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Database: UniProt
Entry: Q6PGR9
LinkDB: Q6PGR9
Original site: Q6PGR9 
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   27-MAR-2024, entry version 99.
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   DNASU; 379612; -.
DR   GeneID; 379612; -.
DR   KEGG; xla:379612; -.
DR   AGR; Xenbase:XB-GENE-5896500; -.
DR   CTD; 379612; -.
DR   Xenbase; XB-GENE-5896500; trim72.L.
DR   OrthoDB; 3453019at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 379612; Expressed in muscle tissue and 11 other cell types or 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: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:0001778; P:plasma membrane repair; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   CDD; cd19797; Bbox2_TRIM72_C-IV; 1.
DR   CDD; cd16612; RING-HC_TRIM72_C-IV; 1.
DR   CDD; cd13742; SPRY_PRY_TRIM72; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR027370; Znf-RING_euk.
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; E3 UBIQUITIN-PROTEIN LIGASE TRIM; 1.
DR   PANTHER; PTHR24103:SF11; TRIPARTITE MOTIF-CONTAINING PROTEIN 72; 1.
DR   Pfam; PF13765; PRY; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   Pfam; PF00643; zf-B_box; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 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; SSF57845; B-box zinc-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 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
//
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