ID   RNF39_RAT               Reviewed;         352 AA.
AC   Q920M2;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=RING finger protein 39;
DE   AltName: Full=LTP-induced RING finger protein;
GN   Name=Rnf39; Synonyms=Lirf;
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 [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Wistar;
RX   PubMed=11716498; DOI=10.1006/bbrc.2001.5975;
RA   Matsuo R., Asada A., Fujitani K., Inokuchi K.;
RT   "LIRF, a gene induced during hippocampal long-term potentiation as an
RT   immediate-early gene, encodes a novel RING finger protein.";
RL   Biochem. Biophys. Res. Commun. 289:479-484(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15060004; DOI=10.1101/gr.1987704;
RA   Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H.,
RA   Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.;
RT   "The genomic sequence and comparative analysis of the rat major
RT   histocompatibility complex.";
RL   Genome Res. 14:631-639(2004).
RN   [3]
RP   FUNCTION.
RX   PubMed=10820183; DOI=10.1046/j.1471-4159.2000.0742239.x;
RA   Matsuo R., Murayama A., Saitoh Y., Sakaki Y., Inokuchi K.;
RT   "Identification and cataloging of genes induced by long-lasting long-term
RT   potentiation in awake rats.";
RL   J. Neurochem. 74:2239-2249(2000).
CC   -!- FUNCTION: May play a role in prolonged long term-potentiation (LTP)
CC       maintenance. {ECO:0000269|PubMed:10820183}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11716498}.
CC   -!- TISSUE SPECIFICITY: Expressed in the hippocampus. Expression is rapidly
CC       up-regulated in granule cells of the dentate gyrus after LTP induction.
CC       {ECO:0000269|PubMed:11716498}.
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DR   EMBL; AB070897; BAB70703.1; -; mRNA.
DR   EMBL; BX883051; CAE84060.1; -; Genomic_DNA.
DR   RefSeq; NP_599201.1; NM_134374.2.
DR   AlphaFoldDB; Q920M2; -.
DR   SMR; Q920M2; -.
DR   STRING; 10116.ENSRNOP00000001014; -.
DR   iPTMnet; Q920M2; -.
DR   PhosphoSitePlus; Q920M2; -.
DR   jPOST; Q920M2; -.
DR   PaxDb; Q920M2; -.
DR   Ensembl; ENSRNOT00000001014; ENSRNOP00000001014; ENSRNOG00000000781.
DR   GeneID; 171387; -.
DR   KEGG; rno:171387; -.
DR   UCSC; RGD:628854; rat.
DR   CTD; 80352; -.
DR   RGD; 628854; Rnf39.
DR   eggNOG; KOG2177; Eukaryota.
DR   GeneTree; ENSGT00940000162641; -.
DR   HOGENOM; CLU_013137_7_5_1; -.
DR   InParanoid; Q920M2; -.
DR   OMA; GESCYAV; -.
DR   OrthoDB; 791427at2759; -.
DR   PhylomeDB; Q920M2; -.
DR   TreeFam; TF317532; -.
DR   PRO; PR:Q920M2; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000000781; Expressed in esophagus and 20 other tissues.
DR   Genevisible; Q920M2; RN.
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   GO; GO:0048168; P:regulation of neuronal synaptic plasticity; NAS:RGD.
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; IPR027370; Znf-RING_LisH.
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; PF13445; zf-RING_UBOX; 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   2: Evidence at transcript level;
KW   Cytoplasm; Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..352
FT                   /note="RING finger protein 39"
FT                   /id="PRO_0000056083"
FT   DOMAIN          142..352
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00548"
FT   ZN_FING         20..67
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          98..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   352 AA;  38345 MW;  153F27B612D28E80 CRC64;
     MEVPELGPGL VERLEQLATC PLCGGPFEDP VLLACEHSFC RSCLARCWGS PAAPGSEEAT
     PSCPCCGQPC PRRSLRSNVR LAVEVRISRG LREKLAEPGA RTGRRRGGRI PTMGCLDPQG
     EDMRKTWRRF DVPVPKSSNS EEDLPEDYPV VKNMLHRLTA DLTLDPRTAH RDLLISSDYR
     GVSLAPPGTP VPLDSPERFD RLRAVLGAQG FASGRHCWEV ETAEGACFRD SLAKDEDAGE
     SCYAVGAAGE SVTRKGLIKL CPSEAIWAVE GRGGRLWALT APEPTLLGGA RPPPQRIRVD
     LDWERGRVAF YDGRSLDLLF AFQAPGPLGE RVFPLLCTCD PRAPLRIVPG EA