RN112_BOVIN
ID RN112_BOVIN Reviewed; 628 AA.
AC Q08DF2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=RING finger protein 112;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Zinc finger protein 179;
GN Name=RNF112; Synonyms=ZNF179;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Brain cortex;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; BC123783; AAI23784.1; -; mRNA.
DR RefSeq; NP_001070607.1; NM_001077139.1.
DR AlphaFoldDB; Q08DF2; -.
DR SMR; Q08DF2; -.
DR STRING; 9913.ENSBTAP00000000703; -.
DR PaxDb; Q08DF2; -.
DR Ensembl; ENSBTAT00000087109; ENSBTAP00000067790; ENSBTAG00000000540.
DR GeneID; 768085; -.
DR KEGG; bta:768085; -.
DR CTD; 7732; -.
DR VEuPathDB; HostDB:ENSBTAG00000000540; -.
DR VGNC; VGNC:34011; RNF112.
DR eggNOG; KOG2037; Eukaryota.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160153; -.
DR InParanoid; Q08DF2; -.
DR OrthoDB; 836337at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000000540; Expressed in Ammon's horn and 89 other tissues.
DR ExpressionAtlas; Q08DF2; baseline.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
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:0030182; P:neuron differentiation; ISS:UniProtKB.
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..628
FT /note="RING finger protein 112"
FT /id="PRO_0000274484"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 167..409
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 132..628
FT /note="Interaction with ZBTB16"
FT /evidence="ECO:0000250|UniProtKB:Q96DY5"
FT BINDING 318..319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q96DY5"
SQ SEQUENCE 628 AA; 67392 MW; 8346859DAFCE86E6 CRC64;
MPRSALSVIS FCHRLGKQER KRSFMGNSSN SWSHTPFPKL ELGLGSRPTA PREPPACSIC
LERPREPISL DCGHDFCPRC FSTHRVPGCG PPCCPECRKT CKRRKGLRGL GERMRLLPQR
PLPAAALQET CAVRAEPLLL VRINASGGLI LRMGAINRCL KHPLARDTPV CLLAVLGGPH
SGKTFLLNHL LQGLPGLASG EGSWPRSAGS GQGFRWGANG LSRGIWMWSH PFLLGKEGRK
VAVFLVDTGD VMSPELSRET RTRLCALTSM LSSYQILTAS QELKDTDLEH LETFVHVAEV
MGRHYGMVPI QHLDLLVRDS SHPSKAWQGH VGDVIQKSSG KYPKVQGLLQ GRRARCYLLP
APGRRWASRG HGSSGDDDAG RLRAYVADVL SAAPQHAKSR CPGYWSEGRP AARGDRRLLT
GQQLAQEVKN LSGWMGRTGP SCASPDEMAA QLHDLRTVEA AKKEFEEYVR QQDAATKRIF
SALRVLPDTM RNLLSAQKDT LLARHGATLL CTGREQTLEA LEAELQAEAK AFMDSYTVRF
CGHLAAVGGA VGAGLMGLAG GVVGAGMAAA ALAAEAGMVA AGAAVGATGA AVVGGGVGAG
LAATVGCMEK EEDERVQEGD REPLLQEE
