TRI27_MOUSE
ID TRI27_MOUSE Reviewed; 513 AA.
AC Q62158; Q62157; Q8C2Q5; Q99LK1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Zinc finger protein RFP;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM27 {ECO:0000305};
DE AltName: Full=Ret finger protein;
DE AltName: Full=Tripartite motif-containing protein 27;
GN Name=Trim27; Synonyms=Rfp;
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].
RC STRAIN=C57BL/6J;
RX PubMed=9023983;
RX DOI=10.1002/(sici)1520-6408(1996)19:4<309::aid-dvg4>3.0.co;2-d;
RA Cao T., Shannon M., Handel M.A., Etkin L.D.;
RT "Mouse ret finger protein (rfp) proto-oncogene is expressed at specific
RT stages of mouse spermatogenesis.";
RL Dev. Genet. 19:309-320(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 8-513.
RC STRAIN=BALB/cJ;
RA Takahashi M.;
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=1437549; DOI=10.1093/nar/20.20.5305;
RA Isomura T., Tamiya-Koizumi K., Suzuki M., Yoshida S., Taniguchi M.,
RA Matsuyama M., Ishigaki T., Sakuma S., Takahashi M.;
RT "RFP is a DNA binding protein associated with the nuclear matrix.";
RL Nucleic Acids Res. 20:5305-5310(1992).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10571821; DOI=10.1046/j.1440-1827.1999.00957.x;
RA Tezel G., Nagasaka T., Iwahashi N., Asai N., Iwashita T., Sakata K.,
RA Takahashi M.;
RT "Different nuclear/cytoplasmic distributions of RET finger protein in
RT different cell types.";
RL Pathol. Int. 49:881-886(1999).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination of
CC PIK3C2B and inhibits its activity; mediates the formation of 'Lys-48'-
CC linked polyubiquitin chains; the function inhibits CD4 T-cell
CC activation. Acts as a regulator of retrograde transport: together with
CC MAGEL2, mediates the formation of 'Lys-63'-linked polyubiquitin chains
CC at 'Lys-220' of WASHC1, leading to promote endosomal F-actin assembly.
CC Has a transcriptional repressor activity. Induces apoptosis by
CC activating Jun N-terminal kinase and p38 kinase and also increases
CC caspase-3-like activity independently of mitochondrial events. May
CC function in male germ cell development. Has DNA-binding activity and
CC preferentially bound to double-stranded DNA.
CC {ECO:0000250|UniProtKB:P14373}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- SUBUNIT: Homomultimerizes. Interacts with PML, EIF3S6, EPC1, CHD4 and
CC EID1. Interacts with MAGED4, MAGEF1 and MAGEL2.
CC {ECO:0000250|UniProtKB:P14373}.
CC -!- INTERACTION:
CC Q62158; Q8CIH5: Plcg2; NbExp=4; IntAct=EBI-642025, EBI-617954;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P14373}. Cytoplasm
CC {ECO:0000250|UniProtKB:P14373}. Nucleus, PML body {ECO:0000250}.
CC Endosome {ECO:0000250}. Note=Nuclear or cytoplasmic depending on the
CC cell type. Recruited to retromer-containing endosomes via interaction
CC with MAGEL2 (By similarity). Colocalized with PML and EIF3S6 in nuclear
CC bodies. {ECO:0000250, ECO:0000269|PubMed:10571821}.
CC -!- TISSUE SPECIFICITY: Expressed strongly in testis. Low levels were
CC detected in spleen, thymus, cerebrum and cerebellum.
CC {ECO:0000269|PubMed:10571821, ECO:0000269|PubMed:1437549}.
CC -!- DOMAIN: The coiled-coil region mediates interaction with EPC1 and CHD4.
CC The B box and coiled-coil domains mediate interaction with PML. The B
CC box and the distal coiled-coil domains mediate homomultimerisation. The
CC B30.2 domain mediates interaction with EIF3S6.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA85354.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L46855; AAA85354.1; ALT_INIT; mRNA.
DR EMBL; AK088180; BAC40192.1; -; mRNA.
DR EMBL; BC003219; AAH03219.1; -; mRNA.
DR EMBL; X75343; CAA53092.1; -; mRNA.
DR CCDS; CCDS36607.1; -.
DR PIR; S37583; S37583.
DR RefSeq; NP_033080.2; NM_009054.3.
DR RefSeq; XP_006516669.1; XM_006516606.3.
DR AlphaFoldDB; Q62158; -.
DR SMR; Q62158; -.
DR BioGRID; 202871; 12.
DR CORUM; Q62158; -.
DR IntAct; Q62158; 3.
DR MINT; Q62158; -.
DR STRING; 10090.ENSMUSP00000021761; -.
DR iPTMnet; Q62158; -.
DR PhosphoSitePlus; Q62158; -.
DR EPD; Q62158; -.
DR MaxQB; Q62158; -.
DR PaxDb; Q62158; -.
DR PeptideAtlas; Q62158; -.
DR PRIDE; Q62158; -.
DR ProteomicsDB; 259183; -.
DR Antibodypedia; 25916; 289 antibodies from 25 providers.
DR DNASU; 19720; -.
DR Ensembl; ENSMUST00000021761; ENSMUSP00000021761; ENSMUSG00000021326.
DR Ensembl; ENSMUST00000222544; ENSMUSP00000152730; ENSMUSG00000021326.
DR GeneID; 19720; -.
DR KEGG; mmu:19720; -.
DR UCSC; uc007ppy.2; mouse.
DR CTD; 5987; -.
DR MGI; MGI:97904; Trim27.
DR VEuPathDB; HostDB:ENSMUSG00000021326; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000158537; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q62158; -.
DR OMA; NHAHSME; -.
DR OrthoDB; 423686at2759; -.
DR PhylomeDB; Q62158; -.
DR TreeFam; TF350411; -.
DR Reactome; R-MMU-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR BioGRID-ORCS; 19720; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Trim27; mouse.
DR PRO; PR:Q62158; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q62158; protein.
DR Bgee; ENSMUSG00000021326; Expressed in internal carotid artery and 251 other tissues.
DR ExpressionAtlas; Q62158; baseline and differential.
DR Genevisible; Q62158; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0030904; C:retromer complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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:0019789; F:SUMO transferase activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
DR GO; GO:0002820; P:negative regulation of adaptive immune response; ISS:UniProtKB.
DR GO; GO:0090281; P:negative regulation of calcium ion import; ISS:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISS:UniProtKB.
DR GO; GO:0032897; P:negative regulation of viral transcription; IDA:UniProtKB.
DR GO; GO:0051127; P:positive regulation of actin nucleation; IGI: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; IBA:GO_Central.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IBA:GO_Central.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
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 GO; GO:0042147; P:retrograde transport, endosome to Golgi; ISS:UniProtKB.
DR GO; GO:0044790; P:suppression of viral release by host; IDA:UniProtKB.
DR CDD; cd15814; SPRY_PRY_TRIM27; 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; IPR035791; SPRY/PRY_TRIM27.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR020457; Znf_B-box_chordata.
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; PR01406; BBOXZNFINGER.
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 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; DNA-binding; Endosome; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Transferase; Transport; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..513
FT /note="Zinc finger protein RFP"
FT /id="PRO_0000056241"
FT DOMAIN 298..492
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 91..132
FT /note="B box-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024"
FT COILED 132..171
FT /evidence="ECO:0000255"
FT COILED 282..311
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 119..120
FT /note="DR -> EP (in Ref. 4; CAA53092)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="G -> D (in Ref. 1; AAA85354)"
FT /evidence="ECO:0000305"
FT CONFLICT 367
FT /note="I -> M (in Ref. 2; BAC40192 and 4; CAA53092)"
FT /evidence="ECO:0000305"
FT CONFLICT 485
FT /note="A -> R (in Ref. 1; AAA85354)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 58513 MW; 9384B6678352A434 CRC64;
MASGSVAECL QQETTCPVCL QYFVEPMMLD CGHNICCACL ARCWGAAETN VSCPQCRETF
PQRHMRPNRH LANVTQLVKQ LRTERPSGPG GEMGVCEKHR EPLKLYCEQD QMPICVVCDR
SREHRGHSVL PLEEAVEGFK EQIQNRLDHL RRVKDLKKRR RAQGEQARAE LLSLTQMERE
KIVWEFEQLY HSLKEHEYRL LARLEELDLA IYNSINGAIT QFSCNISHLS GLIAQLEEKQ
QQPTRELLQD IGDTLSRAER IRIPEPWITP PDLQEKIHIF AQKCLFLTES LKQFTEKMQS
DMEKIQELRE AQLYSVDVTL DPDTAYPSLI LSDNLRQVRY SYLQQDLPDN PERFNLFPCV
LGSPCFIAGR HYWEVEVGDK AKWTIGVCED SVCRKGGVTS APQNGFWAVS LWYGKEYWAL
TSPMTALPLR TPLQRVGIFL DYDAGEVSFY NVTERCHTFT FSHATFCGPV RPYFSLSYSG
GKSAAPLIIC PMSGIDGFSG HVGNHGHSME TSP
