RN112_MOUSE
ID RN112_MOUSE Reviewed; 654 AA.
AC Q96DY5; Q3TNS6; Q5NCN2; Q8JZT5; Q9Z328;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=RING finger protein 112;
DE EC=2.3.2.27 {ECO:0000305};
DE AltName: Full=Brain finger protein;
DE AltName: Full=Neurolastin {ECO:0000303|PubMed:26212327};
DE AltName: Full=Zinc finger protein 179;
GN Name=Rnf112; Synonyms=Bfp, Znf179;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9806830; DOI=10.1006/geno.1998.5541;
RA Orimo A., Inoue S., Ikeda K., Sato M., Kato A., Tominaga N., Suzuki M.,
RA Noda T., Watanabe M., Muramatsu M.;
RT "Molecular cloning, localization, and developmental expression of mouse
RT brain finger protein (Bfp)/ZNF179: distribution of bfp mRNA partially
RT coincides with the affected areas of Smith-Magenis syndrome.";
RL Genomics 54:59-69(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Eye;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 399-654.
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND ALTERNATIVE
RP SPLICING.
RX PubMed=21566658; DOI=10.1038/cdd.2011.52;
RA Pao P.C., Huang N.K., Liu Y.W., Yeh S.H., Lin S.T., Hsieh C.P., Huang A.M.,
RA Huang H.S., Tseng J.T., Chang W.C., Lee Y.C.;
RT "A novel RING finger protein, Znf179, modulates cell cycle exit and
RT neuronal differentiation of P19 embryonal carcinoma cells.";
RL Cell Death Differ. 18:1791-1804(2011).
RN [6]
RP INTERACTION WITH ZBTB16, AND SUBCELLULAR LOCATION.
RX PubMed=24359566; DOI=10.1186/1423-0127-20-98;
RA Lin D.Y., Huang C.C., Hsieh Y.T., Lin H.C., Pao P.C., Tsou J.H., Lai C.Y.,
RA Hung L.Y., Wang J.M., Chang W.C., Lee Y.C.;
RT "Analysis of the interaction between Zinc finger protein 179 (Znf179) and
RT promyelocytic leukemia zinc finger (Plzf).";
RL J. Biomed. Sci. 20:98-98(2013).
RN [7]
RP FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-97 AND ARG-340,
RP SUBCELLULAR LOCATION, AND AUTO-UBIQUITINATION.
RX PubMed=26212327; DOI=10.1016/j.celrep.2015.06.064;
RA Lomash R.M., Gu X., Youle R.J., Lu W., Roche K.W.;
RT "Neurolastin, a dynamin family GTPase, regulates excitatory synapses and
RT spine density.";
RL Cell Rep. 12:743-751(2015).
RN [8]
RP FUNCTION, INTERACTION WITH SIGMAR1, AND DISRUPTION PHENOTYPE.
RX PubMed=26792191; DOI=10.1016/j.neuropharm.2016.01.015;
RA Su T.C., Lin S.H., Lee P.T., Yeh S.H., Hsieh T.H., Chou S.Y., Su T.P.,
RA Hung J.J., Chang W.C., Lee Y.C., Chuang J.Y.;
RT "The sigma-1 receptor-zinc finger protein 179 pathway protects against
RT hydrogen peroxide-induced cell injury.";
RL Neuropharmacology 105:1-9(2016).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=26951452; DOI=10.1007/s12035-016-9812-7;
RA Tsou J.H., Yang Y.C., Pao P.C., Lin H.C., Huang N.K., Lin S.T., Hsu K.S.,
RA Yeh C.M., Lee K.H., Kuo C.J., Yang D.M., Lin J.H., Chang W.C., Lee Y.C.;
RT "Important roles of ring finger protein 112 in embryonic vascular
RT development and brain functions.";
RL Mol. Neurobiol. 54:2286-2300(2017).
RN [10]
RP FUNCTION, INDUCTION, INTERACTION WITH SP1, AND SUBCELLULAR LOCATION.
RX PubMed=27918959; DOI=10.1016/j.redox.2016.11.012;
RA Chuang J.Y., Kao T.J., Lin S.H., Wu A.C., Lee P.T., Su T.P., Yeh S.H.,
RA Lee Y.C., Wu C.C., Chang W.C.;
RT "Specificity protein 1-zinc finger protein 179 pathway is involved in the
RT attenuation of oxidative stress following brain injury.";
RL Redox Biol. 11:135-143(2017).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28684796; DOI=10.1038/s41598-017-05305-0;
RA Lee K.H., Chen C.L., Lee Y.C., Kao T.J., Chen K.Y., Fang C.Y., Chang W.C.,
RA Chiang Y.H., Huang C.C.;
RT "Znf179 induces differentiation and growth arrest of human primary
RT glioblastoma multiforme in a p53-dependent cell cycle pathway.";
RL Sci. Rep. 7:4787-4787(2017).
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
CC (PubMed:21566658, PubMed:28684796). Plays a role not only in the fetal
CC period during the development of the nervous system, but also in the
CC adult brain, where it is involved in the maintenance of neural
CC functions and protection of the nervous tissue cells from oxidative
CC stress-induced damage (PubMed:27918959, PubMed:26792191,
CC PubMed:26951452). Exhibits GTPase and E3 ubiquitin-protein ligase
CC activities. Regulates dendritic spine density and synaptic
CC neurotransmission; its ability to hydrolyze GTP is involved in the
CC maintenance of dendritic spine density (PubMed:26212327).
CC {ECO:0000269|PubMed:21566658, ECO:0000269|PubMed:26212327,
CC ECO:0000269|PubMed:26792191, ECO:0000269|PubMed:26951452,
CC ECO:0000269|PubMed:27918959, ECO:0000269|PubMed:28684796}.
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 (PubMed:26212327). Interacts with SP1 in an
CC oxidative stress-regulated manner (PubMed:27918959). Interacts with
CC SIGMAR1 in an oxidative stress-regulated manner (PubMed:26792191).
CC Interacts with ZBTB16 (via C2H2-type zinc finger domains 1 and 2)
CC (PubMed:24359566). {ECO:0000269|PubMed:24359566,
CC ECO:0000269|PubMed:26212327, ECO:0000269|PubMed:26792191,
CC ECO:0000269|PubMed:27918959}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:26212327}; Multi-
CC pass membrane protein {ECO:0000255}. Membrane
CC {ECO:0000269|PubMed:26212327}; Peripheral membrane protein
CC {ECO:0000269|PubMed:26212327}. Cytoplasm {ECO:0000269|PubMed:24359566,
CC ECO:0000269|PubMed:27918959, ECO:0000269|PubMed:9806830}. Nucleus
CC {ECO:0000269|PubMed:24359566, ECO:0000269|PubMed:26951452,
CC ECO:0000269|PubMed:27918959, ECO:0000269|PubMed:9806830}. Nucleus,
CC nuclear body {ECO:0000269|PubMed:24359566}. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:24359566}. Endosome {ECO:0000269|PubMed:26212327}.
CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle
CC {ECO:0000269|PubMed:26212327}. Postsynaptic density
CC {ECO:0000269|PubMed:26212327}. Perikaryon
CC {ECO:0000269|PubMed:26951452}. Cell projection, neuron projection
CC {ECO:0000269|PubMed:26951452}. Note=Predominantly in the nucleus, but
CC some amounts were also found in the cytoplasm (PubMed:9806830,
CC PubMed:24359566). Oxidative stress stimulates its shuttling from the
CC cytoplasm into the nucleus (PubMed:27918959). Recruited to nuclear
CC bodies via its interaction with ZBTB16 (PubMed:24359566). Localizes to
CC the cell soma and neuritis and only slightly to the nucleus in the
CC neurons of most brain areas (PubMed:26951452).
CC {ECO:0000269|PubMed:24359566, ECO:0000269|PubMed:26951452,
CC ECO:0000269|PubMed:27918959, ECO:0000269|PubMed:9806830}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q96DY5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96DY5-2; Sequence=VSP_042392;
CC Name=3;
CC IsoId=Q96DY5-3; Sequence=VSP_042393;
CC -!- TISSUE SPECIFICITY: Expressed in most of the brain areas, including
CC cortex, striatum, hippocampus, thalamus, and cerebellum (at protein
CC level). Expressed in lateral amygdaloid nucleus, and ventromedial
CC hypothalamus. Also expressed strongly in the marginal zone of brain
CC vesicles, optic stalk, and cartilage primordium.
CC {ECO:0000269|PubMed:21566658, ECO:0000269|PubMed:26951452,
CC ECO:0000269|PubMed:9806830}.
CC -!- INDUCTION: Up-regulated by traumatic brain injury and hydrogen peroxide
CC (at protein level). {ECO:0000269|PubMed:27918959}.
CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:26212327}.
CC -!- DISRUPTION PHENOTYPE: Embryos exhibit blood vascular defects and die in
CC utero. The survivors manifest growth retardation as indicated by
CC smaller size and a reduced weight, and display impairment of brain
CC functions including motor balance, and spatial learning and memory
CC (PubMed:26951452). Mice exhibit a reduction in the size of brains,
CC reduced dendritic spine density, impaired synaptic transmission and
CC reduced levels of antioxidant enzymes in the hippocampus
CC (PubMed:26792191, PubMed:26212327). Knockdown of RNF112 diminishes
CC neuronal differentiation, glial differentiation and dendritic
CC arborization in primary cerebellar granule cells (PubMed:28684796,
CC PubMed:21566658). {ECO:0000269|PubMed:21566658,
CC ECO:0000269|PubMed:26212327, ECO:0000269|PubMed:26792191,
CC ECO:0000269|PubMed:26951452, ECO:0000269|PubMed:28684796}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. GB1 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU01052}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34180.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB013097; BAA34180.1; ALT_FRAME; mRNA.
DR EMBL; AL604029; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013139; AAH13139.1; -; mRNA.
DR EMBL; BC037118; AAH37118.1; -; mRNA.
DR EMBL; AK165038; BAE38012.1; -; mRNA.
DR CCDS; CCDS24812.1; -. [Q96DY5-1]
DR CCDS; CCDS78960.1; -. [Q96DY5-2]
DR CCDS; CCDS88167.1; -. [Q96DY5-3]
DR RefSeq; NP_001277953.1; NM_001291024.1. [Q96DY5-2]
DR RefSeq; NP_033574.2; NM_009548.3. [Q96DY5-1]
DR RefSeq; XP_006533241.1; XM_006533178.2. [Q96DY5-3]
DR RefSeq; XP_006533242.1; XM_006533179.2.
DR RefSeq; XP_006533245.1; XM_006533182.3. [Q96DY5-1]
DR RefSeq; XP_006533246.1; XM_006533183.2. [Q96DY5-2]
DR AlphaFoldDB; Q96DY5; -.
DR SMR; Q96DY5; -.
DR BioGRID; 204645; 9.
DR STRING; 10090.ENSMUSP00000056464; -.
DR iPTMnet; Q96DY5; -.
DR PhosphoSitePlus; Q96DY5; -.
DR PaxDb; Q96DY5; -.
DR PRIDE; Q96DY5; -.
DR ProteomicsDB; 301607; -. [Q96DY5-1]
DR ProteomicsDB; 301608; -. [Q96DY5-2]
DR ProteomicsDB; 301609; -. [Q96DY5-3]
DR Antibodypedia; 3002; 162 antibodies from 23 providers.
DR DNASU; 22671; -.
DR Ensembl; ENSMUST00000054927; ENSMUSP00000056464; ENSMUSG00000010086. [Q96DY5-1]
DR Ensembl; ENSMUST00000060255; ENSMUSP00000059903; ENSMUSG00000010086. [Q96DY5-3]
DR Ensembl; ENSMUST00000102661; ENSMUSP00000099722; ENSMUSG00000010086. [Q96DY5-2]
DR GeneID; 22671; -.
DR KEGG; mmu:22671; -.
DR UCSC; uc007jhj.2; mouse. [Q96DY5-1]
DR UCSC; uc007jhk.2; mouse. [Q96DY5-3]
DR UCSC; uc007jhl.2; mouse. [Q96DY5-2]
DR CTD; 7732; -.
DR MGI; MGI:106611; Rnf112.
DR VEuPathDB; HostDB:ENSMUSG00000010086; -.
DR eggNOG; KOG2037; Eukaryota.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160153; -.
DR HOGENOM; CLU_034812_0_0_1; -.
DR InParanoid; Q96DY5; -.
DR OMA; MGAVNRC; -.
DR OrthoDB; 836337at2759; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22671; 6 hits in 71 CRISPR screens.
DR PRO; PR:Q96DY5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q96DY5; protein.
DR Bgee; ENSMUSG00000010086; Expressed in cerebellar vermis and 118 other tissues.
DR Genevisible; Q96DY5; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044297; C:cell body; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA: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; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IDA:UniProtKB.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IMP:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0036474; P:cell death in response to hydrogen peroxide; IMP:UniProtKB.
DR GO; GO:0036473; P:cell death in response to oxidative stress; IMP:UniProtKB.
DR GO; GO:1990403; P:embryonic brain development; IMP: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; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:UniProtKB.
DR GO; GO:0045687; P:positive regulation of glial cell differentiation; IMP:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; IDA: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; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cytoplasm; Cytoplasmic vesicle;
KW Endosome; GTP-binding; Membrane; Metal-binding; Neurogenesis;
KW Nucleotide-binding; Nucleus; Reference proteome; Synapse; Transferase;
KW Transmembrane; Transmembrane helix; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..654
FT /note="RING finger protein 112"
FT /id="PRO_0000415817"
FT TRANSMEM 570..590
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 603..623
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 189..420
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01052"
FT ZN_FING 80..121
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 154..654
FT /note="Interaction with ZBTB16"
FT /evidence="ECO:0000269|PubMed:24359566"
FT BINDING 340..341
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000269|PubMed:26212327"
FT VAR_SEQ 33..55
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9806830"
FT /id="VSP_042392"
FT VAR_SEQ 332
FT /note="I -> IQVRQFLVSSILTHQSRLPVSGPFLF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042393"
FT MUTAGEN 97
FT /note="H->N: Loss of endosomal localization."
FT /evidence="ECO:0000269|PubMed:26212327"
FT MUTAGEN 340
FT /note="R->Q: Reduced GTP-hydrolysis."
FT /evidence="ECO:0000269|PubMed:26212327"
FT CONFLICT 72
FT /note="S -> P (in Ref. 1; BAA34180)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="E -> K (in Ref. 1; BAA34180)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="G -> A (in Ref. 1; BAA34180)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="N -> D (in Ref. 4; BAE38012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 654 AA; 71275 MW; 491B4A0BCF4F5D72 CRC64;
MPRPVLSVTA FCHRLGKRES KRSFMGNSSN SWVLPREEAQ GWMGQAVQGG TRTSRSHASF
PKLELGLGHR PSPTREPPTC SICLERLREP ISLDCGHDFC IRCFSTHRIP GCELPCCPEC
RKICKQRKGL RSLGERMKLL PQRPLPPALQ ETCAVRAERL LLVRINASGG LILRMGAINR
CLKHPLARDT PVCLLAVLGE QHSGKSFLLD HLLSGLPSLE SGDSGRPRAE GSLPGIRWGA
NGLTRGIWMW SHPFLLGKEG KKVAVFLVDT GDVMSPELSK ETRVKLCALT MMLSSYQILN
TSQELKDTDL GYLEMFVHVA EVMGKHYGMV PIQHLDLLVR DSSHHNKSGQ GHVGDILQKL
SGKYPKVQEL LLGKRARCYL LPAPERQWVN KDQASPRGNT EDDFSHHFRA YILDVLSTAP
QHAKSRCQGY WSEGRAVARG DRRLLTGQQL AQEIKNLSGW MGKTGPSFNS PDEMAAQLHD
LRKVEAAKKE FEEYVRQQDI ATKRIFSALR VLPDTMRNLL STQKDAILAR HGVALLCKER
EQTLEALEAE LQAEAKAFMD SYTMRFCGHL AAVGGAVGAG LMGLAGGVVG AGMAAAALAA
EAGMVAAGAA VGATGAAVVG GGVGAGLAAT VGCMEKEEDE RVQGGDREPL LQEE
