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Protein

Ryanodine receptor 1

Gene

Ryr1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

  • calcium channel activity Source: UniProtKB
  • calcium-induced calcium release activity Source: GO_Central
  • calcium ion binding Source: GO_Central
  • enzyme binding Source: BHF-UCL
  • protease binding Source: UniProtKB
  • ryanodine-sensitive calcium-release channel activity Source: UniProtKB
  • voltage-gated calcium channel activity Source: UniProtKB

GO - Biological processi

  • calcium ion transport Source: MGI
  • cellular response to caffeine Source: UniProtKB
  • muscle contraction Source: UniProtKB
  • ossification involved in bone maturation Source: UniProtKB
  • outflow tract morphogenesis Source: UniProtKB
  • regulation of muscle contraction Source: MGI
  • release of sequestered calcium ion into cytosol Source: MGI
  • release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: UniProtKB
  • response to hypoxia Source: MGI
  • skeletal muscle fiber development Source: UniProtKB
  • 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

ReactomeiR-MMU-2672351. Stimuli-sensing channels.
R-MMU-5578775. Ion homeostasis.

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
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:99659. Ryr1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 4323CytoplasmicSequence analysisAdd BLAST4323
Transmembranei4324 – 4344HelicalSequence analysisAdd BLAST21
Transmembranei4345 – 4365HelicalSequence analysisAdd BLAST21
Transmembranei4557 – 4577HelicalSequence analysisAdd BLAST21
Transmembranei4649 – 4669HelicalSequence analysisAdd BLAST21
Transmembranei4778 – 4798HelicalSequence analysisAdd BLAST21
Transmembranei4805 – 4825HelicalSequence analysisAdd BLAST21
Transmembranei4837 – 4857HelicalSequence analysisAdd BLAST21
Intramembranei4888 – 4897Pore-formingBy similarity10
Transmembranei4918 – 4938HelicalSequence analysisAdd BLAST21
Topological domaini4939 – 5035CytoplasmicSequence analysisAdd BLAST97

GO - Cellular componenti

  • calcium channel complex Source: GO_Central
  • cell cortex Source: MGI
  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • I band Source: MGI
  • junctional membrane complex Source: MGI
  • membrane Source: MGI
  • plasma membrane Source: MGI
  • protein complex Source: UniProtKB
  • sarcoplasmic reticulum Source: MGI
  • sarcoplasmic reticulum membrane Source: UniProtKB
  • smooth endoplasmic reticulum Source: MGI
  • T-tubule Source: MGI
  • Z disc Source: GO_Central
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)DescriptionActionsGraphical viewLength
Mutagenesisi165R → C: Increased channel activity, leading to permanently increased cytoplasmic Ca(2+) levels. Increased activation by calcium, and increased ryanodine binding. 1 Publication1
Mutagenesisi4895I → T: Causes paralysis and perinatal death in homozygous mice, apparently due to asphyxia. Mutant mice have greatly reduced and amorphous skeletal muscle. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL2133.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004155661 – 5035Ryanodine receptor 1Add BLAST5035

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1339PhosphoserineBy similarity1
Modified residuei2346PhosphoserineBy similarity1
Modified residuei2844Phosphoserine; by PKA and PKGCombined sources2 Publications1
Modified residuei3636S-nitrosocysteineBy similarity1
Modified residuei4464PhosphothreonineBy similarity1
Modified residuei4468PhosphoserineBy similarity1
Modified residuei4861PhosphotyrosineBy similarity1
Modified residuei4864PhosphoserineBy similarity1

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-2844.2 Publications
Activated by reversible S-nitrosylation (By similarity). Repeated very high-level exercise increases S-nitrosylation.By similarity1 Publication

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiE9PZQ0.
PaxDbiE9PZQ0.
PeptideAtlasiE9PZQ0.
PRIDEiE9PZQ0.

PTM databases

iPTMnetiE9PZQ0.
PhosphoSitePlusiE9PZQ0.

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

BgeeiENSMUSG00000030592.
ExpressionAtlasiE9PZQ0. baseline and differential.
GenevisibleiE9PZQ0. MM.

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). Interacts with SEPN1 (By similarity).By similarity2 Publications

Binary interactionsi

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

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • protease binding Source: UniProtKB

Protein-protein interaction databases

DIPiDIP-29705N.
IntActiE9PZQ0. 28 interactors.
STRINGi10090.ENSMUSP00000137123.

Chemistry databases

BindingDBiE9PZQ0.

Structurei

3D structure databases

ProteinModelPortaliE9PZQ0.
SMRiE9PZQ0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini99 – 154MIR 1PROSITE-ProRule annotationAdd BLAST56
Domaini161 – 206MIR 2PROSITE-ProRule annotationAdd BLAST46
Domaini212 – 266MIR 3PROSITE-ProRule annotationAdd BLAST55
Domaini272 – 329MIR 4PROSITE-ProRule annotationAdd BLAST58
Domaini337 – 394MIR 5PROSITE-ProRule annotationAdd BLAST58
Domaini583 – 799B30.2/SPRY 1PROSITE-ProRule annotationAdd BLAST217
Repeati843 – 9561Add BLAST114
Repeati957 – 10702Add BLAST114
Domaini1015 – 1210B30.2/SPRY 2PROSITE-ProRule annotationAdd BLAST196
Repeati1346 – 13613; truncatedAdd BLAST16
Domaini1359 – 1572B30.2/SPRY 3PROSITE-ProRule annotationAdd BLAST214
Repeati1374 – 13894; truncatedAdd BLAST16
Repeati2727 – 28465Add BLAST120
Repeati2847 – 29606Add BLAST114

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni843 – 29606 X approximate repeatsAdd BLAST2118
Regioni3615 – 3644Interaction with CALMBy similarityAdd BLAST30

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1869 – 2089Glu-richAdd BLAST221
Compositional biasi3683 – 3762Glu-richAdd BLAST80
Compositional biasi4459 – 4525Pro-richAdd BLAST67

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.PROSITE-ProRule annotation
Contains 5 MIR domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2243. Eukaryota.
ENOG410YCNW. LUCA.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000231428.
HOVERGENiHBG102939.
InParanoidiE9PZQ0.
KOiK04961.
OMAiWSYSAVQ.
OrthoDBiEOG091G00T0.
TreeFamiTF315244.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.25.10.30. 2 hits.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
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.
IPR033215. RyR1.
IPR003877. SPRY_dom.
[Graphical view]
PANTHERiPTHR13715. PTHR13715. 6 hits.
PTHR13715:SF15. PTHR13715:SF15. 6 hits.
PfamiPF13833. EF-hand_8. 1 hit.
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]
PRINTSiPR00795. RYANODINER.
SMARTiSM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMiSSF100909. SSF100909. 2 hits.
SSF47473. SSF47473. 1 hit.
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

« Hide

        10         20         30         40         50
MGDGGGEGED EVQFLRTDDE VVLQCSATVL KEQLKLCLAA EGFGNRLCFL
60 70 80 90 100
EPTSNAQNVP PDLAICCFIL EQSLSVRALQ EMLANTVEAG VESSQGGGHR
110 120 130 140 150
TLLYGHAILL RHAHSRMYLS CLTTSRSMTD KLAFDVGLQE DATGEACWWT
160 170 180 190 200
MHPASKQRSE GEKVRVGDDL ILVSVSSERY LHLSTASGEL QVDASFMQTL
210 220 230 240 250
WNMNPICSGC EEGFVTGGHV LRLFHGHMDE CLTISPSDSD DQRRLVYYEG
260 270 280 290 300
GPVCTHARSL WRLEPLRISW SGSHLRWGQP LRIRHVTTGR YLGLTEDQGL
310 320 330 340 350
VVVDASKAHT KATSFCFRIS KEKLDVAPKR DVEGMGPPEI KYGESLCFVQ
360 370 380 390 400
HVASGLWLTY AAPDPKALRL GVLKKKAMLH QEGHMDDALS LTRCQQEESQ
410 420 430 440 450
AARMIYSTAG LYNQFIKGLD SFSGKPRGSG PPAGSALPIE GVILSLQDLI
460 470 480 490 500
GYFEPPSEEL QHEEKQTKLR SLRNRQSLFQ EEGMLSLVLN CIDRLNVYTT
510 520 530 540 550
AAHFAEFAGE EAAESWKEIV NLLYELLASL IRGNRTNCAL FSTNLDWLVS
560 570 580 590 600
KLDRLEASSG ILEVLYCVLI ESPEVLNIIQ ENHIKSIISL LDKHGRNHKV
610 620 630 640 650
LDVLCSLCVC NGVAVRSNQD LITENLLPGR ELLLQTNLIN YVTSIRPNIF
660 670 680 690 700
VGRAEGSTQY GKWYFEVMVD EVAPFLTAQA THLRVGWALS EGYSPYPGGG
710 720 730 740 750
EGWGGNGVGD DLYSYGFDGL HLWTGHVARP VTSPGQHLLA PEDVVSCCLD
760 770 780 790 800
LSVPSISFRI NGCPVQGVFE SFNLDGLFFP VVSFSAGIKV RFLLGGRHGE
810 820 830 840 850
FKFLPPPGYA PCHEAVLPRE RLHLQPIKEY RREGPRGPHL VGPSRCLSHL
860 870 880 890 900
DFVPCPVDTI QIVLPPHLER IREKLAENIH ELWALTRIEQ GWTYGPVRDD
910 920 930 940 950
NKRLHPCLVN FHSLPEPERN YNLQMSGETL KTLLALGCHV GMADEKAEDN
960 970 980 990 1000
LKKTKLPKTY MMSNGYKPAP LDLSHVRLTP AQTTLVDRLA ENGHNVWARD
1010 1020 1030 1040 1050
RVAQGWSYSA VQDIPARRNP RLVPYRLLDE ATKRSNRDSL CQAVRTLLGY
1060 1070 1080 1090 1100
GYNIEPPDQE PSQVDSQSRG DRARIFRAEK SYAVQSGRWY FEFEAVTTGE
1110 1120 1130 1140 1150
MRVGWARPEL RPDVELGADD LAYVFNGHRG QRWHLGSEPF GRPWQSGDVV
1160 1170 1180 1190 1200
GCMIDLTENT IIFTLNGEVL MSDSGSETAF RDIEIGDGFL PVCSLGPGQV
1210 1220 1230 1240 1250
GHLNLGQDVS SLRFFAICGL QEGFEPFAIN MQRPVTTWFS KSLPQFEPVP
1260 1270 1280 1290 1300
LEHPHYEVAR MDGTVDTPPC LRLTHRTWGS QNSLVEMLFL RLSLPVQFHQ
1310 1320 1330 1340 1350
HFRCTAGATP LASPGLQPPA EDEARAAEPD TDYENLRRSA GGWGEAEGGK
1360 1370 1380 1390 1400
DGTAKEGTPG GTAQAGVEAQ PARAENEKDA TTEKNKKRGF LFKAKKVAMM
1410 1420 1430 1440 1450
TQPPSTPALP RLPRDVVPAD NRDDPEIILN TTTYYYSVRV FAGQEPSCVW
1460 1470 1480 1490 1500
VGWVTPDYHQ HDMSFDLSKV RAVTVTMGDE QGNVHSSLKC SNCYMVWGGD
1510 1520 1530 1540 1550
FVSPGQQGRI SHTDLVIGCL VDLATGLMTF TANGKESNTF FQVEPNTKLF
1560 1570 1580 1590 1600
PAVFVLPTHQ NVVQFELGKQ KNIMPLSAAM FLSERKNPAP QCPPRLEVQM
1610 1620 1630 1640 1650
LMPVSWSRMP NHFLQVDTRR AGERLGWAVQ CQEPLMMMAL HIPEENRCMD
1660 1670 1680 1690 1700
ILELSERLDL QRFHSHTLSL YRSVCALGNN RVAHALCSHV DQAQLLHALE
1710 1720 1730 1740 1750
DARLPGPLRA GYYDLLISIH LESACRSRRS MLSEYIVPLT PETRAITLFP
1760 1770 1780 1790 1800
PGRSAEDGPR RHGLPGVGVT TSLRPPHHFS PPCFVVALPA AGATEAPARL
1810 1820 1830 1840 1850
SPAIPLEALR DKALRMLGEA VRDGGQHARD PVGGSVEFQF VPVLKLVSTL
1860 1870 1880 1890 1900
LVMGVFSDED VKQILKMIEP EVFREEEEVE EEGEEEEEDE EEKEEDEEEE
1910 1920 1930 1940 1950
AHEKEDEEKE EAEDAAEEEK EELEEGLLQM KLPESVKLQM CHLLEYFCDQ
1960 1970 1980 1990 2000
ELQHRVESLA AFAECYVDKM QGNQRGRYGL LMKAFTMSAA ETARRTREFR
2010 2020 2030 2040 2050
SPPQEQINML LHFKNGADEE ECPLPEEIRQ ELVNFHQDLL AHCGIQLEGE
2060 2070 2080 2090 2100
EEEPEEESTL GSRLMSLLEK VKLVKKTEEK PEEEPAPEEH KPQSLQELVS
2110 2120 2130 2140 2150
HTVVRWAQED FVQSPELVRA MFSLLHRQYD GLGELLRALP RAYTISVSSV
2160 2170 2180 2190 2200
EDTMSLLECL GQIRSLLIVQ MGPQEENLMI QSIGNIMNNK VFYQHPNLMR
2210 2220 2230 2240 2250
ALGMHETVME VMVNVLGGGE SKEIRFPKMV TSCCRFLCYF CRISRQNQRS
2260 2270 2280 2290 2300
MFDHLSYLLE NSGIGLGMQG STPLDVAAAS VIDNNELALA LQEQDLEKVV
2310 2320 2330 2340 2350
SYLAGCGLQS CPMLLAKGYP DIGWNPCGGE RYLDFLRFAV FVNGESVEEN
2360 2370 2380 2390 2400
ANVVVRLLIR KPECFGPALR GEGGSGLLAA IEEAIRISED PARDGPGVRR
2410 2420 2430 2440 2450
DRRREHFGEE PPEENRVHLG HAIMSFYAAL IDLLGRCAPE THLIQAGKGE
2460 2470 2480 2490 2500
ALRIRAILRS LVPLDDLVGI ISLPLQIPTL GKDGALVQPK MSASFVPDHK
2510 2520 2530 2540 2550
ASMVLFLDRV YGIENQDFLL HVLDVGFLPD MRAAASLDTA TFSTTEMALA
2560 2570 2580 2590 2600
LNRYLCLAVL PLITKCAPLF AGTEHRAIMV DSMLHTVYRL SRGRSLTKAQ
2610 2620 2630 2640 2650
RDVIEDCLMA LCRYIRPSML QHLLRRLVFD VPILNEFAKM PLKLLTNHYE
2660 2670 2680 2690 2700
RCWKYYCLPT GWANFGVTSE EELHLTRKLF WGIFDSLAHK KYDQELYRIA
2710 2720 2730 2740 2750
MPCLCAIAGA LPPDYVDASY SSKTEKKATV DAEGNFDPRP VETLNVIIPE
2760 2770 2780 2790 2800
KLDSFINKFA EYTHEKWAFD KIQNNWSYGE NIDEELKTHP MLRPYKTFSE
2810 2820 2830 2840 2850
KDKEIYRWPI KESLKAMIAW EWTVEKAREG EEEKTEKKKT RKISQTAQTY
2860 2870 2880 2890 2900
DPREGYNPQP PDLSVVTLSR ELQAMAEQLA ENYHNTWGRK KKQELEAKGG
2910 2920 2930 2940 2950
GSHPLLVPYD TLTAKEKARD REKAQELLKF LQMNGYAVTR GLKDMELDTS
2960 2970 2980 2990 3000
SIEKRFAFGF LQQLLRWMDI SQEFIAHLEA VVSSGRVEKS PHEQEIKFFA
3010 3020 3030 3040 3050
KILLPLINQY FTNHCLYFLS TPAKVLGSGG HASNKEKEMI TSLFCKLAAL
3060 3070 3080 3090 3100
VRHRVSLFGT DAPAVVNCLH ILARSLDART VMKSGPEIVK AGLRSFFESA
3110 3120 3130 3140 3150
SEDIEKMVEN LRLGKVSQAR TQVKGVGQNL TYTTVALLPV LTTLFQHIAQ
3160 3170 3180 3190 3200
HQFGDDVILD DVQVSCYRTL CSIYSLGTTR NPYVEKLRPA LGECLARLAA
3210 3220 3230 3240 3250
AMPVAFLEPE LNEYNACSVY TTKSPRERAI LGLPNSVEEM CPDIPVLERL
3260 3270 3280 3290 3300
MAEIGGLAES GARYTEMPHV IEITLPMLCS YLPRWWERGP EAPPPALPAG
3310 3320 3330 3340 3350
APPPCTAVTS DHLNSLLGNI LRIIVNNLGI DEASWMKRLA VFAQPIVSRA
3360 3370 3380 3390 3400
RPELLRSHFI PTIGRLRKRA GKVVAEEEQL RLEAKAEAEE GELLVRDEFS
3410 3420 3430 3440 3450
VLCRDLYALY PLLIRYVDNN RAHWLTEPNP NAEELFRMVG EIFIYWSKSH
3460 3470 3480 3490 3500
NFKREEQNFV VQNEINNMSF LTADNKSKMA KAGDVQSGGS DQERTKKKRR
3510 3520 3530 3540 3550
GDRYSVQTSL IVATLKKMLP IGLNMCAPTD QDLIVLAKAR YALKDTDEEV
3560 3570 3580 3590 3600
REFLQNNLNL QGKVEGSPSL RWQMALYRGV PGREEDADDP EKIVRRVQEV
3610 3620 3630 3640 3650
SAVLYHLDQT EHPYKSKKAV WHKLLSKQRR RAVVACFRMT PLYNLPTHRA
3660 3670 3680 3690 3700
CNMFLESYKA SWILTEDHSF EDRMIDDLSK AGEQEEEEEE VEEKKPDPLH
3710 3720 3730 3740 3750
QLVLHFSRTA LTEKSKLDED YLYMAYADIM AKSCHLEEGG ENGEEGGEEE
3760 3770 3780 3790 3800
EVEVSFEEKE MEKQRLLYQQ SRLHNRGAAE MVLQMISACK GETGAMVSST
3810 3820 3830 3840 3850
LKLGISILNG GNAEVQQKML DYLKDKKEVG FFQSIQALMQ TCSVLDLNAF
3860 3870 3880 3890 3900
ERQNKAEGLG MVNEDGTVIN RQNGEKVMAD DEFTQDLFRF LQLLCEGHNN
3910 3920 3930 3940 3950
DFQNYLRTQT GNTTTINIII CTVDYLLRLQ ESISDFYWYY SGKDVIEEQG
3960 3970 3980 3990 4000
KRNFSKAMSV AKQVFNSLTE YIQGPCTGNQ QSLAHSRLWD AVVGFLHVFA
4010 4020 4030 4040 4050
HMMMKLAQDS SQIELLKELL DLQKDMVVML LSLLEGNVVN GMIARQMVDM
4060 4070 4080 4090 4100
LVESSSNVEM ILKFFDMFLK LKDIVGSEAF QDYVTDPRGL ISKKDFQKAM
4110 4120 4130 4140 4150
DSQKQFTGPE IQFLLSCSEA DENEMINCEE FANRFQEPAR DIGFNVAVLL
4160 4170 4180 4190 4200
TNLSEHVPHD PRLRNFLELA ESILEYFRPY LGRIEIMGAS RRIERIYFEI
4210 4220 4230 4240 4250
SETNRAQWEM PQVKESKRQF IFDVVNEGGE SEKMEMFVSF CEDTIFEMQI
4260 4270 4280 4290 4300
AAQISEPEGE PEEDEDEGAE EAEEGAAGSD GSGSAAAAGV WVWLAATAGR
4310 4320 4330 4340 4350
TLRGLSYRSL RRRVRRLRRL TAREAATAVA ALLWALVTRA GGAGAGAAAG
4360 4370 4380 4390 4400
ALRLLWGSLF GGGLVDSAKK VTVTELLAGM PDPTGDEVHG QQPSGAGSDA
4410 4420 4430 4440 4450
EGEGEGEGEG DAADGAGDEE AAADQAGTGG ADGAVAVADG SPFRPEGAGG
4460 4470 4480 4490 4500
LGDMGDTTPV EPPTPEGSPI LKRKLGVDGE EEEPPPEPEP EPEPEPEKAD
4510 4520 4530 4540 4550
TENGEKEVPE PPPEPPKKTP PPPPPKKEEA GGAGLEEFWG ELEVQRVKFL
4560 4570 4580 4590 4600
NYLSRNFYTL RFLALFLAFA INFILLFYKV SDSPPGEDDI EGSGAGDMSG
4610 4620 4630 4640 4650
AGSGDGSGWG SRAGEEVEGD EDENMVYYFL EESTGYMEPA LRCLSLLHTL
4660 4670 4680 4690 4700
VAFLCIIGYN CLKVPLVIFK REKELARKLE FDGLYITEQP EDDDVKGQWD
4710 4720 4730 4740 4750
RLVLNTPSFP SNYWDKFVKR KVLDKHGDIF GRERIAELLG MDLASLEITA
4760 4770 4780 4790 4800
HNERKPDPPP GLLTWIMSID VKYQIWKFGV IFTDNSFLYL GWYMVMSLLG
4810 4820 4830 4840 4850
HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYLYT
4860 4870 4880 4890 4900
VVAFNFFRKF YNKSEDEDEP DMKCDDMMTC YLFHMYVGVR AGGGIGDEIE
4910 4920 4930 4940 4950
DPAGDEYELY RVVFDITFFF FVIVILLAII QGLIIDAFGE LRDQQEQVKE
4960 4970 4980 4990 5000
DMETKCFICG IGSDYFDTTP HGFETHTLEE HNLANYMFFL MYLINKDETE
5010 5020 5030
HTGQESYVWK MYQERCWDFF PAGDCFRKQY EDQLS
Length:5,035
Mass (Da):565,039
Last modified:April 5, 2011 - v1
Checksum:iD15D2E764B445573
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti616R → C in CAC34624 (Ref. 4) Curated1
Sequence conflicti1380A → S in AAP29981 (PubMed:18003898).Curated1
Sequence conflicti3484D → V in AAP29981 (PubMed:18003898).Curated1
Sequence conflicti4766I → L in AAA64955 (PubMed:7635066).Curated1
Sequence conflicti4821L → V in CAA58784 (PubMed:7876312).Curated1
Sequence conflicti4888G → A in CAA58784 (PubMed:7876312).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliE9PZQ0.
SMRiE9PZQ0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29705N.
IntActiE9PZQ0. 28 interactors.
STRINGi10090.ENSMUSP00000137123.

Chemistry databases

BindingDBiE9PZQ0.
ChEMBLiCHEMBL2133.

PTM databases

iPTMnetiE9PZQ0.
PhosphoSitePlusiE9PZQ0.

Proteomic databases

MaxQBiE9PZQ0.
PaxDbiE9PZQ0.
PeptideAtlasiE9PZQ0.
PRIDEiE9PZQ0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6261.
MGIiMGI:99659. Ryr1.

Phylogenomic databases

eggNOGiKOG2243. Eukaryota.
ENOG410YCNW. LUCA.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000231428.
HOVERGENiHBG102939.
InParanoidiE9PZQ0.
KOiK04961.
OMAiWSYSAVQ.
OrthoDBiEOG091G00T0.
TreeFamiTF315244.

Enzyme and pathway databases

ReactomeiR-MMU-2672351. Stimuli-sensing channels.
R-MMU-5578775. Ion homeostasis.

Miscellaneous databases

PROiE9PZQ0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000030592.
ExpressionAtlasiE9PZQ0. baseline and differential.
GenevisibleiE9PZQ0. MM.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.25.10.30. 2 hits.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
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.
IPR033215. RyR1.
IPR003877. SPRY_dom.
[Graphical view]
PANTHERiPTHR13715. PTHR13715. 6 hits.
PTHR13715:SF15. PTHR13715:SF15. 6 hits.
PfamiPF13833. EF-hand_8. 1 hit.
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]
PRINTSiPR00795. RYANODINER.
SMARTiSM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMiSSF100909. SSF100909. 2 hits.
SSF47473. SSF47473. 1 hit.
SSF49899. SSF49899. 3 hits.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 59 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.