BCL2L10

The protein encoded by this gene belongs to the BCL-2 protein family. BCL-2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. The protein encoded by this gene contains conserved BH4, BH1 and BH2 domains. This protein can interact with other members of BCL-2 protein family including BCL2, BCL2L1/BCL-X(L), and BAX. Overexpression of this gene has been shown to suppress cell apoptosis possibly through the prevention of cytochrome C release from the mitochondria, and thus activating caspase-3 activation. The mouse counterpart of this protein is found to interact with Apaf1 and forms a protein complex with Caspase 9, which suggests the involvement of this protein in APAF1 and CASPASE 9 related apoptotic pathway. [provided by RefSeq]

BCL2-like 10 (apoptosis facilitator)

Promotes cell survival by suppressing apoptosis induced by BAX but not BAK (PubMed:11689480, PubMed:11278245).
Increases binding of AHCYL1/IRBIT to ITPR1 (PubMed:27995898).
Reduces ITPR1-mediated calcium release from the endoplasmic reticulum cooperatively with AHCYL1/IRBIT under normal cellular conditions (PubMed:27995898).
Under apoptotic stress conditions, dissociates from ITPR1 and is displaced from mitochondria-associated endoplasmic reticulum membranes, leading to increased Ca2+ transfer to mitochondria which promotes apoptosis (PubMed:27995898).

Activation of cysteine-type endopeptidase activity involved in apoptotic process Source: ProtInc
Apoptotic process Source: UniProtKB
Extrinsic apoptotic signaling pathway in absence of ligand Source: GO_Central
Female gamete generation Source: ProtInc
Intrinsic apoptotic signaling pathway in response to DNA damage Source: GO_Central
Negative regulation of apoptotic process Source: HGNC-UCL
Negative regulation of intrinsic apoptotic signaling pathway Source: GO_Central
Spermatogenesis Source: ProtInc

Nucleus membrane; Endoplasmic reticulum; Mitochondrion. Localizes to mitochondria-associated endoplasmic reticulum membranes (MAMs) (PubMed:27995898). Localization to MAMs is greatly reduced under apoptotic stress conditions (PubMed:27995898).

Helical: 183-200 aa