ID   RNF39_MACMU             Reviewed;         420 AA.
AC   Q5TM52;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=RING finger protein 39;
GN   Name=RNF39;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15269276; DOI=10.1093/molbev/msh216;
RA   Kulski J.K., Anzai T., Shiina T., Inoko H.;
RT   "Rhesus macaque class I duplicon structures, organization, and evolution
RT   within the alpha block of the major histocompatibility complex.";
RL   Mol. Biol. Evol. 21:2079-2091(2004).
CC   -!- FUNCTION: May play a role in prolonged long term-potentiation (LTP)
CC       maintenance. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AB128049; BAD69774.1; -; Genomic_DNA.
DR   RefSeq; NP_001108418.1; NM_001114946.1.
DR   AlphaFoldDB; Q5TM52; -.
DR   SMR; Q5TM52; -.
DR   STRING; 9544.ENSMMUP00000015898; -.
DR   PRIDE; Q5TM52; -.
DR   GeneID; 712215; -.
DR   KEGG; mcc:712215; -.
DR   CTD; 80352; -.
DR   eggNOG; KOG2177; Eukaryota.
DR   InParanoid; Q5TM52; -.
DR   OrthoDB; 791427at2759; -.
DR   Proteomes; UP000006718; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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   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; IPR018957; Znf_C3HC4_RING-type.
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; PF00097; zf-C3HC4; 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   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..420
FT                   /note="RING finger protein 39"
FT                   /id="PRO_0000056081"
FT   DOMAIN          210..420
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         88..135
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          166..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   420 AA;  45420 MW;  F42F7F7AE691393D CRC64;
     MSWRDLPRLR LWLKTEAIPG EGRKAAKVNA GVGEKGIYTA SSRGGPPSAR SKAVAVVAQG
     AASRSRLSMD APELGPGLVE RLEQLATCPL CGGSFEDPVL LACEHSFCRA CLARRWGTPP
     ATDTEASPTA CPCCGLPCPR RSLRSNVRLA VEVRISRELR EKLAEPGARA GRRRGGRIPT
     MGCLDPPGED MRKTWRRFEV PTPKSSKSED DLPEDYPVVK NMLHRLTADL TLDPGTAHRR
     LLISADRRSV QLAPPGTPAP PDGPKRFDQL PAVLGAQGFG AGRHCWEVET ADAASCRDSS
     GEDEDDEESH YAVGAAGESV QRKGCVRLCP AGAVWAVEGR GGRLWALTAP EPTLLGGAEP
     PPRRIRVDLD WERGRVAFYD GRSLDLLYAF QASVPLGERI FPLFCTCDPR APLRIVPAES