A0A9L0S5Z5

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005524 ATP binding	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: ATP binding: The N-terminal nucleotide-binding region is retained in the highly conserved horse HSPA4 sequence. Nucleotide binding is plausible, but the internal 40-residue deletion leaves its chaperone regulation less certain and does not establish intrinsic ATP hydrolysis. Reason: The N-terminal nucleotide-binding region is retained in the highly conserved horse HSPA4 sequence. Nucleotide binding is plausible, but the internal 40-residue deletion leaves its chaperone regulation less certain and does not establish intrinsic ATP hydrolysis. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells. file:HORSE/HSPA4/HSPA4-bioinformatics/RESULTS.md The downloaded human P34932 sequence (840 residues) and selected horse A0A9L0S5Z5 sequence (800 residues) share 97.0% identity among 800 paired residues. Paired coverage is 95.2% of human and 100.0% of horse.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: cytoplasm: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Reason: Apg2/HSPA4 acts as a cytosolic Hsp110 nucleotide-exchange factor that supports Hsc70-mediated protein refolding and disaggregation. Primary biochemical experiments identify the mechanism and distinguish it from the RAC Hsp70 paralog. Transfer to horse is an inference; the paired-sequence report records model-specific gaps and limits. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells. file:HORSE/HSPA4/HSPA4-bioinformatics/RESULTS.md The downloaded human P34932 sequence (840 residues) and selected horse A0A9L0S5Z5 sequence (800 residues) share 97.0% identity among 800 paired residues. Paired coverage is 95.2% of human and 100.0% of horse.
GO:0016887 ATP hydrolysis activity	IEA GO_REF:0000002	UNDECIDED	Summary: ATP hydrolysis activity: The primary Apg2 experiments show modulation of Hsc70 ATP hydrolysis, not necessarily substantial hydrolysis catalyzed by Apg2 itself. A direct HSPA4 ATPase assay is needed to separate the intrinsic catalytic claim from nucleotide-exchange regulation. Reason: The primary Apg2 experiments show modulation of Hsc70 ATP hydrolysis, not necessarily substantial hydrolysis catalyzed by Apg2 itself. A direct HSPA4 ATPase assay is needed to separate the intrinsic catalytic claim from nucleotide-exchange regulation. Supporting Evidence: PMID:30521813 Hsp110s support the refolding of aggregated polypeptides acting as specialized nucleotide exchange factors of Hsp70. We have studied how Apg2, one of the three human Hsp110s, regulates the activity of Hsc70 (HspA8), the constitutive Hsp70 in our cells. file:HORSE/HSPA4/HSPA4-bioinformatics/RESULTS.md The downloaded human P34932 sequence (840 residues) and selected horse A0A9L0S5Z5 sequence (800 residues) share 97.0% identity among 800 paired residues. Paired coverage is 95.2% of human and 100.0% of horse.