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Protein

Tripartite motif-containing protein 72

Gene

Trim72

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri14 – 5744RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri81 – 12242B box-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. phosphatidylserine binding Source: UniProtKB
  2. ubiquitin conjugating enzyme binding Source: MGI
  3. ubiquitin protein ligase activity Source: MGI
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. exocytosis Source: UniProtKB
  2. membrane budding Source: UniProtKB
  3. muscle organ development Source: UniProtKB
  4. muscle system process Source: UniProtKB
  5. negative regulation of insulin-like growth factor receptor signaling pathway Source: MGI
  6. negative regulation of insulin receptor signaling pathway Source: MGI
  7. negative regulation of myotube differentiation Source: MGI
  8. plasma membrane repair Source: UniProtKB
  9. proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
  10. protein homooligomerization Source: UniProtKB
  11. protein ubiquitination Source: GOC
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Transport

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Tripartite motif-containing protein 72
Alternative name(s):
Mitsugumin-53
Short name:
Mg53
Gene namesi
Name:Trim72Imported
Synonyms:Mg53Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:3612190. Trim72.

Subcellular locationi

Cell membranesarcolemma. Cytoplasmic vesicle membrane
Note: Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine.

GO - Cellular componenti

  1. cytoplasmic vesicle membrane Source: UniProtKB
  2. sarcolemma Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Membrane

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi14 – 141C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi17 – 171C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi29 – 291C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi34 – 341C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi37 – 371C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi53 – 531C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi55 – 551C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi56 – 561C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi86 – 861C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi97 – 971C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi105 – 1051C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi108 – 1081C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi144 – 1441C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi242 – 2421C → A: Dominent-negative mutant that abolishes homooligomerization and function in membrane repair. 1 Publication
Mutagenesisi313 – 3131C → A: Does not affect homooligomerization. 1 Publication
Mutagenesisi456 – 4561C → A: Does not affect homooligomerization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 477477Tripartite motif-containing protein 72PRO_0000278131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei144 – 1441S-nitrosocysteineBy similarity
Disulfide bondi242 – 242Interchain1 Publication

Post-translational modificationi

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.
S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death.By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ1XH17.
PaxDbiQ1XH17.
PRIDEiQ1XH17.

PTM databases

PhosphoSiteiQ1XH17.

Expressioni

Tissue specificityi

Muscle-specific. Exclusively expressed in cardiac and skeletal muscle.1 Publication

Gene expression databases

BgeeiQ1XH17.
CleanExiMM_TRIM72.
GenevestigatoriQ1XH17.

Interactioni

Subunit structurei

Homooligomer; disulfide-linked. Interacts with DYSF and CAV3.2 Publications

Protein-protein interaction databases

BioGridi241694. 2 interactions.
DIPiDIP-60129N.
STRINGi10090.ENSMUSP00000079832.

Structurei

3D structure databases

ProteinModelPortaliQ1XH17.
SMRiQ1XH17. Positions 8-56, 85-256, 278-470.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini271 – 475205B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili135 – 16935Sequence AnalysisAdd
BLAST
Coiled coili204 – 23229Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the TRIM/RBCC family.Sequence Analysis
Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri14 – 5744RING-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri81 – 12242B box-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG305247.
GeneTreeiENSGT00760000118838.
HOGENOMiHOG000234133.
HOVERGENiHBG098570.
InParanoidiQ1XH17.
KOiK12036.
OMAiPCPCCQA.
OrthoDBiEOG7VTDMR.
PhylomeDBiQ1XH17.
TreeFamiTF342569.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q1XH17-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAAPGLLRQ ELSCPLCLQL FDAPVTAECG HSFCRACLIR VAGEPAADGT
60 70 80 90 100
VACPCCQAPT RPQALSTNLQ LSRLVEGLAQ VPQGHCEEHL DPLSIYCEQD
110 120 130 140 150
RTLVCGVCAS LGSHRGHRLL PAAEAQARLK TQLPQQKMQL QEACMRKEKT
160 170 180 190 200
VAVLEHQLVE VEETVRQFRG AVGEQLGKMR MFLAALESSL DREAERVRGD
210 220 230 240 250
AGVALRRELS SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK FCLVTSRLQK
260 270 280 290 300
ILSESPPPAR LDIQLPVISD DFKFQVWKKM FRALMPALEE LTFDPSSAHP
310 320 330 340 350
SLVVSSSGRR VECSDQKAPP AGEDTRQFDK AVAVVAQQLL SQGEHYWEVE
360 370 380 390 400
VGDKPRWALG VMAADASRRG RLHAVPSQGL WLLGLRDGKI LEAHVEAKEP
410 420 430 440 450
RALRTPERPP ARIGLYLSFA DGVLAFYDAS NPDVLTPIFS FHERLPGPVY
460 470
PIFDVCWHDK GKNAQPLLLV GPEQEQA
Length:477
Mass (Da):52,817
Last modified:May 2, 2006 - v1
Checksum:iDFB52299E5FFB66B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS40148.1.
RefSeqiNP_001073401.1. NM_001079932.3.
XP_006508065.1. XM_006508002.1.
UniGeneiMm.389924.

Genome annotation databases

EnsembliENSMUST00000081042; ENSMUSP00000079832; ENSMUSG00000042828.
ENSMUST00000106248; ENSMUSP00000101855; ENSMUSG00000042828.
GeneIDi434246.
KEGGimmu:434246.
UCSCiuc009jxv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS40148.1.
RefSeqiNP_001073401.1. NM_001079932.3.
XP_006508065.1. XM_006508002.1.
UniGeneiMm.389924.

3D structure databases

ProteinModelPortaliQ1XH17.
SMRiQ1XH17. Positions 8-56, 85-256, 278-470.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi241694. 2 interactions.
DIPiDIP-60129N.
STRINGi10090.ENSMUSP00000079832.

PTM databases

PhosphoSiteiQ1XH17.

Proteomic databases

MaxQBiQ1XH17.
PaxDbiQ1XH17.
PRIDEiQ1XH17.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081042; ENSMUSP00000079832; ENSMUSG00000042828.
ENSMUST00000106248; ENSMUSP00000101855; ENSMUSG00000042828.
GeneIDi434246.
KEGGimmu:434246.
UCSCiuc009jxv.2. mouse.

Organism-specific databases

CTDi493829.
MGIiMGI:3612190. Trim72.

Phylogenomic databases

eggNOGiNOG305247.
GeneTreeiENSGT00760000118838.
HOGENOMiHOG000234133.
HOVERGENiHBG098570.
InParanoidiQ1XH17.
KOiK12036.
OMAiPCPCCQA.
OrthoDBiEOG7VTDMR.
PhylomeDBiQ1XH17.
TreeFamiTF342569.

Miscellaneous databases

NextBioi409468.
PROiQ1XH17.
SOURCEiSearch...

Gene expression databases

BgeeiQ1XH17.
CleanExiMM_TRIM72.
GenevestigatoriQ1XH17.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
4.10.45.10. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR003879. Butyrophylin.
IPR013320. ConA-like_dom.
IPR006574. PRY.
IPR003877. SPRY_dom.
IPR000315. Znf_B-box.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13765. PRY. 1 hit.
PF00622. SPRY. 1 hit.
PF00643. zf-B_box. 1 hit.
[Graphical view]
PRINTSiPR01407. BUTYPHLNCDUF.
SMARTiSM00336. BBOX. 1 hit.
SM00589. PRY. 1 hit.
SM00184. RING. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50119. ZF_BBOX. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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.

Entry informationi

Entry nameiTRI72_MOUSE
AccessioniPrimary (citable) accession number: Q1XH17
Secondary accession number(s): B2RWH7, Q6NX76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: May 2, 2006
Last modified: February 4, 2015
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.