TRI69_RAT
ID TRI69_RAT Reviewed; 499 AA.
AC Q5BK82;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=E3 ubiquitin-protein ligase TRIM69;
DE EC=2.3.2.27;
DE AltName: Full=RING finger protein 36;
DE AltName: Full=RING-type E3 ubiquitin transferase TRIM69 {ECO:0000305};
DE AltName: Full=Tripartite motif-containing protein 69;
GN Name=Trim69; Synonyms=Rnf36;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May have E3 ubiquitin-protein ligase activity. May play a
CC role in apoptosis. {ECO:0000250|UniProtKB:Q80X56}.
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:0000250|UniProtKB:Q80X56}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86WT6}. Nucleus
CC {ECO:0000250|UniProtKB:Q86WT6}. Nucleus speckle.
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:0000250|UniProtKB:Q80X56}.
CC -!- SIMILARITY: Belongs to the TRIM/RBCC family. {ECO:0000305}.
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DR EMBL; BC091171; AAH91171.1; -; mRNA.
DR RefSeq; NP_001013178.1; NM_001013160.1.
DR AlphaFoldDB; Q5BK82; -.
DR SMR; Q5BK82; -.
DR STRING; 10116.ENSRNOP00000023209; -.
DR iPTMnet; Q5BK82; -.
DR PhosphoSitePlus; Q5BK82; -.
DR PaxDb; Q5BK82; -.
DR Ensembl; ENSRNOT00000023209; ENSRNOP00000023209; ENSRNOG00000017157.
DR GeneID; 311373; -.
DR KEGG; rno:311373; -.
DR UCSC; RGD:1305074; rat.
DR CTD; 140691; -.
DR RGD; 1305074; Trim69.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160707; -.
DR HOGENOM; CLU_013137_0_3_1; -.
DR InParanoid; Q5BK82; -.
DR OMA; GNYVEMN; -.
DR OrthoDB; 631080at2759; -.
DR PhylomeDB; Q5BK82; -.
DR TreeFam; TF342569; -.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5BK82; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000017157; Expressed in testis and 11 other tissues.
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: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..499
FT /note="E3 ubiquitin-protein ligase TRIM69"
FT /id="PRO_0000278238"
FT DOMAIN 305..499
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT ZN_FING 41..82
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..152
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250"
FT COILED 160..265
FT /evidence="ECO:0000255"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 499 AA; 57215 MW; 6050B9543D8E9A49 CRC64;
MEVSSRPPSN FDPGNYVEVS DPSTHLPSKV VIQDITTELH CPLCNDWFRD PLMLTCGHNF
CQACIQNYWK MQAKETFCPE CKMLCQYSNC TFNLVLEKLV EKIKRLPLLK GHPQCPEHGE
NLKLFSKPDG KMICFQCKDA RLSMGQSKDF LQISEAVRFF TEELAIYQSQ LQTTLKELQS
LRTMQKDAIA AYKDNKIQLQ QNLSLEFLKL HQFLHNKEKD ILNDLRDEGK VLNEEMDANL
NQIQEQCLLA KDMLANIQAR MEQQNSFDFL TDITKLLENM EKGMKTLVPR QLISKKLSLG
RFKGPIQYTI WREMQSILSP GPSQLTLDPK TAHPNLVLSN SRTSVCHGDV KQVMPDDPER
FDSSVAVLGS KGFTSGKWYW EIEVAKKTKW TIGIVRESII RKGSCPLTPE QGFWLLRLRN
QTDLKALDLP SCSLNLGDLR RVGVYLDYEG GQVSFYNATN MTHLYTFTSV FLEKLFPYLC
PCLNDGGENK EPLHIVHPQ
