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Protein

Ryanodine receptor 2

Gene

Ryr2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering cardiac muscle contraction. Aberrant channel activation can lead to cardiac arrhythmia. In cardiac myocytes, calcium release is triggered by increased Ca2+ levels due to activation of the L-type calcium channel CACNA1C. The calcium channel activity is modulated by formation of heterotetramers with RYR3. Required for cellular calcium ion homeostasis. Required for embryonic heart development (By similarity).By similarity2 Publications

GO - Molecular functioni

  • calcium channel activity Source: UniProtKB
  • calcium-induced calcium release activity Source: RGD
  • calcium ion binding Source: InterPro
  • calcium-release channel activity Source: UniProtKB
  • ryanodine-sensitive calcium-release channel activity Source: RGD
  • scaffold protein binding Source: BHF-UCL

GO - Biological processi

  • calcium ion transmembrane transport Source: RGD
  • calcium ion transport Source: UniProtKB
  • calcium-mediated signaling Source: UniProtKB
  • cellular calcium ion homeostasis Source: UniProtKB
  • cellular response to caffeine Source: UniProtKB
  • embryonic heart tube morphogenesis Source: UniProtKB
  • ion transmembrane transport Source: RGD
  • manganese ion transmembrane transport Source: RGD
  • negative regulation of cytosolic calcium ion concentration Source: RGD
  • regulation of cytosolic calcium ion concentration Source: RGD
  • release of sequestered calcium ion into cytosol Source: GOC
  • response to calcium ion Source: RGD
  • response to drug Source: RGD
  • response to magnesium ion Source: RGD
  • response to nutrient Source: RGD
  • sarcoplasmic reticulum calcium ion transport Source: RGD
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

Names & Taxonomyi

Protein namesi
Recommended name:
Ryanodine receptor 2
Short name:
RYR-2
Short name:
RyR2
Alternative name(s):
Cardiac muscle ryanodine receptor
Cardiac muscle ryanodine receptor-calcium release channel
Type 2 ryanodine receptor
Gene namesi
Name:Ryr2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620314. Ryr2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 42184218CytoplasmicSequence analysisAdd
BLAST
Transmembranei4219 – 423921HelicalSequence analysisAdd
BLAST
Transmembranei4265 – 428521HelicalSequence analysisAdd
BLAST
Transmembranei4489 – 450921HelicalSequence analysisAdd
BLAST
Transmembranei4566 – 458621HelicalSequence analysisAdd
BLAST
Transmembranei4716 – 473621HelicalSequence analysisAdd
BLAST
Transmembranei4755 – 477521HelicalSequence analysisAdd
BLAST
Intramembranei4806 – 481510Pore-formingBy similarity
Transmembranei4836 – 485621HelicalSequence analysisAdd
BLAST
Topological domaini4857 – 495397CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • A band Source: RGD
  • cytoplasm Source: RGD
  • endoplasmic reticulum Source: RGD
  • extrinsic component of cytoplasmic side of plasma membrane Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • neuron projection Source: RGD
  • nuclear envelope Source: BHF-UCL
  • plasma membrane Source: RGD
  • protein complex Source: RGD
  • sarcolemma Source: RGD
  • sarcoplasmic reticulum Source: BHF-UCL
  • sarcoplasmic reticulum membrane Source: BHF-UCL
  • Z disc Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3388.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 49534953Ryanodine receptor 2PRO_0000415583Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1334 – 13341PhosphoserineCombined sources
Modified residuei1863 – 18631PhosphoserineCombined sources
Modified residuei2021 – 20211PhosphoserineCombined sources
Modified residuei2359 – 23591PhosphoserineBy similarity
Modified residuei2787 – 27871PhosphoserineBy similarity
Modified residuei2798 – 27981Phosphoserine; by CaMK2D and PKACombined sources1 Publication
Modified residuei2801 – 28011PhosphoserineCombined sources
Modified residuei2804 – 28041Phosphoserine; by CaMK2DCombined sources1 Publication
Modified residuei2937 – 29371PhosphoserineBy similarity

Post-translational modificationi

Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2798 and Ser-2804 increases the open probability of the calcium channel. Phosphorylation is increased in failing heart, leading to calcium leaks and increased cytoplasmic Ca2+ levels (By similarity).By similarity
Phosphorylation at Ser-2021 by PKA enhances the response to lumenal calcium.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiB0LPN4.
PRIDEiB0LPN4.

PTM databases

iPTMnetiB0LPN4.

Expressioni

Tissue specificityi

Detected in heart muscle myocytes (at protein level). Widely expressed. Detected in heart muscle and cerebral artery smooth muscle. Detected in pancreatic islet cells.4 Publications

Interactioni

Subunit structurei

Homotetramer. Can also form heterotetramers with RYR3. Identified in a complex composed of RYR2, FKBP1B, PKA catalytic subunit, PRKAR2A, AKAP6, and the protein phosphatases PP2A and PP1. Interacts directly with FKBP1B, PKA, PP1 and PP2A (By similarity). Interacts with FKBP1A and FKBP1B; these interactions may stabilize the channel in its closed state and prevent Ca2+ leaks. Interacts with CALM and S100A1; these interactions regulate channel activity. Interacts with SEPN1 (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Calm3P621612EBI-6694167,EBI-397530

GO - Molecular functioni

  • scaffold protein binding Source: BHF-UCL

Protein-protein interaction databases

IntActiB0LPN4. 1 interaction.
STRINGi10116.ENSRNOP00000059019.

Chemistry

BindingDBiB0LPN4.

Structurei

Secondary structure

1
4953
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3562 – 357110Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K2FNMR-C/D3561-3572[»]
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiB0LPN4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini103 – 15856MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini165 – 21046MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini218 – 27356MIR 3PROSITE-ProRule annotationAdd
BLAST
Domaini279 – 33658MIR 4PROSITE-ProRule annotationAdd
BLAST
Domaini344 – 40158MIR 5PROSITE-ProRule annotationAdd
BLAST
Domaini592 – 802211B30.2/SPRY 1PROSITE-ProRule annotationAdd
BLAST
Repeati846 – 9591141Add
BLAST
Repeati960 – 10731142Add
BLAST
Domaini1018 – 1215198B30.2/SPRY 2PROSITE-ProRule annotationAdd
BLAST
Domaini1350 – 1556207B30.2/SPRY 3PROSITE-ProRule annotationAdd
BLAST
Repeati2682 – 28001193Add
BLAST
Repeati2802 – 29151144Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni846 – 291520704 X approximate repeatsAdd
BLAST
Regioni3559 – 358830Interaction with CALMBy similarityAdd
BLAST

Domaini

The calcium release channel activity resides in the C-terminal region while the remaining part of the protein resides in the cytoplasm.Curated

Sequence similaritiesi

Contains 3 B30.2/SPRY domains.PROSITE-ProRule annotation
Contains 5 MIR domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2243. Eukaryota.
ENOG410YCNW. LUCA.
HOGENOMiHOG000231428.
HOVERGENiHBG006699.
InParanoidiB0LPN4.
KOiK04962.

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.
IPR002048. EF_hand_dom.
IPR014821. Ins145_P3_rcpt.
IPR005821. Ion_trans_dom.
IPR016093. MIR_motif.
IPR013662. RIH_assoc-dom.
IPR000699. RIH_dom.
IPR013333. Ryan_recept.
IPR003032. Ryanodine_rcpt.
IPR015925. Ryanodine_recept-rel.
IPR009460. Ryanrecept_TM4-6.
IPR003877. SPRY_dom.
[Graphical view]
PANTHERiPTHR13715. PTHR13715. 5 hits.
PfamiPF13833. EF-hand_8. 1 hit.
PF08709. Ins145_P3_rec. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02815. MIR. 1 hit.
PF08454. RIH_assoc. 1 hit.
PF06459. RR_TM4-6. 1 hit.
PF01365. RYDR_ITPR. 2 hits.
PF02026. RyR. 4 hits.
PF00622. SPRY. 3 hits.
[Graphical view]
PRINTSiPR00795. RYANODINER.
SMARTiSM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMiSSF100909. SSF100909. 2 hits.
SSF47473. SSF47473. 1 hit.
SSF49899. SSF49899. 2 hits.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: B0LPN4-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADAGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE
60 70 80 90 100
STSNSKNVPP DLSICTFVLE QSLSVRALQE MLANTVEKSE GKFMMKTAQG
110 120 130 140 150
GGHRTLLYGH AILLRHSYSG MYLCCLSTSR SSTDKLAFDV GLQEDTTGEA
160 170 180 190 200
CWWTIHPASK QRSEGEKVRV GDDLILVSVS SERYLHLSYG NSSWRVDAAF
210 220 230 240 250
QQTLWSVAPI SSGSEAAQGY LIGGDVLRLL HGHMDECLTV PSGEHGEEQR
260 270 280 290 300
RTVHYEGGAV SVHARSLWRL ETLRVAWSGS HIRWGQPFRL RHVTTGKYLS
310 320 330 340 350
LMEDKNLLLM DKEKADVKST AFAFRSSKEK LDAGVRKEVD GMGTSEIKYG
360 370 380 390 400
DSICYIQHVD TGLWLTYQAV DVKSARMGSI QRKAIMHHEG HMDDGLNLSR
410 420 430 440 450
SQHEESRTAR VIRSTVFLFN RFIRGLDALS KRAKLPTVDL PIESVSLSLQ
460 470 480 490 500
DLIGYFHPPD EHLEHEDKQN RLRALKNRQN LFQEEGMINL VLECIDRLHV
510 520 530 540 550
YSSAAHFADV AGREAGESWK SILNSLYELL AALIRGNRKN CAQFSGSLDW
560 570 580 590 600
LISRLERLEA SSGILEVLHC VLVESPEALN IIKEGHIKSI ISLLDKHGRN
610 620 630 640 650
HKVLDVLCSL CVCHGVAVRS NQHLICDNLL PGRDLLLQTR LVNHVSSMRP
660 670 680 690 700
NIFLGVSEGS AQYKKWYYEL MVDHTEPFVT AEATHLRVGW ASTEGYSPYP
710 720 730 740 750
GGGEEWGGNG VGDDLFSYGF DGLHLWSGCI ARTVSSPNQH LLRTDDVISC
760 770 780 790 800
CLDLSAPSIS FRINGQPVQG MFENFNIDGL FFPVVSFSAG IKVRFLLGGR
810 820 830 840 850
HGEFKFLPPP GYAACYEAVL PKEKLKVEHS REYKQERTYT RDLLGPTVSL
860 870 880 890 900
TQAAFTPVPV DTSQIVLPPH LERIRERLAE NIHELWVMNK IELGWQYGPV
910 920 930 940 950
RDDNKRQHPC LVEFCKLPEQ ERNYNLQMSL ETLKTLLALG CHVGIADEHA
960 970 980 990 1000
EEKVKKMKLP KNYQLTSGYK PAPMDLSFIK LTPSQEAMVD KLAENAHNVW
1010 1020 1030 1040 1050
ARDRIRQGWT YGIQQDVKNR RNPRLVPYTL LDDRTKKSNK DSLREAVRTL
1060 1070 1080 1090 1100
LGYGYHLEAP DQDHASRAEV CSGTGERFRI FRAEKTYAVK AGRWYFEFEA
1110 1120 1130 1140 1150
VTAGDMRVGW SRPGCQPDLE LGSDERAFAF DGFKAQRWHQ GNEHYGRSWQ
1160 1170 1180 1190 1200
AGDVVGCMVD MNEHTMMFTL NGEILLDDSG SELAFKDFDV GDGFIPVCSL
1210 1220 1230 1240 1250
GVAQVGRMNF GKDVSTLKYF TICGLQEGYE PFAVNTNRDI TMWLSKRLPQ
1260 1270 1280 1290 1300
FLQVPSNHEH IEVTRIDGTI DSSPCLKVTQ KSFGSQNSNT DIMFYRLSMP
1310 1320 1330 1340 1350
IECAEVFSKS VAGGIPGAGF YGPKNDLEDF DVDSDFEVLM KTAHGHLVPD
1360 1370 1380 1390 1400
RMDKDKETPK PEFNNHKDYA QEKPSRLKQR FLLRRTKPDY STSHSARLTE
1410 1420 1430 1440 1450
DVLADDRDDY EYLMQTSTYY YSVRIFPGQE PANVWVGWIT SDFHQYDTGF
1460 1470 1480 1490 1500
DLDRVRTVTV TLGDEKGKVH ESIKRSNCYM VCAGESMSPG QGRNNSNGLE
1510 1520 1530 1540 1550
IGCVVDAASG LLTFIANGKE LSTYYQVEPS TKLFPAVFAQ ATSPNVFQFE
1560 1570 1580 1590 1600
LGRIKNVMPL SAGLFKSEHK NPVPQCPPRL HVQFLSHVLW SRMPNQFLKV
1610 1620 1630 1640 1650
DVSRISERQG WLVQCLDPLQ FMSLHIPEEN RSVDILELTE QEELLQFHYH
1660 1670 1680 1690 1700
TLRLYSAVCA LGNHRVAHAL CSHVDEPQLL YAIENKYMPG LLRAGYYDLL
1710 1720 1730 1740 1750
IDIHLSSYAT ARLMMNNEFI VPMTEETKSI TLFPDENKKH GLPGIGLSTS
1760 1770 1780 1790 1800
LRPRMCFSSP SFVSISNECY QYSPEFPLDI LKAKTIQMLT EAVKEGSLHA
1810 1820 1830 1840 1850
RDPVGGTTEF LFVPLIKLFY TLLIMGIFHN EDLKHILQLI EPSVFKEAAT
1860 1870 1880 1890 1900
PEEEGGAPEK EISIDDSKLE VKEEAKAGKR PKEGLLQMKL PEPVKLQMCL
1910 1920 1930 1940 1950
LLQYLCDCQV RHRIEAIVAF SDDFVAKLQD NQRFRYNEVM QALNMSAALT
1960 1970 1980 1990 2000
ARKEFRSPPQ EQINMLLNFK DDKSECPCPE EIRDQLLDFH EDLMTHCGIE
2010 2020 2030 2040 2050
LDEDGSLDGS NDLTIRGRLL SLVEKVTYLK KKQAEKPVAS DSRKSSSLQQ
2060 2070 2080 2090 2100
LISETMVRWA QESVIEDPEL VRAMFVLLHR QYDGIGGLVR ALPKTYTING
2110 2120 2130 2140 2150
VSVEDTINLL ASLGQIRSLL SVRMGKEEEK LMIRGLGDIM NNKVFYQHPN
2160 2170 2180 2190 2200
LMRALGMHET VMEVMVNVLG GGESKEITFP KMVANCCRFL CYFCRISRQN
2210 2220 2230 2240 2250
QKAMFDHLSY LLENSSVGLA SPAMRGSTPL DVAAASVMDN NELALALREP
2260 2270 2280 2290 2300
DLEKVVRYLA GCGLQSCQML VSKGYPDIGW NPVEGERYLD FLRFAVFCNG
2310 2320 2330 2340 2350
ESVEENANVV VRLLIRRPEC FGPALRGEGG NGLLAAMEEA IKIAEDPSRD
2360 2370 2380 2390 2400
GPSPTSGSSK TLDAEEEEDD TIHMGNAIMT FYAALIDLLG RCAPEMHLIH
2410 2420 2430 2440 2450
AGKGEAIRIR SILRSLIPLG DLVGVISIAF QMPTIAKDGK VVEPDMSAGF
2460 2470 2480 2490 2500
CPDHKAAMVL FLDRVYGIEV QDFLLHLLEV GFLPDLRAAA SLDTAALSAT
2510 2520 2530 2540 2550
DMALALNRYL CTAVLPLLTR CAPLFAGTEH HASLIDSLLH TVYRLSKGCS
2560 2570 2580 2590 2600
LTKAQRDSIE VCLLSICGQL RPSMMQHLLR RLVFDVPLLN EHAKMPLKLL
2610 2620 2630 2640 2650
TNHYERCWKY YCLPGGWSNF GAASEEELHL SRKLFWGIFD ALSQKKYEQE
2660 2670 2680 2690 2700
LFKLALPCLS AVAGALPPDY MESNYVSMME KQSSMDSEGN FNPQPVDTSN
2710 2720 2730 2740 2750
ITIPEKLEYF INKYAEHSHD KWSMDKLANG WIYGEIYSDS SKIQPLMKPY
2760 2770 2780 2790 2800
KLLSEKEKEI YRWPIKESLK TMLAWGWRIE RTREGDSMAL YNRTRRISQT
2810 2820 2830 2840 2850
SQVSIDAAHG YSPRAIDMSN VTLSRDLHAM AEMMAENYHN IWAKKKKMEL
2860 2870 2880 2890 2900
ESKGGGNHPL LVPYDTLTAK EKAKDREKAQ DIFKFLQISG YAVSRGFKDL
2910 2920 2930 2940 2950
DLDTPSIEKR FAYSFLQQLI RYVDEAHQYI LEFDGGSRSK GEHFPYEQEI
2960 2970 2980 2990 3000
KFFAKVVLPL IDQYFKNHRL YFLSAASRPL CTGGHASNKE KEMVTSLFCK
3010 3020 3030 3040 3050
LGVLVRHRIS LFGNDATSIV NCLHILGQTL DARTVMKTGL DSVKSALRAF
3060 3070 3080 3090 3100
LDNAAEDLEK TMENLKQGQF THTRSQPKGV TQIINYTTVA LLPMLSSLFE
3110 3120 3130 3140 3150
HIGQHQFGED LILEDVQVSC YRILTSLYAL GTSKSIYVER QRSALGECLA
3160 3170 3180 3190 3200
AFAGAFPIAF LETHLDKHNV YSIYNTRSSR ERAALSLPAN VEDVCPNIPS
3210 3220 3230 3240 3250
LEKLMTEIIE LAESGIRYTQ MPHMMEVVLP MLCSYMSRWW EHGPENHPER
3260 3270 3280 3290 3300
AEMCCTALNS EHMNTLLGNI LKIIYNNLGI DEGAWMKRLA VFSQPIINKV
3310 3320 3330 3340 3350
KPQLLKTHFL PLMEKLKKKA AMVVSEEDHL KAEARGDMSE AELLILDEFT
3360 3370 3380 3390 3400
TLARDLYAFY PLLIRFVDYN RAKWLKEPNP EAEELFRMVA EVFIYWSKSH
3410 3420 3430 3440 3450
NFKREEQNFV VQNEINNMSF LITDTKSKMS KAAISDQERK KMKRKGDRYS
3460 3470 3480 3490 3500
MQTSLIVAAL KRLLPIGLNI CAPGDQELIA LAKNRFSLKD TEEEVRDVIR
3510 3520 3530 3540 3550
SNIHLQGKLE DPAIRWQMAL YKDLPNRAED TSDPERTVER VLDIANVLFH
3560 3570 3580 3590 3600
LEQVEHPQRS KKAVWHKLLS KQRKRAVVAC FRMAPLYNLP RHRAVNLFLQ
3610 3620 3630 3640 3650
GYEKSWIETE EHYFEDKLIE DLAKPGSELP EEDEAMKRVD PLHQLILLFS
3660 3670 3680 3690 3700
RTALTEKCKL EEDFLYMAYA DIMAKSCHDE EDDDGEEEVK SFEVTGSQRS
3710 3720 3730 3740 3750
KEKEMEKQKL LYQQARLHDR GAAEMVLQTF SASKGETGPM VAATLKLGIA
3760 3770 3780 3790 3800
ILNGGNSTVQ QKMLDYLKEK KDVGFFQSLA GLMQSCSVLD LNAFERQNKA
3810 3820 3830 3840 3850
EGLGMVTEEG SGEKVLQDDE FTCDLFRFLQ LLCEGHNSDF QNYLRTQTGN
3860 3870 3880 3890 3900
NTTVNIIIST VDYLLRVQES ISDFYWYYSG KDIIDEQGQR NFSKAIQVAK
3910 3920 3930 3940 3950
QVFNTLTEYI QGPCTGNQQS LAHSRLWDAV VGFLHVFAHM QMKLSQDSSQ
3960 3970 3980 3990 4000
IELLKELMDL QKDMVVMLLS MLEGNVVNGT IGKQMVDMLV ESSNNVEMIL
4010 4020 4030 4040 4050
KFFDMFLKLK DLTSSDTFKE YDPDGKGVIS KRDFHKAMES HKHYTQSETE
4060 4070 4080 4090 4100
FLLSCAETDE NETLDYEEFV KRFHEPAKDI GFNVAVLLTN LSEHMPNDTR
4110 4120 4130 4140 4150
LQTFLELAES VLNYFQPFLG RIEIMGSAKR IERVYFEISE SSRTQWEKPQ
4160 4170 4180 4190 4200
VKESKRQFIF DVVNEGGEKE KMELFVNFCE DTIFEMQLAA QISESDLNER
4210 4220 4230 4240 4250
SANKEESEKE RPEEQAPRMG FFSLLTVQSA LFALRYNVLT LVRMLSLKSL
4260 4270 4280 4290 4300
KKQMKRMKKM TVKDMVSAFF SSYWSVFVTL LHFVASVCRG FFRIVSSLLL
4310 4320 4330 4340 4350
GGSLVEGAKK IKVAELLANM PDPTQDEVRG DEEEGERKPL ESALPSEDLT
4360 4370 4380 4390 4400
DLKELTEESD LLSDIFGLDL KREGGQYKLI PHNPNAGLSD LMTNPIPVPE
4410 4420 4430 4440 4450
VQEKFQEQKV KEEKEGKEET KSEPEKAEGE DGEKEEKAKD DKGKQKLRQL
4460 4470 4480 4490 4500
HTHRYGEPEV PESAFWKKII AYQQKLLNYF ARNFYNMRML ALFVAFAINF
4510 4520 4530 4540 4550
ILLFYKVSTS SVVEGKELPT RTSSDAAKVT TSLDSSPHRI IAVHYVLEES
4560 4570 4580 4590 4600
SGYMEPTLRI LAILHTIISF FCIIGYYCLK VPLVIFKREK EVARKLEFDG
4610 4620 4630 4640 4650
LYITEQPSED DIKGQWDRLV INTQSFPNNY WDKFVKRKVM DKYGEFYGRD
4660 4670 4680 4690 4700
RISELLGMDK AALDFSDARE KKKPKKDSSL SAVLNSIDVK YQMWKLGVVF
4710 4720 4730 4740 4750
TDNSFLYLAW YMTMSVLGHY NNFFFAAHLL DIAMGFKTLR TILSSVTHNG
4760 4770 4780 4790 4800
KQLVLTVGLL AVVVYLYTVV AFNFFRKFYN KSEDGDTPDM KCDDMLTCYM
4810 4820 4830 4840 4850
FHMYVGVRAG GGIGDEIEDP AGDEYEIYRI IFDITFFFFV IVILLAIIQG
4860 4870 4880 4890 4900
LIIDAFGELR DQQEQVKEDM ETKCFICGIG NDYFDTVPHG FETHTLQEHN
4910 4920 4930 4940 4950
LANYLFFLMY LINKDETEHT GQESYVWKMY QERCWEFFPA GDCFRKQYED

QLN
Length:4,953
Mass (Da):562,955
Last modified:February 22, 2012 - v2
Checksum:i2C2798E8A2C4564A
GO
Isoform 2 (identifier: B0LPN4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1952-1952: R → RKT
     3694-3701: Missing.

Show »
Length:4,947
Mass (Da):562,340
Checksum:i2A7FC7A98D194D23
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401E → G in ABY79796 (PubMed:20445169).Curated
Sequence conflicti364 – 3641W → R in ABY79796 (PubMed:20445169).Curated
Sequence conflicti1838 – 18381Q → R in ABY79796 (PubMed:20445169).Curated
Sequence conflicti2691 – 26911F → S in ABY79796 (PubMed:20445169).Curated
Sequence conflicti3216 – 32161I → T in ABY79796 (PubMed:20445169).Curated
Sequence conflicti3226 – 32261E → G in ABY79796 (PubMed:20445169).Curated
Sequence conflicti3355 – 33551D → N in ABY79796 (PubMed:20445169).Curated
Sequence conflicti3541 – 35411V → I in ABY79796 (PubMed:20445169).Curated
Sequence conflicti3751 – 37511I → T in ABY79796 (PubMed:20445169).Curated
Sequence conflicti3885 – 38851D → G in ABY79796 (PubMed:20445169).Curated
Sequence conflicti3990 – 39901V → A in ABY79796 (PubMed:20445169).Curated
Sequence conflicti4196 – 41961D → G in ABY79796 (PubMed:20445169).Curated
Sequence conflicti4262 – 42621V → A in ABY79796 (PubMed:20445169).Curated
Sequence conflicti4536 – 45361S → G in ABY79796 (PubMed:20445169).Curated
Sequence conflicti4667 – 46671D → G in ABY79796 (PubMed:20445169).Curated
Sequence conflicti4930 – 49301Y → H in ABY79796 (PubMed:20445169).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1952 – 19521R → RKT in isoform 2. 1 PublicationVSP_042299
Alternative sequencei3694 – 37018Missing in isoform 2. 1 PublicationVSP_042300

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU346200 mRNA. Translation: ABY79796.1.
AB204523 mRNA. Translation: BAJ10276.1.
RefSeqiNP_001177972.1. NM_001191043.1.
NP_114467.1. NM_032078.2.
UniGeneiRn.20442.

Genome annotation databases

GeneIDi689560.
KEGGirno:689560.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU346200 mRNA. Translation: ABY79796.1.
AB204523 mRNA. Translation: BAJ10276.1.
RefSeqiNP_001177972.1. NM_001191043.1.
NP_114467.1. NM_032078.2.
UniGeneiRn.20442.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K2FNMR-C/D3561-3572[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiB0LPN4. 1 interaction.
STRINGi10116.ENSRNOP00000059019.

Chemistry

BindingDBiB0LPN4.
ChEMBLiCHEMBL3388.

PTM databases

iPTMnetiB0LPN4.

Proteomic databases

PaxDbiB0LPN4.
PRIDEiB0LPN4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi689560.
KEGGirno:689560.

Organism-specific databases

CTDi6262.
RGDi620314. Ryr2.

Phylogenomic databases

eggNOGiKOG2243. Eukaryota.
ENOG410YCNW. LUCA.
HOGENOMiHOG000231428.
HOVERGENiHBG006699.
InParanoidiB0LPN4.
KOiK04962.

Miscellaneous databases

EvolutionaryTraceiB0LPN4.
PROiB0LPN4.

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.
IPR002048. EF_hand_dom.
IPR014821. Ins145_P3_rcpt.
IPR005821. Ion_trans_dom.
IPR016093. MIR_motif.
IPR013662. RIH_assoc-dom.
IPR000699. RIH_dom.
IPR013333. Ryan_recept.
IPR003032. Ryanodine_rcpt.
IPR015925. Ryanodine_recept-rel.
IPR009460. Ryanrecept_TM4-6.
IPR003877. SPRY_dom.
[Graphical view]
PANTHERiPTHR13715. PTHR13715. 5 hits.
PfamiPF13833. EF-hand_8. 1 hit.
PF08709. Ins145_P3_rec. 1 hit.
PF00520. Ion_trans. 1 hit.
PF02815. MIR. 1 hit.
PF08454. RIH_assoc. 1 hit.
PF06459. RR_TM4-6. 1 hit.
PF01365. RYDR_ITPR. 2 hits.
PF02026. RyR. 4 hits.
PF00622. SPRY. 3 hits.
[Graphical view]
PRINTSiPR00795. RYANODINER.
SMARTiSM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMiSSF100909. SSF100909. 2 hits.
SSF47473. SSF47473. 1 hit.
SSF49899. SSF49899. 2 hits.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Subtype identification and functional characterization of ryanodine receptors in rat cerebral artery myocytes."
    Vaithianathan T., Narayanan D., Asuncion-Chin M.T., Jeyakumar L.H., Liu J., Fleischer S., Jaggar J.H., Dopico A.M.
    Am. J. Physiol. 299:C264-C278(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Cerebral artery.
  2. "A novel ryanodine receptor expressed in pancreatic islets by alternative splicing from type 2 ryanodine receptor gene."
    Takasawa S., Kuroki M., Nata K., Noguchi N., Ikeda T., Yamauchi A., Ota H., Itaya-Hironaka A., Sakuramoto-Tsuchida S., Takahashi I., Yoshikawa T., Shimosegawa T., Okamoto H.
    Biochem. Biophys. Res. Commun. 397:140-145(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Pancreatic islet.
  3. "Ryanodine receptor phosphorylation at serine 2030, 2808 and 2814 in rat cardiomyocytes."
    Huke S., Bers D.M.
    Biochem. Biophys. Res. Commun. 376:80-85(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-2798 AND SER-2804, TISSUE SPECIFICITY.
  4. "Kinetics of FKBP12.6 binding to ryanodine receptors in permeabilized cardiac myocytes and effects on Ca sparks."
    Guo T., Cornea R.L., Huke S., Camors E., Yang Y., Picht E., Fruen B.R., Bers D.M.
    Circ. Res. 106:1743-1752(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FKBP1A AND FKBP1B, TISSUE SPECIFICITY.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1334; SER-1863; SER-2021; SER-2798; SER-2801 AND SER-2804, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "S100A1 and calmodulin compete for the same binding site on ryanodine receptor."
    Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., Weber D.J.
    J. Biol. Chem. 283:26676-26683(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 3561-3572 IN COMPLEX WITH S100A1, INTERACTION WITH CALM AND S100A1.

Entry informationi

Entry nameiRYR2_RAT
AccessioniPrimary (citable) accession number: B0LPN4
Secondary accession number(s): D7UNT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: February 22, 2012
Last modified: June 8, 2016
This is version 76 of the entry and version 2 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 (By similarity).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

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