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Protein

Ryanodine receptor 1

Gene

RYR1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: -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 (PubMed:3722165, PubMed:10388749, PubMed:10097181, PubMed:12732639, PubMed:22036948, PubMed:26245150, PubMed:27662087). Repeated very high-level exercise increases the open probability of the channel and leads to Ca2+ leaking into the cytoplasm (By similarity). 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 (By similarity).By similarity3 Publications4 Publications

Miscellaneous

Coexpression of normal and mutant Thr-4897 RYR1 in a 1:1 ratio produces RYR1 channels with normal halothane and caffeine sensitivities, but maximal levels of Ca2+ release are reduced by 67%. Binding of [3H]ryanodine indicates that the heterozygous channel is activated by Ca2+ concentrations 4-fold lower than normal. Single-cell analysis of cotransfected cells shows a significantly increased resting cytoplasmic Ca2+ level and a significantly reduced luminal Ca2+ level. These data indicated a leaky channel, possibly caused by a reduction in the Ca2+ concentration required for channel activation.1 Publication

Activity regulationi

Channel activity is modulated by the alkaloid ryanodine that binds to the open Ca-release channel with high affinity (PubMed:27662087). At low concentrations, ryanodine maintains the channel in an open conformation (PubMed:27662087). High ryanodine concentrations inhibit channel activity (PubMed:27662087). Channel activity is regulated by calmodulin (CALM). The calcium release is activated by increased cytoplasmic calcium levels, by nitric oxyde (NO), caffeine and ATP (PubMed:12732639, PubMed:22036948, PubMed:26245150, PubMed:27662087). Channel activity is inhibited by magnesium ions, possibly by competition for calcium binding sites (PubMed:12732639).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi3893CalciumCombined sources1 Publication1
Metal bindingi3967CalciumCombined sources1 Publication1
Binding sitei4716CaffeineCombined sources1 Publication1
Metal bindingi5001Calcium; via carbonyl oxygenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi4211 – 4215ATPCombined sources1 Publication5
Nucleotide bindingi4954 – 4959ATPCombined sources1 Publication6
Nucleotide bindingi4979 – 4985ATPCombined sources1 Publication7

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionCalcium channel, Calmodulin-binding, Developmental protein, Ion channel, Ligand-gated ion channel, Receptor
Biological processCalcium transport, Ion transport, Transport
LigandATP-binding, Calcium, Metal-binding, Nucleotide-binding

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
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 4558Cytoplasmic4 PublicationsAdd BLAST4558
Transmembranei4559 – 4579Helical; Name=14 PublicationsAdd BLAST21
Topological domaini4580 – 4640Lumenal4 PublicationsAdd BLAST61
Transmembranei4641 – 4661Helical; Name=24 PublicationsAdd BLAST21
Topological domaini4662 – 4779Cytoplasmic4 PublicationsAdd BLAST118
Transmembranei4780 – 4802Helical; Name=34 PublicationsAdd BLAST23
Topological domaini4803Lumenal4 Publications1
Transmembranei4804 – 4820Helical; Name=44 PublicationsAdd BLAST17
Topological domaini4821 – 4835Cytoplasmic4 PublicationsAdd BLAST15
Transmembranei4836 – 4856Helical; Name=54 PublicationsAdd BLAST21
Topological domaini4857 – 4879Lumenal4 PublicationsAdd BLAST23
Intramembranei4880 – 4899Pore-forming4 PublicationsAdd BLAST20
Topological domaini4900 – 4919Lumenal4 PublicationsAdd BLAST20
Transmembranei4920 – 4940Helical; Name=64 PublicationsAdd BLAST21
Topological domaini4941 – 5037Cytoplasmic4 PublicationsAdd BLAST97

Keywords - Cellular componenti

Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi164R → C: Decreases threshold for channel activation by K(+), caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg(2+). 1 Publication1
Mutagenesisi342G → R: Decreases threshold for channel activation by K(+), caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg(2+). 1 Publication1
Mutagenesisi615R → C: Decreases threshold for channel activation by K(+), caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg(2+). 1 Publication1
Mutagenesisi674 – 675FL → AA: Loss of interaction with FKBP1A. 1 Publication2
Mutagenesisi760N → D: Impairs interaction with FKBP1A. 1 Publication1
Mutagenesisi1044R → C: Decreases protein stability. 1 Publication1
Mutagenesisi1050G → S: Decreases protein stability. 1 Publication1
Mutagenesisi1076R → W: Decreases protein stability. 1 Publication1
Mutagenesisi2163R → C: Decreases threshold for channel activation by K(+), caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg(2+). 1 Publication1
Mutagenesisi2168V → M: Decreases threshold for channel activation by K(+), caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg(2+). 1 Publication1
Mutagenesisi2458R → H: Decreases threshold for channel activation by K(+), caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg(2+). 1 Publication1
Mutagenesisi2461V → G: Impairs interaction with FKBP1A. 1 Publication1
Mutagenesisi2867L → G: Decreases protein stability. 1 Publication1
Mutagenesisi3635C → A: Abolishes S-nitrosocysteine formation. 2 Publications1
Mutagenesisi4825T → I: Decreases threshold for channel activation by K(+), caffeine and 4-chloro-m-cresol. Decreases inhibition by Mg(2+). 1 Publication1
Mutagenesisi4897I → T: Loss of channel activation by halothane and caffeine due to Ca(2+) store depletion, probably due to constant Ca(2+) leakage through the mutant channel. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL3288

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002193601 – 5037Ryanodine receptor 1Add BLAST5037

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1338PhosphoserineBy similarity1
Modified residuei2345PhosphoserineBy similarity1
Modified residuei2843Phosphoserine; by PKA and PKG1 Publication1
Modified residuei3635S-nitrosocysteine3 Publications1
Modified residuei4466PhosphothreonineBy similarity1
Modified residuei4470PhosphoserineBy similarity1
Modified residuei4863PhosphotyrosineBy similarity1
Modified residuei4866PhosphoserineBy similarity1

Post-translational modificationi

The N-terminus is blocked.
Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2843 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2843.By similarity
Activated by reversible S-nitrosylation (PubMed:22036948). Repeated very high-level exercise increases S-nitrosylation (By similarity).By similarity1 Publication

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

PRIDEiP11716

PTM databases

iPTMnetiP11716
SwissPalmiP11716

Expressioni

Tissue specificityi

Detected in skeletal muscle (at protein level) (PubMed:2725677, PubMed:3722165, PubMed:25470059, PubMed:25517095, PubMed:27573175, PubMed:27468892). Fast- or slow-twitch skeletal muscle.8 Publications

Interactioni

Subunit structurei

Homotetramer (PubMed:10097181, PubMed:15908964, PubMed:17027503, PubMed:18621707, PubMed:25470059, PubMed:25517095, PubMed:27662087, PubMed:27573175, PubMed:27468892). Can also form heterotetramers with RYR2 (PubMed:12213830). 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 similarity). Interacts with CALM; CALM with bound calcium inhibits the RYR1 channel activity (PubMed:10601232, PubMed:11562475, PubMed:17027503). Interacts with S100A1 (By similarity). Interacts with FKBP1A; this stabilizes the closed conformation of the channel (PubMed:7669046, PubMed:10603943, PubMed:26245150, PubMed:25517095, PubMed:27468892). Interacts with CACNA1S; interaction with CACNA1S is important for activation of the RYR1 channel (PubMed:10388749). Interacts with CACNB1 (PubMed:21320436). Interacts with TRDN and ASPH; these interactions stimulate RYR1 channel activity (PubMed:9737879, PubMed:19398037). Interacts with SELENON (PubMed:18713863).By similarity20 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi1172559, 3 interactors
ComplexPortaliCPX-3136 Ryanodine 1 complex
DIPiDIP-41872N
IntActiP11716, 8 interactors
MINTiP11716

Chemistry databases

BindingDBiP11716

Structurei

Secondary structure

15037
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP11716
SMRiP11716
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11716

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini98 – 153MIR 1PROSITE-ProRule annotationAdd BLAST56
Domaini160 – 205MIR 2PROSITE-ProRule annotationAdd BLAST46
Domaini211 – 265MIR 3PROSITE-ProRule annotationAdd BLAST55
Domaini271 – 334MIR 4PROSITE-ProRule annotationAdd BLAST64
Domaini336 – 394MIR 5PROSITE-ProRule annotationAdd BLAST59
Domaini582 – 798B30.2/SPRY 1PROSITE-ProRule annotationAdd BLAST217
Repeati842 – 9551Add BLAST114
Repeati956 – 10692Add BLAST114
Domaini1014 – 1209B30.2/SPRY 2PROSITE-ProRule annotationAdd BLAST196
Repeati1345 – 13603; truncatedAdd BLAST16
Domaini1358 – 1571B30.2/SPRY 3PROSITE-ProRule annotationAdd BLAST214
Repeati1373 – 13884; truncatedAdd BLAST16
Repeati2726 – 28455Add BLAST120
Repeati2846 – 29596Add BLAST114
Domaini4075 – 4103EF-handPROSITE-ProRule annotation1 PublicationAdd BLAST29

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni670 – 681Interaction with FKBP1A1 PublicationAdd BLAST12
Regioni842 – 29596 X approximate repeatsAdd BLAST2118
Regioni3614 – 3643Interaction with CALMAdd BLAST30

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi4894 – 4900Selectivity filter3 Publications7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1873 – 1913Glu-rich (acidic)Add BLAST41

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 (PubMed:2725677, PubMed:25517095, PubMed:27662087, PubMed:27573175, PubMed:27468892). Pore opening is mediated via the cytoplasmic calcium-binding domains that mediate a small rotation of the channel-forming transmembrane regions that then leads to channel opening (PubMed:27468892).5 Publications

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

HOVERGENiHBG006699
InParanoidiP11716
KOiK04961

Family and domain databases

CDDicd12877 SPRY1_RyR, 1 hit
cd12878 SPRY2_RyR, 1 hit
cd12879 SPRY3_RyR, 1 hit
InterProiView protein in InterPro
IPR001870 B30.2/SPRY
IPR013320 ConA-like_dom_sf
IPR011992 EF-hand-dom_pair
IPR002048 EF_hand_dom
IPR014821 Ins145_P3_rcpt
IPR005821 Ion_trans_dom
IPR036300 MIR_dom_sf
IPR016093 MIR_motif
IPR013662 RIH_assoc-dom
IPR000699 RIH_dom
IPR013333 Ryan_recept
IPR003032 Ryanodine_rcpt
IPR015925 Ryanodine_recept-rel
IPR009460 Ryanrecept_TM4-6
IPR035910 RyR/IP3R_RIH_dom_sf
IPR033215 RyR1
IPR035761 SPRY1_RyR
IPR035764 SPRY2_RyR
IPR035762 SPRY3_RyR
IPR003877 SPRY_dom
PANTHERiPTHR13715 PTHR13715, 1 hit
PTHR13715:SF15 PTHR13715:SF15, 1 hit
PfamiView protein in Pfam
PF13833 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
PRINTSiPR00795 RYANODINER
SMARTiView protein in SMART
SM00472 MIR, 4 hits
SM00449 SPRY, 3 hits
SUPFAMiSSF100909 SSF100909, 1 hit
SSF47473 SSF47473, 1 hit
SSF49899 SSF49899, 3 hits
SSF82109 SSF82109, 2 hits
PROSITEiView protein in PROSITE
PS50188 B302_SPRY, 3 hits
PS50919 MIR, 5 hits

Sequencei

Sequence statusi: Complete.

P11716-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGDGGEGEDE VQFLRTDDEV VLQCSATVLK EQLKLCLAAE GFGNRLCFLE
60 70 80 90 100
PTSNAQNVPP DLAICCFTLE QSLSVRALQE MLANTVEAGV ESSQGGGHRT
110 120 130 140 150
LLYGHAILLR HAHSRMYLSC LTTSRSMTDK LAFDVGLQED ATGEACWWTM
160 170 180 190 200
HPASKQRSEG EKVRVGDDLI LVSVSSERYL HLSTASGELQ VDASFMQTLW
210 220 230 240 250
NMNPICSCCE EGYVTGGHVL RLFHGHMDEC LTISAADSDD QRRLVYYEGG
260 270 280 290 300
AVCTHARSLW RLEPLRISWS GSHLRWGQPL RIRHVTTGRY LALTEDQGLV
310 320 330 340 350
VVDACKAHTK ATSFCFRVSK EKLDTAPKRD VEGMGPPEIK YGESLCFVQH
360 370 380 390 400
VASGLWLTYA APDPKALRLG VLKKKAILHQ EGHMDDALFL TRCQQEESQA
410 420 430 440 450
ARMIHSTAGL YNQFIKGLDS FSGKPRGSGP PAGPALPIEA VILSLQDLIG
460 470 480 490 500
YFEPPSEELQ HEEKQSKLRS LRNRQSLFQE EGMLSLVLNC IDRLNVYTTA
510 520 530 540 550
AHFAEYAGEE AAESWKEIVN LLYELLASLI RGNRANCALF STNLDWVVSK
560 570 580 590 600
LDRLEASSGI LEVLYCVLIE SPEVLNIIQE NHIKSIISLL DKHGRNHKVL
610 620 630 640 650
DVLCSLCVCN GVAVRSNQDL ITENLLPGRE LLLQTNLINY VTSIRPNIFV
660 670 680 690 700
GRAEGSTQYG KWYFEVMVDE VVPFLTAQAT HLRVGWALTE GYSPYPGGGE
710 720 730 740 750
GWGGNGVGDD LYSYGFDGLH LWTGHVARPV TSPGQHLLAP EDVVSCCLDL
760 770 780 790 800
SVPSISFRIN GCPVQGVFEA FNLDGLFFPV VSFSAGVKVR FLLGGRHGEF
810 820 830 840 850
KFLPPPGYAP CHEAVLPRER LRLEPIKEYR REGPRGPHLV GPSRCLSHTD
860 870 880 890 900
FVPCPVDTVQ IVLPPHLERI REKLAENIHE LWALTRIEQG WTYGPVRDDN
910 920 930 940 950
KRLHPCLVNF HSLPEPERNY NLQMSGETLK TLLALGCHVG MADEKAEDNL
960 970 980 990 1000
KKTKLPKTYM MSNGYKPAPL DLSHVRLTPA QTTLVDRLAE NGHNVWARDR
1010 1020 1030 1040 1050
VAQGWSYSAV QDIPARRNPR LVPYRLLDEA TKRSNRDSLC QAVRTLLGYG
1060 1070 1080 1090 1100
YNIEPPDQEP SQVENQSRWD RVRIFRAEKS YTVQSGRWYF EFEAVTTGEM
1110 1120 1130 1140 1150
RVGWARPELR PDVELGADEL AYVFNGHRGQ RWHLGSEPFG RPWQSGDVVG
1160 1170 1180 1190 1200
CMIDLTENTI IFTLNGEVLM SDSGSETAFR EIEIGDGFLP VCSLGPGQVG
1210 1220 1230 1240 1250
HLNLGQDVSS LRFFAICGLQ EGFEPFAINM QRPVTTWFSK SLPQFEPVPP
1260 1270 1280 1290 1300
EHPHYEVARM DGTVDTPPCL RLAHRTWGSQ NSLVEMLFLR LSLPVQFHQH
1310 1320 1330 1340 1350
FRCTAGATPL APPGLQPPAE DEARAAEPDP DYENLRRSAG GWGEAEGGKE
1360 1370 1380 1390 1400
GTAKEGTPGG TPQPGVEAQP VRAENEKDAT TEKNKKRGFL FKAKKAAMMT
1410 1420 1430 1440 1450
QPPATPALPR LPHDVVPADN RDDPEIILNT TTYYYSVRVF AGQEPSCVWV
1460 1470 1480 1490 1500
GWVTPDYHQH DMNFDLSKVR AVTVTMGDEQ GNVHSSLKCS NCYMVWGGDF
1510 1520 1530 1540 1550
VSPGQQGRIS HTDLVIGCLV DLATGLMTFT ANGKESNTFF QVEPNTKLFP
1560 1570 1580 1590 1600
AVFVLPTHQN VIQFELGKQK NIMPLSAAMF LSERKNPAPQ CPPRLEVQML
1610 1620 1630 1640 1650
MPVSWSRMPN HFLQVETRRA GERLGWAVQC QDPLTMMALH IPEENRCMDI
1660 1670 1680 1690 1700
LELSERLDLQ RFHSHTLRLY RAVCALGNNR VAHALCSHVD QAQLLHALED
1710 1720 1730 1740 1750
AHLPGPLRAG YYDLLISIHL ESACRSRRSM LSEYIVPLTP ETRAITLFPP
1760 1770 1780 1790 1800
GRKGGNARRH GLPGVGVTTS LRPPHHFSPP CFVAALPAAG VAEAPARLSP
1810 1820 1830 1840 1850
AIPLEALRDK ALRMLGEAVR DGGQHARDPV GGSVEFQFVP VLKLVSTLLV
1860 1870 1880 1890 1900
MGIFGDEDVK QILKMIEPEV FTEEEEEEEE EEEEEEEEEE DEEEKEEDEE
1910 1920 1930 1940 1950
EEEKEDAEKE EEEAPEGEKE DLEEGLLQMK LPESVKLQMC NLLEYFCDQE
1960 1970 1980 1990 2000
LQHRVESLAA FAERYVDKLQ ANQRSRYALL MRAFTMSAAE TARRTREFRS
2010 2020 2030 2040 2050
PPQEQINMLL HFKDEADEED CPLPEDIRQD LQDFHQDLLA HCGIQLEGEE
2060 2070 2080 2090 2100
EEPEEETSLS SRLRSLLETV RLVKKKEEKP EEELPAEEKK PQSLQELVSH
2110 2120 2130 2140 2150
MVVRWAQEDY VQSPELVRAM FSLLHRQYDG LGELLRALPR AYTISPSSVE
2160 2170 2180 2190 2200
DTMSLLECLG QIRSLLIVQM GPQEENLMIQ SIGNIMNNKV FYQHPNLMRA
2210 2220 2230 2240 2250
LGMHETVMEV MVNVLGGGET KEIRFPKMVT SCCRFLCYFC RISRQNQRSM
2260 2270 2280 2290 2300
FDHLSYLLEN SGIGLGMQGS TPLDVAAASV IDNNELALAL QEQDLEKVVS
2310 2320 2330 2340 2350
YLAGCGLQSC PMLLAKGYPD IGWNPCGGER YLDFLRFAVF VNGESVEENA
2360 2370 2380 2390 2400
NVVVRLLIRK PECFGPALRG EGGSGLLAAI EEAIRISEDP ARDGPGVRRD
2410 2420 2430 2440 2450
RRREHFGEEP PEENRVHLGH AIMSFYAALI DLLGRCAPEM HLIQAGKGEA
2460 2470 2480 2490 2500
LRIRAILRSL VPLDDLVGII SLPLQIPTLG KDGALVQPKM SASFVPDHKA
2510 2520 2530 2540 2550
SMVLFLDRVY GIENQDFLLH VLDVGFLPDM RAAASLDTAT FSTTEMALAL
2560 2570 2580 2590 2600
NRYLCLAVLP LITKCAPLFA GTEHRAIMVD SMLHTVYRLS RGRSLTKAQR
2610 2620 2630 2640 2650
DVIEDCLMAL CRYIRPSMLQ HLLRRLVFDV PILNEFAKMP LKLLTNHYER
2660 2670 2680 2690 2700
CWKYYCLPTG WANFGVTSEE ELHLTRKLFW GIFDSLAHKK YDQELYRMAM
2710 2720 2730 2740 2750
PCLCAIAGAL PPDYVDASYS SKAEKKATVD AEGNFDPRPV ETLNVIIPEK
2760 2770 2780 2790 2800
LDSFINKFAE YTHEKWAFDK IQNNWSYGEN VDEELKTHPM LRPYKTFSEK
2810 2820 2830 2840 2850
DKEIYRWPIK ESLKAMIAWE WTIEKAREGE EERTEKKKTR KISQTAQTYD
2860 2870 2880 2890 2900
PREGYNPQPP DLSGVTLSRE LQAMAEQLAE NYHNTWGRKK KQELEAKGGG
2910 2920 2930 2940 2950
THPLLVPYDT LTAKEKARDR EKAQELLKFL QMNGYAVTRG LKDMELDTSS
2960 2970 2980 2990 3000
IEKRFAFGFL QQLLRWMDIS QEFIAHLEAV VSSGRVEKSP HEQEIKFFAK
3010 3020 3030 3040 3050
ILLPLINQYF TNHCLYFLST PAKVLGSGGH ASNKEKEMIT SLFCKLAALV
3060 3070 3080 3090 3100
RHRVSLFGTD APAVVNCLHI LARSLDARTV MKSGPEIVKA GLRSFFESAS
3110 3120 3130 3140 3150
EDIEKMVENL RLGKVSQART QVKGVGQNLT YTTVALLPVL TTLFQHIAQH
3160 3170 3180 3190 3200
QFGDDVILDD VQVSCYRTLC SIYSLGTTKN TYVEKLRPAL GECLARLAAA
3210 3220 3230 3240 3250
MPVAFLEPQL NEYNACSVYT TKSPRERAIL GLPNSVEEMC PDIPVLDRLM
3260 3270 3280 3290 3300
ADIGGLAESG ARYTEMPHVI EITLPMLCSY LPRWWERGPE APPPALPAGA
3310 3320 3330 3340 3350
PPPCTAVTSD HLNSLLGNIL RIIVNNLGID EATWMKRLAV FAQPIVSRAR
3360 3370 3380 3390 3400
PELLHSHFIP TIGRLRKRAG KVVAEEEQLR LEAKAEAEEG ELLVRDEFSV
3410 3420 3430 3440 3450
LCRDLYALYP LLIRYVDNNR AHWLTEPNAN AEELFRMVGE IFIYWSKSHN
3460 3470 3480 3490 3500
FKREEQNFVV QNEINNMSFL TADSKSKMAK AGDAQSGGSD QERTKKKRRG
3510 3520 3530 3540 3550
DRYSVQTSLI VATLKKMLPI GLNMCAPTDQ DLIMLAKTRY ALKDTDEEVR
3560 3570 3580 3590 3600
EFLQNNLHLQ GKVEGSPSLR WQMALYRGLP GREEDADDPE KIVRRVQEVS
3610 3620 3630 3640 3650
AVLYHLEQTE HPYKSKKAVW HKLLSKQRRR AVVACFRMTP LYNLPTHRAC
3660 3670 3680 3690 3700
NMFLESYKAA WILTEDHSFE DRMIDDLSKA GEQEEEEEEV EEKKPDPLHQ
3710 3720 3730 3740 3750
LVLHFSRTAL TEKSKLDEDY LYMAYADIMA KSCHLEEGGE NGEAEEEEVE
3760 3770 3780 3790 3800
VSFEEKEMEK QRLLYQQSRL HTRGAAEMVL QMISACKGET GAMVSSTLKL
3810 3820 3830 3840 3850
GISILNGGNA EVQQKMLDYL KDKKEVGFFQ SIQALMQTCS VLDLNAFERQ
3860 3870 3880 3890 3900
NKAEGLGMVN EDGTVINRQN GEKVMADDEF TQDLFRFLQL LCEGHNNDFQ
3910 3920 3930 3940 3950
NYLRTQTGNT TTINIIICTV DYLLRLQESI SDFYWYYSGK DVIEEQGKRN
3960 3970 3980 3990 4000
FSKAMSVAKQ VFNSLTEYIQ GPCTGNQQSL AHSRLWDAVV GFLHVFAHMM
4010 4020 4030 4040 4050
MKLAQDSSQI ELLKELLDLQ KDMVVMLLSL LEGNVVNGMI ARQMVDMLVE
4060 4070 4080 4090 4100
SSSNVEMILK FFDMFLKLKD IVGSEAFQDY VTDPRGLISK KDFQKAMDSQ
4110 4120 4130 4140 4150
KQFTGPEIQF LLSCSEADEN EMINFEEFAN RFQEPARDIG FNVAVLLTNL
4160 4170 4180 4190 4200
SEHVPHDPRL RNFLELAESI LEYFRPYLGR IEIMGASRRI ERIYFEISET
4210 4220 4230 4240 4250
NRAQWEMPQV KESKRQFIFD VVNEGGEAEK MELFVSFCED TIFEMQIAAQ
4260 4270 4280 4290 4300
ISEPEGEPEA DEDEGMGEAA AEGAEEGAAG AEGAAGTVAA GATARLAAAA
4310 4320 4330 4340 4350
ARALRGLSYR SLRRRVRRLR RLTAREAATA LAALLWAVVA RAGAAGAGAA
4360 4370 4380 4390 4400
AGALRLLWGS LFGGGLVEGA KKVTVTELLA GMPDPTSDEV HGEQPAGPGG
4410 4420 4430 4440 4450
DADGAGEGEG EGDAAEGDGD EEVAGHEAGP GGAEGVVAVA DGGPFRPEGA
4460 4470 4480 4490 4500
GGLGDMGDTT PAEPPTPEGS PILKRKLGVD GEEEELVPEP EPEPEPEPEK
4510 4520 4530 4540 4550
ADEENGEKEE VPEAPPEPPK KAPPSPPAKK EEAGGAGMEF WGELEVQRVK
4560 4570 4580 4590 4600
FLNYLSRNFY TLRFLALFLA FAINFILLFY KVSDSPPGED DMEGSAAGDL
4610 4620 4630 4640 4650
AGAGSGGGSG WGSGAGEEAE GDEDENMVYY FLEESTGYME PALWCLSLLH
4660 4670 4680 4690 4700
TLVAFLCIIG YNCLKVPLVI FKREKELARK LEFDGLYITE QPGDDDVKGQ
4710 4720 4730 4740 4750
WDRLVLNTPS FPSNYWDKFV KRKVLDKHGD IFGRERIAEL LGMDLASLEI
4760 4770 4780 4790 4800
TAHNERKPDP PPGLLTWLMS IDVKYQIWKF GVIFTDNSFL YLGWYMVMSL
4810 4820 4830 4840 4850
LGHYNNFFFA AHLLDIAMGV KTLRTILSSV THNGKQLVMT VGLLAVVVYL
4860 4870 4880 4890 4900
YTVVAFNFFR KFYNKSEDED EPDMKCDDMM TCYLFHMYVG VRAGGGIGDE
4910 4920 4930 4940 4950
IEDPAGDEYE LYRVVFDITF FFFVIVILLA IIQGLIIDAF GELRDQQEQV
4960 4970 4980 4990 5000
KEDMETKCFI CGIGSDYFDT TPHGFETHTL EEHNLANYMF FLMYLINKDE
5010 5020 5030
TEHTGQESYV WKMYQERCWD FFPAGDCFRK QYEDQLS
Length:5,037
Mass (Da):565,253
Last modified:October 1, 1989 - v1
Checksum:i4ABD87AA26697070
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2015E → D no nucleotide entry (PubMed:2298749).Curated1
Sequence conflicti3481 – 3485Missing no nucleotide entry (PubMed:2298749).Curated5

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15209 mRNA Translation: CAA33279.1
X15750 mRNA Translation: CAA33762.1
PIRiS04654 B35041
RefSeqiNP_001095188.1, NM_001101718.1
UniGeneiOcu.2092

Genome annotation databases

GeneIDi100009540
KEGGiocu:100009540

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15209 mRNA Translation: CAA33279.1
X15750 mRNA Translation: CAA33762.1
PIRiS04654 B35041
RefSeqiNP_001095188.1, NM_001101718.1
UniGeneiOcu.2092

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BCXX-ray2.00B3614-3643[»]
2XOAX-ray2.50A1-559[»]
3HSMX-ray2.50A/B1-210[»]
3ILAX-ray2.90A/B/C/D/E/F/G/H/I9-205[»]
3J8Helectron microscopy3.80A/C/E/G1-5037[»]
3RQRX-ray2.16A2733-2940[»]
4ERTX-ray1.95A2734-2940[»]
4ESUX-ray1.59A2734-2940[»]
4ETTX-ray2.20A2734-2940[»]
4ETUX-ray2.19A2734-2938[»]
4I0YX-ray2.80A1-536[»]
4I1EX-ray2.40A1-536[»]
4I2SX-ray2.50A1-536[»]
4I37X-ray2.95A1-536[»]
4I3NX-ray2.95A1-536[»]
4I6IX-ray2.50A1-559[»]
4I7IX-ray2.90A1-536[»]
4I8MX-ray2.80A1-536[»]
4I96X-ray2.73A217-536[»]
4P9JX-ray1.84A/B/C1070-1246[»]
4UWAelectron microscopy6.10A/B/C/D1-5037[»]
4UWEelectron microscopy8.50A/B/C/D1-5037[»]
5C30X-ray1.55A857-1054[»]
5GKYelectron microscopy3.80A/C/E/G1-5037[»]
5GKZelectron microscopy4.00A/C/E/G1-5037[»]
5GL0electron microscopy4.20A/C/E/G1-5037[»]
5GL1electron microscopy5.70A/C/E/G1-5037[»]
5J8Velectron microscopy4.90A/B/C/D1-5037[»]
5T15electron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-5037[»]
5T9Melectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-5037[»]
5T9Nelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-5037[»]
5T9Relectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-5037[»]
5T9Selectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-5037[»]
5T9Velectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4540-5037[»]
5TA3electron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TALelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TAMelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TANelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TAPelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TAQelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TASelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TATelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TAUelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TAVelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TAWelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TAXelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TAYelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TAZelectron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TB0electron microscopy3.80B/E/G/I1-5037[»]
5TB1electron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TB2electron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TB3electron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
5TB4electron microscopy3.80B/E/G/I12-1275[»]
B/E/G/I1573-2479[»]
B/E/G/I2734-2939[»]
B/E/G/I3639-4253[»]
B/E/G/I4541-5037[»]
6FG3electron microscopy7.30A/B/C/D1-5037[»]
6FOOelectron microscopy8.20A/B/C/D1-5037[»]
ProteinModelPortaliP11716
SMRiP11716
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1172559, 3 interactors
ComplexPortaliCPX-3136 Ryanodine 1 complex
DIPiDIP-41872N
IntActiP11716, 8 interactors
MINTiP11716

Chemistry databases

BindingDBiP11716
ChEMBLiCHEMBL3288

PTM databases

iPTMnetiP11716
SwissPalmiP11716

Proteomic databases

PRIDEiP11716

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100009540
KEGGiocu:100009540

Organism-specific databases

CTDi6261

Phylogenomic databases

HOVERGENiHBG006699
InParanoidiP11716
KOiK04961

Miscellaneous databases

EvolutionaryTraceiP11716
PROiPR:P11716

Family and domain databases

CDDicd12877 SPRY1_RyR, 1 hit
cd12878 SPRY2_RyR, 1 hit
cd12879 SPRY3_RyR, 1 hit
InterProiView protein in InterPro
IPR001870 B30.2/SPRY
IPR013320 ConA-like_dom_sf
IPR011992 EF-hand-dom_pair
IPR002048 EF_hand_dom
IPR014821 Ins145_P3_rcpt
IPR005821 Ion_trans_dom
IPR036300 MIR_dom_sf
IPR016093 MIR_motif
IPR013662 RIH_assoc-dom
IPR000699 RIH_dom
IPR013333 Ryan_recept
IPR003032 Ryanodine_rcpt
IPR015925 Ryanodine_recept-rel
IPR009460 Ryanrecept_TM4-6
IPR035910 RyR/IP3R_RIH_dom_sf
IPR033215 RyR1
IPR035761 SPRY1_RyR
IPR035764 SPRY2_RyR
IPR035762 SPRY3_RyR
IPR003877 SPRY_dom
PANTHERiPTHR13715 PTHR13715, 1 hit
PTHR13715:SF15 PTHR13715:SF15, 1 hit
PfamiView protein in Pfam
PF13833 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
PRINTSiPR00795 RYANODINER
SMARTiView protein in SMART
SM00472 MIR, 4 hits
SM00449 SPRY, 3 hits
SUPFAMiSSF100909 SSF100909, 1 hit
SSF47473 SSF47473, 1 hit
SSF49899 SSF49899, 3 hits
SSF82109 SSF82109, 2 hits
PROSITEiView protein in PROSITE
PS50188 B302_SPRY, 3 hits
PS50919 MIR, 5 hits
ProtoNetiSearch...

Entry informationi

Entry nameiRYR1_RABIT
AccessioniPrimary (citable) accession number: P11716
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: October 10, 2018
This is version 171 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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