ID A0A096P347_PAPAN Unreviewed; 631 AA.
AC A0A096P347;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Ring finger protein 112 {ECO:0000313|Ensembl:ENSPANP00000019772.1};
GN Name=RNF112 {ECO:0000313|Ensembl:ENSPANP00000019772.1};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000019772.1, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000019772.1, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000019772.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. GB1/RHD3 GTPase family. {ECO:0000256|PROSITE-
CC ProRule:PRU01052}.
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DR RefSeq; XP_003912498.1; XM_003912449.3.
DR AlphaFoldDB; A0A096P347; -.
DR Ensembl; ENSPANT00000022302.3; ENSPANP00000019772.1; ENSPANG00000023652.3.
DR GeneID; 100999998; -.
DR KEGG; panu:100999998; -.
DR CTD; 7732; -.
DR eggNOG; KOG2037; Eukaryota.
DR eggNOG; KOG2177; Eukaryota.
DR GeneTree; ENSGT00940000160153; -.
DR HOGENOM; CLU_034812_0_0_1; -.
DR OMA; QQDMATK; -.
DR OrthoDB; 5363212at2759; -.
DR Proteomes; UP000028761; Chromosome 17.
DR Bgee; ENSPANG00000023652; Expressed in cerebellum and 47 other cell types or tissues.
DR ExpressionAtlas; A0A096P347; baseline.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005768; C:endosome; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0005525; F:GTP binding; IEA:Ensembl.
DR GO; GO:0003924; F:GTPase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:1990403; P:embryonic brain development; IEA:Ensembl.
DR GO; GO:0070315; P:G1 to G0 transition involved in cell differentiation; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0045687; P:positive regulation of glial cell differentiation; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0033194; P:response to hydroperoxide; IEA:Ensembl.
DR CDD; cd01851; GBP; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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 PANTHER; PTHR10751; GUANYLATE BINDING PROTEIN; 1.
DR PANTHER; PTHR10751:SF1; RING FINGER PROTEIN 112; 1.
DR Pfam; PF02263; GBP; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51715; G_GB1_RHD3; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 57..98
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 166..397
FT /note="GB1/RHD3-type G"
FT /evidence="ECO:0000259|PROSITE:PS51715"
SQ SEQUENCE 631 AA; 68434 MW; 08F922CE2C292E56 CRC64;
MPRPALSVTS FCHRLGKRER KQSFMGNSGN SWSHTPFPKL ELGLGPRPMA PRELPTCSIC
LERLREPISL ECGHDFCIRC FSTHRVPGCE PPCCPECRKI CKQKRGLRSL GEKMKLLPQR
PLPPALQETC PVRAEPLLLV RVNASGGLIL RMGAINRCLK HPLARDTPVC LLAVLGEQHS
GKSFLLNHLL QGLPGLESGE GGWPRGGEAS LQGCRWGANG LARGIWMWSH PFLLGKEGKK
VAVFLVDTGD AMSPELSRET RIKLCALTTM LSSYQILNTC QELKDTDLDY LEMFVHVAEV
MGKHYGMVPI QHLDLLVRDS SHPNKAGQGH VGNIFQRLSG RYPKVQELLQ GKRARCCLLP
APGRRWMNQG HASPDDTDDD FCHLLGAYVS DVLSAAPQHA KSRCQGYWNE GRAVARGDRR
LLTGQQLAQE IKNLSGWMGR TGPGFTSPDE MAAQLHDLRK VEAAKREFEE YVRQQDIATK
RIFSALRVLP DTMRNLLSTQ KDAILARHGV ALLCKGRDQT LEALEAELQA TAKAFMDSYT
MRFCGHLAAV GGAVGAGLMG LAGGVVGAGM AAAALAAEAG MVAAGAAVGA TGAAVVGGGV
GAGLAATVGC MEKEEDERVL EGDREPLLQE E
//
