TRI75_MOUSE
ID TRI75_MOUSE Reviewed; 467 AA.
AC Q3UWZ0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Tripartite motif-containing protein 75 {ECO:0000305};
GN Name=Trim75 {ECO:0000312|MGI:MGI:2685640}; Synonyms=Gm794;
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=Egg;
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 FUNCION, AND SUBCELLULAR LOCATION.
RX PubMed=26974323; DOI=10.1371/journal.pone.0150462;
RA Jin Z., Li R., Zhou C., Shi L., Zhang X., Yang Z., Zhang D.;
RT "Efficient Gene Knockdown in Mouse Oocytes through Peptide Nanoparticle-
RT Mediated SiRNA Transfection.";
RL PLoS ONE 11:e0150462-e0150462(2016).
CC -!- FUNCTION: May play a role in female meiosis.
CC {ECO:0000269|PubMed:26974323}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000305|PubMed:26974323}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK136018; BAE22774.1; -; mRNA.
DR CCDS; CCDS22330.1; -.
DR RefSeq; NP_001028601.1; NM_001033429.2.
DR AlphaFoldDB; Q3UWZ0; -.
DR SMR; Q3UWZ0; -.
DR STRING; 10090.ENSMUSP00000092932; -.
DR PhosphoSitePlus; Q3UWZ0; -.
DR PaxDb; Q3UWZ0; -.
DR PRIDE; Q3UWZ0; -.
DR Antibodypedia; 1279; 285 antibodies from 26 providers.
DR Ensembl; ENSMUST00000095295; ENSMUSP00000092932; ENSMUSG00000071089.
DR GeneID; 333307; -.
DR KEGG; mmu:333307; -.
DR UCSC; uc009lvd.1; mouse.
DR CTD; 391714; -.
DR MGI; MGI:2685640; Trim75.
DR VEuPathDB; HostDB:ENSMUSG00000071089; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000163787; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q3UWZ0; -.
DR OMA; CVRFTKR; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q3UWZ0; -.
DR TreeFam; TF342569; -.
DR BioGRID-ORCS; 333307; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q3UWZ0; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3UWZ0; protein.
DR Bgee; ENSMUSG00000071089; Expressed in animal zygote and 13 other tissues.
DR ExpressionAtlas; Q3UWZ0; baseline and differential.
DR Genevisible; Q3UWZ0; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
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:0007144; P:female meiosis I; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; 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 CDD; cd15829; SPRY_PRY_TRIM75; 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; IPR035785; SPRY/PRY_TRIM75.
DR InterPro; IPR003877; SPRY_dom.
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; Cytoskeleton; Metal-binding; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..467
FT /note="Tripartite motif-containing protein 75"
FT /id="PRO_0000331193"
FT DOMAIN 276..466
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 16..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 90..131
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 168..222
FT /evidence="ECO:0000255"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
SQ SEQUENCE 467 AA; 53385 MW; 501AA7B5CD8BBE93 CRC64;
MAHVEVLARL QKETKCPICL DDLTDPVTVE CGHNFCRSCI KDFWAGQQAT SSCPVCRHQC
QHRNLRSNAQ LGNMIETAQL LQGMENKRHE SSTSCERHNQ ALTLFCEDDL QLLCDQCVEP
ESHGRHQVLS ITEAASLHRK HLQDYSKLLK WEVKEIQGLM SALNKRTVTL REQAEAQRSQ
LTSECEKLMR FLDQEERAAF SRLEDEEMRL EKRLLDNIAA LEHHGSSLRD LLRHLMLTGE
LSEAKMLSTV KDFYLNCRRQ LISPSIFPVQ LRRVEYSFPL QYSALQKVIQ HFTDNVTLDL
KTAHPNLLIS KDRTCVTFTK KRQRIPGSSS FTKSPVVLGI PHFNSGRHFW EVQVGKKPKW
AIGICKADSS IGERQSPNPW GYWRIVWQGD SFNVSGADPD SRLKAARATS IGVFLDYELG
EVSFYGMPEK CHLYTFRDTF SGPVCPYFYI GPQSEPLRLC SATDSEC
