TRI72_RABIT
ID TRI72_RABIT Reviewed; 477 AA.
AC Q1XH18;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Tripartite motif-containing protein 72;
DE AltName: Full=Mitsugumin-53;
DE Short=Mg53;
GN Name=TRIM72 {ECO:0000250|UniProtKB:Q6ZMU5};
GN Synonyms=MG53 {ECO:0000312|EMBL:BAE93013.1};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=19043407; DOI=10.1038/ncb1812;
RA Cai C., Masumiya H., Weisleder N., Matsuda N., Nishi M., Hwang M.,
RA Ko J.-K., Lin P., Thornton A., Zhao X., Pan Z., Komazaki S., Brotto M.,
RA Takeshima H., Ma J.;
RT "MG53 nucleates assembly of cell membrane repair machinery.";
RL Nat. Cell Biol. 11:56-64(2009).
CC -!- FUNCTION: Muscle-specific protein that plays a central role in cell
CC membrane repair by nucleating the assembly of the repair machinery at
CC injury sites. Specifically binds phosphatidylserine. Acts as a sensor
CC of oxidation: upon membrane damage, entry of extracellular oxidative
CC environment results in disulfide bond formation and homooligomerization
CC at the injury site. This oligomerization acts as a nucleation site for
CC recruitment of TRIM72-containing vesicles to the injury site, leading
CC to membrane patch formation. Probably acts upstream of the Ca(2+)-
CC dependent membrane resealing process. Required for transport of DYSF to
CC sites of cell injury during repair patch formation. Regulates membrane
CC budding and exocytosis. May be involved in the regulation of the
CC mobility of KCNB1-containing endocytic vesicles (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer; disulfide-linked. Interacts with DYSF and CAV3
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250}.
CC Cytoplasmic vesicle membrane {ECO:0000250}. Note=Tethered to plasma
CC membrane and cytoplasmic vesicles via its interaction with
CC phosphatidylserine. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Muscle-specific. {ECO:0000269|PubMed:19043407}.
CC -!- PTM: Disulfide bond formation at Cys-242 occurs in case of membrane
CC damage that cause the entry of the oxidized milieu of the extracellular
CC space, resulting in homooligomerization. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000255}.
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DR EMBL; AB231473; BAE93013.1; -; mRNA.
DR RefSeq; NP_001075484.1; NM_001082015.1.
DR AlphaFoldDB; Q1XH18; -.
DR SMR; Q1XH18; -.
DR STRING; 9986.ENSOCUP00000013255; -.
DR GeneID; 100008639; -.
DR KEGG; ocu:100008639; -.
DR CTD; 493829; -.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; Q1XH18; -.
DR OrthoDB; 574602at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; ISS:UniProtKB.
DR GO; GO:0003012; P:muscle system process; ISS:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; IEA:InterPro.
DR GO; GO:0001778; P:plasma membrane repair; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR035038; TRIM72.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24103:SF11; PTHR24103:SF11; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; Exocytosis; Membrane; Metal-binding; Phosphoprotein;
KW Reference proteome; Transport; Zinc; Zinc-finger.
FT CHAIN 1..477
FT /note="Tripartite motif-containing protein 72"
FT /id="PRO_0000278132"
FT DOMAIN 271..475
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 14..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 81..122
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 128..169
FT /evidence="ECO:0000255"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A0JPQ4"
FT DISULFID 242
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 52779 MW; 91C4062FB5C5AAFA CRC64;
MSAAPGLLHQ ELSCPLCLQL FDAPVTAECG HSFCRACLSR VAGEPAADGT VNCPCCQAPT
RPQALSTNLQ LARLVEGLAQ VPQGHCEEHL DPLSIYCEQD RVLVCGVCAS LGSHRGHRLL
PAAEAHSRLK TQLPQQKLQL QEASMRKEKS VAVLEHQLTE VEETVRQFRG AVGEQLGKMR
VFLAALEGSL DREAERVRSE AGVALRRELG GLHSYLEQLR QMEKVLEEVA DKPQTEFLMK
YCLVTSRLQK ILAESPPPAR LDIQLPIISD DFKFQVWRKM FRALMPALEE LTFDPSSAHP
SLVVSPTGRR VECSEQKAPP AGDDARQFDK AVAVVAQQLL SDGEHYWEVE VGDKPRWALG
VMASEASRRG RLHAVPSQGL WLLGLRDGKT LEAHVEAKEP RALRTPERRP TRLGLYLSFG
DGVLAFYDAS DADALELLFA FRERLPGPVY PFFDVCWHDK GKNAQPLLLV GPDGQEA
