TR34A_MOUSE
ID TR34A_MOUSE Reviewed; 485 AA.
AC Q99PP6; Q99PP4; Q99PP5;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tripartite motif-containing protein 34A;
GN Name=Trim34a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA).
RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140;
RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L.,
RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S.,
RA Pelicci P.G., Ballabio A.;
RT "The tripartite motif family identifies cell compartments.";
RL EMBO J. 20:2140-2151(2001).
CC -!- FUNCTION: May function as antiviral protein and may contribute to the
CC defense against retroviral infections. {ECO:0000250|UniProtKB:Q9BYJ4}.
CC -!- SUBUNIT: Homotrimer. Interacts (via B-box and SPRY domain) with TRIM5.
CC {ECO:0000250|UniProtKB:Q9BYJ4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BYJ4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Alpha;
CC IsoId=Q99PP6-1; Sequence=Displayed;
CC Name=Beta;
CC IsoId=Q99PP6-2; Sequence=VSP_011923, VSP_011924;
CC Name=Gamma;
CC IsoId=Q99PP6-3; Sequence=VSP_011925, VSP_011926;
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF220139; AAG53512.1; -; mRNA.
DR EMBL; AF220140; AAG53513.1; -; mRNA.
DR EMBL; AF220141; AAG53514.1; -; mRNA.
DR CCDS; CCDS52342.1; -. [Q99PP6-1]
DR RefSeq; NP_109609.2; NM_030684.3.
DR AlphaFoldDB; Q99PP6; -.
DR SMR; Q99PP6; -.
DR STRING; 10090.ENSMUSP00000055058; -.
DR iPTMnet; Q99PP6; -.
DR PhosphoSitePlus; Q99PP6; -.
DR SwissPalm; Q99PP6; -.
DR EPD; Q99PP6; -.
DR jPOST; Q99PP6; -.
DR MaxQB; Q99PP6; -.
DR PaxDb; Q99PP6; -.
DR PRIDE; Q99PP6; -.
DR ProteomicsDB; 258838; -. [Q99PP6-1]
DR ProteomicsDB; 258839; -. [Q99PP6-2]
DR ProteomicsDB; 258840; -. [Q99PP6-3]
DR DNASU; 94094; -.
DR GeneID; 94094; -.
DR KEGG; mmu:94094; -.
DR UCSC; uc029wnk.1; mouse. [Q99PP6-2]
DR UCSC; uc029wnl.1; mouse. [Q99PP6-3]
DR CTD; 94094; -.
DR MGI; MGI:2137359; Trim34a.
DR eggNOG; KOG2177; Eukaryota.
DR HOGENOM; CLU_013137_6_1_1; -.
DR InParanoid; Q99PP6; -.
DR OrthoDB; 165920at2759; -.
DR PhylomeDB; Q99PP6; -.
DR BioGRID-ORCS; 94094; 0 hits in 42 CRISPR screens.
DR ChiTaRS; Trim34a; mouse.
DR PRO; PR:Q99PP6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q99PP6; protein.
DR Genevisible; Q99PP6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
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:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0032880; P:regulation of protein localization; IBA:GO_Central.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR CDD; cd15825; SPRY_PRY_TRIM34; 1.
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; IPR003877; SPRY_dom.
DR InterPro; IPR035826; TRIM34_PRY/SPRY.
DR InterPro; IPR027370; Znf-RING_LisH.
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 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; 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 Alternative splicing; Antiviral defense; Coiled coil; Cytoplasm;
KW Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..485
FT /note="Tripartite motif-containing protein 34A"
FT /id="PRO_0000056249"
FT DOMAIN 282..485
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 15..59
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 91..132
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 130..241
FT /evidence="ECO:0000255"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT VAR_SEQ 300..339
FT /note="DNFTFNPENLNLNLILSEDHRQVTSVSIWPFKCCNNGILG -> GKKLQMLK
FT SLCSDHLSQVCGSMWPYHLCLLCYLIHIMNSS (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_011923"
FT VAR_SEQ 300..326
FT /note="DNFTFNPENLNLNLILSEDHRQVTSVS -> GSYSVYKVGFKYRAIFLPQLP
FT RCSTAG (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_011925"
FT VAR_SEQ 327..485
FT /note="Missing (in isoform Gamma)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_011926"
FT VAR_SEQ 340..485
FT /note="Missing (in isoform Beta)"
FT /evidence="ECO:0000303|PubMed:11331580"
FT /id="VSP_011924"
FT CONFLICT 293
FT /note="S -> T (in Ref. 1; AAG53512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 55908 MW; 977AF683D5553609 CRC64;
MASTGLTNIQ EKTTCPVCQE LLTKALSLGC GHRVCQACLI TKKNAVINPR EKSSCPVCGT
RFSLENLQAN KHLANVVERL GEVKLKPDIG TKRDLCVHHG EKLLLFCKED KKAICWVCER
SQEHRGHHTF LWEEAVRECQ ENLQKALTRL RKEQEKVETL EADIKEDRLS WKCQVQTERQ
RIQTGFNQLR RILDKEEQRE LKRLREEEQM ILDSLAGAEA ELAQQSQLVE ELISDLELRR
EWSDTELLQD MSGILKWSQI WTLKKPKAVS KKLSMVFQAP DLSGMLQKFR ELSAVRAYWD
NFTFNPENLN LNLILSEDHR QVTSVSIWPF KCCNNGILGS KCFSSGKHYW EVDVSEKKAW
TLGVYTRKRT LRFDVRQRKG QPNGYHRYKP QNGYWVIGLQ HGSKYSIFED SSNCDPTVLN
PFVATPLHRA GVFLDCEEGT VSFLNVTNHG SLIYKFSQCC FSQPAYPYFN PWDCPAPMTL
CPLNS
