TRI69_MOUSE
ID TRI69_MOUSE Reviewed; 500 AA.
AC Q80X56; Q8VHZ6;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM69;
DE EC=2.3.2.27;
DE AltName: Full=RING finger B-box coiled-coil transcription factor;
DE AltName: Full=RING finger protein 36;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM69 {ECO:0000305};
DE AltName: Full=Testis-specific RING finger protein;
DE AltName: Full=Tripartite motif-containing protein 69;
GN Name=Trim69; Synonyms=Rnf36, Trif;
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 TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=11578878; DOI=10.1016/s0925-4773(01)00485-3;
RA Shyu H.-W., Hsu S.-H., Hsieh-Li H.-L., Li H.;
RT "A novel member of the RBCC family, Trif, expressed specifically in the
RT spermatids of mouse testis.";
RL Mech. Dev. 108:213-216(2001).
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 TISSUE=Testis;
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 FUNCTION, INTERACTION WITH PML, AND PHOSPHORYLATION.
RX PubMed=12837286; DOI=10.1016/s0014-4827(03)00110-1;
RA Shyu H.-W., Hsu S.-H., Hsieh-Li H.-M., Li H.;
RT "Forced expression of RNF36 induces cell apoptosis.";
RL Exp. Cell Res. 287:301-313(2003).
CC -!- FUNCTION: May have E3 ubiquitin-protein ligase activity. May play a
CC role in apoptosis. {ECO:0000269|PubMed:12837286}.
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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with PML. {ECO:0000269|PubMed:12837286}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86WT6}. Nucleus
CC {ECO:0000250|UniProtKB:Q86WT6}. Nucleus speckle.
CC -!- TISSUE SPECIFICITY: Expressed in spermatid.
CC {ECO:0000269|PubMed:11578878}.
CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3
CC ubiquitin ligase activity and for nuclear localization and aggregation.
CC {ECO:0000250|UniProtKB:Q86WT6}.
CC -!- PTM: Phosphorylated. Phosphorylation is necessary for nuclear
CC localization. {ECO:0000269|PubMed:12837286}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; AF334958; AAL41031.1; -; mRNA.
DR EMBL; AL845457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC050815; AAH50815.1; -; mRNA.
DR CCDS; CCDS16655.1; -.
DR RefSeq; NP_536771.2; NM_080510.2.
DR AlphaFoldDB; Q80X56; -.
DR SMR; Q80X56; -.
DR BioGRID; 214351; 40.
DR IntAct; Q80X56; 40.
DR STRING; 10090.ENSMUSP00000047627; -.
DR iPTMnet; Q80X56; -.
DR PhosphoSitePlus; Q80X56; -.
DR PaxDb; Q80X56; -.
DR PRIDE; Q80X56; -.
DR ProteomicsDB; 259095; -.
DR Antibodypedia; 24281; 326 antibodies from 35 providers.
DR DNASU; 70928; -.
DR Ensembl; ENSMUST00000036089; ENSMUSP00000047627; ENSMUSG00000033368.
DR GeneID; 70928; -.
DR KEGG; mmu:70928; -.
DR UCSC; uc008mah.1; mouse.
DR CTD; 140691; -.
DR MGI; MGI:1918178; Trim69.
DR VEuPathDB; HostDB:ENSMUSG00000033368; -.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160707; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q80X56; -.
DR OMA; GNYVEMN; -.
DR OrthoDB; 631080at2759; -.
DR PhylomeDB; Q80X56; -.
DR TreeFam; TF342569; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 70928; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Trim69; mouse.
DR PRO; PR:Q80X56; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80X56; protein.
DR Bgee; ENSMUSG00000033368; Expressed in spermatid and 8 other tissues.
DR Genevisible; Q80X56; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
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; 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 PRINTS; PR01407; BUTYPHLNCDUF.
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; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Coiled coil; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..500
FT /note="E3 ubiquitin-protein ligase TRIM69"
FT /id="PRO_0000278237"
FT DOMAIN 306..500
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 42..83
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..153
FT /note="Necessary for nuclear localization"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 217..256
FT /evidence="ECO:0000255"
FT MOD_RES 342
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5BK82"
FT CONFLICT 117
FT /note="P -> A (in Ref. 1; AAL41031)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="M -> L (in Ref. 1; AAL41031)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="F -> L (in Ref. 1; AAL41031)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 57312 MW; 607B0CEB02213754 CRC64;
MEVSSRPPSN FDPGNYVEMS DPTTTHLPSK VVIQDLTTEL HCPLCNDWFR DPLMLTCGHN
FCQDCIQSFW KVHSKETFCP DCKMLCQYSN CTFNLVLEKL VEKIKKLPLL KGHPQCPEHG
ENLKLFSKPE GKMICFQCKD ARLSMGQSKD FLQISEAVRF FTEELAIYQS QLQTTLKELQ
SLRTIQKDAI SAYKDNKIQL QQNLSLEFLK LHQFLHNKEK DILNDLRDEG KLLNEEMEVN
LNQIQEQCLV AKDMLATIQA RMEQQNSFDF LTDITKLIES MEKGMKTIVP RQLIAKKLSL
GRFKGPIQYI IWKEMQAILS PGPSQLTLDP KTAHPNLVLS KSQTSVCHCD VKQVMPDDPE
RFDSSVAVLG SKGFTSGKWY WEIEVGKKTK WTIGVVRESI IRKGSCPLTP EQGFWLLRLR
NQTDLKALDL PSRSLTLGDL RRVGVYLDYE GGQVSFYNAT TMTHLYTFSS VFQEKLFPYL
CPCLNDGGEN KEPLHIVHPQ
