TRI72_XENTR
ID TRI72_XENTR Reviewed; 477 AA.
AC Q640S6;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Tripartite motif-containing protein 72;
DE AltName: Full=Mitsugumin-53;
DE Short=Mg53;
GN Name=trim72; Synonyms=mg53;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer; disulfide-linked. {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-244 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:0000305}.
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DR EMBL; BC082513; AAH82513.1; -; mRNA.
DR RefSeq; NP_001008188.1; NM_001008187.1.
DR AlphaFoldDB; Q640S6; -.
DR SMR; Q640S6; -.
DR STRING; 8364.ENSXETP00000056209; -.
DR PaxDb; Q640S6; -.
DR DNASU; 493550; -.
DR GeneID; 493550; -.
DR KEGG; xtr:493550; -.
DR CTD; 493829; -.
DR Xenbase; XB-GENE-5896447; trim72.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q640S6; -.
DR OMA; WEDERSC; -.
DR OrthoDB; 574602at2759; -.
DR PhylomeDB; Q640S6; -.
DR TreeFam; TF342569; -.
DR Reactome; R-XTR-445355; Smooth Muscle Contraction.
DR Proteomes; UP000008143; Chromosome 9.
DR Proteomes; UP000790000; Unplaced.
DR ExpressionAtlas; Q640S6; baseline.
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:0001786; F:phosphatidylserine binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Cell membrane; Coiled coil; Cytoplasmic vesicle; Disulfide bond;
KW Exocytosis; Membrane; Metal-binding; Reference proteome; Transport; Zinc;
KW Zinc-finger.
FT CHAIN 1..477
FT /note="Tripartite motif-containing protein 72"
FT /id="PRO_0000383154"
FT DOMAIN 272..476
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..59
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 83..124
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 126..162
FT /evidence="ECO:0000255"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT DISULFID 244
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 54101 MW; 54AD1668E45A5D6B CRC64;
MSTPQLMQGM QKDLTCPLCL ELFRAPVTPE CGHTFCQGCL TGAPKNQDQN GSTPCPTCQT
PSRPETLQIN RQLEHLVQSF KQVPKGHCLE HLDPLSVYCE QDKELICGVC ASLGKHKGHN
IITAAEAYAK LKRQLPQQQV ILQEARLKKE KTVAVLDRQV AEVQDTVSRF KGNVKHQLNA
MRSYLSIMEA SLSKEADNAE HTATEALLVE RKTMGHYLDQ LRQMDGVLKD VESQEQTEFL
RKYCVVAARL NKILAESPPP GRLDIQLPII SDEFKFQVWR KMFRALMPAL ENLTFDPDTA
QQNLVVFSDG KSVECSEQKQ SVSDEPNRFD KSNCLVSKES FTEGEHYWEV LVEDKPRWAL
GVISETANRK GKLHASPSNG FWLIGCKEGK VYEAHTEQKE PRVLRVEGRP EKIGIYLSFS
DGVVSFFDSS DEDNIKLLYT FNERFSGRLH PFFDVCWHDK GKNAQPLKIF YPPAEQL
