UniProt functional annotation for Q6ZMU5



	UniProt functional annotation for Q6ZMU5

UniProt code: Q6ZMU5.

Organism: Homo sapiens (Human).

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

Function: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)- dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity). {ECO:0000250}.

Subunit: Homooligomer; disulfide-linked. Interacts with DYSF and CAV3 (By similarity). {ECO:0000250}.

Subcellular location: Cell membrane, sarcolemma {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. {ECO:0000250}.

Ptm: Disulfide bond formation at Cys-242 occurs in case of membrane damage that cause the entry of the oxidized milieu of the extracellular space, resulting in homooligomerization. {ECO:0000250}.

Ptm: S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death. {ECO:0000269|PubMed:24487118}.

Similarity: Belongs to the TRIM/RBCC family. {ECO:0000255}.

Sequence caution: Sequence=BAC03506.1; Type=Erroneous initiation; Evidence={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:		Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)- dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity). {ECO:0000250}.


Subunit:		Homooligomer; disulfide-linked. Interacts with DYSF and CAV3 (By similarity). {ECO:0000250}.
Subcellular location:		Cell membrane, sarcolemma {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. {ECO:0000250}.
Ptm:		Disulfide bond formation at Cys-242 occurs in case of membrane damage that cause the entry of the oxidized milieu of the extracellular space, resulting in homooligomerization. {ECO:0000250}.
Ptm:		S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death. {ECO:0000269\|PubMed:24487118}.
Similarity:		Belongs to the TRIM/RBCC family. {ECO:0000255}.
Sequence caution:		Sequence=BAC03506.1; Type=Erroneous initiation; Evidence={ECO:0000305};