TRI59_MOUSE
ID TRI59_MOUSE Reviewed; 403 AA.
AC Q922Y2; E9QKA7; Q9CSP2; Q9CUD5; Q9D740;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Tripartite motif-containing protein 59;
DE AltName: Full=RING finger protein 1;
GN Name=Trim59; Synonyms=Mrf1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Testis, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=12095697; DOI=10.1016/s0378-1119(02)00603-0;
RA Chang R., Xu X., Li M.D.;
RT "Molecular cloning, mapping and characterization of a novel mouse RING
RT finger gene, Mrf1.";
RL Gene 291:241-249(2002).
RN [5]
RP INTERACTION WITH ECSIT, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22588174; DOI=10.1016/j.bbrc.2012.05.028;
RA Kondo T., Watanabe M., Hatakeyama S.;
RT "TRIM59 interacts with ECSIT and negatively regulates NF-kappaB and IRF-
RT 3/7-mediated signal pathways.";
RL Biochem. Biophys. Res. Commun. 422:501-507(2012).
CC -!- FUNCTION: May serve as a multifunctional regulator for innate immune
CC signaling pathways. {ECO:0000269|PubMed:22588174}.
CC -!- SUBUNIT: Interacts with ECSIT (PubMed:22588174).
CC {ECO:0000269|PubMed:22588174}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:22588174}; Single-pass membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Moderately expressed in the spleen, brain and heart
CC and very highly expressed in the testis (PubMed:12095697).
CC {ECO:0000269|PubMed:12095697}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AK009637; BAB26408.2; -; mRNA.
DR EMBL; AK012269; BAB28131.1; -; mRNA.
DR EMBL; AK016642; BAB30354.1; -; mRNA.
DR EMBL; AC122876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006700; AAH06700.1; -; mRNA.
DR EMBL; BC025430; AAH25430.1; -; mRNA.
DR CCDS; CCDS17402.1; -.
DR RefSeq; NP_080139.3; NM_025863.3.
DR RefSeq; XP_006501980.1; XM_006501917.3.
DR RefSeq; XP_011238502.1; XM_011240200.1.
DR RefSeq; XP_011238503.1; XM_011240201.2.
DR AlphaFoldDB; Q922Y2; -.
DR SMR; Q922Y2; -.
DR BioGRID; 211830; 13.
DR STRING; 10090.ENSMUSP00000103432; -.
DR PhosphoSitePlus; Q922Y2; -.
DR EPD; Q922Y2; -.
DR MaxQB; Q922Y2; -.
DR PaxDb; Q922Y2; -.
DR PRIDE; Q922Y2; -.
DR ProteomicsDB; 298304; -.
DR DNASU; 66949; -.
DR Ensembl; ENSMUST00000107802; ENSMUSP00000103432; ENSMUSG00000034317.
DR GeneID; 66949; -.
DR KEGG; mmu:66949; -.
DR UCSC; uc008pmd.2; mouse.
DR CTD; 286827; -.
DR MGI; MGI:1914199; Trim59.
DR VEuPathDB; HostDB:ENSMUSG00000034317; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160146; -.
DR InParanoid; Q922Y2; -.
DR OMA; ILCHTLY; -.
DR OrthoDB; 635534at2759; -.
DR PhylomeDB; Q922Y2; -.
DR TreeFam; TF331669; -.
DR BioGRID-ORCS; 66949; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Trim59; mouse.
DR PRO; PR:Q922Y2; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q922Y2; protein.
DR Bgee; ENSMUSG00000034317; Expressed in primitive streak and 243 other tissues.
DR ExpressionAtlas; Q922Y2; baseline and differential.
DR Genevisible; Q922Y2; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:MGI.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
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; PF00643; zf-B_box; 1.
DR Pfam; PF13445; zf-RING_UBOX; 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 1: Evidence at protein level;
KW Coiled coil; Endoplasmic reticulum; Membrane; Metal-binding;
KW Reference proteome; Transmembrane; Transmembrane helix; Zinc; Zinc-finger.
FT CHAIN 1..403
FT /note="Tripartite motif-containing protein 59"
FT /id="PRO_0000249680"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ZN_FING 10..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 92..134
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 163..246
FT /evidence="ECO:0000255"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT CONFLICT 53
FT /note="P -> E (in Ref. 1; BAB30354)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="P -> A (in Ref. 1; BAB30354)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="S -> N (in Ref. 1; BAB30354)"
FT /evidence="ECO:0000305"
FT CONFLICT 68
FT /note="T -> S (in Ref. 1; BAB30354)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="E -> K (in Ref. 1; BAB30354)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="V -> I (in Ref. 1; BAB30354)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="T -> S (in Ref. 1; BAB30354)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="G -> V (in Ref. 1; BAB30354)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="I -> T (in Ref. 3; AAH06700/AAH25430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 47238 MW; 60AF4F97398DDDBF CRC64;
MHNFEEELTC PICYSIFEDP RVLPCSHTFC RNCLENVLQA SGNFYIWRPL RIPLKCPNCR
SIIEIASTGI ESLPVNFALR AIIEKYQQED HPDVVTCPEH YRQPLNVYCL LDKKLVCGHC
LTIGQHHGHP IDDLQSAYLK EKDTPQKLLK QLTDTHWTDI TRLIEKLEEQ KCHSEKIVQG
DKEVVLQYFK ELIDTLEQKK KYFLAALCDV GKMINQEYTP QIQGMKEIRE QQLELMTITT
SLQDESPLKF LEKIDEVRQR VQMLKQRPLP EVQPVEIYPR VSNVLKEEWS RIEIGRIKKA
VIPEMRVSSK RTPCSWSDND EKEMELFKIL NIAIVSLISV ILMLILLFNH HIITFLNEIT
SICFSEVFLS VYQSLSKNLY DLNNTVCYTL YLLKEFMWKI VSR
