| Tag | Content |
|---|
| CPLM ID | CPLM-024213 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Tripartite motif-containing protein 72 |
Protein Synonyms/Alias | Mitsugumin-53; Mg53 |
Gene Name | Trim72 |
Gene Synonyms/Alias | Mg53 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 278 | DFKFQVWKKMFRALM | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | 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). |
Sequence Annotation | DOMAIN 271 475 B30.2/SPRY.
ZN_FING 14 57 RING-type.
ZN_FING 81 122 B box-type.
DISULFID 242 242 Interchain (By similarity). |
Keyword | Cell membrane; Coiled coil; Complete proteome; Cytoplasmic vesicle; Disulfide bond; Exocytosis; Membrane; Metal-binding; Reference proteome; Transport; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 477 AA |
Protein Sequence | MSTAPGLLRQ ELSCPLCLQL FDAPVTAECG HSFCRACLIR VAGEPADDGT VACPCCQAST 60
RPQALSTNLQ LARLVEGLAQ VPQGHCEEHL DPLSIYCEQD RTLVCGVCAS LGSHRGHRLL 120
PAAEAHARLK TQLPQQKAQL QEACMRKEKS VAVLEHQLVE VEETVRQFRG AVGEQLGKMR 180
MFLAALESSL DREAERVRGE AGVALRRELS SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK 240
FCLVTSRLQK ILSESPPPAR LDIQLPVISD DFKFQVWKKM FRALMPELEE LTFDPSSAHP 300
SLVVSASGRR VECSEQKAPP AGEDTCQFDK TVAVVAKQLL SQGEHYWEVE VGDKPRWALG 360
VMAADASRRG RLHAVPSQGL WLLGLRDGKI LEAHVEAKEP RALRTPERPP ARIGLYLSFA 420
DGVLTFYDAS NTDALTPLFS FHERLPGPVY PMFDVCWHDK GKNSQPLLLV GPDSEQA 477 |
Gene Ontology | GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB. GO:0042383; C:sarcolemma; ISS:UniProtKB. GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006887; P:exocytosis; IEA:UniProtKB-KW. GO:0007517; P:muscle organ development; ISS:UniProtKB. GO:0003012; P:muscle system process; ISS:UniProtKB. GO:0001778; P:plasma membrane repair; ISS:UniProtKB. GO:0051260; P:protein homooligomerization; ISS:UniProtKB. |
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Pfam | |
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PROSITE | |
PRINTS | |