A0A0R4I9Y1 · R213B_DANRE
- ProteinE3 ubiquitin-protein ligase rnf213-beta
- Genernf213b
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids5061 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
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. 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. Ubiquitination of LPS triggers cell-autonomous immunity, such as antibacterial autophagy, leading to degradation of the microbial invader (By similarity).
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. Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger. Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of proteins downstream of rspo3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression. Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (By similarity).
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. Also acts as an E3 ubiquitin-protein ligase via its RING-type zinc finger. Involved in the non-canonical Wnt signaling pathway in vascular development: acts by mediating ubiquitination and degradation of proteins downstream of rspo3, leading to inhibit the non-canonical Wnt signaling pathway and promoting vessel regression. Also has ATPase activity; ATPase activity is required for ubiquitination of LPS (By similarity).
Catalytic activity
- ATP + H2O = ADP + H+ + phosphateThis reaction proceeds in the forward direction.
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 1923-1928 | ATP (UniProtKB | ChEBI) | ||||
Sequence: AVGKSL | ||||||
Binding site | 2023 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 2074 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 2417 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 2492 | ATP (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 3957 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3960 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3972 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3974 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 3977 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3980 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3993 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3996 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4451 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4455 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 4462 | Nucleophile; for E3 ubiquitin-lipopolysaccharide ligase activity | ||||
Sequence: C | ||||||
Binding site | 4471 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 4474 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | lipid droplet | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | angiogenesis | |
Biological Process | defense response to bacterium | |
Biological Process | immune system process | |
Biological Process | lipid droplet formation | |
Biological Process | lipid ubiquitination | |
Biological Process | protein K63-linked ubiquitination | |
Biological Process | regulation of lipid metabolic process | |
Biological Process | xenophagy |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase rnf213-beta
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionA0A0R4I9Y1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435805 | 1-5061 | E3 ubiquitin-protein ligase rnf213-beta | |||
Sequence: MTRKRKSGKKGKPLAQKKEAQKRGGSTSSSTTQKEGAQKGDGSSSSSTTQKDGAQKRDDSTSSSSTAQKEEGQKSDGSTSSSTTNKEGAQKRDGSTSSRLQKKGPQKRKGSTSSSRAHSRSRSKSKQTSYPSQARSRSHGQHNISTTESGPLSKEAQTQTSASLLVDKDTQTETVGQASQQTQTEINGNTETAEVSQPPQLSHEDVEMEGTVQPRTKGSESDGEKEESVKRKKRKLSEIGEPAKETEDSTKLSHECEEKVGDNQKNEDTNKHYGGDSLKDLKSVTEEPKSYAAAAATGKTGKVSKEQTNQIEANQDSTMESKSTQRKPSPVRAPAGPPMLTFYIYAVLDKRFRFNEQYDSLFLDYGNGNIKLQMKHFNIGKDGYLIEATFSVEDSAVRGGTIQYKYVVQQRQNQKSEIAVRYIEVPSYTTEKEFHLYEGYISCSSTVSITEWMMSLFHSEQKAVYKGWETSAHVLLDRIFLKWHPSNEESNMTFVQHLRSYKNAFESGFVEFPGNYTPFPIKVSELISAKLRMILKKESEALRTSESLDGVKSEALSVALSVFKVCCGCDVDLSLKDWGKLCQVVSECMGSFGEIQTTQTAPFINTVTGLMNLCAKKLITEVVLLVPVLHLLRNSEVNEAGPGSSMDEQRWTGLENISYQSFRERIRGLPDKRRMILKLIKDNLPMTKDNPKLLKSWLSLVAFEDVSEFVQLTGSFPELLIQSLMCRIIEAEKNTDANRTEKNLEVTGKVLNLLLKSIKKDRERIMKTEQLKLILQCCCNVHKSVCKTARLVPQYKVTVLSFQLLLKMAEIVYDGFFKGGEQMKQHQNEVLSKLNIIQEDFRKWRVELLLKPLMQTTGFTYPREMELWNDLYGIESSIPGVTERWKGFLDHDLRRRISQISDTDKIVVYVLVTSAKAVENSHANIQSCLKELCEAAIKNQCQSKKEGTLLCHLFSKTISWPVLSSIIVESAACFGEDHKGRLLDPQSAINFFLSQDKWNEWKLEDGASQLIAESQSFLGRLIQTLCQGSIPLGHLKTIFKYKTQFQKLYNQYKNNNKEMNVSISVSDLLSQREDDLKAFEQQKGYMTNLINMLGKISDVINVPELSSLEEIAKTNVQEVALDKLVEVETYFSKDDLKKNNTRRVLFYSDDQQVQDMAREMHDVNSSNLILSFWQEKAKDYFMAGPELLSLDLTEIYEDIWTPCLTKFLNFGNRIAVGQACFKEVEEALVGCGETGEGDRLKKEFMLMATMLDGHNENWPEQRLKQIREYRCLYDAAESAEVILKLKDRLGLQGDFSHIHSLTLVRDDSFKQNTLGSLSEDLIKARQKLADVERRHTACLEAFLKSDTLIKWIKAEIPSLKELKVFMELATISAGENDADIDRLASFETAVMGYAPLLYSLPQNVGFEEFFDYAKQVLDTLNKDEKLGDKLVDSNRWLDWLKGLRETHGSVEQSSLSLASAINTGGVYHVGWPDDFNGKTGLDNIFYVKVTKNNEEKTYRLNELLELQNKLMLMSSKGEKGKEQVIKFTQVFEGIQRMGRILLQLHRSGNMLFRNWAAEITCNHQNQPCIQVKFPLLSKCIVYQGEVEEELQKLSRSLEDFHKDWCNHLTKMRSQYYPLNHYSSEQIVYLCEWINSINIKKKPVPQQVWHLLTPIKPDCMLNDIKEAFEIATEPQSILQEDTAEELGPNSDFDLPLSFSLLDVSTECLEDLWKQFKENMSGFLTHHVDVETLGRFLSNLSNMNQLHIKRKIPSFLQEGRPNLVQCPAAELMSTTLSFYMESPENPLPTTDEVLMCQEETTEEEVEIFLRRCLGGAASNHKKIYTLVNPGSMSYDVSVALVEYFETQEVCAGPYYRLVMVCPVNQDRYIPSFFSNYKVQTGITISAERSQKYIRHHFKISYELATHSSVYPERLSVWMIASKRPAVGKSLYVRRLFEKFKGEFPRATLLTIRLIDPYIDMDGFVQTLSERLAPLRQQDPVLLHIDVAAVCHGLEEFLFKLLILECISDSKGTIWRRNKAHLVVIETLQRGHKTQTKMEPSHGFLNTLPTIFCRPPKDIKEIMKTNESFRSLDPLMDKEEFESEDIQRPYQYLRRFNRSMNLDRFTYQAHSVEGDPVDCLHHLLSNYGLKDPSWAELKHFTWFLNLQLKDCEKSLFCDSDFCGETLSGFKDFIVKFMIHMARDFASPSIDISDQSPSFFSKNEDEEEILSFRKRWENESHPYIFFNADHVSMSFLGFHVKQNGTILNAVDSKSGKVLMRNVMTQELFSDIQRQMINLSKDFDDLTREDKLQKMSFVVGAEKGCEKGKFDPDPTYELTTDNVMKMLAIHMRFRCEIPVIIMGETGCGKTRLVRFLCDLQREGRDVENMKLVKVHGGTTSETIYKKVREAEELAQKNRQKYKLDTVLFFDEANTTEAIFAIKEVLCDKTVKGYPLKKNSGLKIIAACNPYRRHTTKMVDRLERAGLGYRVKAEETEDRLGKVPMRQLVYRVHPLPPSMVPLVWDFGQLSDSTELSYIRQIVKKKMRDHRLPLSCQNVITNVLAASQKYMRNQADECSFVSLRDVERSMGVLLWFYNHRDIFFPSQDFPRFENVQMVLKCLVLAVGVCYYPSLENKRPYLATISKCFPDQFNSEESLEQEIASCQDFLLKNIQTRETIAKNMALKENVFLMVVCIELRIPLFLVGKPGSSKSLAKTVIADAMQRQASHCDLFKKLKEVHMVSFQCSPHSSPEGIIGTFRNCARFQKDKNLDEYVSVVVLDEIGLAEDSPQMPLKTLHPLLEDGCIDSDNPESYMKVGFVGISNWALDPAKMNRGIFVSRWDPSEKDLVETAEGICSSSQPVLLKIKHLLSKLAKCFLSICKTDSEQFFGLRDYYGLIKMLFDTVKCSDQEPSDKELAEAVLRNFSGQRDGFDPLDYFKDIFQNIQNVQRPNTLNMIEQNLDHHIDKECRYLLLLTTNNAALYIIQHHIFSKENYTQKCPEIVFGSGFPKDQEYAQICRNVSRIKACMETGRTVILLNLLNLYESLYDALNQYYVYFSGQQYVDLGLGSHRVKCRVHRDFRLVVVEDQEKVYKKFPVPLKNRLEKHKVDRSTDLAPWQHRVLEKLKKWAREFSKIQHSDSSEANFSVTDAFVGFHGDACASALLQALKKIDKLHHNKEENREESEAHHIDREFTEFQEKVNKFPDEAQEDDASMEVDKVQDAEIDEEMETLEDDSDLVKMVEGPVFVETRDKIESNKTMDEEEVYEIAKSFLLNCSTPDSVLRLKYSEFGNQETEELQKMYFHLQTHQSLRDLLNNHLNKTNQDKNRFLEVTTFSNLLTGADVRNLGPALGLSTERFLLLSLHQFDTEASFCNKIQSFLRESGPSVHILLIQMDMEESLCKNELIASAKYCTMNEILHLKSDECNIYTVFITKLSRIGEQCTSITGDKYIGFQGGVWLSAHIDDLRDSDDLCLNLKAFCGIPISQLISQTIESDVKESDEMNTNRQQSEKGDSVHLHSLSLLRSCTQKAVSLLRDTDEKTSRSMERMNILLGLLACDPGRTGARFQQVLLKRLVFALIQKEELIPNAKDWVYKVAKNHEALQECGTLRHTLWRYLQDFLTPVLARILEVIDRDCNLYQLYGEGLSEGLTQFWLDIFEDQQLLDLIPSQNTRAPDQEINVQCHLFVGEVEQPCAAPYSWLIKTYCQSLWEESEFVRSSEQDIKARIQQFVSAVSGSRLGSYIQKLSDVENVELGQRYLTDYVLLAFKVNSEDEHWVLQSAVLGCVFTLQTMMSVSPELSPSWIHAAAQIYNPRMDTLSHVLQLNPQLVSLIQQERPKRESPDMCEDILAVGICVEETKLLPVTSLTECLTFLQRVEQLQPCIERVLSPDYSALCSPGCLKYLETIQSVWQGILLVAVFIEKVVIKMKKGDERIIALTLKHCSQLHGLVEGSPDFRSKDNLQQIIRILNDYHEESISSELRYGVKCRVCLMELSEPFALPCEHVFCRSCLRRSMEREEAQHCPVCREPLSNNYQPTVSTTLNYSFALKQHKEIIKCCNTFFLEVVSRFCLTDDQDPPDDLVELLFSLLISAQGDVYKTRELTPFLECVDQSPVVRSVLPKLLMQYSLKQVKKHIQSYLEDLENKLLDKEDRTELYRLFVNCFQDTLLCSDSNGDHKHLRENTNFLSRLARKQTPSRQNDPAEFLMSMARLRMCLDSAAYILSKAICQKNNFVEAEFKFMEQVKAVCDYCDNDWYRVYLLRALNRQAGMDFLQALINSTDYEWIFPAEMMRLHRLIPAEVDRFLCCGQSYRALRDGVGESTQVGTTDGLKEALQASVGSSPLKNALLTLAVFRQVTCHFMSPERTLHPQEQQISILEKVIRDNMSGHAREFCTALLSNHIGGPGSNLRLGTGVPAQRRPVLELLVHACTVFYSGNRLISPLFNIASQPQNMTGAFLPTMPDDHTSEAKQWLSEKKLKMYFCSNSHACFVGECGRPMAKSKCATCGVEIGGEGHIPVPGFTEAYGDYDRTRPGHILGQARTRSEAPNRKLTLAQSCVLRLCLHLAMLQGLIHYQQGIRNMIHPEVSDVYQFLWQHLEKDMEVLGKTLTLNIDDSAIVIHLIFSRFLQTTPVANVDLSTRKSREQWEITVCKTAISPVLQNLDRELNNAQDLIAADNRLSNSPLVKVLRGDPQRMLQLPANCPTEHSAFWSPSSVLAVESISQQIDQAQAPLLTLFVQKVHYIRQLDCLPALAALLSDLIKVLPPGSETQNHTIASLLHCIPAGHQKKLMSERVEIYMKVWNQLRMEISSNASLGLDSTHCEKDITSESSGQFLFPSRKGAGSCLHAVIDVLSETHNSLVREARKLCQQTDSDYKVPLAVLSKSQLALCHPEREFLPLVLANCHYTLEKGQQTVSSYDHQGIERELSRRFFAGKPRIQTDTEKYLRRHHQNFTEVLNEVRAKIPQEMFWNPKQIHQAFSTNYHSTNRHKGLSRFYPDQPLSITTVPDLVIPRRPVGFQTQERHTLTPPGSHLTALNSLPAFSFCAPPISIRSTMELHLEEKDITSFPGLDSLPEELTWAKAAEIWRLAVQFKH |
Proteomic databases
Interaction
Protein-protein interaction databases
Family & Domains
Features
Showing features for region, compositional bias, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-334 | Disordered | ||||
Sequence: MTRKRKSGKKGKPLAQKKEAQKRGGSTSSSTTQKEGAQKGDGSSSSSTTQKDGAQKRDDSTSSSSTAQKEEGQKSDGSTSSSTTNKEGAQKRDGSTSSRLQKKGPQKRKGSTSSSRAHSRSRSKSKQTSYPSQARSRSHGQHNISTTESGPLSKEAQTQTSASLLVDKDTQTETVGQASQQTQTEINGNTETAEVSQPPQLSHEDVEMEGTVQPRTKGSESDGEKEESVKRKKRKLSEIGEPAKETEDSTKLSHECEEKVGDNQKNEDTNKHYGGDSLKDLKSVTEEPKSYAAAAATGKTGKVSKEQTNQIEANQDSTMESKSTQRKPSPVRAP | ||||||
Compositional bias | 21-51 | Polar residues | ||||
Sequence: QKRGGSTSSSTTQKEGAQKGDGSSSSSTTQK | ||||||
Compositional bias | 59-91 | Polar residues | ||||
Sequence: DSTSSSSTAQKEEGQKSDGSTSSSTTNKEGAQK | ||||||
Compositional bias | 124-199 | Polar residues | ||||
Sequence: KSKQTSYPSQARSRSHGQHNISTTESGPLSKEAQTQTSASLLVDKDTQTETVGQASQQTQTEINGNTETAEVSQPP | ||||||
Compositional bias | 218-286 | Basic and acidic residues | ||||
Sequence: GSESDGEKEESVKRKKRKLSEIGEPAKETEDSTKLSHECEEKVGDNQKNEDTNKHYGGDSLKDLKSVTE | ||||||
Compositional bias | 301-328 | Polar residues | ||||
Sequence: GKVSKEQTNQIEANQDSTMESKSTQRKP | ||||||
Zinc finger | 3957-3997 | RING-type | ||||
Sequence: CRVCLMELSEPFALPCEHVFCRSCLRRSMEREEAQHCPVCR | ||||||
Zinc finger | 4429-4501 | RZ-type | ||||
Sequence: MPDDHTSEAKQWLSEKKLKMYFCSNSHACFVGECGRPMAKSKCATCGVEIGGEGHIPVPGFTEAYGDYDRTRP |
Domain
Composed of an N-terminal stalk, a dynein-like core comprised of two catalytically active and four inactive ATPase domains, and a C-terminal E3 module. The ATPase regions do not generate movement but rather act like an intricate molecular 'switch'.
The RING-type zinc finger domain is required for the ubiquitin-protein ligase activity.
The RZ-type (RNF213-ZNFX1) zinc-finger is required for the ubiquitination of the lipid A moiety of bacterial lipopolysaccharide (LPS).
Sequence similarities
Belongs to the AAA ATPase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length5,061
- Mass (Da)577,550
- Last updated2016-01-20 v1
- Checksum11C60D242B171DE7
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 21-51 | Polar residues | ||||
Sequence: QKRGGSTSSSTTQKEGAQKGDGSSSSSTTQK | ||||||
Compositional bias | 59-91 | Polar residues | ||||
Sequence: DSTSSSSTAQKEEGQKSDGSTSSSTTNKEGAQK | ||||||
Compositional bias | 124-199 | Polar residues | ||||
Sequence: KSKQTSYPSQARSRSHGQHNISTTESGPLSKEAQTQTSASLLVDKDTQTETVGQASQQTQTEINGNTETAEVSQPP | ||||||
Compositional bias | 218-286 | Basic and acidic residues | ||||
Sequence: GSESDGEKEESVKRKKRKLSEIGEPAKETEDSTKLSHECEEKVGDNQKNEDTNKHYGGDSLKDLKSVTE | ||||||
Compositional bias | 301-328 | Polar residues | ||||
Sequence: GKVSKEQTNQIEANQDSTMESKSTQRKP |
Keywords
- Technical term