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E9PZQ0

- RYR1_MOUSE

UniProt

E9PZQ0 - RYR1_MOUSE

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Protein
Ryanodine receptor 1
Gene
Ryr1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules. Repeated very high-level exercise increases the open probability of the channel and leads to Ca2+ leaking into the cytoplasm. 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.6 Publications

GO - Molecular functioni

  1. calcium channel activity Source: UniProtKB
  2. calcium ion binding Source: InterPro
  3. enzyme binding Source: BHF-UCL
  4. protease binding Source: UniProtKB
  5. protein binding Source: IntAct
  6. ryanodine-sensitive calcium-release channel activity Source: UniProtKB
  7. voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  1. calcium ion transport Source: MGI
  2. cellular response to caffeine Source: UniProtKB
  3. muscle contraction Source: UniProtKB
  4. ossification involved in bone maturation Source: UniProtKB
  5. outflow tract morphogenesis Source: UniProtKB
  6. regulation of muscle contraction Source: MGI
  7. release of sequestered calcium ion into cytosol Source: MGI
  8. release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: UniProtKB
  9. response to hypoxia Source: Ensembl
  10. skeletal muscle fiber development Source: UniProtKB
  11. skin development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Developmental protein, Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_196640. Stimuli-sensing channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Ryanodine receptor 1
Short name:
RYR-1
Short name:
RyR1
Alternative name(s):
Skeletal muscle calcium release channel
Skeletal muscle ryanodine receptor
Skeletal muscle-type ryanodine receptor
Type 1 ryanodine receptor
Gene namesi
Name:Ryr1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:99659. Ryr1.

Subcellular locationi

Sarcoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein Inferred
Note: The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic.3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 43234323Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei4324 – 434421Helical; Reviewed prediction
Add
BLAST
Transmembranei4345 – 436521Helical; Reviewed prediction
Add
BLAST
Transmembranei4557 – 457721Helical; Reviewed prediction
Add
BLAST
Transmembranei4649 – 466921Helical; Reviewed prediction
Add
BLAST
Transmembranei4778 – 479821Helical; Reviewed prediction
Add
BLAST
Transmembranei4805 – 482521Helical; Reviewed prediction
Add
BLAST
Transmembranei4837 – 485721Helical; Reviewed prediction
Add
BLAST
Intramembranei4888 – 489710Pore-forming; By similarity
Transmembranei4918 – 493821Helical; Reviewed prediction
Add
BLAST
Topological domaini4939 – 503597Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. I band Source: Ensembl
  2. T-tubule Source: MGI
  3. cell cortex Source: Ensembl
  4. integral component of membrane Source: UniProtKB-KW
  5. junctional membrane complex Source: MGI
  6. membrane Source: MGI
  7. protein complex Source: UniProtKB
  8. sarcoplasmic reticulum Source: MGI
  9. sarcoplasmic reticulum membrane Source: UniProtKB
  10. smooth endoplasmic reticulum Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Perinatal lethality, due to severe defects in skeletal muscle development. Neonates do not breathe and do not move. Mutant mice show defects in muscle fiber development. Their muscles do not show a contractile response to electrical stimulation. In addition, mice display abnormal curvature of the spine, thin limbs, and an abnormal rib cage.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi165 – 1651R → C: Increased channel activity, leading to permanently increased cytoplasmic Ca(2+) levels. Increased activation by calcium, and increased ryanodine binding. 1 Publication
Mutagenesisi4895 – 48951I → T: Causes paralysis and perinatal death in homozygous mice, apparently due to asphyxia. Mutant mice have greatly reduced and amorphous skeletal muscle. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 50355035Ryanodine receptor 1
PRO_0000415566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2844 – 28441Phosphoserine; by PKA and PKG2 Publications
Modified residuei3636 – 36361S-nitrosocysteine By similarity
Modified residuei4861 – 48611Phosphotyrosine By similarity
Modified residuei4864 – 48641Phosphoserine By similarity

Post-translational modificationi

Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2844 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2844.
Activated by reversible S-nitrosylation By similarity. Repeated very high-level exercise increases S-nitrosylation.

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiE9PZQ0.
PRIDEiE9PZQ0.

PTM databases

PhosphoSiteiE9PZQ0.

Expressioni

Tissue specificityi

Detected in muscle and myotubes (at protein level). Ubiquitous. Detected in diaphragm, skeletal muscle, esophagus, spleen, submaxillary gland, adrenal gland, cerebellum, brain and in testis germ cells.4 Publications

Gene expression databases

ArrayExpressiE9PZQ0.
BgeeiE9PZQ0.
GenevestigatoriQ62235.

Interactioni

Subunit structurei

Homotetramer. Can also form heterotetramers with RYR2. Interacts with CALM; CALM with bound calcium inhibits the RYR1 channel activity. Interacts with S100A1. Interacts with FKBP1A; this stabilizes the closed conformation of the channel. Interacts with CACNA1S; interaction with CACNA1S is important for activation of the RYR1 channel. Interacts with CACNB1. Interacts with TRDN and ASPH; these interactions stimulate RYR1 channel activity By similarity. 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).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BsgO551083EBI-642079,EBI-643315
CamlgP490703EBI-642079,EBI-309114

Protein-protein interaction databases

DIPiDIP-29705N.
IntActiE9PZQ0. 27 interactions.
STRINGi10090.ENSMUSP00000032813.

Structurei

3D structure databases

ProteinModelPortaliE9PZQ0.
SMRiE9PZQ0. Positions 13-535, 2735-2941, 3615-3641.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini99 – 15456MIR 1
Add
BLAST
Domaini161 – 20646MIR 2
Add
BLAST
Domaini212 – 26655MIR 3
Add
BLAST
Domaini272 – 32958MIR 4
Add
BLAST
Domaini337 – 39458MIR 5
Add
BLAST
Domaini583 – 799217B30.2/SPRY 1
Add
BLAST
Repeati843 – 9561141
Add
BLAST
Repeati957 – 10701142
Add
BLAST
Domaini1015 – 1210196B30.2/SPRY 2
Add
BLAST
Repeati1346 – 1361163; truncated
Add
BLAST
Domaini1359 – 1572214B30.2/SPRY 3
Add
BLAST
Repeati1374 – 1389164; truncated
Add
BLAST
Repeati2727 – 28461205
Add
BLAST
Repeati2847 – 29601146
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni843 – 296021186 X approximate repeats
Add
BLAST
Regioni3615 – 364430Interaction with CALM By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1869 – 2089221Glu-rich
Add
BLAST
Compositional biasi3683 – 376280Glu-rich
Add
BLAST
Compositional biasi4459 – 452567Pro-rich
Add
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Contains 3 B30.2/SPRY domains.
Contains 5 MIR domains.

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00690000101961.
HOGENOMiHOG000231428.
HOVERGENiHBG102939.
KOiK04961.
OMAiQCSATVL.
OrthoDBiEOG71K622.
TreeFamiTF315244.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
IPR011992. EF-hand-dom_pair.
IPR014821. Ins145_P3_rcpt.
IPR005821. Ion_trans_dom.
IPR016093. MIR_motif.
IPR013662. RIH_assoc-dom.
IPR000699. RIH_dom.
IPR013333. Ryan_recept.
IPR003032. Ryanodine_rcpt.
IPR015925. Ryanodine_recept-rel.
IPR009460. Ryanrecept_TM4-6.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]
PANTHERiPTHR13715. PTHR13715. 1 hit.
PfamiPF08709. Ins145_P3_rec. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02815. MIR. 1 hit.
PF08454. RIH_assoc. 1 hit.
PF06459. RR_TM4-6. 1 hit.
PF01365. RYDR_ITPR. 2 hits.
PF02026. RyR. 4 hits.
PF00622. SPRY. 3 hits.
[Graphical view]
PRINTSiPR00795. RYANODINER.
SMARTiSM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMiSSF100909. SSF100909. 2 hits.
SSF49899. SSF49899. 3 hits.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E9PZQ0-1 [UniParc]FASTAAdd to Basket

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MGDGGGEGED EVQFLRTDDE VVLQCSATVL KEQLKLCLAA EGFGNRLCFL     50
EPTSNAQNVP PDLAICCFIL EQSLSVRALQ EMLANTVEAG VESSQGGGHR 100
TLLYGHAILL RHAHSRMYLS CLTTSRSMTD KLAFDVGLQE DATGEACWWT 150
MHPASKQRSE GEKVRVGDDL ILVSVSSERY LHLSTASGEL QVDASFMQTL 200
WNMNPICSGC EEGFVTGGHV LRLFHGHMDE CLTISPSDSD DQRRLVYYEG 250
GPVCTHARSL WRLEPLRISW SGSHLRWGQP LRIRHVTTGR YLGLTEDQGL 300
VVVDASKAHT KATSFCFRIS KEKLDVAPKR DVEGMGPPEI KYGESLCFVQ 350
HVASGLWLTY AAPDPKALRL GVLKKKAMLH QEGHMDDALS LTRCQQEESQ 400
AARMIYSTAG LYNQFIKGLD SFSGKPRGSG PPAGSALPIE GVILSLQDLI 450
GYFEPPSEEL QHEEKQTKLR SLRNRQSLFQ EEGMLSLVLN CIDRLNVYTT 500
AAHFAEFAGE EAAESWKEIV NLLYELLASL IRGNRTNCAL FSTNLDWLVS 550
KLDRLEASSG ILEVLYCVLI ESPEVLNIIQ ENHIKSIISL LDKHGRNHKV 600
LDVLCSLCVC NGVAVRSNQD LITENLLPGR ELLLQTNLIN YVTSIRPNIF 650
VGRAEGSTQY GKWYFEVMVD EVAPFLTAQA THLRVGWALS EGYSPYPGGG 700
EGWGGNGVGD DLYSYGFDGL HLWTGHVARP VTSPGQHLLA PEDVVSCCLD 750
LSVPSISFRI NGCPVQGVFE SFNLDGLFFP VVSFSAGIKV RFLLGGRHGE 800
FKFLPPPGYA PCHEAVLPRE RLHLQPIKEY RREGPRGPHL VGPSRCLSHL 850
DFVPCPVDTI QIVLPPHLER IREKLAENIH ELWALTRIEQ GWTYGPVRDD 900
NKRLHPCLVN FHSLPEPERN YNLQMSGETL KTLLALGCHV GMADEKAEDN 950
LKKTKLPKTY MMSNGYKPAP LDLSHVRLTP AQTTLVDRLA ENGHNVWARD 1000
RVAQGWSYSA VQDIPARRNP RLVPYRLLDE ATKRSNRDSL CQAVRTLLGY 1050
GYNIEPPDQE PSQVDSQSRG DRARIFRAEK SYAVQSGRWY FEFEAVTTGE 1100
MRVGWARPEL RPDVELGADD LAYVFNGHRG QRWHLGSEPF GRPWQSGDVV 1150
GCMIDLTENT IIFTLNGEVL MSDSGSETAF RDIEIGDGFL PVCSLGPGQV 1200
GHLNLGQDVS SLRFFAICGL QEGFEPFAIN MQRPVTTWFS KSLPQFEPVP 1250
LEHPHYEVAR MDGTVDTPPC LRLTHRTWGS QNSLVEMLFL RLSLPVQFHQ 1300
HFRCTAGATP LASPGLQPPA EDEARAAEPD TDYENLRRSA GGWGEAEGGK 1350
DGTAKEGTPG GTAQAGVEAQ PARAENEKDA TTEKNKKRGF LFKAKKVAMM 1400
TQPPSTPALP RLPRDVVPAD NRDDPEIILN TTTYYYSVRV FAGQEPSCVW 1450
VGWVTPDYHQ HDMSFDLSKV RAVTVTMGDE QGNVHSSLKC SNCYMVWGGD 1500
FVSPGQQGRI SHTDLVIGCL VDLATGLMTF TANGKESNTF FQVEPNTKLF 1550
PAVFVLPTHQ NVVQFELGKQ KNIMPLSAAM FLSERKNPAP QCPPRLEVQM 1600
LMPVSWSRMP NHFLQVDTRR AGERLGWAVQ CQEPLMMMAL HIPEENRCMD 1650
ILELSERLDL QRFHSHTLSL YRSVCALGNN RVAHALCSHV DQAQLLHALE 1700
DARLPGPLRA GYYDLLISIH LESACRSRRS MLSEYIVPLT PETRAITLFP 1750
PGRSAEDGPR RHGLPGVGVT TSLRPPHHFS PPCFVVALPA AGATEAPARL 1800
SPAIPLEALR DKALRMLGEA VRDGGQHARD PVGGSVEFQF VPVLKLVSTL 1850
LVMGVFSDED VKQILKMIEP EVFREEEEVE EEGEEEEEDE EEKEEDEEEE 1900
AHEKEDEEKE EAEDAAEEEK EELEEGLLQM KLPESVKLQM CHLLEYFCDQ 1950
ELQHRVESLA AFAECYVDKM QGNQRGRYGL LMKAFTMSAA ETARRTREFR 2000
SPPQEQINML LHFKNGADEE ECPLPEEIRQ ELVNFHQDLL AHCGIQLEGE 2050
EEEPEEESTL GSRLMSLLEK VKLVKKTEEK PEEEPAPEEH KPQSLQELVS 2100
HTVVRWAQED FVQSPELVRA MFSLLHRQYD GLGELLRALP RAYTISVSSV 2150
EDTMSLLECL GQIRSLLIVQ MGPQEENLMI QSIGNIMNNK VFYQHPNLMR 2200
ALGMHETVME VMVNVLGGGE SKEIRFPKMV TSCCRFLCYF CRISRQNQRS 2250
MFDHLSYLLE NSGIGLGMQG STPLDVAAAS VIDNNELALA LQEQDLEKVV 2300
SYLAGCGLQS CPMLLAKGYP DIGWNPCGGE RYLDFLRFAV FVNGESVEEN 2350
ANVVVRLLIR KPECFGPALR GEGGSGLLAA IEEAIRISED PARDGPGVRR 2400
DRRREHFGEE PPEENRVHLG HAIMSFYAAL IDLLGRCAPE THLIQAGKGE 2450
ALRIRAILRS LVPLDDLVGI ISLPLQIPTL GKDGALVQPK MSASFVPDHK 2500
ASMVLFLDRV YGIENQDFLL HVLDVGFLPD MRAAASLDTA TFSTTEMALA 2550
LNRYLCLAVL PLITKCAPLF AGTEHRAIMV DSMLHTVYRL SRGRSLTKAQ 2600
RDVIEDCLMA LCRYIRPSML QHLLRRLVFD VPILNEFAKM PLKLLTNHYE 2650
RCWKYYCLPT GWANFGVTSE EELHLTRKLF WGIFDSLAHK KYDQELYRIA 2700
MPCLCAIAGA LPPDYVDASY SSKTEKKATV DAEGNFDPRP VETLNVIIPE 2750
KLDSFINKFA EYTHEKWAFD KIQNNWSYGE NIDEELKTHP MLRPYKTFSE 2800
KDKEIYRWPI KESLKAMIAW EWTVEKAREG EEEKTEKKKT RKISQTAQTY 2850
DPREGYNPQP PDLSVVTLSR ELQAMAEQLA ENYHNTWGRK KKQELEAKGG 2900
GSHPLLVPYD TLTAKEKARD REKAQELLKF LQMNGYAVTR GLKDMELDTS 2950
SIEKRFAFGF LQQLLRWMDI SQEFIAHLEA VVSSGRVEKS PHEQEIKFFA 3000
KILLPLINQY FTNHCLYFLS TPAKVLGSGG HASNKEKEMI TSLFCKLAAL 3050
VRHRVSLFGT DAPAVVNCLH ILARSLDART VMKSGPEIVK AGLRSFFESA 3100
SEDIEKMVEN LRLGKVSQAR TQVKGVGQNL TYTTVALLPV LTTLFQHIAQ 3150
HQFGDDVILD DVQVSCYRTL CSIYSLGTTR NPYVEKLRPA LGECLARLAA 3200
AMPVAFLEPE LNEYNACSVY TTKSPRERAI LGLPNSVEEM CPDIPVLERL 3250
MAEIGGLAES GARYTEMPHV IEITLPMLCS YLPRWWERGP EAPPPALPAG 3300
APPPCTAVTS DHLNSLLGNI LRIIVNNLGI DEASWMKRLA VFAQPIVSRA 3350
RPELLRSHFI PTIGRLRKRA GKVVAEEEQL RLEAKAEAEE GELLVRDEFS 3400
VLCRDLYALY PLLIRYVDNN RAHWLTEPNP NAEELFRMVG EIFIYWSKSH 3450
NFKREEQNFV VQNEINNMSF LTADNKSKMA KAGDVQSGGS DQERTKKKRR 3500
GDRYSVQTSL IVATLKKMLP IGLNMCAPTD QDLIVLAKAR YALKDTDEEV 3550
REFLQNNLNL QGKVEGSPSL RWQMALYRGV PGREEDADDP EKIVRRVQEV 3600
SAVLYHLDQT EHPYKSKKAV WHKLLSKQRR RAVVACFRMT PLYNLPTHRA 3650
CNMFLESYKA SWILTEDHSF EDRMIDDLSK AGEQEEEEEE VEEKKPDPLH 3700
QLVLHFSRTA LTEKSKLDED YLYMAYADIM AKSCHLEEGG ENGEEGGEEE 3750
EVEVSFEEKE MEKQRLLYQQ SRLHNRGAAE MVLQMISACK GETGAMVSST 3800
LKLGISILNG GNAEVQQKML DYLKDKKEVG FFQSIQALMQ TCSVLDLNAF 3850
ERQNKAEGLG MVNEDGTVIN RQNGEKVMAD DEFTQDLFRF LQLLCEGHNN 3900
DFQNYLRTQT GNTTTINIII CTVDYLLRLQ ESISDFYWYY SGKDVIEEQG 3950
KRNFSKAMSV AKQVFNSLTE YIQGPCTGNQ QSLAHSRLWD AVVGFLHVFA 4000
HMMMKLAQDS SQIELLKELL DLQKDMVVML LSLLEGNVVN GMIARQMVDM 4050
LVESSSNVEM ILKFFDMFLK LKDIVGSEAF QDYVTDPRGL ISKKDFQKAM 4100
DSQKQFTGPE IQFLLSCSEA DENEMINCEE FANRFQEPAR DIGFNVAVLL 4150
TNLSEHVPHD PRLRNFLELA ESILEYFRPY LGRIEIMGAS RRIERIYFEI 4200
SETNRAQWEM PQVKESKRQF IFDVVNEGGE SEKMEMFVSF CEDTIFEMQI 4250
AAQISEPEGE PEEDEDEGAE EAEEGAAGSD GSGSAAAAGV WVWLAATAGR 4300
TLRGLSYRSL RRRVRRLRRL TAREAATAVA ALLWALVTRA GGAGAGAAAG 4350
ALRLLWGSLF GGGLVDSAKK VTVTELLAGM PDPTGDEVHG QQPSGAGSDA 4400
EGEGEGEGEG DAADGAGDEE AAADQAGTGG ADGAVAVADG SPFRPEGAGG 4450
LGDMGDTTPV EPPTPEGSPI LKRKLGVDGE EEEPPPEPEP EPEPEPEKAD 4500
TENGEKEVPE PPPEPPKKTP PPPPPKKEEA GGAGLEEFWG ELEVQRVKFL 4550
NYLSRNFYTL RFLALFLAFA INFILLFYKV SDSPPGEDDI EGSGAGDMSG 4600
AGSGDGSGWG SRAGEEVEGD EDENMVYYFL EESTGYMEPA LRCLSLLHTL 4650
VAFLCIIGYN CLKVPLVIFK REKELARKLE FDGLYITEQP EDDDVKGQWD 4700
RLVLNTPSFP SNYWDKFVKR KVLDKHGDIF GRERIAELLG MDLASLEITA 4750
HNERKPDPPP GLLTWIMSID VKYQIWKFGV IFTDNSFLYL GWYMVMSLLG 4800
HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYLYT 4850
VVAFNFFRKF YNKSEDEDEP DMKCDDMMTC YLFHMYVGVR AGGGIGDEIE 4900
DPAGDEYELY RVVFDITFFF FVIVILLAII QGLIIDAFGE LRDQQEQVKE 4950
DMETKCFICG IGSDYFDTTP HGFETHTLEE HNLANYMFFL MYLINKDETE 5000
HTGQESYVWK MYQERCWDFF PAGDCFRKQY EDQLS 5035
Length:5,035
Mass (Da):565,039
Last modified:April 5, 2011 - v1
Checksum:iD15D2E764B445573
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti616 – 6161R → C in CAC34624. 1 Publication
Sequence conflicti1380 – 13801A → S in AAP29981. 1 Publication
Sequence conflicti3484 – 34841D → V in AAP29981. 1 Publication
Sequence conflicti4766 – 47661I → L in AAA64955. 1 Publication
Sequence conflicti4821 – 48211L → V in CAA58784. 1 Publication
Sequence conflicti4888 – 48881G → A in CAA58784. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY268935 mRNA. Translation: AAP29981.1.
AC164564 Genomic DNA. No translation available.
AC165142 Genomic DNA. No translation available.
D21798 Genomic DNA. Translation: BAA21010.1.
D21796 mRNA. Translation: BAA04821.1.
D21797 Genomic DNA. Translation: BAA04822.1.
AJ308737 Genomic DNA. Translation: CAC34624.1.
BC051248 mRNA. Translation: AAH51248.1.
BC055487 mRNA. Translation: AAH55487.1.
X83932 mRNA. Translation: CAA58784.1.
U23754 mRNA. Translation: AAA64955.1.
D38216 mRNA. Translation: BAA07391.1.
CCDSiCCDS39866.1.
PIRiI48741.
I58087.
I78376.
I78377.
S56105.
RefSeqiNP_033135.2. NM_009109.2.
UniGeneiMm.439745.

Genome annotation databases

EnsembliENSMUST00000179893; ENSMUSP00000137123; ENSMUSG00000030592.
GeneIDi20190.
KEGGimmu:20190.
UCSCiuc009gao.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY268935 mRNA. Translation: AAP29981.1 .
AC164564 Genomic DNA. No translation available.
AC165142 Genomic DNA. No translation available.
D21798 Genomic DNA. Translation: BAA21010.1 .
D21796 mRNA. Translation: BAA04821.1 .
D21797 Genomic DNA. Translation: BAA04822.1 .
AJ308737 Genomic DNA. Translation: CAC34624.1 .
BC051248 mRNA. Translation: AAH51248.1 .
BC055487 mRNA. Translation: AAH55487.1 .
X83932 mRNA. Translation: CAA58784.1 .
U23754 mRNA. Translation: AAA64955.1 .
D38216 mRNA. Translation: BAA07391.1 .
CCDSi CCDS39866.1.
PIRi I48741.
I58087.
I78376.
I78377.
S56105.
RefSeqi NP_033135.2. NM_009109.2.
UniGenei Mm.439745.

3D structure databases

ProteinModelPortali E9PZQ0.
SMRi E9PZQ0. Positions 13-535, 2735-2941, 3615-3641.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29705N.
IntActi E9PZQ0. 27 interactions.
STRINGi 10090.ENSMUSP00000032813.

Chemistry

BindingDBi E9PZQ0.
ChEMBLi CHEMBL2133.

PTM databases

PhosphoSitei E9PZQ0.

Proteomic databases

MaxQBi E9PZQ0.
PRIDEi E9PZQ0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000179893 ; ENSMUSP00000137123 ; ENSMUSG00000030592 .
GeneIDi 20190.
KEGGi mmu:20190.
UCSCi uc009gao.1. mouse.

Organism-specific databases

CTDi 6261.
MGIi MGI:99659. Ryr1.

Phylogenomic databases

GeneTreei ENSGT00690000101961.
HOGENOMi HOG000231428.
HOVERGENi HBG102939.
KOi K04961.
OMAi QCSATVL.
OrthoDBi EOG71K622.
TreeFami TF315244.

Enzyme and pathway databases

Reactomei REACT_196640. Stimuli-sensing channels.

Miscellaneous databases

NextBioi 297735.
PROi E9PZQ0.
SOURCEi Search...

Gene expression databases

ArrayExpressi E9PZQ0.
Bgeei E9PZQ0.
Genevestigatori Q62235.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProi IPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
IPR011992. EF-hand-dom_pair.
IPR014821. Ins145_P3_rcpt.
IPR005821. Ion_trans_dom.
IPR016093. MIR_motif.
IPR013662. RIH_assoc-dom.
IPR000699. RIH_dom.
IPR013333. Ryan_recept.
IPR003032. Ryanodine_rcpt.
IPR015925. Ryanodine_recept-rel.
IPR009460. Ryanrecept_TM4-6.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view ]
PANTHERi PTHR13715. PTHR13715. 1 hit.
Pfami PF08709. Ins145_P3_rec. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02815. MIR. 1 hit.
PF08454. RIH_assoc. 1 hit.
PF06459. RR_TM4-6. 1 hit.
PF01365. RYDR_ITPR. 2 hits.
PF02026. RyR. 4 hits.
PF00622. SPRY. 3 hits.
[Graphical view ]
PRINTSi PR00795. RYANODINER.
SMARTi SM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view ]
SUPFAMi SSF100909. SSF100909. 2 hits.
SSF49899. SSF49899. 3 hits.
SSF82109. SSF82109. 2 hits.
PROSITEi PS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "An Ryr1I4895T mutation abolishes Ca2+ release channel function and delays development in homozygous offspring of a mutant mouse line."
    Zvaritch E., Depreux F., Kraeva N., Loy R.E., Goonasekera S.A., Boncompagni S., Kraev A., Gramolini A.O., Dirksen R.T., Franzini-Armstrong C., Seidman C.E., Seidman J.G., MacLennan D.H.
    Proc. Natl. Acad. Sci. U.S.A. 104:18537-18542(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF ILE-4895.
    Strain: BALB/c X CD-1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene."
    Takeshima H., Iino M., Takekura H., Nishi M., Kuno J., Minowa O., Takano H., Noda T.
    Nature 369:556-559(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57, NUCLEOTIDE SEQUENCE [MRNA] OF 1-27, FUNCTION, DISRUPTION PHENOTYPE.
    Strain: 129/J and BALB/c.
    Tissue: Skeletal muscle.
  4. "Characterisation of the murine Ryr1 gene."
    Kathirvel P.
    Thesis (2000), University of Edinburgh, United Kingdom
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 483-861.
    Strain: 129.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4500-5035.
    Strain: FVB/N-3.
    Tissue: Eye and Mammary tumor.
  6. "The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues."
    Giannini G., Conti A., Mammarella S., Scrobogna M., Sorrentino V.
    J. Cell Biol. 128:893-904(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4537-5035, TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Brain.
  7. "Regulation of mouse egg activation: presence of ryanodine receptors and effects of microinjected ryanodine and cyclic ADP ribose on uninseminated and inseminated eggs."
    Ayabe T., Kopf G.S., Schultz R.M.
    Development 121:2233-2244(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4762-5013.
    Tissue: Brain.
  8. "Ca(2+)-induced Ca2+ release in myocytes from dyspedic mice lacking the type-1 ryanodine receptor."
    Takeshima H., Yamazawa T., Ikemoto T., Takekura H., Nishi M., Noda T., Iino M.
    EMBO J. 14:2999-3006(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4913-5035, FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Skeletal muscle.
  9. "Abnormal junctions between surface membrane and sarcoplasmic reticulum in skeletal muscle with a mutation targeted to the ryanodine receptor."
    Takekura H., Nishi M., Noda T., Takeshima H., Franzini-Armstrong C.
    Proc. Natl. Acad. Sci. U.S.A. 92:3381-3385(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY, DOMAIN.
  10. "Remodeling of ryanodine receptor complex causes 'leaky' channels: a molecular mechanism for decreased exercise capacity."
    Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.
    Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-2844, S-NITROSYLATION, IDENTIFICATION IN A COMPLEX WITH PDE4D; PKA; FKBP1A AND PROTEIN PHOSPHATASE 1.
  11. "Nitric oxide-induced calcium release via ryanodine receptors regulates neuronal function."
    Kakizawa S., Yamazawa T., Chen Y., Ito A., Murayama T., Oyamada H., Kurebayashi N., Sato O., Watanabe M., Mori N., Oguchi K., Sakurai T., Takeshima H., Saito N., Iino M.
    EMBO J. 31:417-428(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BRAIN, TISSUE SPECIFICITY.
  12. "Functional and biochemical properties of ryanodine receptor type 1 channels from heterozygous R163C malignant hyperthermia-susceptible mice."
    Feng W., Barrientos G.C., Cherednichenko G., Yang T., Padilla I.T., Truong K., Allen P.D., Lopez J.R., Pessah I.N.
    Mol. Pharmacol. 79:420-431(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ARG-165, PHOSPHORYLATION AT SER-2844.
  13. "Ryanodine receptor studies using genetically engineered mice."
    Kushnir A., Betzenhauser M.J., Marks A.R.
    FEBS Lett. 584:1956-1965(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiRYR1_MOUSE
AccessioniPrimary (citable) accession number: E9PZQ0
Secondary accession number(s): Q60834
, Q61779, Q61780, Q62173, Q62196, Q62235, Q78EJ6, Q7TNG1, Q80UQ5, Q80X16, Q99JF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 5, 2011
Last modified: September 3, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Channel activity is modulated by the alkaloid ryanodine that binds to the open Ca-release channel with high affinity. At low concentrations, ryanodine maintains the channel in an open conformation. High ryanodine concentrations inhibit channel activity. Channel activity is regulated by calmodulin (CALM). The calcium release is activated by increased cytoplasmic calcium levels, by nitric oxyde (NO), caffeine and ATP. Channel activity is inhibited by magnesium ions, possibly by competition for calcium binding sites.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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