Q1XH17 (TRI72_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tripartite motif-containing protein 72

Alternative name(s):
Mitsugumin-53
Short name=Mg53

Gene names

Name:	Trim72
Synonyms:	Mg53

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	477 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 Ca2+-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. Ref.1 Ref.3 Ref.4 Ref.5
Subunit structure	Homooligomer; disulfide-linked. Interacts with DYSF and CAV3. Ref.1 Ref.5
Subcellular location	Cell membrane › sarcolemma. Cytoplasmic vesicle membrane. Note: Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. Ref.1 Ref.4
Tissue specificity	Muscle-specific. Exclusively expressed in cardiac and skeletal muscle. Ref.1
Post-translational modification	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.
Disruption phenotype	Viable until at least 11 months of age under unstressed conditions, and develop progressive muscle pathology with age. Mice show progressive myopathy and reduced exercise capability, associated with defective membrane-repair capacity. Ref.1
Sequence similarities	Belongs to the TRIM/RBCC family. Contains 1 B box-type zinc finger. Contains 1 B30.2/SPRY domain. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Exocytosis Transport
Cellular component	Cell membrane Cytoplasmic vesicle Membrane
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	exocytosis Traceable author statement Ref.4. Source: UniProtKB membrane budding Traceable author statement Ref.4. Source: UniProtKB muscle organ development Inferred from mutant phenotype Ref.1. Source: UniProtKB muscle system process Inferred from mutant phenotype Ref.1. Source: UniProtKB plasma membrane repair Inferred from mutant phenotype Ref.1. Source: UniProtKB protein homooligomerization Inferred from physical interaction Ref.1. Source: UniProtKB
Cellular_component	cytoplasmic vesicle membrane Inferred from direct assay Ref.4Ref.1. Source: UniProtKB sarcolemma Inferred from direct assay Ref.4Ref.1. Source: UniProtKB
Molecular_function	phosphatidylserine binding Inferred from direct assay Ref.1. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 477	477	Tripartite motif-containing protein 72		PRO_0000278131
Regions
	Domain	271 – 475	205	B30.2/SPRY
	Zinc finger	14 – 57	44	RING-type
	Zinc finger	81 – 122	42	B box-type
	Coiled coil	135 – 169	35	Potential
	Coiled coil	204 – 232	29	Potential
Amino acid modifications
	Disulfide bond	242		Interchain Ref.1
Experimental info
	Mutagenesis	14	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	17	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	29	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	34	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	37	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	53	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	55	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	56	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	86	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	97	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	105	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	108	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	144	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	242	1	C → A: Dominent-negative mutant that abolishes homooligomerization and function in membrane repair. Ref.1
	Mutagenesis	313	1	C → A: Does not affect homooligomerization. Ref.1
	Mutagenesis	456	1	C → A: Does not affect homooligomerization. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q1XH17 [UniParc]. Last modified May 2, 2006. Version 1. Checksum: DFB52299E5FFB66B	FASTA	477	52,817
	10 20 30 40 50 60 MSAAPGLLRQ ELSCPLCLQL FDAPVTAECG HSFCRACLIR VAGEPAADGT VACPCCQAPT 70 80 90 100 110 120 RPQALSTNLQ LSRLVEGLAQ VPQGHCEEHL DPLSIYCEQD RTLVCGVCAS LGSHRGHRLL 130 140 150 160 170 180 PAAEAQARLK TQLPQQKMQL QEACMRKEKT VAVLEHQLVE VEETVRQFRG AVGEQLGKMR 190 200 210 220 230 240 MFLAALESSL DREAERVRGD AGVALRRELS SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK 250 260 270 280 290 300 FCLVTSRLQK ILSESPPPAR LDIQLPVISD DFKFQVWKKM FRALMPALEE LTFDPSSAHP 310 320 330 340 350 360 SLVVSSSGRR VECSDQKAPP AGEDTRQFDK AVAVVAQQLL SQGEHYWEVE VGDKPRWALG 370 380 390 400 410 420 VMAADASRRG RLHAVPSQGL WLLGLRDGKI LEAHVEAKEP RALRTPERPP ARIGLYLSFA 430 440 450 460 470 DGVLAFYDAS NPDVLTPIFS FHERLPGPVY PIFDVCWHDK GKNAQPLLLV GPEQEQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MG53 nucleates assembly of cell membrane repair machinery." Cai C., Masumiya H., Weisleder N., Matsuda N., Nishi M., Hwang M., Ko J.-K., Lin P., Thornton A., Zhao X., Pan Z., Komazaki S., Brotto M., Takeshima H., Ma J. Nat. Cell Biol. 11:56-64(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, PHOSPHATIDYLSERINE-BINDING, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DISULFIDE BOND AT CYS-242, MUTAGENESIS OF CYS-14; CYS-17; CYS-29; CYS-34; CYS-37; CYS-53; CYS-55; CYS-56; CYS-86; CYS-97; CYS-105; CYS-108; CYS-144; CYS-242; CYS-313 AND CYS-456. Strain: C57BL/6J. Tissue: Skeletal muscle.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Jaw and Limb.
[3]	"Mitsugumin 53-mediated maintenance of K+ currents in cardiac myocytes." Masumiya H., Asaumi Y., Nishi M., Minamisawa S., Adachi-Akahane S., Yoshida M., Kangawa K., Ito K., Kagaya Y., Yanagisawa T., Yamazaki T., Ma J., Takeshima H. Channels 3:6-11(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[4]	"MG53 regulates membrane budding and exocytosis in muscle cells." Cai C., Masumiya H., Weisleder N., Pan Z., Nishi M., Komazaki S., Takeshima H., Ma J. J. Biol. Chem. 284:3314-3322(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]	"Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin." Cai C., Weisleder N., Ko J.-K., Komazaki S., Sunada Y., Nishi M., Takeshima H., Ma J. J. Biol. Chem. 284:15894-15902(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH DYSF AND CAV3.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB231474 mRNA. Translation: BAE93014.1. BC067209 mRNA. Translation: AAH67209.1. BC147789 mRNA. Translation: AAI47790.1. BC158111 mRNA. Translation: AAI58112.1. BC158120 mRNA. Translation: AAI58121.1.
IPI	IPI00462157.
RefSeq	NP_001073401.1. NM_001079932.3.
UniGene	Mm.389924.
3D structure databases
ProteinModelPortal	Q1XH17.
SMR	Q1XH17. Positions 8-56, 278-470.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000079832.
PTM databases
PhosphoSite	Q1XH17.
Proteomic databases
PaxDb	Q1XH17.
PRIDE	Q1XH17.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000081042; ENSMUSP00000079832; ENSMUSG00000042828. ENSMUST00000106248; ENSMUSP00000101855; ENSMUSG00000042828.
GeneID	434246.
KEGG	mmu:434246.
UCSC	uc009jxv.2. mouse.
Organism-specific databases
CTD	493829.
MGI	MGI:3612190. Trim72.
Phylogenomic databases
eggNOG	NOG305247.
GeneTree	ENSGT00680000099496.
HOGENOM	HOG000234133.
HOVERGEN	HBG098570.
InParanoid	Q6NX76.
KO	K12036.
OMA	QDRVLVC.
OrthoDB	EOG498V10.
Gene expression databases
Bgee	Q1XH17.
CleanEx	MM_TRIM72.
Genevestigator	Q1XH17.
Family and domain databases
Gene3D	3.30.40.10. 1 hit. 4.10.45.10. 1 hit.
InterPro	IPR001870. B30.2/SPRY. IPR003879. Butyrophylin. IPR008985. ConA-like_lec_gl_sf. IPR006574. PRY. IPR003877. SPRY_rcpt. IPR000315. Znf_B-box. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfam	PF00622. SPRY. 1 hit. PF00643. zf-B_box. 1 hit. [Graphical view]
PRINTS	PR01407. BUTYPHLNCDUF.
SMART	SM00336. BBOX. 1 hit. SM00589. PRY. 1 hit. SM00184. RING. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit.
PROSITE	PS50188. B302_SPRY. 1 hit. PS50119. ZF_BBOX. 1 hit. PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	409468.
SOURCE	Search...

Entry information

Entry name

TRI72_MOUSE

Accession

Primary (citable) accession number: Q1XH17
Secondary accession number(s): B2RWH7, Q6NX76

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 20, 2007
Last sequence update:	May 2, 2006
Last modified:	May 29, 2013
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program