TRI10_MOUSE
ID TRI10_MOUSE Reviewed; 489 AA.
AC Q9WUH5; Q80WA9; Q9CY03;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Tripartite motif-containing protein 10;
DE AltName: Full=Hematopoietic RING finger 1;
DE AltName: Full=RING finger protein 9;
GN Name=Trim10; Synonyms=Herf1, Rnf9;
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], AND FUNCTION.
RC TISSUE=Spleen;
RX PubMed=10207104; DOI=10.1128/mcb.19.5.3808;
RA Harada H., Harada Y., O'Brien D.P., Rice D.S., Naeve C.W., Downing J.R.;
RT "HERF1, a novel hematopoiesis-specific RING finger protein, is required for
RT terminal differentiation of erythroid cells.";
RL Mol. Cell. Biol. 19:3808-3815(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic liver;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb;
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 [5]
RP FUNCTION.
RX PubMed=18560381; DOI=10.1038/cr.2008.68;
RA Blaybel R., Theoleyre O., Douablin A., Baklouti F.;
RT "Downregulation of the Spi-1/PU.1 oncogene induces the expression of
RT TRIM10/HERF1, a key factor required for terminal erythroid cell
RT differentiation and survival.";
RL Cell Res. 18:834-845(2008).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=32343488; DOI=10.1111/jcmm.15257;
RA Yang H., Wang X.X., Zhou C.Y., Xiao X., Tian C., Li H.H., Yin C.L.,
RA Wang H.X.;
RT "Tripartite motif 10 regulates cardiac hypertrophy by targeting the
RT PTEN/AKT pathway.";
RL J. Cell. Mol. Med. 24:6233-6241(2020).
CC -!- FUNCTION: E3 ligase that plays an essential role in the differentiation
CC and survival of terminal erythroid cells (PubMed:18560381). May
CC directly bind to PTEN and promote its ubiquitination, resulting in its
CC proteasomal degradation and activation of hypertrophic signaling
CC (PubMed:32343488). In addition, plays a role in immune response
CC regulation by repressing the phosphorylation of STAT1 and STAT2 in the
CC interferon/JAK/STAT signaling pathway independent of its E3 ligase
CC activity. Mechanistically, interacts with the intracellular domain of
CC IFNAR1 and thereby inhibits the association between TYK2 and IFNAR1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9UDY6,
CC ECO:0000269|PubMed:18560381, ECO:0000269|PubMed:32343488}.
CC -!- SUBUNIT: Interacts with IFNAR1; this interaction prevents association
CC of IFNAR1 with TYK2. {ECO:0000250|UniProtKB:Q9UDY6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9UDY6}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic liver.
CC {ECO:0000269|PubMed:11331580}.
CC -!- DISRUPTION PHENOTYPE: Deletion mice inhibit hypertrophic remodeling
CC after transverse aortic constriction surgery.
CC {ECO:0000269|PubMed:32343488}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF134811; AAD28534.1; -; mRNA.
DR EMBL; AF220121; AAG53494.1; -; mRNA.
DR EMBL; AK011082; BAB27386.1; -; mRNA.
DR EMBL; BC051632; AAH51632.1; -; mRNA.
DR CCDS; CCDS37614.1; -.
DR RefSeq; NP_035410.2; NM_011280.2.
DR AlphaFoldDB; Q9WUH5; -.
DR SMR; Q9WUH5; -.
DR STRING; 10090.ENSMUSP00000057928; -.
DR iPTMnet; Q9WUH5; -.
DR PhosphoSitePlus; Q9WUH5; -.
DR PaxDb; Q9WUH5; -.
DR PRIDE; Q9WUH5; -.
DR ProteomicsDB; 259089; -.
DR Antibodypedia; 26232; 178 antibodies from 19 providers.
DR DNASU; 19824; -.
DR Ensembl; ENSMUST00000060524; ENSMUSP00000057928; ENSMUSG00000073400.
DR GeneID; 19824; -.
DR KEGG; mmu:19824; -.
DR UCSC; uc008clj.2; mouse.
DR CTD; 10107; -.
DR MGI; MGI:1338757; Trim10.
DR VEuPathDB; HostDB:ENSMUSG00000073400; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000161525; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q9WUH5; -.
DR OMA; SCTMGVV; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q9WUH5; -.
DR TreeFam; TF342569; -.
DR BioGRID-ORCS; 19824; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Trim10; mouse.
DR PRO; PR:Q9WUH5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9WUH5; protein.
DR Bgee; ENSMUSG00000073400; Expressed in fetal liver hematopoietic progenitor cell and 91 other tissues.
DR Genevisible; Q9WUH5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
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:0030218; P:erythrocyte differentiation; IDA:MGI.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR CDD; cd16593; RING-HC_TRIM10_C-IV; 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; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR042784; TRIM10_RING-HC.
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; 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 Coiled coil; Cytoplasm; Metal-binding; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..489
FT /note="Tripartite motif-containing protein 10"
FT /id="PRO_0000056212"
FT DOMAIN 292..486
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..61
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 94..135
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 144..180
FT /evidence="ECO:0000255"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 127
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT CONFLICT 133
FT /note="R -> H (in Ref. 1; AAD28534)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="R -> Q (in Ref. 1; AAD28534)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="H -> Y (in Ref. 1; AAD28534)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="M -> V (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 55630 MW; AA7E26FABD120804 CRC64;
MASAPSVTSL ADEVNCPICQ GTLREPVTID CGHNFCRGCL TRYCEIPGPE SEESLSCPLC
KEPFRPGSFR PNWQLANVVE NIERLQLAST RGLEVEDACP EHGEKIYFFC EEDEAQLCVV
CRETGQHGAH TVRFLEDAAG PYREQIQKCL VCLRKEREEI QETQSRENKR IQVLLTQVAT
KRQQVISQFA HLSQFLQQQQ TALLAQLEGL DGDILKQQEE FDSLATGEIC RFSTLIEELE
EKNKRTARGL LTDIRSTLIR CETRKCRKPE AISPELGQRI RDFPQQAIPL RQEMKTFLEK
LCFELDYEPA HISLDPQTSH PKLLLSEDHR RARFSYKWQN SPDTPQRFDR VTCVLAQCGF
TGGRHTWMVN VDLAHGGSCT VGVVREDVRR KGELRLRPEE GIWAVRLAWG FVSALGSFPT
RLALEEQPRK VQVSLDYEVG WITFVNAVTQ EHIYTFTASF TQKIFPLFGL WGRGSSFSLS
CQEGAVSLL
