RN112_RAT
ID RN112_RAT Reviewed; 631 AA.
AC O70418;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=RING finger protein 112;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Brain finger protein;
DE AltName: Full=Zinc finger protein 179;
GN Name=Rnf112; Synonyms=Bfp, Zfp179, Znf179;
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].
RX PubMed=9367872; DOI=10.1006/bbrc.1997.7589;
RA Inoue S., Orimo A., Saito T., Ikeda K., Sakata K., Hosoi T., Orimo H.,
RA Ouchi Y., Muramatsu M.;
RT "A novel RING finger protein, BFP, predominantly expressed in the brain.";
RL Biochem. Biophys. Res. Commun. 240:8-14(1997).
CC -!- FUNCTION: E3 ubiquitin-protein ligase that plays an important role in
CC neuronal differentiation, including neurogenesis and gliogenesis,
CC during brain development. During embryonic development initiates
CC neuronal differentiation by inducing cell cycle arrest at the G0/G1
CC phase through up-regulation of cell-cycle regulatory proteins. Plays a
CC role not only in the fetal period during the development of the nervous
CC system, but also in the adult brain, where it is involved in the
CC maintenance of neural functions and protection of the nervous tissue
CC cells from oxidative stress-induced damage. Exhibits GTPase and E3
CC ubiquitin-protein ligase activities. Regulates dendritic spine density
CC and synaptic neurotransmission; its ability to hydrolyze GTP is
CC involved in the maintenance of dendritic spine density.
CC {ECO:0000250|UniProtKB:Q96DY5}.
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; Evidence={ECO:0000305};
CC -!- PATHWAY: Protein modification; protein ubiquitination. {ECO:0000305}.
CC -!- SUBUNIT: Self-associates. Interacts with SP1 in an oxidative stress-
CC regulated manner. Interacts with SIGMAR1 in an oxidative stress-
CC regulated manner. Interacts with ZBTB16 (via C2H2-type zinc finger
CC domains 1 and 2). {ECO:0000250|UniProtKB:Q96DY5}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q96DY5}; Multi-
CC pass membrane protein {ECO:0000255}. Membrane
CC {ECO:0000250|UniProtKB:Q96DY5}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q96DY5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96DY5}. Nucleus {ECO:0000250|UniProtKB:Q96DY5}.
CC Nucleus, nuclear body {ECO:0000250|UniProtKB:Q96DY5}. Nucleus,
CC nucleoplasm {ECO:0000250|UniProtKB:Q96DY5}. Endosome
CC {ECO:0000250|UniProtKB:Q96DY5}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle {ECO:0000250|UniProtKB:Q96DY5}. Postsynaptic density
CC {ECO:0000250|UniProtKB:Q96DY5}. Perikaryon
CC {ECO:0000250|UniProtKB:Q96DY5}. Cell projection, neuron projection
CC {ECO:0000250|UniProtKB:Q96DY5}. Note=Predominantly in the nucleus, but
CC some amounts were also found in the cytoplasm. Oxidative stress
CC stimulates its shuttling from the cytoplasm into the nucleus. Recruited
CC to nuclear bodies via its interaction with ZBTB16. Localizes to the
CC cell soma and neuritis and only slightly to the nucleus in the neurons
CC of most brain areas. {ECO:0000250|UniProtKB:Q96DY5}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000250|UniProtKB:Q96DY5}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
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DR EMBL; AF054586; AAC08583.1; -; mRNA.
DR PIR; JC5803; JC5803.
DR RefSeq; NP_619516.1; NM_138613.1.
DR AlphaFoldDB; O70418; -.
DR SMR; O70418; -.
DR STRING; 10116.ENSRNOP00000003228; -.
DR PhosphoSitePlus; O70418; -.
DR PaxDb; O70418; -.
DR GeneID; 24916; -.
DR KEGG; rno:24916; -.
DR UCSC; RGD:3986; rat.
DR CTD; 7732; -.
DR RGD; 3986; Rnf112.
DR eggNOG; KOG2037; Eukaryota.
DR eggNOG; KOG2177; Eukaryota.
DR InParanoid; O70418; -.
DR OrthoDB; 836337at2759; -.
DR PhylomeDB; O70418; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:O70418; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000002364; Expressed in frontal cortex and 13 other tissues.
DR ExpressionAtlas; O70418; baseline and differential.
DR Genevisible; O70418; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044297; C:cell body; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-SubCell.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; NAS:RGD.
DR GO; GO:0036474; P:cell death in response to hydrogen peroxide; ISS:UniProtKB.
DR GO; GO:0036473; P:cell death in response to oxidative stress; ISS:UniProtKB.
DR GO; GO:1990403; P:embryonic brain development; ISS:UniProtKB.
DR GO; GO:0007029; P:endoplasmic reticulum organization; IBA:GO_Central.
DR GO; GO:0070315; P:G1 to G0 transition involved in cell differentiation; ISO:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045687; P:positive regulation of glial cell differentiation; ISO:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:RGD.
DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0033194; P:response to hydroperoxide; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030386; G_GB1_RHD3_dom.
DR InterPro; IPR015894; Guanylate-bd_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02263; GBP; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Cell projection; Cytoplasm; Cytoplasmic vesicle; Endosome; GTP-binding;
KW Membrane; Metal-binding; Neurogenesis; Nucleotide-binding; Nucleus;
KW Reference proteome; Synapse; Transferase; Transmembrane;
KW Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..631
FT /note="RING finger protein 112"
FT /id="PRO_0000056302"
FT TRANSMEM 547..567
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 580..600
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 166..397
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT ZN_FING 57..98
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 131..631
FT /note="Interaction with ZBTB16"
FT /evidence="ECO:0000250|UniProtKB:Q96DY5"
FT BINDING 317..318
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96DY5"
SQ SEQUENCE 631 AA; 68646 MW; 6C997B8890CAB564 CRC64;
MPRPVLSVTA FCHRLGKRES KRSFMGNSSN SWSHASFPKL ELGLGQRPSP PRESPTCSIC
LERLREPISL DCGHDFCIRC FSTHRIPGCE LPCCPECRKI CKQKKGLRSL GERMKLLPQR
PLPPALQETC AVRAERLLLV RINASGGLIL RMGAINRCLK HPLARDTPVC LLAVLGEQHS
GKSFLLDHLL RGLPGLESGD STRPRAEGSL PGIRWGANGL TRGIWMWSHP FLLGKEGKKV
AVFLVDTGDV MSPELSRETR VKLCALTMML SSYQILNTSQ ELKDTDLGYL EMFVHVAEVM
GKHYGMVPIQ HLDLLVRDSS HHNKSGQGHV GDILQKLSGK YPKVQELLLG KRARCYLLPA
PERQWVNKGQ ASPGGNTEDD FSHHFRAYIS DVLSTAPQHA KSRCQGYWSE GRAMARGDRR
LLTGQQLAQE IKNLSGWMGK SGPSFSSPDE MAAQLHDLRK VEAAKKEFEE YVRQQDIATK
RIFSALRVLP DTMRNLLSTQ KDAILARHGV ALLCKEREQT LEALEAELQA EAKAFMDSYT
MRFCGHLAAV GGAVGAGLMG LAGGVVGAGM AAAALAAEAG MVAAGAAVGA TGAAVVGGGV
GAGLAATVGC MEKEEDERVQ GGDREPLLQE E
