E9PZQ0 (RYR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Ryr1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	5035 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Calcium transport Ion transport Transport
Cellular component	Membrane Sarcoplasmic reticulum
Domain	Repeat Transmembrane Transmembrane helix
Ligand	Calcium Calmodulin-binding
Molecular function	Calcium channel Developmental protein Ion channel Ligand-gated ion channel Receptor
PTM	Phosphoprotein S-nitrosylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 by sarcoplasmic reticulum Inferred from mutant phenotype Ref.1. Source: UniProtKB response to hypoxia Inferred from electronic annotation. Source: Compara skeletal muscle fiber development Inferred from mutant phenotype Ref.1. Source: UniProtKB skin development Inferred from mutant phenotype Ref.1. Source: UniProtKB
Cellular_component	I band Inferred from electronic annotation. Source: Compara T-tubule Inferred from direct assay PubMed 15536090PubMed 8943043. Source: MGI cell cortex Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW junctional membrane complex Inferred from direct assay PubMed 10444070. Source: MGI sarcoplasmic reticulum membrane Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro 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

With	Entry	#Exp.	IntAct	Notes
Bsg	O55108	3	EBI-642079,EBI-643315
Camlg	P49070	3	EBI-642079,EBI-309114

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 5035	5035	Ryanodine receptor 1		PRO_0000415566
Regions
	Topological domain	1 – 4323	4323	Cytoplasmic Potential
	Transmembrane	4324 – 4344	21	Helical; Potential
	Transmembrane	4345 – 4365	21	Helical; Potential
	Transmembrane	4557 – 4577	21	Helical; Potential
	Transmembrane	4649 – 4669	21	Helical; Potential
	Transmembrane	4778 – 4798	21	Helical; Potential
	Transmembrane	4805 – 4825	21	Helical; Potential
	Transmembrane	4837 – 4857	21	Helical; Potential
	Intramembrane	4888 – 4897	10	Pore-forming; By similarity
	Transmembrane	4918 – 4938	21	Helical; Potential
	Topological domain	4939 – 5035	97	Cytoplasmic Potential
	Domain	99 – 154	56	MIR 1
	Domain	161 – 206	46	MIR 2
	Domain	212 – 266	55	MIR 3
	Domain	272 – 329	58	MIR 4
	Domain	337 – 394	58	MIR 5
	Domain	583 – 799	217	B30.2/SPRY 1
	Repeat	843 – 956	114	1
	Repeat	957 – 1070	114	2
	Domain	1015 – 1210	196	B30.2/SPRY 2
	Repeat	1346 – 1361	16	3; truncated
	Domain	1359 – 1572	214	B30.2/SPRY 3
	Repeat	1374 – 1389	16	4; truncated
	Repeat	2727 – 2846	120	5
	Repeat	2847 – 2960	114	6
	Region	843 – 2960	2118	6 X approximate repeats
	Region	3615 – 3644	30	Interaction with CALM By similarity
	Compositional bias	1869 – 2089	221	Glu-rich
	Compositional bias	3683 – 3762	80	Glu-rich
	Compositional bias	4459 – 4525	67	Pro-rich
Amino acid modifications
	Modified residue	2844	1	Phosphoserine; by PKA and PKG Ref.11 Ref.13
	Modified residue	3636	1	S-nitrosocysteine By similarity
	Modified residue	4861	1	Phosphotyrosine By similarity
	Modified residue	4864	1	Phosphoserine By similarity
Experimental info
	Mutagenesis	165	1	R → C: Increased channel activity, leading to permanently increased cytoplasmic Ca(2+) levels. Increased activation by calcium, and increased ryanodine binding. Ref.13
	Mutagenesis	4895	1	I → 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 conflict	616	1	R → C in CAC34624. Ref.5
	Sequence conflict	1380	1	A → S in AAP29981. Ref.1
	Sequence conflict	3484	1	D → V in AAP29981. Ref.1
	Sequence conflict	4766	1	I → L in AAA64955. Ref.8
	Sequence conflict	4821	1	L → V in CAA58784. Ref.7
	Sequence conflict	4888	1	G → A in CAA58784. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	E9PZQ0 [UniParc]. Last modified April 5, 2011. Version 1. Checksum: D15D2E764B445573	FASTA	5,035	565,039
	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

References

	« Hide 'large scale' referencesShow '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. , 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(2011) [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.
IPI	IPI00622912.
PIR	I48741. I58087. I78376. I78377. S56105.
RefSeq	NP_033135.2. NM_009109.2.
UniGene	Mm.439745.
3D structure databases
ProteinModelPortal	E9PZQ0.
SMR	E9PZQ0. Positions 13-533, 2735-2941, 3615-3641.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29705N.
IntAct	E9PZQ0. 25 interactions.
STRING	10090.ENSMUSP00000032813.
PTM databases
PhosphoSite	E9PZQ0.
Proteomic databases
PRIDE	E9PZQ0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000179893; ENSMUSP00000137123; ENSMUSG00000030592.
GeneID	20190.
KEGG	mmu:20190.
Organism-specific databases
CTD	6261.
MGI	MGI:99659. Ryr1.
Phylogenomic databases
GeneTree	ENSGT00690000101961.
HOGENOM	HOG000231428.
HOVERGEN	HBG102939.
KO	K04961.
OMA	TENTIIF.
Gene expression databases
ArrayExpress	E9PZQ0.
Bgee	E9PZQ0.
Genevestigator	Q62235.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR001870. B30.2/SPRY. IPR000699. Ca-rel_channel. IPR008985. ConA-like_lec_gl_sf. IPR011992. EF-hand-like_dom. IPR014821. Ins145_P3_rcpt. IPR005821. Ion_trans_dom. IPR016093. MIR_motif. IPR013662. RIH_assoc-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]
PANTHER	PTHR13715. PTHR13715. 1 hit.
Pfam	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]
PRINTS	PR00795. RYANODINER.
SMART	SM00472. MIR. 4 hits. SM00449. SPRY. 3 hits. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 3 hits. SSF82109. MIR. 1 hit.
PROSITE	PS50188. B302_SPRY. 3 hits. PS50919. MIR. 5 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	E9PZQ0.
ChEMBL	CHEMBL2133.
NextBio	297735.
SOURCE	Search...

Entry information

Entry name

RYR1_MOUSE

Accession

Primary (citable) accession number: E9PZQ0
Secondary accession number(s): Q60834 , 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:	May 1, 2013
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program