TR12A_MOUSE
ID TR12A_MOUSE Reviewed; 284 AA.
AC Q99PQ1; Q9D704;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Tripartite motif-containing protein 12A;
GN Name=Trim12a; Synonyms=Trim12;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
RX PubMed=11217851; DOI=10.1038/35055500;
RA Kawai J., Shinagawa A., Shibata K., Yoshino M., Itoh M., Ishii Y.,
RA Arakawa T., Hara A., Fukunishi Y., Konno H., Adachi J., Fukuda S.,
RA Aizawa K., Izawa M., Nishi K., Kiyosawa H., Kondo S., Yamanaka I.,
RA Saito T., Okazaki Y., Gojobori T., Bono H., Kasukawa T., Saito R.,
RA Kadota K., Matsuda H.A., Ashburner M., Batalov S., Casavant T.,
RA Fleischmann W., Gaasterland T., Gissi C., King B., Kochiwa H., Kuehl P.,
RA Lewis S., Matsuo Y., Nikaido I., Pesole G., Quackenbush J., Schriml L.M.,
RA Staubli F., Suzuki R., Tomita M., Wagner L., Washio T., Sakai K., Okido T.,
RA Furuno M., Aono H., Baldarelli R., Barsh G., Blake J., Boffelli D.,
RA Bojunga N., Carninci P., de Bonaldo M.F., Brownstein M.J., Bult C.,
RA Fletcher C., Fujita M., Gariboldi M., Gustincich S., Hill D., Hofmann M.,
RA Hume D.A., Kamiya M., Lee N.H., Lyons P., Marchionni L., Mashima J.,
RA Mazzarelli J., Mombaerts P., Nordone P., Ring B., Ringwald M.,
RA Rodriguez I., Sakamoto N., Sasaki H., Sato K., Schoenbach C., Seya T.,
RA Shibata Y., Storch K.-F., Suzuki H., Toyo-oka K., Wang K.H., Weitz C.,
RA Whittaker C., Wilming L., Wynshaw-Boris A., Yoshida K., Hasegawa Y.,
RA Kawaji H., Kohtsuki S., Hayashizaki Y.;
RT "Functional annotation of a full-length mouse cDNA collection.";
RL Nature 409:685-690(2001).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11331580}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic CNS, liver, kidney,
CC olfactory epithelium. {ECO:0000269|PubMed:11331580}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF220126; AAG53499.1; -; mRNA.
DR EMBL; AK009769; BAB26491.1; -; mRNA.
DR CCDS; CCDS90296.1; -.
DR RefSeq; NP_076324.2; NM_023835.2.
DR RefSeq; XP_017167861.1; XM_017312372.1.
DR RefSeq; XP_017167862.1; XM_017312373.1.
DR RefSeq; XP_017167863.1; XM_017312374.1.
DR AlphaFoldDB; Q99PQ1; -.
DR SMR; Q99PQ1; -.
DR BioGRID; 218256; 1.
DR STRING; 10090.ENSMUSP00000102452; -.
DR EPD; Q99PQ1; -.
DR MaxQB; Q99PQ1; -.
DR PaxDb; Q99PQ1; -.
DR PRIDE; Q99PQ1; -.
DR ProteomicsDB; 259084; -.
DR DNASU; 76681; -.
DR Ensembl; ENSMUST00000070943; ENSMUSP00000065008; ENSMUSG00000066258.
DR GeneID; 76681; -.
DR KEGG; mmu:76681; -.
DR UCSC; uc009ivw.1; mouse.
DR CTD; 76681; -.
DR MGI; MGI:1923931; Trim12a.
DR VEuPathDB; HostDB:ENSMUSG00000066258; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000154647; -.
DR InParanoid; Q99PQ1; -.
DR OrthoDB; 1487641at2759; -.
DR BioGRID-ORCS; 76681; 1 hit in 38 CRISPR screens.
DR ChiTaRS; Trim12a; mouse.
DR PRO; PR:Q99PQ1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q99PQ1; protein.
DR Bgee; ENSMUSG00000066258; Expressed in granulocyte and 123 other tissues.
DR ExpressionAtlas; Q99PQ1; baseline and differential.
DR Genevisible; Q99PQ1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:1990462; C:omegasome; ISO:MGI.
DR GO; GO:0000932; C:P-body; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0038187; F:pattern recognition receptor activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
DR GO; GO:0006914; P:autophagy; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; ISO:MGI.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:MGI.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:MGI.
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:0031664; P:regulation of lipopolysaccharide-mediated signaling pathway; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0046596; P:regulation of viral entry into host cell; IBA:GO_Central.
DR GO; GO:0044790; P:suppression of viral release by host; ISO:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032917; TRIM5.
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:SF416; PTHR24103:SF416; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM00184; RING; 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 Coiled coil; Cytoplasm; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..284
FT /note="Tripartite motif-containing protein 12A"
FT /id="PRO_0000056217"
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..234
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 CONFLICT 250..284
FT /note="VRLQDVPGSESQKAWKPLPFLSAAVVFLVMTVSSS -> GVENIIERSHTFS
FT MKKPKAIAREQRKFRAPDLQGMLQVLQEVTEAHRY (in Ref. 2; BAB26491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 33320 MW; B551B4C4D9CFF527 CRC64;
MASQFMKNLK EEVTCPVCLN LMVKPVSADC GHTFCQGCIT LYFESIKCDK KVFICPVCRI
SYQFSNLRPN RNVANIVERL KMFKPSPEEE QKVFNCARHG KKLQLFCRKD MMAICWLCER
SQEHRGHKTA LIEEVAQEYK EQLQVVLQRL MADKKKFENW KDDLQKDRTY WENQIQKDVQ
NVRSEFKRMR DIMDSEEKKE LQKLRQEKED ILNNLAESES EHAQQSKLLE DFISDVEHQL
QCSDIEILQV RLQDVPGSES QKAWKPLPFL SAAVVFLVMT VSSS
