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E9PZQ0 (RYR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ryr1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length5035 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.4 Ref.9 Ref.11 Ref.12 Ref.13

Subunit structure

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). Ref.1 Ref.11

Subcellular location

Sarcoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein Probable. Note: The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic. Ref.1 Ref.10 Ref.13

Tissue specificity

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. Ref.7 Ref.9 Ref.12 Ref.13

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. Ref.10

Post-translational modification

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.

Disruption phenotype

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. Ref.4

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.

Sequence similarities

Belongs to the ryanodine receptor (TC 1.A.3.1) family. RYR1 subfamily. [View classification]

Contains 3 B30.2/SPRY domains.

Contains 5 MIR domains.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentMembrane
Sarcoplasmic reticulum
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Calmodulin-binding
   Molecular functionCalcium channel
Developmental protein
Ion channel
Ligand-gated ion channel
Receptor
   PTMPhosphoprotein
S-nitrosylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transport

Inferred from direct assay PubMed 12954602. Source: MGI

cellular response to caffeine

Inferred from mutant phenotype Ref.9. Source: UniProtKB

muscle contraction

Inferred from mutant phenotype Ref.4. Source: UniProtKB

ossification involved in bone maturation

Inferred from mutant phenotype Ref.1. Source: UniProtKB

outflow tract morphogenesis

Inferred from mutant phenotype Ref.1. Source: UniProtKB

regulation of muscle contraction

Traceable author statement PubMed 11784029. Source: MGI

release of sequestered calcium ion into cytosol

Inferred from mutant phenotype PubMed 12704193. Source: MGI

release of sequestered calcium ion into cytosol by sarcoplasmic reticulum

Inferred from mutant phenotype Ref.1. Source: UniProtKB

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

skeletal muscle fiber development

Inferred from mutant phenotype Ref.1. Source: UniProtKB

skin development

Inferred from mutant phenotype Ref.1. Source: UniProtKB

   Cellular_componentI band

Inferred from electronic annotation. Source: Ensembl

T-tubule

Inferred from direct assay PubMed 15536090PubMed 8943043. Source: MGI

cell cortex

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

junctional membrane complex

Inferred from direct assay PubMed 10444070. Source: MGI

membrane

Inferred from direct assay PubMed 12704193PubMed 7832748. Source: MGI

protein complex

Inferred from direct assay PubMed 18676612. Source: UniProtKB

sarcoplasmic reticulum

Inferred from direct assay PubMed 11784029PubMed 12954602PubMed 15536090PubMed 7832748PubMed 8943043. Source: MGI

sarcoplasmic reticulum membrane

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functioncalcium channel activity

Inferred from mutant phenotype Ref.1. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

enzyme binding

Inferred from physical interaction PubMed 19198614. Source: BHF-UCL

protease binding

Inferred from physical interaction PubMed 18676612. Source: UniProtKB

ryanodine-sensitive calcium-release channel activity

Inferred from mutant phenotype Ref.9. Source: UniProtKB

voltage-gated calcium channel activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 50355035Ryanodine receptor 1
PRO_0000415566

Regions

Topological domain1 – 43234323Cytoplasmic Potential
Transmembrane4324 – 434421Helical; Potential
Transmembrane4345 – 436521Helical; Potential
Transmembrane4557 – 457721Helical; Potential
Transmembrane4649 – 466921Helical; Potential
Transmembrane4778 – 479821Helical; Potential
Transmembrane4805 – 482521Helical; Potential
Transmembrane4837 – 485721Helical; Potential
Intramembrane4888 – 489710Pore-forming; By similarity
Transmembrane4918 – 493821Helical; Potential
Topological domain4939 – 503597Cytoplasmic Potential
Domain99 – 15456MIR 1
Domain161 – 20646MIR 2
Domain212 – 26655MIR 3
Domain272 – 32958MIR 4
Domain337 – 39458MIR 5
Domain583 – 799217B30.2/SPRY 1
Repeat843 – 9561141
Repeat957 – 10701142
Domain1015 – 1210196B30.2/SPRY 2
Repeat1346 – 1361163; truncated
Domain1359 – 1572214B30.2/SPRY 3
Repeat1374 – 1389164; truncated
Repeat2727 – 28461205
Repeat2847 – 29601146
Region843 – 296021186 X approximate repeats
Region3615 – 364430Interaction with CALM By similarity
Compositional bias1869 – 2089221Glu-rich
Compositional bias3683 – 376280Glu-rich
Compositional bias4459 – 452567Pro-rich

Amino acid modifications

Modified residue28441Phosphoserine; by PKA and PKG Ref.11 Ref.13
Modified residue36361S-nitrosocysteine By similarity
Modified residue48611Phosphotyrosine By similarity
Modified residue48641Phosphoserine By similarity

Experimental info

Mutagenesis1651R → C: Increased channel activity, leading to permanently increased cytoplasmic Ca(2+) levels. Increased activation by calcium, and increased ryanodine binding. Ref.13
Mutagenesis48951I → T: Causes paralysis and perinatal death in homozygous mice, apparently due to asphyxia. Mutant mice have greatly reduced and amorphous skeletal muscle. Ref.1
Sequence conflict6161R → C in CAC34624. Ref.5
Sequence conflict13801A → S in AAP29981. Ref.1
Sequence conflict34841D → V in AAP29981. Ref.1
Sequence conflict47661I → L in AAA64955. Ref.8
Sequence conflict48211L → V in CAA58784. Ref.7
Sequence conflict48881G → A in CAA58784. Ref.7

Sequences

Sequence LengthMass (Da)Tools
E9PZQ0 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: D15D2E764B445573

FASTA5,035565,039
        10         20         30         40         50         60 
MGDGGGEGED EVQFLRTDDE VVLQCSATVL KEQLKLCLAA EGFGNRLCFL EPTSNAQNVP 

        70         80         90        100        110        120 
PDLAICCFIL EQSLSVRALQ EMLANTVEAG VESSQGGGHR TLLYGHAILL RHAHSRMYLS 

       130        140        150        160        170        180 
CLTTSRSMTD KLAFDVGLQE DATGEACWWT MHPASKQRSE GEKVRVGDDL ILVSVSSERY 

       190        200        210        220        230        240 
LHLSTASGEL QVDASFMQTL WNMNPICSGC EEGFVTGGHV LRLFHGHMDE CLTISPSDSD 

       250        260        270        280        290        300 
DQRRLVYYEG GPVCTHARSL WRLEPLRISW SGSHLRWGQP LRIRHVTTGR YLGLTEDQGL 

       310        320        330        340        350        360 
VVVDASKAHT KATSFCFRIS KEKLDVAPKR DVEGMGPPEI KYGESLCFVQ HVASGLWLTY 

       370        380        390        400        410        420 
AAPDPKALRL GVLKKKAMLH QEGHMDDALS LTRCQQEESQ AARMIYSTAG LYNQFIKGLD 

       430        440        450        460        470        480 
SFSGKPRGSG PPAGSALPIE GVILSLQDLI GYFEPPSEEL QHEEKQTKLR SLRNRQSLFQ 

       490        500        510        520        530        540 
EEGMLSLVLN CIDRLNVYTT AAHFAEFAGE EAAESWKEIV NLLYELLASL IRGNRTNCAL 

       550        560        570        580        590        600 
FSTNLDWLVS KLDRLEASSG ILEVLYCVLI ESPEVLNIIQ ENHIKSIISL LDKHGRNHKV 

       610        620        630        640        650        660 
LDVLCSLCVC NGVAVRSNQD LITENLLPGR ELLLQTNLIN YVTSIRPNIF VGRAEGSTQY 

       670        680        690        700        710        720 
GKWYFEVMVD EVAPFLTAQA THLRVGWALS EGYSPYPGGG EGWGGNGVGD DLYSYGFDGL 

       730        740        750        760        770        780 
HLWTGHVARP VTSPGQHLLA PEDVVSCCLD LSVPSISFRI NGCPVQGVFE SFNLDGLFFP 

       790        800        810        820        830        840 
VVSFSAGIKV RFLLGGRHGE FKFLPPPGYA PCHEAVLPRE RLHLQPIKEY RREGPRGPHL 

       850        860        870        880        890        900 
VGPSRCLSHL DFVPCPVDTI QIVLPPHLER IREKLAENIH ELWALTRIEQ GWTYGPVRDD 

       910        920        930        940        950        960 
NKRLHPCLVN FHSLPEPERN YNLQMSGETL KTLLALGCHV GMADEKAEDN LKKTKLPKTY 

       970        980        990       1000       1010       1020 
MMSNGYKPAP LDLSHVRLTP AQTTLVDRLA ENGHNVWARD RVAQGWSYSA VQDIPARRNP 

      1030       1040       1050       1060       1070       1080 
RLVPYRLLDE ATKRSNRDSL CQAVRTLLGY GYNIEPPDQE PSQVDSQSRG DRARIFRAEK 

      1090       1100       1110       1120       1130       1140 
SYAVQSGRWY FEFEAVTTGE MRVGWARPEL RPDVELGADD LAYVFNGHRG QRWHLGSEPF 

      1150       1160       1170       1180       1190       1200 
GRPWQSGDVV GCMIDLTENT IIFTLNGEVL MSDSGSETAF RDIEIGDGFL PVCSLGPGQV 

      1210       1220       1230       1240       1250       1260 
GHLNLGQDVS SLRFFAICGL QEGFEPFAIN MQRPVTTWFS KSLPQFEPVP LEHPHYEVAR 

      1270       1280       1290       1300       1310       1320 
MDGTVDTPPC LRLTHRTWGS QNSLVEMLFL RLSLPVQFHQ HFRCTAGATP LASPGLQPPA 

      1330       1340       1350       1360       1370       1380 
EDEARAAEPD TDYENLRRSA GGWGEAEGGK DGTAKEGTPG GTAQAGVEAQ PARAENEKDA 

      1390       1400       1410       1420       1430       1440 
TTEKNKKRGF LFKAKKVAMM TQPPSTPALP RLPRDVVPAD NRDDPEIILN TTTYYYSVRV 

      1450       1460       1470       1480       1490       1500 
FAGQEPSCVW VGWVTPDYHQ HDMSFDLSKV RAVTVTMGDE QGNVHSSLKC SNCYMVWGGD 

      1510       1520       1530       1540       1550       1560 
FVSPGQQGRI SHTDLVIGCL VDLATGLMTF TANGKESNTF FQVEPNTKLF PAVFVLPTHQ 

      1570       1580       1590       1600       1610       1620 
NVVQFELGKQ KNIMPLSAAM FLSERKNPAP QCPPRLEVQM LMPVSWSRMP NHFLQVDTRR 

      1630       1640       1650       1660       1670       1680 
AGERLGWAVQ CQEPLMMMAL HIPEENRCMD ILELSERLDL QRFHSHTLSL YRSVCALGNN 

      1690       1700       1710       1720       1730       1740 
RVAHALCSHV DQAQLLHALE DARLPGPLRA GYYDLLISIH LESACRSRRS MLSEYIVPLT 

      1750       1760       1770       1780       1790       1800 
PETRAITLFP PGRSAEDGPR RHGLPGVGVT TSLRPPHHFS PPCFVVALPA AGATEAPARL 

      1810       1820       1830       1840       1850       1860 
SPAIPLEALR DKALRMLGEA VRDGGQHARD PVGGSVEFQF VPVLKLVSTL LVMGVFSDED 

      1870       1880       1890       1900       1910       1920 
VKQILKMIEP EVFREEEEVE EEGEEEEEDE EEKEEDEEEE AHEKEDEEKE EAEDAAEEEK 

      1930       1940       1950       1960       1970       1980 
EELEEGLLQM KLPESVKLQM CHLLEYFCDQ ELQHRVESLA AFAECYVDKM QGNQRGRYGL 

      1990       2000       2010       2020       2030       2040 
LMKAFTMSAA ETARRTREFR SPPQEQINML LHFKNGADEE ECPLPEEIRQ ELVNFHQDLL 

      2050       2060       2070       2080       2090       2100 
AHCGIQLEGE EEEPEEESTL GSRLMSLLEK VKLVKKTEEK PEEEPAPEEH KPQSLQELVS 

      2110       2120       2130       2140       2150       2160 
HTVVRWAQED FVQSPELVRA MFSLLHRQYD GLGELLRALP RAYTISVSSV EDTMSLLECL 

      2170       2180       2190       2200       2210       2220 
GQIRSLLIVQ MGPQEENLMI QSIGNIMNNK VFYQHPNLMR ALGMHETVME VMVNVLGGGE 

      2230       2240       2250       2260       2270       2280 
SKEIRFPKMV TSCCRFLCYF CRISRQNQRS MFDHLSYLLE NSGIGLGMQG STPLDVAAAS 

      2290       2300       2310       2320       2330       2340 
VIDNNELALA LQEQDLEKVV SYLAGCGLQS CPMLLAKGYP DIGWNPCGGE RYLDFLRFAV 

      2350       2360       2370       2380       2390       2400 
FVNGESVEEN ANVVVRLLIR KPECFGPALR GEGGSGLLAA IEEAIRISED PARDGPGVRR 

      2410       2420       2430       2440       2450       2460 
DRRREHFGEE PPEENRVHLG HAIMSFYAAL IDLLGRCAPE THLIQAGKGE ALRIRAILRS 

      2470       2480       2490       2500       2510       2520 
LVPLDDLVGI ISLPLQIPTL GKDGALVQPK MSASFVPDHK ASMVLFLDRV YGIENQDFLL 

      2530       2540       2550       2560       2570       2580 
HVLDVGFLPD MRAAASLDTA TFSTTEMALA LNRYLCLAVL PLITKCAPLF AGTEHRAIMV 

      2590       2600       2610       2620       2630       2640 
DSMLHTVYRL SRGRSLTKAQ RDVIEDCLMA LCRYIRPSML QHLLRRLVFD VPILNEFAKM 

      2650       2660       2670       2680       2690       2700 
PLKLLTNHYE RCWKYYCLPT GWANFGVTSE EELHLTRKLF WGIFDSLAHK KYDQELYRIA 

      2710       2720       2730       2740       2750       2760 
MPCLCAIAGA LPPDYVDASY SSKTEKKATV DAEGNFDPRP VETLNVIIPE KLDSFINKFA 

      2770       2780       2790       2800       2810       2820 
EYTHEKWAFD KIQNNWSYGE NIDEELKTHP MLRPYKTFSE KDKEIYRWPI KESLKAMIAW 

      2830       2840       2850       2860       2870       2880 
EWTVEKAREG EEEKTEKKKT RKISQTAQTY DPREGYNPQP PDLSVVTLSR ELQAMAEQLA 

      2890       2900       2910       2920       2930       2940 
ENYHNTWGRK KKQELEAKGG GSHPLLVPYD TLTAKEKARD REKAQELLKF LQMNGYAVTR 

      2950       2960       2970       2980       2990       3000 
GLKDMELDTS SIEKRFAFGF LQQLLRWMDI SQEFIAHLEA VVSSGRVEKS PHEQEIKFFA 

      3010       3020       3030       3040       3050       3060 
KILLPLINQY FTNHCLYFLS TPAKVLGSGG HASNKEKEMI TSLFCKLAAL VRHRVSLFGT 

      3070       3080       3090       3100       3110       3120 
DAPAVVNCLH ILARSLDART VMKSGPEIVK AGLRSFFESA SEDIEKMVEN LRLGKVSQAR 

      3130       3140       3150       3160       3170       3180 
TQVKGVGQNL TYTTVALLPV LTTLFQHIAQ HQFGDDVILD DVQVSCYRTL CSIYSLGTTR 

      3190       3200       3210       3220       3230       3240 
NPYVEKLRPA LGECLARLAA AMPVAFLEPE LNEYNACSVY TTKSPRERAI LGLPNSVEEM 

      3250       3260       3270       3280       3290       3300 
CPDIPVLERL MAEIGGLAES GARYTEMPHV IEITLPMLCS YLPRWWERGP EAPPPALPAG 

      3310       3320       3330       3340       3350       3360 
APPPCTAVTS DHLNSLLGNI LRIIVNNLGI DEASWMKRLA VFAQPIVSRA RPELLRSHFI 

      3370       3380       3390       3400       3410       3420 
PTIGRLRKRA GKVVAEEEQL RLEAKAEAEE GELLVRDEFS VLCRDLYALY PLLIRYVDNN 

      3430       3440       3450       3460       3470       3480 
RAHWLTEPNP NAEELFRMVG EIFIYWSKSH NFKREEQNFV VQNEINNMSF LTADNKSKMA 

      3490       3500       3510       3520       3530       3540 
KAGDVQSGGS DQERTKKKRR GDRYSVQTSL IVATLKKMLP IGLNMCAPTD QDLIVLAKAR 

      3550       3560       3570       3580       3590       3600 
YALKDTDEEV REFLQNNLNL QGKVEGSPSL RWQMALYRGV PGREEDADDP EKIVRRVQEV 

      3610       3620       3630       3640       3650       3660 
SAVLYHLDQT EHPYKSKKAV WHKLLSKQRR RAVVACFRMT PLYNLPTHRA CNMFLESYKA 

      3670       3680       3690       3700       3710       3720 
SWILTEDHSF EDRMIDDLSK AGEQEEEEEE VEEKKPDPLH QLVLHFSRTA LTEKSKLDED 

      3730       3740       3750       3760       3770       3780 
YLYMAYADIM AKSCHLEEGG ENGEEGGEEE EVEVSFEEKE MEKQRLLYQQ SRLHNRGAAE 

      3790       3800       3810       3820       3830       3840 
MVLQMISACK GETGAMVSST LKLGISILNG GNAEVQQKML DYLKDKKEVG FFQSIQALMQ 

      3850       3860       3870       3880       3890       3900 
TCSVLDLNAF ERQNKAEGLG MVNEDGTVIN RQNGEKVMAD DEFTQDLFRF LQLLCEGHNN 

      3910       3920       3930       3940       3950       3960 
DFQNYLRTQT GNTTTINIII CTVDYLLRLQ ESISDFYWYY SGKDVIEEQG KRNFSKAMSV 

      3970       3980       3990       4000       4010       4020 
AKQVFNSLTE YIQGPCTGNQ QSLAHSRLWD AVVGFLHVFA HMMMKLAQDS SQIELLKELL 

      4030       4040       4050       4060       4070       4080 
DLQKDMVVML LSLLEGNVVN GMIARQMVDM LVESSSNVEM ILKFFDMFLK LKDIVGSEAF 

      4090       4100       4110       4120       4130       4140 
QDYVTDPRGL ISKKDFQKAM DSQKQFTGPE IQFLLSCSEA DENEMINCEE FANRFQEPAR 

      4150       4160       4170       4180       4190       4200 
DIGFNVAVLL TNLSEHVPHD PRLRNFLELA ESILEYFRPY LGRIEIMGAS RRIERIYFEI 

      4210       4220       4230       4240       4250       4260 
SETNRAQWEM PQVKESKRQF IFDVVNEGGE SEKMEMFVSF CEDTIFEMQI AAQISEPEGE 

      4270       4280       4290       4300       4310       4320 
PEEDEDEGAE EAEEGAAGSD GSGSAAAAGV WVWLAATAGR TLRGLSYRSL RRRVRRLRRL 

      4330       4340       4350       4360       4370       4380 
TAREAATAVA ALLWALVTRA GGAGAGAAAG ALRLLWGSLF GGGLVDSAKK VTVTELLAGM 

      4390       4400       4410       4420       4430       4440 
PDPTGDEVHG QQPSGAGSDA EGEGEGEGEG DAADGAGDEE AAADQAGTGG ADGAVAVADG 

      4450       4460       4470       4480       4490       4500 
SPFRPEGAGG LGDMGDTTPV EPPTPEGSPI LKRKLGVDGE EEEPPPEPEP EPEPEPEKAD 

      4510       4520       4530       4540       4550       4560 
TENGEKEVPE PPPEPPKKTP PPPPPKKEEA GGAGLEEFWG ELEVQRVKFL NYLSRNFYTL 

      4570       4580       4590       4600       4610       4620 
RFLALFLAFA INFILLFYKV SDSPPGEDDI EGSGAGDMSG AGSGDGSGWG SRAGEEVEGD 

      4630       4640       4650       4660       4670       4680 
EDENMVYYFL EESTGYMEPA LRCLSLLHTL VAFLCIIGYN CLKVPLVIFK REKELARKLE 

      4690       4700       4710       4720       4730       4740 
FDGLYITEQP EDDDVKGQWD RLVLNTPSFP SNYWDKFVKR KVLDKHGDIF GRERIAELLG 

      4750       4760       4770       4780       4790       4800 
MDLASLEITA HNERKPDPPP GLLTWIMSID VKYQIWKFGV IFTDNSFLYL GWYMVMSLLG 

      4810       4820       4830       4840       4850       4860 
HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYLYT VVAFNFFRKF 

      4870       4880       4890       4900       4910       4920 
YNKSEDEDEP DMKCDDMMTC YLFHMYVGVR AGGGIGDEIE DPAGDEYELY RVVFDITFFF 

      4930       4940       4950       4960       4970       4980 
FVIVILLAII QGLIIDAFGE LRDQQEQVKE DMETKCFICG IGSDYFDTTP HGFETHTLEE 

      4990       5000       5010       5020       5030 
HNLANYMFFL MYLINKDETE HTGQESYVWK MYQERCWDFF PAGDCFRKQY EDQLS 

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References

« Hide 'large scale' references
[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]Erratum
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. 105:825-825(2008)
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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.
[5]"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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI48741.
I58087.
I78376.
I78377.
S56105.
RefSeqNP_033135.2. NM_009109.2.
UniGeneMm.439745.

3D structure databases

ProteinModelPortalE9PZQ0.
SMRE9PZQ0. Positions 13-535, 2735-2941, 3615-3641.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29705N.
IntActE9PZQ0. 27 interactions.
STRING10090.ENSMUSP00000032813.

Chemistry

BindingDBE9PZQ0.
ChEMBLCHEMBL2133.

PTM databases

PhosphoSiteE9PZQ0.

Proteomic databases

PRIDEE9PZQ0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000179893; ENSMUSP00000137123; ENSMUSG00000030592.
GeneID20190.
KEGGmmu:20190.
UCSCuc009gao.1. mouse.

Organism-specific databases

CTD6261.
MGIMGI:99659. Ryr1.

Phylogenomic databases

GeneTreeENSGT00690000101961.
HOGENOMHOG000231428.
HOVERGENHBG102939.
KOK04961.
OMAQCSATVL.
OrthoDBEOG71K622.
TreeFamTF315244.

Gene expression databases

ArrayExpressE9PZQ0.
BgeeE9PZQ0.
GenevestigatorQ62235.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProIPR001870. 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]
PANTHERPTHR13715. PTHR13715. 1 hit.
PfamPF08709. 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]
PRINTSPR00795. RYANODINER.
SMARTSM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMSSF100909. SSF100909. 2 hits.
SSF49899. SSF49899. 3 hits.
SSF82109. SSF82109. 2 hits.
PROSITEPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio297735.
PROE9PZQ0.
SOURCESearch...

Entry information

Entry nameRYR1_MOUSE
AccessionPrimary (citable) accession number: E9PZQ0
Secondary accession number(s): Q60834 expand/collapse secondary AC list , Q61779, Q61780, Q62173, Q62196, Q62235, Q78EJ6, Q7TNG1, Q80UQ5, Q80X16, Q99JF9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: April 5, 2011
Last modified: April 16, 2014
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot