Rnf213
entrez
672511
canonical
uniprot
E9Q555
canonical
ensembl
ENSMUSG00000070327
resolver
ensp
ENSMUSP00000091429
resolver
genesymbol
Rnf213
resolver
genesymbol_syn
Mystr
resolver
uniprot
F7A6H4
resolver
uniprot
Q8BVK6
resolver
uniprot_entry
RN213_MOUSE
resolver
uniprot_sec
F7A6H4
resolver
uniprot_sec
Q8BVK6
resolver
amino_acid_sequence
MECPQCGHVSSEKAPKFCSECGQKLPSAATVQGDLKNDNTLVVSSTPEGKTEQGAVLREEEVLLSSTDPGKELEKPEESDSNASWTTQMSKKEKRRRKRQGTISSSEAPSSGLWSLDMPPSPGSHNSALPQNQAQQGGAASQPGHPLDTENMPMEDGFVHTEGSGSPLQGQAAERTDAQSNLAPSDLAEVKDLNTSKPSVDKGLPLDGGPALSAFKGHPKMTDASQKAPLPESKGETSGQEKKVPPIDAAASPVKTAGKETGEDVRKPKPSPVSPVASKHGDQEAELKGKLATPVRKSNEGGNTQPEDQRKPGEGRNFAAAVKTQQAAAPQQAAAPEPTSAFNPRDTVTVYFHAIVSRHFGFNPEEHKVYVRGGEGLGQKGWTDACEMYCTQDLHDLGSLVEGKMDIPRQSLDKPIPYKYVIHRGGSSKDTVEYEFIYEQAQKKGEHVNRCLRVVSTSLGNGDWHQYDDIICMRSTGFFQQAKNRILDSTRKELLKGKKQAAVVMLDRIFSVLQPWSDINLQSFMTQFLQFYSVVREPMIHDGRARKWTSLQYEEKEVWTNLWEHVKKQMAPFLEGKSGESLPADCPVRSKLTLGLSILFMVEAAEFTVPKKDLDSLCYLLIPSAGSPEALHSDLSPVLRIRQRWRIYLTNLCLRCIDERCDRWLGILPLLHTCMQKSPPKKNSKSQPEDTWAGLEGISFSEFRDKAPTRSQPLQFMQSKMALLRVDEYLFRSWLSVVPLESLSSYLENSIDYLSDVPVRVLDCLQGISYRLPGLRKISNQNMKKDVENVFKMLMHLVDIYQHRIFGENLLQIYLTECLTLHETVCNITANHQFFEIPALSAELICKLLELSPPGHTDEGLPEKSYEDLVTSTLQEALATTRNWLRSLFKSRMLSISSAYVRLTYSEEMAVWRRLVEIGFPEKHGWKGSLLGDMEGRLKQEPPRLQISFFCSSQCRDGGLHDSVSRSFEKCVIEAVSSACQSQTSVLEGLSCQDLQKFGTLLSAVITKSWPVHNGEPVFDVDEIFKYLLKWPDVRQLFELCGTNEKIIDNITEEGRQLMATAESVFQKVAGELENGTIVVGQLELILEHQSQFLDIWNLNRRRLPSQEKACDVRSLLKRRRDDLLFLKQEKRYVESLLRQLGRVKHLVQVDFGNIEIIHSQDLSNKKLNEAVIKLPNSSSYKRETHYCLSPDIREMASKLDSLKDSHIFQDFWQETAESLNTLDKDPRELKVSLPEVLEYLYNPCYDNFYTLYENLKSGKITFAEVDAIFKDFVDKYDELKNDLKFMCTMNPQDQKGWISERVGQIKEYHTLHQAVSSAKVILQVRRALGVTGDFSVLNPLLNFADSFEDFGNEKLDQISPQFIKAKQLLQDISEPRQRCLEELARQTELVAWLHKALEDINELKVFVDLASISAGENDIDVDRVACFHDAVQGYASLLYKMDERTNFSDFMNHLQELWRALDNDQHLPDKLKDSARNLEWLKTVKESHGSVELSSLSLATAINSRGVYVIEAPKDGQKISPDTVLRLLLPDGHGYPEALRTYSTEELKELLNKLMLMSGKKDHNSNTEVEKFSEVFSNMQRLVHVFIKLHCAGNMLFRTWTAKVYCCPDGGIFMNFGLELLSQLTEKGDVIQLLGALCRQMEDFLDNWKTVVAQKRAEHFYLNFYTAEQLVYLSSELRKPRPSEAALMMLSFIKGKCTVQDLVQATSACESKADRYCLREVMKKLPQQLLSEPSLMGKLQVIMMQSLVYMSAFLPHCLDLDALGRCLAHLATMGGTPVERPLPKGLQAGQPNLILCGHSEVLPAALAIYMQAPRQPLPTFDEVLLCTPATTIEEVELLLRRCLTSGSQGHKVYSLLFADQLSYEVGCQAEEFFQSLCTRAHREDYQLVILCDAAREHCYIPSTFSQYKVPLVPQAPLPNIQAYLQSHYQVPKRLLSAATVFRDGLCVGIVTSERAGVGKSLYVNTLHTKLKAKLRDETVPLKIIRLTEPHLDENQVLSALLPFLKEKYQKMPVIFHIDISTSVQTGIPIFLFKLLILQYLMDINGKIWRRSPGHLYLVEIPQGLSVQPKRSSKLNARAPLFKFLDLFPKVTCRPPKEVIDMELTPERSHTDPAMDPVEFCSEAFQRPYQYLKRFHQQQNLDTFQYEKGSVEGSPEECLQHFLIYCGLINPSWSELRNFAWFLNCQLKDCEASIFCKSAFTGDTLRGFKNFVVTFMILMARDFATPTLHTSDQSPGRQSVTIGEVVEEDLAPFSLRKRWESEPHPYVFFNGDHMTMTFIGFHLETNNNGYVDAINPSNGKVIKKDVMTKELFDGLRLQRVPFNIDFDNLPRYEKLERLCLALGIEWPIDPDETYELTTDNMLKILAIEMRFRCGIPVIIMGETGCGKTRLIKFLSDLKRGSVEAETMKLVKVHGGTTPSMIYSKVKEAERTAFSNKAQHKLDTILFFDEANTTEAVSCIKEILCDRTVDGEHLHEDSGLHIIAACNPYRKHSQEMILRLESAGLGYRVSAEETADRLGSIPLRQLVYRVHALPPSLIPLVWDFGQLNDSAEKLYIQQIVQRLVDSVSVNPSETCVIADVLSASQMFMRKRENECGFVSLRDVERCVKVFRWFHDHSDMLLKELDKFLHESSDSTHTFERDPVLWSLVMAIGVCYHASLEEKASYRTAIARCFPKPYNSSRAILDEVTHVQDLFLRGAPIRTNIARNLALKENVFMMVICIELKIPLFLVGKPGSSKSLAKIIVADAMQGQAAFSELFRCLKQVHLVSFQCSPHSTPQGIISTFKQCARFQQGKDLGQYVSVVVLDEVGLAEDSPKMPLKTLHPLLEDGCIEDDPAPYKKVGFVGISNWALDPAKMNRGIFVSRGSPNEKELIESAEGICSSDRLVQDKIRGYFAPFAKAYETVCQKQDKEFFGLRDYYSLIKMVFAKAKASKRGLSPQDITHAVLRNFSGKDNIQALSIFTASLPEARYKEEVSTVELIKQNIYPGPQASSRGLDGAESRYLLVLTRNYVALQILQQTFFEGQQPEIIFGSSFPQDQEYTQICRNINRVKICMETGKMVVLLNLQNLYESLYDALNQYYVYLGGQKYVDLGLGTHRVKCRVHTAFRLIVIEEKDVVYKQFPVPLINRLEKHYLDMNTVLQPWQKSIVQELQQWAHEFADVKADQFIARHKYSPADVFIGYHSDACASVVLQAVERQGCRDLTEELYRKVSEEARSILLDCATPDAVVRLSGSSLGSFTAKQLSQEYYYAQQHNSFVDFLQAHLRMTHHECRAVFTEITTFSRLLTGNDCDVLASELRGLASKPVVLSLQQYDTEYSFLKDVRSWLTNPGKRKVLVIQADFDDGTRSAQLVASAKYTAINEINKTQGTKDFVFVYFVTKLSRMGSGTSYVGFHGGLWRSVHIDDLRRSTIMASDVTKLQNVTISQLFKPEDKPEQEEMEIETSQSKELAEEQMEVEDSEEMKKASDPRSCDCSQFLDTTRLVQSCVQGAVGMLRDQNESCARNMRRVTILLDLLNEDNTRNASFLRESKMRLHVLLNKQEENQVRSLKEWVTREAANQDALQEAGTFRHTLWKRVQDVVTPILASMIAHIDRDGNLELLAQPDSPAWVQDLWMFIYSDIKFLNISLVLNNTRSNSEMSFILVQSHMNLLKDAYNAVPFSWRIRDYLEELWVQAQYITDTEGLSKKFVEIFQKTPLGVFLAQFPVAQQQKLLQSYLKDFLLLTMKVSSREELMFLQMALWSCLRELQEASGTPDETYKFPLSLPWVHLAFQHFRTRLQNFSRILTIHPQVLSSLSQAAEKHSLAGCEMTLDAFAAMACAEMLKGDLLKPSPKAWLQLVKNLSTPLELVCSEGYLCDSGSMTRSVIQEVRALWNRIFSIALFVEHVLLGTESHIPELSPLVTTYVSLLDKCLEEDSNLKTCRPFVAVMTTLCDCKDKASKKFSRFGIQPCFICHGDAQDPVCLPCDHVYCLRCIQTWLIPGQMMCPYCLTDLPDKFSPTVSQDHRKAIEKHAQFRHMCNSFFVDLVSTMCFKDNTPPEKSVIDTLLSLLFVQKELLRDASQKHREHTKSLSPFDDVVDQTPVIRSVLLKLLLKYSFHEVKDYIQNYLTQLEKKAFLTEDKTELYLLFISCLEDSVHQKTSAGCRNLEQVLREEGHFLRTYSPGLQGQEPVRIASVEYLQEVARVRLCLDLAADFLSELQEGSELAEDKRRFLKHVEEFCTRVNNDWHRVYLVRKLSSQRGMEFVQSFSKQGHPCQWVFPRKVIAQQKDHVSLMDRYLVHGNEYKAVRDATAKAVLECKTLDIGNALMACRSPKPQQTAYLLLALYTEVAALYRSPNGSLHPEAKQLEAVNKFIKESKILSDPNIRCFARSLVDNTLPLLKIRSANSILKGTVTEMAVHVATILLCGHNQILKPLRNLAFYPVNMANAFLPTMPEDLLVHARTWRGLENVTWYTCPRGHPCSVGECGRPMQESTCLDCGLPVGGLNHTPHEGFSAIRNNEDRTQTGHVLGSPQSSGVAEVSDRGQSPVVFILTRLLTHLAMLVGATHNPQALTVIIKPWVQDPQGFLQQHIQRDLEQLTKMLGRSADETIHVVHLILSSLLRVQSHGVLNFNAELSTKGCRNNWEKHFETLLLRELKHLDKNLPAINALISQDERISSNPVTKIIYGDPATFLPHLPQKSIIHCSKIWSCRRKITVEYLQHIVEQKNGKETVPVLWHFLQKEAELRLVKFLPEILALQRDLVKQFQNVSRVEYSSIRGFIHSHSSDGLRKLLHDRITIFLSTWNALRRSLETNGEIKLPKDYCCSDLDLDAEFEVILPRRQGLGLCGTALVSYLISLHNNMVYTVQKFSNEDNSYSVDISEVADLHVISYEVERDLNPLILSNCQYQVQQGGETSQEFDLEKIQRQISSRFLQGKPRLTLKGIPTLVYRRDWNYEHLFMDIKNKMAQSSLPNLAISTISGQLQSYSDACEALSIIEITLGFLSTAGGDPGMDLNVYIEEVLRMCDQTAQVLKAFSRCQLRHIIALWQFLSAHKSEQRLRLNKELFREIDVQYKEELSTQHQRLLGTFLNEAGLDAFLLELHEMIVLKLKGPRAANSFNPNWSLKDTLVSYMETKDSDILSEVESQFPEEILMSSCISVWKIAATRKWDRQSR
uniprot
proteins
ec_number
2.3.2.-
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
ec_number
3.6.4.-
uniprot
proteins
function
FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination of both proteins and lipids, and which is involved in various processes, such as lipid metabolism, angiogenesis and cell-autonomous immunity (PubMed:32573437). Acts as a key immune sensor by catalyzing ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS) via its RZ-type zinc-finger: restricts the proliferation of cytosolic bacteria, such as Salmonella, by generating the bacterial ubiquitin coat through the ubiquitination of LPS (PubMed:34012115). Also acts indirectly by mediating the recruitment of the LUBAC complex, which conjugates linear polyubiquitin chains (By similarity). Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (By similarity). Also functions as an intracellular sensor for ISGylated proteins: upon type I interferon stimulation, undergoes ISGylation and oligomerizes on lipid droplets to form a binding platform for ISG15-modified substrate proteins, thereby acting as a broad-spectrum antimicrobial effector. Restricts intracellular bacterial pathogens in an ISG15-dependent manner by decorating the bacterial surface with ubiquitin to promote autophagic clearance (PubMed:34599178). Involved in lipid metabolism by regulating fat storage and lipid droplet formation; act by inhibiting the lipolytic process (By similarity). Also regulates lipotoxicity by inhibiting desaturation of fatty acids (By similarity). Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger: mediates 'Lys-63'-linked ubiquitination of target proteins (By similarity). Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of FLNA and NFATC2 downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression (By similarity). Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (PubMed:32573437). {ECO:0000250|UniProtKB:Q63HN8, ECO:0000269|PubMed:32573437, ECO:0000269|PubMed:34012115, ECO:0000269|PubMed:34599178}.
uniprot
proteins
mass_dalton
584258
uniprot
proteins
mutagenesis
MUTAGEN 4753; /note="R->K: Knockin mice grow normally and do not show any visible phenotype. Slightly impaired angiogenesis. Does not affect ATPase or E3 ubiquitin ligase activities."; /evidence="ECO:0000269|PubMed:26126547, ECO:0000269|PubMed:26315378, ECO:0000269|PubMed:32573437
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000250|UniProtKB:Q63HN8}.
uniprot
proteins
post_translational_modification
PTM: ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation positively regulates oligomerization on lipid droplets. {ECO:0000269|PubMed:34599178}.
uniprot
proteins
protein_family
AAA ATPase family
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23410753
uniprot
proteins
pubmed
24440776
uniprot
proteins
pubmed
25383461
uniprot
proteins
pubmed
26126547
uniprot
proteins
pubmed
26315378
uniprot
proteins
pubmed
32573437
uniprot
proteins
pubmed
33420513
uniprot
proteins
pubmed
34012115
uniprot
proteins
pubmed
34599178
uniprot
proteins
sequence_length
5148
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet {ECO:0000250|UniProtKB:Q63HN8}.
uniprot
proteins