ID A0A0C4N073_ACISI Unreviewed; 227 AA. AC A0A0C4N073; DT 29-APR-2015, integrated into UniProtKB/TrEMBL. DT 29-APR-2015, sequence version 1. DT 07-OCT-2020, entry version 17. DE RecName: Full=E3 ubiquitin-protein ligase RNF114 {ECO:0000256|ARBA:ARBA00014143}; DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483}; DE AltName: Full=RING finger protein 114 {ECO:0000256|ARBA:ARBA00022132}; DE AltName: Full=RING-type E3 ubiquitin transferase RNF114 {ECO:0000256|ARBA:ARBA00014453}; DE AltName: Full=Zinc finger protein 313 {ECO:0000256|ARBA:ARBA00015529}; OS Acipenser sinensis (Chinese sturgeon). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser. OX NCBI_TaxID=61970 {ECO:0000313|EMBL:AIT71674.1}; RN [1] {ECO:0000313|EMBL:AIT71674.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Spleen {ECO:0000313|EMBL:AIT71674.1}; RX PubMed=25290666; DOI=10.1016/j.fsi.2014.09.030; RA Liao Z., Chen X., Nie D., Wang J., Wu M.; RT "A RING finger protein 114 (RNF114) homolog from Chinese sturgeon RT (Acipenser sinensis) possesses immune-regulation properties via modulating RT RIG-I signaling pathway-mediated interferon expression."; RL Fish Shellfish Immunol. 41:507-516(2014). 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:0000256|ARBA:ARBA00000900}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000256|ARBA:ARBA00004906}. CC -!- SUBUNIT: Interacts with XAF1, the interaction increases XAF1 stability CC and proapoptotic effects, and may regulate IFN signaling. CC {ECO:0000256|ARBA:ARBA00011624}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KJ473607; AIT71674.1; -; mRNA. DR UniPathway; UPA00143; -. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR008598; Di19_Zn_binding_dom. DR InterPro; IPR034734; ZF_C2HC_RNF. 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; PF05605; zf-Di19; 1. DR Pfam; PF13445; zf-RING_UBOX; 1. DR Pfam; PF18574; zf_C2HC_14; 1. DR SMART; SM00184; RING; 1. DR PROSITE; PS51803; ZF_C2HC_RNF; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. PE 2: Evidence at transcript level; KW Developmental protein {ECO:0000256|ARBA:ARBA00022473}; KW Differentiation {ECO:0000256|ARBA:ARBA00022782}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Spermatogenesis {ECO:0000256|ARBA:ARBA00022871}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00175}. FT DOMAIN 28..67 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT DOMAIN 90..109 FT /note="C2HC RNF-type" FT /evidence="ECO:0000259|PROSITE:PS51803" SQ SEQUENCE 227 AA; 25622 MW; C4CADC6D7F742369 CRC64; MAMFRSLDSG LKKRSGSESE RDISEFVCPV CLEIYDRPMA TQCGHTFCSS CLQECLRPQK PVCAVCRTAL TKWTASVGLE AHIQNSQGTC KGCRAQVYLS QMRSHTAACP KFQEYIMEGV STTAKSQPSR LSAVPNRFTF TCPYCGSQNL DQEGLVERCN AQHSRDPRQV VCPICASMPW GDPYYKSANF FQHLKMRHTF SYDTFVDYSA DEHAMMQEAL QRSMLDN //