TRI72_RAT
ID TRI72_RAT Reviewed; 477 AA.
AC A0JPQ4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Tripartite motif-containing protein 72;
DE AltName: Full=Mitsugumin-53;
DE Short=Mg53;
GN Name=Trim72 {ECO:0000250|UniProtKB:Q8N4X6}; Synonyms=Mg53;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAI27540.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart {ECO:0000312|EMBL:AAI27540.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- 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 -!- PTM: S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against
CC oxidation-induced protein degradation and cell death.
CC {ECO:0000250|UniProtKB:Q6ZMU5}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000255}.
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DR EMBL; BC127539; AAI27540.1; -; mRNA.
DR RefSeq; NP_001071143.1; NM_001077675.1.
DR AlphaFoldDB; A0JPQ4; -.
DR SMR; A0JPQ4; -.
DR BioGRID; 265327; 1.
DR STRING; 10116.ENSRNOP00000030976; -.
DR iPTMnet; A0JPQ4; -.
DR PhosphoSitePlus; A0JPQ4; -.
DR PaxDb; A0JPQ4; -.
DR PeptideAtlas; A0JPQ4; -.
DR PRIDE; A0JPQ4; -.
DR Ensembl; ENSRNOT00000029994; ENSRNOP00000030976; ENSRNOG00000022099.
DR GeneID; 365377; -.
DR KEGG; rno:365377; -.
DR UCSC; RGD:1562778; rat.
DR CTD; 493829; -.
DR RGD; 1562778; Trim72.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000161791; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; A0JPQ4; -.
DR OMA; VECVEHK; -.
DR OrthoDB; 574602at2759; -.
DR PhylomeDB; A0JPQ4; -.
DR TreeFam; TF342569; -.
DR Reactome; R-RNO-445355; Smooth Muscle Contraction.
DR PRO; PR:A0JPQ4; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000022099; Expressed in skeletal muscle tissue and 9 other tissues.
DR Genevisible; A0JPQ4; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; ISO:RGD.
DR GO; GO:0001778; P:plasma membrane repair; ISS:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISO:RGD.
DR GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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; Disulfide bond;
KW Exocytosis; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW S-nitrosylation; Transport; Zinc; Zinc-finger.
FT CHAIN 1..477
FT /note="Tripartite motif-containing protein 72"
FT /id="PRO_0000278133"
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 122..169
FT /evidence="ECO:0000255"
FT COILED 204..232
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 144
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZMU5"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT DISULFID 242
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 52832 MW; 7D095A96969D69B1 CRC64;
MSTAPGLLRQ ELSCPLCLQL FDAPVTAECG HSFCRACLIR VAGEPADDGT VACPCCQAST
RPQALSTNLQ LARLVEGLAQ VPQGHCEEHL DPLSIYCEQD RTLVCGVCAS LGSHRGHRLL
PAAEAHARLK TQLPQQKAQL QEACMRKEKS VAVLEHQLVE VEETVRQFRG AVGEQLGKMR
MFLAALESSL DREAERVRGE AGVALRRELS SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK
FCLVTSRLQK ILSESPPPAR LDIQLPVISD DFKFQVWKKM FRALMPELEE LTFDPSSAHP
SLVVSASGRR VECSEQKAPP AGEDTCQFDK TVAVVAKQLL SQGEHYWEVE VGDKPRWALG
VMAADASRRG RLHAVPSQGL WLLGLRDGKI LEAHVEAKEP RALRTPERPP ARIGLYLSFA
DGVLTFYDAS NTDALTPLFS FHERLPGPVY PMFDVCWHDK GKNSQPLLLV GPDSEQA
