P11716 · RYR1_RABIT
- ProteinRyanodine receptor 1
- GeneRYR1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids5037 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Cytosolic calcium-activated calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (PubMed:10097181, PubMed:10388749, PubMed:12732639, PubMed:22036948, PubMed:26245150, PubMed:27662087, PubMed:3722165).
Repeated very high-level exercise increases the open probability of the channel and leads to Ca2+ leaking into the cytoplasm (By similarity).
Can also mediate the release of Ca2+ from intracellular stores in neurons, and may thereby promote prolonged Ca2+ signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity).
Repeated very high-level exercise increases the open probability of the channel and leads to Ca2+ leaking into the cytoplasm (By similarity).
Can also mediate the release of Ca2+ from intracellular stores in neurons, and may thereby promote prolonged Ca2+ signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity).
Miscellaneous
Coexpression of normal and mutant Thr-4897 RYR1 in a 1:1 ratio produces RYR1 channels with normal halothane and caffeine sensitivities, but maximal levels of Ca2+ release are reduced by 67%. Binding of [3H]ryanodine indicates that the heterozygous channel is activated by Ca2+ concentrations 4-fold lower than normal. Single-cell analysis of cotransfected cells shows a significantly increased resting cytoplasmic Ca2+ level and a significantly reduced luminal Ca2+ level. These data indicated a leaky channel, possibly caused by a reduction in the Ca2+ concentration required for channel activation.
Catalytic activity
- Ca2+(in) = Ca2+(out)
Activity regulation
The calcium release is activated by increased cytosolic calcium levels, by nitric oxyde (NO), caffeine and ATP (PubMed:12732639, PubMed:22036948, PubMed:26245150, PubMed:27662087).
Channel activity is modulated by the alkaloid ryanodine that binds to the open Ca-release channel with high affinity (PubMed:27662087).
At low concentrations, ryanodine maintains the channel in an open conformation (PubMed:27662087).
High ryanodine concentrations inhibit channel activity (PubMed:27662087).
Channel activity is regulated by calmodulin (CALM). Channel activity is inhibited by magnesium ions, possibly by competition for calcium binding sites (PubMed:12732639).
Channel activity is modulated by the alkaloid ryanodine that binds to the open Ca-release channel with high affinity (PubMed:27662087).
At low concentrations, ryanodine maintains the channel in an open conformation (PubMed:27662087).
High ryanodine concentrations inhibit channel activity (PubMed:27662087).
Channel activity is regulated by calmodulin (CALM). Channel activity is inhibited by magnesium ions, possibly by competition for calcium binding sites (PubMed:12732639).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 3893 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 3967 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 4211-4215 | ATP (UniProtKB | ChEBI) | ||||
Sequence: KESKR | ||||||
Binding site | 4716 | caffeine (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 4954-4959 | ATP (UniProtKB | ChEBI) | ||||
Sequence: METKCF | ||||||
Binding site | 4979-4985 | ATP (UniProtKB | ChEBI) | ||||
Sequence: TLEEHNL | ||||||
Binding site | 5001 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: T |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameRyanodine receptor 1
- Short namesRYR-1; RyR1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionP11716
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Sarcoplasmic reticulum membrane ; Multi-pass membrane protein
Note: The number of predicted transmembrane domains varies between orthologs, but the 3D-structures show the presence of six transmembrane regions. Both N-terminus and C-terminus are cytoplasmic.
Features
Showing features for topological domain, transmembrane, intramembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-4558 | Cytoplasmic | ||||
Sequence: MGDGGEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFTLEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSCCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLALTEDQGLVVVDACKAHTKATSFCFRVSKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAILHQEGHMDDALFLTRCQQEESQAARMIHSTAGLYNQFIKGLDSFSGKPRGSGPPAGPALPIEAVILSLQDLIGYFEPPSEELQHEEKQSKLRSLRNRQSLFQEEGMLSLVLNCIDRLNVYTTAAHFAEYAGEEAAESWKEIVNLLYELLASLIRGNRANCALFSTNLDWVVSKLDRLEASSGILEVLYCVLIESPEVLNIIQENHIKSIISLLDKHGRNHKVLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNLINYVTSIRPNIFVGRAEGSTQYGKWYFEVMVDEVVPFLTAQATHLRVGWALTEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLWTGHVARPVTSPGQHLLAPEDVVSCCLDLSVPSISFRINGCPVQGVFEAFNLDGLFFPVVSFSAGVKVRFLLGGRHGEFKFLPPPGYAPCHEAVLPRERLRLEPIKEYRREGPRGPHLVGPSRCLSHTDFVPCPVDTVQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVNFHSLPEPERNYNLQMSGETLKTLLALGCHVGMADEKAEDNLKKTKLPKTYMMSNGYKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVENQSRWDRVRIFRAEKSYTVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCMIDLTENTIIFTLNGEVLMSDSGSETAFREIEIGDGFLPVCSLGPGQVGHLNLGQDVSSLRFFAICGLQEGFEPFAINMQRPVTTWFSKSLPQFEPVPPEHPHYEVARMDGTVDTPPCLRLAHRTWGSQNSLVEMLFLRLSLPVQFHQHFRCTAGATPLAPPGLQPPAEDEARAAEPDPDYENLRRSAGGWGEAEGGKEGTAKEGTPGGTPQPGVEAQPVRAENEKDATTEKNKKRGFLFKAKKAAMMTQPPATPALPRLPHDVVPADNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMNFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGGDFVSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVIQFELGKQKNIMPLSAAMFLSERKNPAPQCPPRLEVQMLMPVSWSRMPNHFLQVETRRAGERLGWAVQCQDPLTMMALHIPEENRCMDILELSERLDLQRFHSHTLRLYRAVCALGNNRVAHALCSHVDQAQLLHALEDAHLPGPLRAGYYDLLISIHLESACRSRRSMLSEYIVPLTPETRAITLFPPGRKGGNARRHGLPGVGVTTSLRPPHHFSPPCFVAALPAAGVAEAPARLSPAIPLEALRDKALRMLGEAVRDGGQHARDPVGGSVEFQFVPVLKLVSTLLVMGIFGDEDVKQILKMIEPEVFTEEEEEEEEEEEEEEEEEEDEEEKEEDEEEEEKEDAEKEEEEAPEGEKEDLEEGLLQMKLPESVKLQMCNLLEYFCDQELQHRVESLAAFAERYVDKLQANQRSRYALLMRAFTMSAAETARRTREFRSPPQEQINMLLHFKDEADEEDCPLPEDIRQDLQDFHQDLLAHCGIQLEGEEEEPEEETSLSSRLRSLLETVRLVKKKEEKPEEELPAEEKKPQSLQELVSHMVVRWAQEDYVQSPELVRAMFSLLHRQYDGLGELLRALPRAYTISPSSVEDTMSLLECLGQIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGETKEIRFPKMVTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGIGLGMQGSTPLDVAAASVIDNNELALALQEQDLEKVVSYLAGCGLQSCPMLLAKGYPDIGWNPCGGERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALRGEGGSGLLAAIEEAIRISEDPARDGPGVRRDRRREHFGEEPPEENRVHLGHAIMSFYAALIDLLGRCAPEMHLIQAGKGEALRIRAILRSLVPLDDLVGIISLPLQIPTLGKDGALVQPKMSASFVPDHKASMVLFLDRVYGIENQDFLLHVLDVGFLPDMRAAASLDTATFSTTEMALALNRYLCLAVLPLITKCAPLFAGTEHRAIMVDSMLHTVYRLSRGRSLTKAQRDVIEDCLMALCRYIRPSMLQHLLRRLVFDVPILNEFAKMPLKLLTNHYERCWKYYCLPTGWANFGVTSEEELHLTRKLFWGIFDSLAHKKYDQELYRMAMPCLCAIAGALPPDYVDASYSSKAEKKATVDAEGNFDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENVDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLKAMIAWEWTIEKAREGEEERTEKKKTRKISQTAQTYDPREGYNPQPPDLSGVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGGTHPLLVPYDTLTAKEKARDREKAQELLKFLQMNGYAVTRGLKDMELDTSSIEKRFAFGFLQQLLRWMDISQEFIAHLEAVVSSGRVEKSPHEQEIKFFAKILLPLINQYFTNHCLYFLSTPAKVLGSGGHASNKEKEMITSLFCKLAALVRHRVSLFGTDAPAVVNCLHILARSLDARTVMKSGPEIVKAGLRSFFESASEDIEKMVENLRLGKVSQARTQVKGVGQNLTYTTVALLPVLTTLFQHIAQHQFGDDVILDDVQVSCYRTLCSIYSLGTTKNTYVEKLRPALGECLARLAAAMPVAFLEPQLNEYNACSVYTTKSPRERAILGLPNSVEEMCPDIPVLDRLMADIGGLAESGARYTEMPHVIEITLPMLCSYLPRWWERGPEAPPPALPAGAPPPCTAVTSDHLNSLLGNILRIIVNNLGIDEATWMKRLAVFAQPIVSRARPELLHSHFIPTIGRLRKRAGKVVAEEEQLRLEAKAEAEEGELLVRDEFSVLCRDLYALYPLLIRYVDNNRAHWLTEPNANAEELFRMVGEIFIYWSKSHNFKREEQNFVVQNEINNMSFLTADSKSKMAKAGDAQSGGSDQERTKKKRRGDRYSVQTSLIVATLKKMLPIGLNMCAPTDQDLIMLAKTRYALKDTDEEVREFLQNNLHLQGKVEGSPSLRWQMALYRGLPGREEDADDPEKIVRRVQEVSAVLYHLEQTEHPYKSKKAVWHKLLSKQRRRAVVACFRMTPLYNLPTHRACNMFLESYKAAWILTEDHSFEDRMIDDLSKAGEQEEEEEEVEEKKPDPLHQLVLHFSRTALTEKSKLDEDYLYMAYADIMAKSCHLEEGGENGEAEEEEVEVSFEEKEMEKQRLLYQQSRLHTRGAAEMVLQMISACKGETGAMVSSTLKLGISILNGGNAEVQQKMLDYLKDKKEVGFFQSIQALMQTCSVLDLNAFERQNKAEGLGMVNEDGTVINRQNGEKVMADDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISDFYWYYSGKDVIEEQGKRNFSKAMSVAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMMMKLAQDSSQIELLKELLDLQKDMVVMLLSLLEGNVVNGMIARQMVDMLVESSSNVEMILKFFDMFLKLKDIVGSEAFQDYVTDPRGLISKKDFQKAMDSQKQFTGPEIQFLLSCSEADENEMINFEEFANRFQEPARDIGFNVAVLLTNLSEHVPHDPRLRNFLELAESILEYFRPYLGRIEIMGASRRIERIYFEISETNRAQWEMPQVKESKRQFIFDVVNEGGEAEKMELFVSFCEDTIFEMQIAAQISEPEGEPEADEDEGMGEAAAEGAEEGAAGAEGAAGTVAAGATARLAAAAARALRGLSYRSLRRRVRRLRRLTAREAATALAALLWAVVARAGAAGAGAAAGALRLLWGSLFGGGLVEGAKKVTVTELLAGMPDPTSDEVHGEQPAGPGGDADGAGEGEGEGDAAEGDGDEEVAGHEAGPGGAEGVVAVADGGPFRPEGAGGLGDMGDTTPAEPPTPEGSPILKRKLGVDGEEEELVPEPEPEPEPEPEKADEENGEKEEVPEAPPEPPKKAPPSPPAKKEEAGGAGMEFWGELEVQRVKFLNYLSRN | ||||||
Transmembrane | 4559-4579 | Helical; Name=1 | ||||
Sequence: FYTLRFLALFLAFAINFILLF | ||||||
Topological domain | 4580-4640 | Lumenal | ||||
Sequence: YKVSDSPPGEDDMEGSAAGDLAGAGSGGGSGWGSGAGEEAEGDEDENMVYYFLEESTGYME | ||||||
Transmembrane | 4641-4661 | Helical; Name=2 | ||||
Sequence: PALWCLSLLHTLVAFLCIIGY | ||||||
Topological domain | 4662-4779 | Cytoplasmic | ||||
Sequence: NCLKVPLVIFKREKELARKLEFDGLYITEQPGDDDVKGQWDRLVLNTPSFPSNYWDKFVKRKVLDKHGDIFGRERIAELLGMDLASLEITAHNERKPDPPPGLLTWLMSIDVKYQIWK | ||||||
Transmembrane | 4780-4802 | Helical; Name=3 | ||||
Sequence: FGVIFTDNSFLYLGWYMVMSLLG | ||||||
Topological domain | 4803 | Lumenal | ||||
Sequence: H | ||||||
Transmembrane | 4804-4820 | Helical; Name=4 | ||||
Sequence: YNNFFFAAHLLDIAMGV | ||||||
Topological domain | 4821-4835 | Cytoplasmic | ||||
Sequence: KTLRTILSSVTHNGK | ||||||
Transmembrane | 4836-4856 | Helical; Name=5 | ||||
Sequence: QLVMTVGLLAVVVYLYTVVAF | ||||||
Topological domain | 4857-4879 | Lumenal | ||||
Sequence: NFFRKFYNKSEDEDEPDMKCDDM | ||||||
Intramembrane | 4880-4899 | Pore-forming | ||||
Sequence: MTCYLFHMYVGVRAGGGIGD | ||||||
Topological domain | 4900-4919 | Lumenal | ||||
Sequence: EIEDPAGDEYELYRVVFDIT | ||||||
Transmembrane | 4920-4940 | Helical; Name=6 | ||||
Sequence: FFFFVIVILLAIIQGLIIDAF | ||||||
Topological domain | 4941-5037 | Cytoplasmic | ||||
Sequence: GELRDQQEQVKEDMETKCFICGIGSDYFDTTPHGFETHTLEEHNLANYMFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLS |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 164 | Decreases threshold for channel activation by K+, caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg2+. | ||||
Sequence: R → C | ||||||
Mutagenesis | 342 | Decreases threshold for channel activation by K+, caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg2+. | ||||
Sequence: G → R | ||||||
Mutagenesis | 615 | Decreases threshold for channel activation by K+, caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg2+. | ||||
Sequence: R → C | ||||||
Mutagenesis | 674-675 | Loss of interaction with FKBP1A. | ||||
Sequence: FL → AA | ||||||
Mutagenesis | 760 | Impairs interaction with FKBP1A. | ||||
Sequence: N → D | ||||||
Mutagenesis | 1044 | Decreases protein stability. | ||||
Sequence: R → C | ||||||
Mutagenesis | 1050 | Decreases protein stability. | ||||
Sequence: G → S | ||||||
Mutagenesis | 1076 | Decreases protein stability. | ||||
Sequence: R → W | ||||||
Mutagenesis | 2163 | Decreases threshold for channel activation by K+, caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg2+. | ||||
Sequence: R → C | ||||||
Mutagenesis | 2168 | Decreases threshold for channel activation by K+, caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg2+. | ||||
Sequence: V → M | ||||||
Mutagenesis | 2458 | Decreases threshold for channel activation by K+, caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg2+. | ||||
Sequence: R → H | ||||||
Mutagenesis | 2461 | Impairs interaction with FKBP1A. | ||||
Sequence: V → G | ||||||
Mutagenesis | 2867 | Decreases protein stability. | ||||
Sequence: L → G | ||||||
Mutagenesis | 3635 | Abolishes S-nitrosocysteine formation. | ||||
Sequence: C → A | ||||||
Mutagenesis | 4825 | Decreases threshold for channel activation by K+, caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg2+. | ||||
Sequence: T → I | ||||||
Mutagenesis | 4897 | Loss of channel activation by halothane and caffeine due to Ca2+ store depletion, probably due to constant Ca2+ leakage through the mutant channel. | ||||
Sequence: I → T |
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000219360 | 1-5037 | Ryanodine receptor 1 | |||
Sequence: MGDGGEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFTLEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSCCEEGYVTGGHVLRLFHGHMDECLTISAADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRIRHVTTGRYLALTEDQGLVVVDACKAHTKATSFCFRVSKEKLDTAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAILHQEGHMDDALFLTRCQQEESQAARMIHSTAGLYNQFIKGLDSFSGKPRGSGPPAGPALPIEAVILSLQDLIGYFEPPSEELQHEEKQSKLRSLRNRQSLFQEEGMLSLVLNCIDRLNVYTTAAHFAEYAGEEAAESWKEIVNLLYELLASLIRGNRANCALFSTNLDWVVSKLDRLEASSGILEVLYCVLIESPEVLNIIQENHIKSIISLLDKHGRNHKVLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNLINYVTSIRPNIFVGRAEGSTQYGKWYFEVMVDEVVPFLTAQATHLRVGWALTEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLWTGHVARPVTSPGQHLLAPEDVVSCCLDLSVPSISFRINGCPVQGVFEAFNLDGLFFPVVSFSAGVKVRFLLGGRHGEFKFLPPPGYAPCHEAVLPRERLRLEPIKEYRREGPRGPHLVGPSRCLSHTDFVPCPVDTVQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVNFHSLPEPERNYNLQMSGETLKTLLALGCHVGMADEKAEDNLKKTKLPKTYMMSNGYKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVENQSRWDRVRIFRAEKSYTVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCMIDLTENTIIFTLNGEVLMSDSGSETAFREIEIGDGFLPVCSLGPGQVGHLNLGQDVSSLRFFAICGLQEGFEPFAINMQRPVTTWFSKSLPQFEPVPPEHPHYEVARMDGTVDTPPCLRLAHRTWGSQNSLVEMLFLRLSLPVQFHQHFRCTAGATPLAPPGLQPPAEDEARAAEPDPDYENLRRSAGGWGEAEGGKEGTAKEGTPGGTPQPGVEAQPVRAENEKDATTEKNKKRGFLFKAKKAAMMTQPPATPALPRLPHDVVPADNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMNFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGGDFVSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVIQFELGKQKNIMPLSAAMFLSERKNPAPQCPPRLEVQMLMPVSWSRMPNHFLQVETRRAGERLGWAVQCQDPLTMMALHIPEENRCMDILELSERLDLQRFHSHTLRLYRAVCALGNNRVAHALCSHVDQAQLLHALEDAHLPGPLRAGYYDLLISIHLESACRSRRSMLSEYIVPLTPETRAITLFPPGRKGGNARRHGLPGVGVTTSLRPPHHFSPPCFVAALPAAGVAEAPARLSPAIPLEALRDKALRMLGEAVRDGGQHARDPVGGSVEFQFVPVLKLVSTLLVMGIFGDEDVKQILKMIEPEVFTEEEEEEEEEEEEEEEEEEDEEEKEEDEEEEEKEDAEKEEEEAPEGEKEDLEEGLLQMKLPESVKLQMCNLLEYFCDQELQHRVESLAAFAERYVDKLQANQRSRYALLMRAFTMSAAETARRTREFRSPPQEQINMLLHFKDEADEEDCPLPEDIRQDLQDFHQDLLAHCGIQLEGEEEEPEEETSLSSRLRSLLETVRLVKKKEEKPEEELPAEEKKPQSLQELVSHMVVRWAQEDYVQSPELVRAMFSLLHRQYDGLGELLRALPRAYTISPSSVEDTMSLLECLGQIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGETKEIRFPKMVTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGIGLGMQGSTPLDVAAASVIDNNELALALQEQDLEKVVSYLAGCGLQSCPMLLAKGYPDIGWNPCGGERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALRGEGGSGLLAAIEEAIRISEDPARDGPGVRRDRRREHFGEEPPEENRVHLGHAIMSFYAALIDLLGRCAPEMHLIQAGKGEALRIRAILRSLVPLDDLVGIISLPLQIPTLGKDGALVQPKMSASFVPDHKASMVLFLDRVYGIENQDFLLHVLDVGFLPDMRAAASLDTATFSTTEMALALNRYLCLAVLPLITKCAPLFAGTEHRAIMVDSMLHTVYRLSRGRSLTKAQRDVIEDCLMALCRYIRPSMLQHLLRRLVFDVPILNEFAKMPLKLLTNHYERCWKYYCLPTGWANFGVTSEEELHLTRKLFWGIFDSLAHKKYDQELYRMAMPCLCAIAGALPPDYVDASYSSKAEKKATVDAEGNFDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENVDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLKAMIAWEWTIEKAREGEEERTEKKKTRKISQTAQTYDPREGYNPQPPDLSGVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGGTHPLLVPYDTLTAKEKARDREKAQELLKFLQMNGYAVTRGLKDMELDTSSIEKRFAFGFLQQLLRWMDISQEFIAHLEAVVSSGRVEKSPHEQEIKFFAKILLPLINQYFTNHCLYFLSTPAKVLGSGGHASNKEKEMITSLFCKLAALVRHRVSLFGTDAPAVVNCLHILARSLDARTVMKSGPEIVKAGLRSFFESASEDIEKMVENLRLGKVSQARTQVKGVGQNLTYTTVALLPVLTTLFQHIAQHQFGDDVILDDVQVSCYRTLCSIYSLGTTKNTYVEKLRPALGECLARLAAAMPVAFLEPQLNEYNACSVYTTKSPRERAILGLPNSVEEMCPDIPVLDRLMADIGGLAESGARYTEMPHVIEITLPMLCSYLPRWWERGPEAPPPALPAGAPPPCTAVTSDHLNSLLGNILRIIVNNLGIDEATWMKRLAVFAQPIVSRARPELLHSHFIPTIGRLRKRAGKVVAEEEQLRLEAKAEAEEGELLVRDEFSVLCRDLYALYPLLIRYVDNNRAHWLTEPNANAEELFRMVGEIFIYWSKSHNFKREEQNFVVQNEINNMSFLTADSKSKMAKAGDAQSGGSDQERTKKKRRGDRYSVQTSLIVATLKKMLPIGLNMCAPTDQDLIMLAKTRYALKDTDEEVREFLQNNLHLQGKVEGSPSLRWQMALYRGLPGREEDADDPEKIVRRVQEVSAVLYHLEQTEHPYKSKKAVWHKLLSKQRRRAVVACFRMTPLYNLPTHRACNMFLESYKAAWILTEDHSFEDRMIDDLSKAGEQEEEEEEVEEKKPDPLHQLVLHFSRTALTEKSKLDEDYLYMAYADIMAKSCHLEEGGENGEAEEEEVEVSFEEKEMEKQRLLYQQSRLHTRGAAEMVLQMISACKGETGAMVSSTLKLGISILNGGNAEVQQKMLDYLKDKKEVGFFQSIQALMQTCSVLDLNAFERQNKAEGLGMVNEDGTVINRQNGEKVMADDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISDFYWYYSGKDVIEEQGKRNFSKAMSVAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMMMKLAQDSSQIELLKELLDLQKDMVVMLLSLLEGNVVNGMIARQMVDMLVESSSNVEMILKFFDMFLKLKDIVGSEAFQDYVTDPRGLISKKDFQKAMDSQKQFTGPEIQFLLSCSEADENEMINFEEFANRFQEPARDIGFNVAVLLTNLSEHVPHDPRLRNFLELAESILEYFRPYLGRIEIMGASRRIERIYFEISETNRAQWEMPQVKESKRQFIFDVVNEGGEAEKMELFVSFCEDTIFEMQIAAQISEPEGEPEADEDEGMGEAAAEGAEEGAAGAEGAAGTVAAGATARLAAAAARALRGLSYRSLRRRVRRLRRLTAREAATALAALLWAVVARAGAAGAGAAAGALRLLWGSLFGGGLVEGAKKVTVTELLAGMPDPTSDEVHGEQPAGPGGDADGAGEGEGEGDAAEGDGDEEVAGHEAGPGGAEGVVAVADGGPFRPEGAGGLGDMGDTTPAEPPTPEGSPILKRKLGVDGEEEELVPEPEPEPEPEPEKADEENGEKEEVPEAPPEPPKKAPPSPPAKKEEAGGAGMEFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDMEGSAAGDLAGAGSGGGSGWGSGAGEEAEGDEDENMVYYFLEESTGYMEPALWCLSLLHTLVAFLCIIGYNCLKVPLVIFKREKELARKLEFDGLYITEQPGDDDVKGQWDRLVLNTPSFPSNYWDKFVKRKVLDKHGDIFGRERIAELLGMDLASLEITAHNERKPDPPPGLLTWLMSIDVKYQIWKFGVIFTDNSFLYLGWYMVMSLLGHYNNFFFAAHLLDIAMGVKTLRTILSSVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDEYELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGSDYFDTTPHGFETHTLEEHNLANYMFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLS | ||||||
Modified residue | 1338 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2345 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2843 | Phosphoserine; by PKA and PKG | ||||
Sequence: S | ||||||
Modified residue | 3635 | S-nitrosocysteine | ||||
Sequence: C | ||||||
Modified residue | 4466 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 4470 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 4863 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 4866 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
The N-terminus is blocked.
Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2843 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2843.
Activated by reversible S-nitrosylation (PubMed:22036948).
Repeated very high-level exercise increases S-nitrosylation (By similarity).
Repeated very high-level exercise increases S-nitrosylation (By similarity).
Keywords
- PTM
PTM databases
Interaction
Subunit
Homotetramer (PubMed:10097181, PubMed:15908964, PubMed:17027503, PubMed:18621707, PubMed:25470059, PubMed:25517095, PubMed:27468892, PubMed:27573175, PubMed:27662087).
Can also form heterotetramers with RYR2 (PubMed:12213830).
Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Repeated very high-level exercise decreases interaction with PDE4D and protein phosphatase 1 (PP1) (By similarity).
Interacts with CALM; CALM with bound calcium inhibits the RYR1 channel activity (PubMed:10601232, PubMed:11562475, PubMed:17027503).
Interacts with S100A1 (By similarity).
Interacts with FKBP1A; this stabilizes the closed conformation of the channel (PubMed:10603943, PubMed:25517095, PubMed:26245150, PubMed:27468892, PubMed:7669046).
Interacts with CACNA1S; interaction with CACNA1S is important for activation of the RYR1 channel (PubMed:10388749).
Interacts with CACNB1 (PubMed:21320436).
Interacts with TRDN and ASPH; these interactions stimulate RYR1 channel activity (PubMed:19398037, PubMed:9737879).
Interacts with SELENON (PubMed:18713863).
Interacts with scorpion calcins (AC P0DPT1; AC P0DM30; AC A0A1L4BJ42; AC P59868; AC P60254; AC B8QG00; AC L0GBR1; AC P60252; AC P60253) (PubMed:27114612).
Can also form heterotetramers with RYR2 (PubMed:12213830).
Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Repeated very high-level exercise decreases interaction with PDE4D and protein phosphatase 1 (PP1) (By similarity).
Interacts with CALM; CALM with bound calcium inhibits the RYR1 channel activity (PubMed:10601232, PubMed:11562475, PubMed:17027503).
Interacts with S100A1 (By similarity).
Interacts with FKBP1A; this stabilizes the closed conformation of the channel (PubMed:10603943, PubMed:25517095, PubMed:26245150, PubMed:27468892, PubMed:7669046).
Interacts with CACNA1S; interaction with CACNA1S is important for activation of the RYR1 channel (PubMed:10388749).
Interacts with CACNB1 (PubMed:21320436).
Interacts with TRDN and ASPH; these interactions stimulate RYR1 channel activity (PubMed:19398037, PubMed:9737879).
Interacts with SELENON (PubMed:18713863).
Interacts with scorpion calcins (AC P0DPT1; AC P0DM30; AC A0A1L4BJ42; AC P59868; AC P60254; AC B8QG00; AC L0GBR1; AC P60252; AC P60253) (PubMed:27114612).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | P11716 | Camk2b P28652 | 4 | EBI-6477441, EBI-397029 | |
BINARY | P11716 | FKBP1A P62943 | 2 | EBI-6477441, EBI-16134925 | |
XENO | P11716 | FKBP1A P62942 | 2 | EBI-6477441, EBI-1027571 | |
XENO | P11716 | FKBP1B P68106-1 | 2 | EBI-6477441, EBI-15766566 | |
BINARY | P11716 | RYR1 P11716 | 7 | EBI-6477441, EBI-6477441 | |
XENO | P11716 | S100A1 P02639 | 3 | EBI-6477441, EBI-6477285 |
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for domain, region, repeat, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 98-153 | MIR 1 | ||||
Sequence: HRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPA | ||||||
Domain | 160-205 | MIR 2 | ||||
Sequence: GEKVRVGDDLILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPI | ||||||
Domain | 211-265 | MIR 3 | ||||
Sequence: EGYVTGGHVLRLFHGHMDECLTISAADSDDQRRLVYYEGGAVCTHARSLWRLEPL | ||||||
Domain | 271-334 | MIR 4 | ||||
Sequence: GSHLRWGQPLRIRHVTTGRYLALTEDQGLVVVDACKAHTKATSFCFRVSKEKLDTAPKRDVEGM | ||||||
Domain | 336-394 | MIR 5 | ||||
Sequence: PPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAILHQEGHMDDALFLTRCQ | ||||||
Domain | 582-798 | B30.2/SPRY 1 | ||||
Sequence: HIKSIISLLDKHGRNHKVLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNLINYVTSIRPNIFVGRAEGSTQYGKWYFEVMVDEVVPFLTAQATHLRVGWALTEGYSPYPGGGEGWGGNGVGDDLYSYGFDGLHLWTGHVARPVTSPGQHLLAPEDVVSCCLDLSVPSISFRINGCPVQGVFEAFNLDGLFFPVVSFSAGVKVRFLLGGRHG | ||||||
Region | 670-681 | Interaction with FKBP1A | ||||
Sequence: EVVPFLTAQATH | ||||||
Repeat | 842-955 | 1 | ||||
Sequence: PSRCLSHTDFVPCPVDTVQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVNFHSLPEPERNYNLQMSGETLKTLLALGCHVGMADEKAEDNLKKTKL | ||||||
Region | 842-2959 | 6 X approximate repeats | ||||
Sequence: PSRCLSHTDFVPCPVDTVQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVNFHSLPEPERNYNLQMSGETLKTLLALGCHVGMADEKAEDNLKKTKLPKTYMMSNGYKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVENQSRWDRVRIFRAEKSYTVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCMIDLTENTIIFTLNGEVLMSDSGSETAFREIEIGDGFLPVCSLGPGQVGHLNLGQDVSSLRFFAICGLQEGFEPFAINMQRPVTTWFSKSLPQFEPVPPEHPHYEVARMDGTVDTPPCLRLAHRTWGSQNSLVEMLFLRLSLPVQFHQHFRCTAGATPLAPPGLQPPAEDEARAAEPDPDYENLRRSAGGWGEAEGGKEGTAKEGTPGGTPQPGVEAQPVRAENEKDATTEKNKKRGFLFKAKKAAMMTQPPATPALPRLPHDVVPADNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMNFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGGDFVSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVIQFELGKQKNIMPLSAAMFLSERKNPAPQCPPRLEVQMLMPVSWSRMPNHFLQVETRRAGERLGWAVQCQDPLTMMALHIPEENRCMDILELSERLDLQRFHSHTLRLYRAVCALGNNRVAHALCSHVDQAQLLHALEDAHLPGPLRAGYYDLLISIHLESACRSRRSMLSEYIVPLTPETRAITLFPPGRKGGNARRHGLPGVGVTTSLRPPHHFSPPCFVAALPAAGVAEAPARLSPAIPLEALRDKALRMLGEAVRDGGQHARDPVGGSVEFQFVPVLKLVSTLLVMGIFGDEDVKQILKMIEPEVFTEEEEEEEEEEEEEEEEEEDEEEKEEDEEEEEKEDAEKEEEEAPEGEKEDLEEGLLQMKLPESVKLQMCNLLEYFCDQELQHRVESLAAFAERYVDKLQANQRSRYALLMRAFTMSAAETARRTREFRSPPQEQINMLLHFKDEADEEDCPLPEDIRQDLQDFHQDLLAHCGIQLEGEEEEPEEETSLSSRLRSLLETVRLVKKKEEKPEEELPAEEKKPQSLQELVSHMVVRWAQEDYVQSPELVRAMFSLLHRQYDGLGELLRALPRAYTISPSSVEDTMSLLECLGQIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGETKEIRFPKMVTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGIGLGMQGSTPLDVAAASVIDNNELALALQEQDLEKVVSYLAGCGLQSCPMLLAKGYPDIGWNPCGGERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALRGEGGSGLLAAIEEAIRISEDPARDGPGVRRDRRREHFGEEPPEENRVHLGHAIMSFYAALIDLLGRCAPEMHLIQAGKGEALRIRAILRSLVPLDDLVGIISLPLQIPTLGKDGALVQPKMSASFVPDHKASMVLFLDRVYGIENQDFLLHVLDVGFLPDMRAAASLDTATFSTTEMALALNRYLCLAVLPLITKCAPLFAGTEHRAIMVDSMLHTVYRLSRGRSLTKAQRDVIEDCLMALCRYIRPSMLQHLLRRLVFDVPILNEFAKMPLKLLTNHYERCWKYYCLPTGWANFGVTSEEELHLTRKLFWGIFDSLAHKKYDQELYRMAMPCLCAIAGALPPDYVDASYSSKAEKKATVDAEGNFDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENVDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLKAMIAWEWTIEKAREGEEERTEKKKTRKISQTAQTYDPREGYNPQPPDLSGVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGGTHPLLVPYDTLTAKEKARDREKAQELLKFLQMNGYAVTRGLKDMELDTSSIEKRFAFGF | ||||||
Repeat | 956-1069 | 2 | ||||
Sequence: PKTYMMSNGYKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVAQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVENQSRW | ||||||
Domain | 1014-1209 | B30.2/SPRY 2 | ||||
Sequence: PARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVENQSRWDRVRIFRAEKSYTVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQRWHLGSEPFGRPWQSGDVVGCMIDLTENTIIFTLNGEVLMSDSGSETAFREIEIGDGFLPVCSLGPGQVGHLNLGQDVS | ||||||
Region | 1308-1383 | Disordered | ||||
Sequence: TPLAPPGLQPPAEDEARAAEPDPDYENLRRSAGGWGEAEGGKEGTAKEGTPGGTPQPGVEAQPVRAENEKDATTEK | ||||||
Repeat | 1345-1360 | 3; truncated | ||||
Sequence: AEGGKEGTAKEGTPGG | ||||||
Domain | 1358-1571 | B30.2/SPRY 3 | ||||
Sequence: PGGTPQPGVEAQPVRAENEKDATTEKNKKRGFLFKAKKAAMMTQPPATPALPRLPHDVVPADNRDDPEIILNTTTYYYSVRVFAGQEPSCVWVGWVTPDYHQHDMNFDLSKVRAVTVTMGDEQGNVHSSLKCSNCYMVWGGDFVSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVIQFELGKQKN | ||||||
Repeat | 1373-1388 | 4; truncated | ||||
Sequence: AENEKDATTEKNKKRG | ||||||
Region | 1867-1922 | Disordered | ||||
Sequence: EPEVFTEEEEEEEEEEEEEEEEEEDEEEKEEDEEEEEKEDAEKEEEEAPEGEKEDL | ||||||
Compositional bias | 1870-1920 | Acidic residues | ||||
Sequence: VFTEEEEEEEEEEEEEEEEEEDEEEKEEDEEEEEKEDAEKEEEEAPEGEKE | ||||||
Region | 2390-2412 | Disordered | ||||
Sequence: PARDGPGVRRDRRREHFGEEPPE | ||||||
Repeat | 2726-2845 | 5 | ||||
Sequence: KATVDAEGNFDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENVDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLKAMIAWEWTIEKAREGEEERTEKKKTRKISQT | ||||||
Compositional bias | 2828-2843 | Basic and acidic residues | ||||
Sequence: EGEEERTEKKKTRKIS | ||||||
Region | 2828-2858 | Disordered | ||||
Sequence: EGEEERTEKKKTRKISQTAQTYDPREGYNPQ | ||||||
Repeat | 2846-2959 | 6 | ||||
Sequence: AQTYDPREGYNPQPPDLSGVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGGTHPLLVPYDTLTAKEKARDREKAQELLKFLQMNGYAVTRGLKDMELDTSSIEKRFAFGF | ||||||
Region | 3478-3501 | Disordered | ||||
Sequence: MAKAGDAQSGGSDQERTKKKRRGD | ||||||
Region | 3614-3643 | Interaction with CALM | ||||
Sequence: KSKKAVWHKLLSKQRRRAVVACFRMTPLYN | ||||||
Domain | 4075-4103 | EF-hand | ||||
Sequence: EAFQDYVTDPRGLISKKDFQKAMDSQKQF | ||||||
Region | 4252-4282 | Disordered | ||||
Sequence: SEPEGEPEADEDEGMGEAAAEGAEEGAAGAE | ||||||
Compositional bias | 4255-4270 | Acidic residues | ||||
Sequence: EGEPEADEDEGMGEAA | ||||||
Region | 4381-4534 | Disordered | ||||
Sequence: GMPDPTSDEVHGEQPAGPGGDADGAGEGEGEGDAAEGDGDEEVAGHEAGPGGAEGVVAVADGGPFRPEGAGGLGDMGDTTPAEPPTPEGSPILKRKLGVDGEEEELVPEPEPEPEPEPEKADEENGEKEEVPEAPPEPPKKAPPSPPAKKEEAG | ||||||
Compositional bias | 4484-4504 | Acidic residues | ||||
Sequence: EELVPEPEPEPEPEPEKADEE | ||||||
Region | 4588-4620 | Disordered | ||||
Sequence: GEDDMEGSAAGDLAGAGSGGGSGWGSGAGEEAE | ||||||
Motif | 4894-4900 | Selectivity filter | ||||
Sequence: GGGIGDE |
Domain
The calcium release channel activity resides in the C-terminal region while the remaining part of the protein constitutes the 'foot' structure spanning the junctional gap between the sarcoplasmic reticulum (SR) and the T-tubule (PubMed:25517095, PubMed:2725677, PubMed:27468892, PubMed:27573175, PubMed:27662087).
Pore opening is mediated via the cytoplasmic calcium-binding domains that mediate a small rotation of the channel-forming transmembrane regions that then leads to channel opening (PubMed:27468892).
Pore opening is mediated via the cytoplasmic calcium-binding domains that mediate a small rotation of the channel-forming transmembrane regions that then leads to channel opening (PubMed:27468892).
Sequence similarities
Belongs to the ryanodine receptor (TC 1.A.3.1) family. RYR1 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length5,037
- Mass (Da)565,253
- Last updated1989-10-01 v1
- Checksum4ABD87AA26697070
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1870-1920 | Acidic residues | ||||
Sequence: VFTEEEEEEEEEEEEEEEEEEDEEEKEEDEEEEEKEDAEKEEEEAPEGEKE | ||||||
Sequence conflict | 2015 | in Ref. 2; no nucleotide entry | ||||
Sequence: E → D | ||||||
Compositional bias | 2828-2843 | Basic and acidic residues | ||||
Sequence: EGEEERTEKKKTRKIS | ||||||
Sequence conflict | 3481-3485 | in Ref. 2; no nucleotide entry | ||||
Sequence: Missing | ||||||
Compositional bias | 4255-4270 | Acidic residues | ||||
Sequence: EGEPEADEDEGMGEAA | ||||||
Compositional bias | 4484-4504 | Acidic residues | ||||
Sequence: EELVPEPEPEPEPEPEKADEE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X15209 EMBL· GenBank· DDBJ | CAA33279.1 EMBL· GenBank· DDBJ | mRNA | ||
X15750 EMBL· GenBank· DDBJ | CAA33762.1 EMBL· GenBank· DDBJ | mRNA |