TRI72_XENLA
ID TRI72_XENLA Reviewed; 477 AA.
AC Q6PGR9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Tripartite motif-containing protein 72;
DE AltName: Full=Mitsugumin-53;
DE Short=Mg53;
GN Name=trim72; Synonyms=mg53;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2003) 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; BC056854; AAH56854.1; -; mRNA.
DR RefSeq; NP_001079922.1; NM_001086453.2.
DR AlphaFoldDB; Q6PGR9; -.
DR SMR; Q6PGR9; -.
DR PRIDE; Q6PGR9; -.
DR DNASU; 379612; -.
DR GeneID; 379612; -.
DR KEGG; xla:379612; -.
DR CTD; 379612; -.
DR Xenbase; XB-GENE-5896500; trim72.L.
DR OrthoDB; 574602at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 379612; Expressed in muscle tissue and 11 other tissues.
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 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_0000383153"
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 130..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; 54115 MW; E7E1F1096062F3D3 CRC64;
MSTPQLMQGM QKDLTCQLCL ELFRAPVTPE CGHTFCQGCL TGVPKNQDQN GSTPCPTCQS
PSRPETLQIN RQLEHLVQSF KQVPQGHCLE HMDPLSVYCE QDKELICGVC ASLGKHKGHN
IITASEAFAK LKRQLPQQQV ILQEARLKKE KTVAVLDRQV AEVQDTVSRF KGNVKHQLNA
MRSYLNIMEA SLGKEADKAE SAATEALLVE RKTMGHYLDQ LRQMEGVLKD VEGQEQTEFL
RKYCVVAARL NKILSESPPP GRLDIQLPII SDEFKFQVWR KMFRALMPAL ENMTFDPDTA
QQYLVVSSEG KSVECADQKQ SVSDEPNRFD KSNCLVSKQS FTEGEHYWEV IVEDKPRWAL
GIISETANRK GKLHATPSNG FWIIGCKEGK VYEAHTEQKE PRVLRVEGRP EKIGVYLSFS
DGVVSFFDSS DEDNLKLLYT FNERFSGRLH PFFDVCWHDK GKNSQPLKIF YPPAEQL
