ID A0A182R2I4_ANOFN Unreviewed; 810 AA. AC A0A182R2I4; DT 07-SEP-2016, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 2. DT 27-NOV-2024, entry version 39. DE SubName: Full=RING-type domain-containing protein {ECO:0000313|EnsemblMetazoa:AFUN000375-PA}; OS Anopheles funestus (African malaria mosquito). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae; OC Anophelinae; Anopheles. OX NCBI_TaxID=62324 {ECO:0000313|EnsemblMetazoa:AFUN000375-PA}; RN [1] {ECO:0000313|EnsemblMetazoa:AFUN000375-PA} RP IDENTIFICATION. RC STRAIN=FUMOZ {ECO:0000313|EnsemblMetazoa:AFUN000375-PA}; RG EnsemblMetazoa; RL Submitted (MAY-2020) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202}; CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. 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 AlphaFoldDB; A0A182R2I4; -. DR STRING; 62324.A0A182R2I4; -. DR EnsemblMetazoa; AFUN000375-RA; AFUN000375-PA; AFUN000375. DR VEuPathDB; VectorBase:AFUN000375; -. DR VEuPathDB; VectorBase:AFUN2_001511; -. DR OrthoDB; 383715at2759; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:TreeGrafter. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:2001271; P:negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis; IEA:TreeGrafter. DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:TreeGrafter. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:TreeGrafter. DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:TreeGrafter. DR CDD; cd15750; FYVE_CARP; 1. DR CDD; cd16500; RING-HC_CARP; 1. DR FunFam; 3.30.40.10:FF:000110; E3 ubiquitin-protein ligase RNF34 isoform X1; 1. DR Gene3D; 1.10.720.140; -; 1. DR Gene3D; 1.10.720.30; SAP domain; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR051728; RING-FYVE_E3_ubiquitin-ligase. DR InterPro; IPR055111; RNF34L-like_HeH. DR InterPro; IPR036361; SAP_dom_sf. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR14879; CASPASE REGULATOR, RING FINGER DOMAIN-CONTAINING; 1. DR PANTHER; PTHR14879:SF5; RING-TYPE DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF22968; RNF34L-like_3rd; 1. DR Pfam; PF13920; zf-C3HC4_3; 1. DR SMART; SM00184; RING; 2. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF68906; SAP domain; 2. DR PROSITE; PS50089; ZF_RING_2; 1. PE 4: Predicted; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Zinc {ECO:0000256|ARBA:ARBA00022833}; KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE- KW ProRule:PRU00175}. FT DOMAIN 763..798 FT /note="RING-type" FT /evidence="ECO:0000259|PROSITE:PS50089" FT REGION 96..121 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 180..264 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 318..386 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 423..482 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 180..194 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 207..221 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 228..259 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 334..380 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 423..471 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 810 AA; 87868 MW; A77A256A2BE593F2 CRC64; MPCEKCNVKF GIITRKKSCY ECHRLFCRNC LTKRQERFLC PNCTIFTKRP LSRIDLAQLK VKDLIFYLQS KHISTSGCVE KDDLINLVIA HVNSGGSSPR TPGSFSGTSS NAESASGGSS RYGSFYRNGT KNCTNTFDQI KNTCQNLFST FSDKLNGDLP ETGRPSTGFA TQEEQRHIFT QPRFGSNNVY HSVDPSVRPN AGASNFPLHS EGDNNQRTDA QYNGEQEERP VHFSSGSSGT TSGADSSAAS SSFSSPSRDA CSPLLGDRQQ LTANGQTQAM LDDRIESILA RETGGTGCEC CTDDEDEERT GIAIRMENTL AAKSEEDMPP RSKQSRRSLS QSNLLSPQMA GPSADTSAAT TKVASRSQTP SSSFDDLLAD AEGSSSNADH AIAQDTLAVT TDTEALATTV ASIDDTEQWQ IINTSDTNGG GTLEAATNSE LPMTDATNEA STTNEDEASS DSISNSVELK SKPPSMVPVL GHSPSVGSAT TIITRRRSDS YLLAECYATL RQCSVGTGRM DVPQSPLIQR ASTTRLLQTV DAQSPAIASG GILSSDAMPT TSHPINHGTA AHGMCFRCGK RRNGIRRQLK KFRKQLDAAT VTEGEKRRQL EAFLNYLERR SKGSFELTDS ESITEEASIS MGDEACGVAA SALDGRGTIT AGVDEQHTLS YPNSSEETPI CTNLYSSGNQ DLVNMKQIKL SDIKESADLD VLSVKQLKGI LMVNRVDFKG CCEKAELRER VLRLWRDYKS IPSIEKLPSD DLCKICMDAP IECVILECGH MTTCTACGKV LSECPICRQY IVRVVRFFRA //