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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. ryanodine-sensitive calcium-release channel activity Source: UniProtKB
  6. 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 Curated; Multi-pass membrane protein Curated
Note: The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic.

GO - Cellular componenti

  1. cell cortex Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. I band 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
  11. T-tubule 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 1PRO_0000415566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2844 – 28441Phosphoserine; by PKA and PKG2 Publications
Modified residuei3636 – 36361S-nitrosocysteineBy similarity
Modified residuei4861 – 48611PhosphotyrosineBy similarity
Modified residuei4864 – 48641PhosphoserineBy 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-2844.2 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.
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

BgeeiE9PZQ0.
ExpressionAtlasiE9PZQ0. baseline and differential.
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).By similarity2 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.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 43234323CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini4939 – 503597CytoplasmicSequence AnalysisAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei4888 – 489710Pore-formingBy similarity

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4324 – 434421HelicalSequence AnalysisAdd
BLAST
Transmembranei4345 – 436521HelicalSequence AnalysisAdd
BLAST
Transmembranei4557 – 457721HelicalSequence AnalysisAdd
BLAST
Transmembranei4649 – 466921HelicalSequence AnalysisAdd
BLAST
Transmembranei4778 – 479821HelicalSequence AnalysisAdd
BLAST
Transmembranei4805 – 482521HelicalSequence AnalysisAdd
BLAST
Transmembranei4837 – 485721HelicalSequence AnalysisAdd
BLAST
Transmembranei4918 – 493821HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni843 – 296021186 X approximate repeatsAdd
BLAST
Regioni3615 – 364430Interaction with CALMBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1869 – 2089221Glu-richAdd
BLAST
Compositional biasi3683 – 376280Glu-richAdd
BLAST
Compositional biasi4459 – 452567Pro-richAdd
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.PROSITE-ProRule annotation
Contains 5 MIR domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00760000119152.
HOGENOMiHOG000231428.
HOVERGENiHBG102939.
InParanoidiE9PZQ0.
KOiK04961.
OMAiQCSATVL.
OrthoDBiEOG71K622.
TreeFamiTF315244.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
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.
IPR003877. SPRY_dom.
[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 [UniParc]FASTAAdd to Basket

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        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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti616 – 6161R → C in CAC34624. 1 PublicationCurated
Sequence conflicti1380 – 13801A → S in AAP29981. (PubMed:18003898)Curated
Sequence conflicti3484 – 34841D → V in AAP29981. (PubMed:18003898)Curated
Sequence conflicti4766 – 47661I → L in AAA64955. (PubMed:7635066)Curated
Sequence conflicti4821 – 48211L → V in CAA58784. (PubMed:7876312)Curated
Sequence conflicti4888 – 48881G → A in CAA58784. (PubMed:7876312)Curated

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 ENSGT00760000119152.
HOGENOMi HOG000231428.
HOVERGENi HBG102939.
InParanoidi E9PZQ0.
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

Bgeei E9PZQ0.
ExpressionAtlasi E9PZQ0. baseline and differential.
Genevestigatori Q62235.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProi IPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
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.
IPR003877. SPRY_dom.
[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: October 29, 2014
This is version 37 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