response to erythropoietin Source: RGD
  • response to hydrogen peroxide Source: RGD
  • response to hypoxia Source: RGD
  • response to inorganic substance Source: RGD
  • response to ischemia Source: RGD
  • response to lead ion Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to organonitrogen compound Source: RGD
  • response to oxidative stress Source: RGD
  • response to peptide hormone Source: RGD
  • synaptic vesicle recycling via endosome Source: CAFA

Keywordsi

Biological processApoptosis, Endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Bcl-2-like protein 1
Short name:
Bcl2-L-1
Alternative name(s):
Apoptosis regulator Bcl-X
Gene namesi
Name:Bcl2l1
Synonyms:Bclx, Blc2l
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi2200 Bcl2l1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei210 – 226HelicalSequence analysisAdd BLAST17

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane, Nucleus, Synapse

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL1075182

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001430651 – 233Bcl-2-like protein 1Add BLAST233

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei49Phosphoserine; by PLK3By similarity1
Modified residuei62Phosphoserine; by CDK1By similarity1

Post-translational modificationi

Proteolytically cleaved by caspases during apoptosis. The cleaved protein, lacking the BH4 motif, has pro-apoptotic activity (By similarity).By similarity
Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial in normal mitotic cells, but complete in G2-arrested cells upon DNA-damage, thus promoting subsequent apoptosis probably by triggering caspases-mediated proteolysis. Phosphorylated by PLK3, leading to regulate the G2 checkpoint and progression to cytokinesis during mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, disappears rapidly in early mitosis during prometaphase, metaphase and early anaphase, and re-appears during telophase and cytokinesis (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP53563
PRIDEiP53563

PTM databases

iPTMnetiP53563
PhosphoSitePlusiP53563
SwissPalmiP53563

Expressioni

Tissue specificityi

Expressed in most tissues. Bcl-X(beta) is specifically expressed in cerebellum, heart, and thymus. In the ovary, the predominant form is Bcl-X(L), with a small but detectable level of Bcl-X(S).

Gene expression databases

BgeeiENSRNOG00000007946
ExpressionAtlasiP53563 baseline and differential
GenevisibleiP53563 RN

Interactioni

Subunit structurei

Homodimer. Isoform Bcl-X(L) forms heterodimers with BAX, BAK or BCL2. Heterodimerization with BAX does not seem to be required for anti-apoptotic activity. Interacts with BCL2L11. Interacts with BAD. Isoform Bcl-X(L) interacts with SIVA1 isoform 1; the interaction inhibits the anti-apoptotic activity. Interacts with BECN1 and PGAM5. Isoform Bcl-X(L) interacts with IKZF3. Interacts with HEBP2. Isoform Bcl-X(L) interacts with BOP. Interacts with p53/TP53 and BBC3; interaction with BBC3 disrupts the interaction with p53/TP53. Isoform Bcl-X(L) interacts with DNM1L and CLTA; DNM1L and BCL2L1 isoform BCL-X(L) may form a complex in synaptic vesicles that also contains clathrin and MFF. Interacts with ATP5F1A and ATP5F1B; the interactions mediate the association of isoform Bcl-X(L) with the mitochondrial membrane ATP synthase F1F0 ATP synthase. Interacts with VDAC1 (By similarity). Isoform Bcl-X(L) interacts (via the loop between motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with NLRP2, NLRP3, NLRP4, PYCARD, nor MEFV (By similarity). Interacts with BCL2L11 (via BH3) (By similarity).By similarity3 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • BH domain binding Source: RGD
  • clathrin binding Source: CAFA
  • GTPase binding Source: CAFA
  • MDM2/MDM4 family protein binding Source: RGD
  • protein heterodimerization activity Source: RGD
  • protein homodimerization activity Source: GO_Central
  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi246998, 5 interactors
ComplexPortaliCPX-2022 BAD:BCL-XL complex [P53563-1]
CPX-2026 BIM:BCL-XL complex [P53563-1]
CPX-2030 PUMA:BCL-XL complex [P53563-1]
CPX-2038 BID:BCL-XL complex [P53563-1]
CPX-300 BCL-XL complex [P53563-1]
CORUMiP53563
DIPiDIP-29698N
IntActiP53563, 5 interactors
STRINGi10116.ENSRNOP00000043542

Structurei

Secondary structure

1233
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 19Combined sources18
Turni25 – 28Combined sources4
Helixi82 – 100Combined sources19
Helixi102 – 111Combined sources10
Turni116 – 118Combined sources3
Helixi119 – 130Combined sources12
Turni131 – 133Combined sources3
Helixi137 – 156Combined sources20
Helixi162 – 177Combined sources16
Helixi179 – 184Combined sources6
Helixi187 – 196Combined sources10

3D structure databases

DisProtiDP00449
ProteinModelPortaliP53563
SMRiP53563
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53563

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi4 – 24BH4Add BLAST21
Motifi86 – 100BH3Add BLAST15
Motifi129 – 148BH1Add BLAST20
Motifi180 – 195BH2Add BLAST16

Domaini

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.
The loop between motifs BH4 and BH3 is required for the interaction with NLRP1.By similarity

Sequence similaritiesi

Belongs to the Bcl-2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4728 Eukaryota
ENOG41123S0 LUCA
GeneTreeiENSGT00530000062935
InParanoidiP53563
KOiK04570
OMAiNGSPSWH
PhylomeDBiP53563

Family and domain databases

Gene3Di1.10.437.10, 1 hit
InterProiView protein in InterPro
IPR013279 Apop_reg_BclX
IPR002475 Bcl2-like
IPR004725 Bcl2/BclX
IPR020717 Bcl2_BH1_motif_CS
IPR020726 Bcl2_BH2_motif_CS
IPR020728 Bcl2_BH3_motif_CS
IPR003093 Bcl2_BH4
IPR020731 Bcl2_BH4_motif_CS
IPR036834 Blc2-like_sf
IPR026298 Blc2_fam
PANTHERiPTHR11256 PTHR11256, 1 hit
PTHR11256:SF12 PTHR11256:SF12, 1 hit
PfamiView protein in Pfam
PF00452 Bcl-2, 1 hit
PF02180 BH4, 1 hit
PRINTSiPR01864 APOPREGBCLX
PR01862 BCL2FAMILY
SMARTiView protein in SMART
SM00265 BH4, 1 hit
SUPFAMiSSF56854 SSF56854, 1 hit
TIGRFAMsiTIGR00865 bcl-2, 1 hit
PROSITEiView protein in 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

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Bcl-X(L) (identifier: P53563-1) [UniParc]FASTAAdd to basket
Also known as: Bcl-xL

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.

« Hide

        10         20         30         40         50
MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEPERETPSA
60 70 80 90 100
INGNPSWHLA DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR
110 120 130 140 150
YRRAFSDLTS QLHITPGTAY QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL
160 170 180 190 200
CVESVDKEMQ VLVSRIASWM ATYLNDHLEP WIQENGGWDT FVDLYGNNAA
210 220 230
AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK
Length:233
Mass (Da):26,158
Last modified:November 1, 1997 - v2
Checksum:i2B62B6C63864BC8F
GO
Isoform Bcl-X(S) (identifier: P53563-2) [UniParc]FASTAAdd to basket
Also known as: Bcl-xS

The sequence of this isoform differs from the canonical sequence as follows:
     126-188: Missing.

Show »
Length:170
Mass (Da):18,987
Checksum:iD90868EC7F69ED59
GO
Isoform Bcl-X(beta) (identifier: P53563-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     189-233: DTFVDLYGNN...VLLGSLFSRK → VRTTPLVCPP...DYSGDIPGLL

Show »
Length:232
Mass (Da):25,865
Checksum:i5B44307AB9D2975E
GO

Sequence cautioni

The sequence AAC60701 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAC60702 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti6R → Q in CAA57886 (Ref. 1) Curated1
Sequence conflicti6R → Q in CAA57887 (Ref. 1) Curated1
Sequence conflicti12F → S in AAA19257 (Ref. 2) Curated1
Sequence conflicti64A → E in AAA19257 (Ref. 2) Curated1
Sequence conflicti81I → L in AAA77686 (PubMed:7828536).Curated1
Sequence conflicti81I → L in AAC60701 (PubMed:7828536).Curated1
Sequence conflicti81I → L in AAC60702 (PubMed:7828536).Curated1
Sequence conflicti119A → V in AAA77686 (PubMed:7828536).Curated1
Sequence conflicti119A → V in AAC60701 (PubMed:7828536).Curated1
Sequence conflicti119A → V in AAC60702 (PubMed:7828536).Curated1
Sequence conflicti143 – 144FF → SS in AAA77686 (PubMed:7828536).Curated2
Sequence conflicti143 – 144FF → SS in AAC60701 (PubMed:7828536).Curated2
Sequence conflicti199A → T in AAA77686 (PubMed:7828536).Curated1
Sequence conflicti199A → T in AAC60701 (PubMed:7828536).Curated1
Sequence conflicti199A → T in AAC60702 (PubMed:7828536).Curated1
Sequence conflicti201A → P in AAA77686 (PubMed:7828536).Curated1
Sequence conflicti201A → P in AAC60701 (PubMed:7828536).Curated1
Sequence conflicti201A → P in AAC60702 (PubMed:7828536).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_000520126 – 188Missing in isoform Bcl-X(S). CuratedAdd BLAST63
Alternative sequenceiVSP_000521189 – 233DTFVD…LFSRK → VRTTPLVCPPLVCLSSVEIP NCPFWSPGMVVEDIDYSGDI PGLL in isoform Bcl-X(beta). CuratedAdd BLAST45

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82537 Genomic DNA Translation: CAA57886.1
X82537 Genomic DNA Translation: CAA57887.1
U10579 Unassigned DNA Translation: AAA19257.1
U72350 mRNA Translation: AAB17353.1
U72349 mRNA Translation: AAB17352.1
U34963 mRNA Translation: AAA77686.1
S76513 mRNA Translation: AAC60701.2 Different initiation.
S78284 mRNA Translation: AAC60702.1 Different initiation.
BC094213 mRNA Translation: AAH94213.1
PIRiI67431
I67435
S51761
RefSeqiNP_001028842.1, NM_001033670.1 [P53563-1]
NP_001028843.1, NM_001033671.1 [P53563-2]
NP_113723.2, NM_031535.2
XP_006235327.1, XM_006235265.3 [P53563-1]
UniGeneiRn.10323

Genome annotation databases

EnsembliENSRNOT00000010762; ENSRNOP00000010762; ENSRNOG00000007946 [P53563-1]
GeneIDi24888
KEGGirno:24888
UCSCiRGD:2200 rat [P53563-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiB2CL1_RAT
AccessioniPrimary (citable) accession number: P53563
Secondary accession number(s): P70613
, P70614, Q52KS0, Q62678, Q62836, Q64087, Q64128
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 1, 1997
Last modified: June 20, 2018
This is version 173 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health