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Q1XH17 (TRI72_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tripartite motif-containing protein 72
Alternative name(s):
Mitsugumin-53
Short name=Mg53
Gene names
Name:Trim72
Synonyms:Mg53
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceEvidence 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 membranesarcolemma. 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477Tripartite motif-containing protein 72
PRO_0000278131

Regions

Domain271 – 475205B30.2/SPRY
Zinc finger14 – 5744RING-type
Zinc finger81 – 12242B box-type
Coiled coil135 – 16935 Potential
Coiled coil204 – 23229 Potential

Amino acid modifications

Disulfide bond242Interchain Ref.1

Experimental info

Mutagenesis141C → A: Does not affect homooligomerization. Ref.1
Mutagenesis171C → A: Does not affect homooligomerization. Ref.1
Mutagenesis291C → A: Does not affect homooligomerization. Ref.1
Mutagenesis341C → A: Does not affect homooligomerization. Ref.1
Mutagenesis371C → A: Does not affect homooligomerization. Ref.1
Mutagenesis531C → A: Does not affect homooligomerization. Ref.1
Mutagenesis551C → A: Does not affect homooligomerization. Ref.1
Mutagenesis561C → A: Does not affect homooligomerization. Ref.1
Mutagenesis861C → A: Does not affect homooligomerization. Ref.1
Mutagenesis971C → A: Does not affect homooligomerization. Ref.1
Mutagenesis1051C → A: Does not affect homooligomerization. Ref.1
Mutagenesis1081C → A: Does not affect homooligomerization. Ref.1
Mutagenesis1441C → A: Does not affect homooligomerization. Ref.1
Mutagenesis2421C → A: Dominent-negative mutant that abolishes homooligomerization and function in membrane repair. Ref.1
Mutagenesis3131C → A: Does not affect homooligomerization. Ref.1
Mutagenesis4561C → A: Does not affect homooligomerization. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q1XH17 [UniParc].

Last modified May 2, 2006. Version 1.
Checksum: DFB52299E5FFB66B

FASTA47752,817
        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 

« Hide

References

« Hide '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.
RefSeqNP_001073401.1. NM_001079932.3.
XP_006508065.1. XM_006508002.1.
UniGeneMm.389924.

3D structure databases

ProteinModelPortalQ1XH17.
SMRQ1XH17. Positions 8-56, 85-122, 278-470.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid241694. 2 interactions.
DIPDIP-60129N.
STRING10090.ENSMUSP00000079832.

PTM databases

PhosphoSiteQ1XH17.

Proteomic databases

PaxDbQ1XH17.
PRIDEQ1XH17.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000081042; ENSMUSP00000079832; ENSMUSG00000042828.
ENSMUST00000106248; ENSMUSP00000101855; ENSMUSG00000042828.
GeneID434246.
KEGGmmu:434246.
UCSCuc009jxv.2. mouse.

Organism-specific databases

CTD493829.
MGIMGI:3612190. Trim72.

Phylogenomic databases

eggNOGNOG305247.
GeneTreeENSGT00750000117341.
HOGENOMHOG000234133.
HOVERGENHBG098570.
InParanoidQ6NX76.
KOK12036.
OMAQDRVLVC.
OrthoDBEOG7VTDMR.
PhylomeDBQ1XH17.
TreeFamTF342569.

Gene expression databases

BgeeQ1XH17.
CleanExMM_TRIM72.
GenevestigatorQ1XH17.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProIPR001870. 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]
PfamPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSPR01407. BUTYPHLNCDUF.
SMARTSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
PROSITEPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio409468.
PROQ1XH17.
SOURCESearch...

Entry information

Entry nameTRI72_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot