MYL10

Summary: Calcium-binding EF-hand architecture supports the conserved molecular function.

Reason: Human MYL10 has PROSITE-ProRule calcium-coordinating positions in the first EF-hand. The horse protein retains the EF-hand core, including the corresponding binding-region sequence. The IBA represents curated placement of calcium binding in the light-chain phylogeny; the InterPro evidence is compatible sequence support. Direct calcium-binding measurements on horse MYL10 are not asserted.

Summary: Calcium-binding EF-hand architecture supports the conserved molecular function.

Reason: Human MYL10 has PROSITE-ProRule calcium-coordinating positions in the first EF-hand. The horse protein retains the EF-hand core, including the corresponding binding-region sequence. The IBA represents curated placement of calcium binding in the light-chain phylogeny; the InterPro evidence is compatible sequence support. Direct calcium-binding measurements on horse MYL10 are not asserted.

Summary: The ZNF76 binary interaction is retained as a non-core experimental observation.

Reason: The cited human interactome study supplies an IPI interaction, and the reviewed UniProt record independently lists Q9BUA6–P36508 with three experiments. Generic protein binding does not identify the physiological role of MYL10 or establish a myosin partner. Retain the observation without treating it as a core function.

Summary: Cytoplasmic distribution is compatible with the conserved myosin light-chain role.

Reason: The curated ancestral IBA supports cytoplasmic activity within the myosin light-chain family. This is an appropriate location for a soluble light-chain protein and there is no target-specific evidence of loss. It does not imply that all MYL10 is exclusively cytoplasmic.

Summary: Retain the reported mitochondrial localization as a non-core localization.

Reason: Human MYL10 has a direct expressed-fusion-protein localization annotation under GO_REF:0000054. The PAINT IBA is experimentally grounded on that human observation and is not circular because human MYL10 appears as its own descendant source. The horse transfer is plausible but the physiological function of this mitochondrial pool is unresolved; do not infer a mitochondrial targeting sequence or a mitochondrial myosin motor from this observation.

Summary: Retain the reported mitochondrial localization as a non-core localization.

Reason: Human MYL10 has a direct expressed-fusion-protein localization annotation under GO_REF:0000054. The PAINT IBA is experimentally grounded on that human observation and is not circular because human MYL10 appears as its own descendant source. The horse transfer is plausible but the physiological function of this mitochondrial pool is unresolved; do not infer a mitochondrial targeting sequence or a mitochondrial myosin motor from this observation.

Summary: Cytosolic association is compatible with a soluble regulatory light-chain protein.

Reason: The cytoplasmic IBA and conserved light-chain architecture support an intracellular soluble pool. Reactome places this protein in myosin-associated reactions, but these location annotations alone do not establish a specific MYL10-dependent contractile mechanism. The ARBA row is an annotation overlap, not independent validation.

Summary: Cytosolic association is compatible with a soluble regulatory light-chain protein.

Reason: The cytoplasmic IBA and conserved light-chain architecture support an intracellular soluble pool. Reactome places this protein in myosin-associated reactions, but these location annotations alone do not establish a specific MYL10-dependent contractile mechanism. The ARBA row is an annotation overlap, not independent validation.

Summary: Cytosolic association is compatible with a soluble regulatory light-chain protein.

Reason: The cytoplasmic IBA and conserved light-chain architecture support an intracellular soluble pool. Reactome places this protein in myosin-associated reactions, but these location annotations alone do not establish a specific MYL10-dependent contractile mechanism. The ARBA row is an annotation overlap, not independent validation.

Summary: Cytosolic association is compatible with a soluble regulatory light-chain protein.

Reason: The cytoplasmic IBA and conserved light-chain architecture support an intracellular soluble pool. Reactome places this protein in myosin-associated reactions, but these location annotations alone do not establish a specific MYL10-dependent contractile mechanism. The ARBA row is an annotation overlap, not independent validation.

Summary: Cytosolic association is compatible with a soluble regulatory light-chain protein.

Reason: The cytoplasmic IBA and conserved light-chain architecture support an intracellular soluble pool. Reactome places this protein in myosin-associated reactions, but these location annotations alone do not establish a specific MYL10-dependent contractile mechanism. The ARBA row is an annotation overlap, not independent validation.

Summary: Cytosolic association is compatible with a soluble regulatory light-chain protein.

Reason: The cytoplasmic IBA and conserved light-chain architecture support an intracellular soluble pool. Reactome places this protein in myosin-associated reactions, but these location annotations alone do not establish a specific MYL10-dependent contractile mechanism. The ARBA row is an annotation overlap, not independent validation.