UniProt functional annotation for P63098



	UniProt functional annotation for P63098

UniProt code: P63098.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity. {ECO:0000269|PubMed:26794871}.

Subunit: Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding subunit (also known as calcineurin B) (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:26794871, PubMed:27974827). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). Interacts with catalytic subunit PPP3CA/calcineurin A (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:27974827). Interacts with catalytic subunit PPP3CB/calcineurin A (PubMed:26794871). Interacts with CIB1 (via C-terminal region); the interaction increases upon cardiomyocyte hypertrophy (By similarity). Interacts with RCAN1 (PubMed:12809556). {ECO:0000250|UniProtKB:Q63810, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:12809556, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402}.

Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63810}. Cell membrane {ECO:0000250|UniProtKB:Q63810}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q63810}. Cell membrane {ECO:0000269|PubMed:25255805}; Lipid-anchor {ECO:0000269|PubMed:25255805}. Note=Translocates from the cytosol to the sarcolemma in a CIB1-dependent manner during cardiomyocyte hypertrophy. {ECO:0000250|UniProtKB:Q63810}.

Miscellaneous: This protein has four functional calcium-binding sites (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:26794871, PubMed:27974827). Although African swine fever virus infects pigs and not humans, human PPP3R1 and PPP3CA have been used for the crystallization. PPP3CA and PPP3R1 interact with African swine fever virus Mal-047/A238L (via PKIIIT and FLCVK motifs); the interaction does not block catalytic activity per se but inhibits PPP3CA function by blocking the access to the two substrate recognition (PubMed:23468591). {ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402}.

Similarity: Belongs to the calcineurin regulatory subunit family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity. {ECO:0000269\|PubMed:26794871}.


Subunit:		Forms a complex composed of a calmodulin-dependent catalytic subunit (also known as calcineurin A) and a regulatory Ca(2+)-binding subunit (also known as calcineurin B) (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:26794871, PubMed:27974827). There are three catalytic subunits, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two regulatory subunits which are also encoded by separate genes (PPP3R1 and PPP3R2). Interacts with catalytic subunit PPP3CA/calcineurin A (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:27974827). Interacts with catalytic subunit PPP3CB/calcineurin A (PubMed:26794871). Interacts with CIB1 (via C-terminal region); the interaction increases upon cardiomyocyte hypertrophy (By similarity). Interacts with RCAN1 (PubMed:12809556). {ECO:0000250\|UniProtKB:Q63810, ECO:0000269\|PubMed:12218175, ECO:0000269\|PubMed:12357034, ECO:0000269\|PubMed:12809556, ECO:0000269\|PubMed:17498738, ECO:0000269\|PubMed:22343722, ECO:0000269\|PubMed:23468591, ECO:0000269\|PubMed:26794871, ECO:0000269\|PubMed:27974827, ECO:0000269\|PubMed:8524402}.
Subcellular location:		Cytoplasm, cytosol {ECO:0000250\|UniProtKB:Q63810}. Cell membrane {ECO:0000250\|UniProtKB:Q63810}. Cell membrane, sarcolemma {ECO:0000250\|UniProtKB:Q63810}. Cell membrane {ECO:0000269\|PubMed:25255805}; Lipid-anchor {ECO:0000269\|PubMed:25255805}. Note=Translocates from the cytosol to the sarcolemma in a CIB1-dependent manner during cardiomyocyte hypertrophy. {ECO:0000250\|UniProtKB:Q63810}.
Miscellaneous:		This protein has four functional calcium-binding sites (PubMed:8524402, PubMed:12218175, PubMed:12357034, PubMed:17498738, PubMed:22343722, PubMed:23468591, PubMed:26794871, PubMed:27974827). Although African swine fever virus infects pigs and not humans, human PPP3R1 and PPP3CA have been used for the crystallization. PPP3CA and PPP3R1 interact with African swine fever virus Mal-047/A238L (via PKIIIT and FLCVK motifs); the interaction does not block catalytic activity per se but inhibits PPP3CA function by blocking the access to the two substrate recognition (PubMed:23468591). {ECO:0000269\|PubMed:12218175, ECO:0000269\|PubMed:12357034, ECO:0000269\|PubMed:17498738, ECO:0000269\|PubMed:22343722, ECO:0000269\|PubMed:23468591, ECO:0000269\|PubMed:26794871, ECO:0000269\|PubMed:27974827, ECO:0000269\|PubMed:8524402}.
Similarity:		Belongs to the calcineurin regulatory subunit family. {ECO:0000305}.