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Q1XH17

- TRI72_MOUSE

UniProt

Q1XH17 - TRI72_MOUSE

Protein

Tripartite motif-containing protein 72

Gene

Trim72

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 76 (01 Oct 2014)
      Sequence version 1 (02 May 2006)
      Previous versions | rss
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    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. protein binding Source: MGI
    3. 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. plasma membrane repair Source: UniProtKB
    6. protein homooligomerization Source: UniProtKB

    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

    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
    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.

    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, 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.
    GeneTreeiENSGT00750000117341.
    HOGENOMiHOG000234133.
    HOVERGENiHBG098570.
    InParanoidiQ6NX76.
    KOiK12036.
    OMAiQDRVLVC.
    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.
    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]
    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

    MSAAPGLLRQ ELSCPLCLQL FDAPVTAECG HSFCRACLIR VAGEPAADGT    50
    VACPCCQAPT RPQALSTNLQ LSRLVEGLAQ VPQGHCEEHL DPLSIYCEQD 100
    RTLVCGVCAS LGSHRGHRLL PAAEAQARLK TQLPQQKMQL QEACMRKEKT 150
    VAVLEHQLVE VEETVRQFRG AVGEQLGKMR MFLAALESSL DREAERVRGD 200
    AGVALRRELS SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK FCLVTSRLQK 250
    ILSESPPPAR LDIQLPVISD DFKFQVWKKM FRALMPALEE LTFDPSSAHP 300
    SLVVSSSGRR VECSDQKAPP AGEDTRQFDK AVAVVAQQLL SQGEHYWEVE 350
    VGDKPRWALG VMAADASRRG RLHAVPSQGL WLLGLRDGKI LEAHVEAKEP 400
    RALRTPERPP ARIGLYLSFA DGVLAFYDAS NPDVLTPIFS FHERLPGPVY 450
    PIFDVCWHDK GKNAQPLLLV GPEQEQA 477
    Length:477
    Mass (Da):52,817
    Last modified:May 2, 2006 - v1
    Checksum:iDFB52299E5FFB66B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS40148.1.
    RefSeqi NP_001073401.1. NM_001079932.3.
    XP_006508065.1. XM_006508002.1.
    UniGenei Mm.389924.

    3D structure databases

    ProteinModelPortali Q1XH17.
    SMRi Q1XH17. Positions 8-56, 278-470.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 241694. 2 interactions.
    DIPi DIP-60129N.
    STRINGi 10090.ENSMUSP00000079832.

    PTM databases

    PhosphoSitei Q1XH17.

    Proteomic databases

    MaxQBi Q1XH17.
    PaxDbi Q1XH17.
    PRIDEi Q1XH17.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000081042 ; ENSMUSP00000079832 ; ENSMUSG00000042828 .
    ENSMUST00000106248 ; ENSMUSP00000101855 ; ENSMUSG00000042828 .
    GeneIDi 434246.
    KEGGi mmu:434246.
    UCSCi uc009jxv.2. mouse.

    Organism-specific databases

    CTDi 493829.
    MGIi MGI:3612190. Trim72.

    Phylogenomic databases

    eggNOGi NOG305247.
    GeneTreei ENSGT00750000117341.
    HOGENOMi HOG000234133.
    HOVERGENi HBG098570.
    InParanoidi Q6NX76.
    KOi K12036.
    OMAi QDRVLVC.
    OrthoDBi EOG7VTDMR.
    PhylomeDBi Q1XH17.
    TreeFami TF342569.

    Miscellaneous databases

    NextBioi 409468.
    PROi Q1XH17.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q1XH17.
    CleanExi MM_TRIM72.
    Genevestigatori Q1XH17.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    4.10.45.10. 1 hit.
    InterProi 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 ]
    Pfami PF13765. PRY. 1 hit.
    PF00622. SPRY. 1 hit.
    PF00643. zf-B_box. 1 hit.
    [Graphical view ]
    PRINTSi PR01407. BUTYPHLNCDUF.
    SMARTi SM00336. BBOX. 1 hit.
    SM00589. PRY. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS50188. B302_SPRY. 1 hit.
    PS50119. ZF_BBOX. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 76 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