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Protein

Ryanodine receptor 2

Gene

RYR2

Organism
Oryctolagus cuniculus (Rabbit)
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. Required for cellular calcium ion homeostasis. Required for embryonic heart development (By similarity). The calcium channel activity is modulated by formation of heterotetramers with RYR3.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

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
Cardiac muscle-type ryanodine receptor
Type 2 ryanodine receptor
Gene namesi
Name:RYR2
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Unplaced

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 42824282CytoplasmicSequence analysisAdd
BLAST
Transmembranei4283 – 430321HelicalSequence analysisAdd
BLAST
Transmembranei4505 – 452521HelicalSequence analysisAdd
BLAST
Transmembranei4582 – 460221HelicalSequence analysisAdd
BLAST
Transmembranei4732 – 475221HelicalSequence analysisAdd
BLAST
Transmembranei4771 – 479121HelicalSequence analysisAdd
BLAST
Intramembranei4822 – 483110Pore-formingBy similarity
Transmembranei4852 – 487221HelicalSequence analysisAdd
BLAST
Topological domaini4873 – 496997CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • intracellular membrane-bounded organelle Source: AgBase
  • sarcoplasmic reticulum Source: UniProtKB
  • sarcoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Sarcoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 49694969Ryanodine receptor 2PRO_0000219362Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1341 – 13411PhosphoserineBy similarity
Modified residuei1869 – 18691PhosphoserineBy similarity
Modified residuei2031 – 20311Phosphoserine; by PKABy similarity
Modified residuei2370 – 23701PhosphoserineBy similarity
Modified residuei2698 – 26981PhosphoserineBy similarity
Modified residuei2798 – 27981PhosphoserineBy similarity
Modified residuei2809 – 28091Phosphoserine; by CaMK2D and PKA1 Publication
Modified residuei2812 – 28121PhosphoserineBy similarity
Modified residuei2815 – 28151Phosphoserine; by CaMK2DBy similarity
Modified residuei2948 – 29481PhosphoserineBy similarity

Post-translational modificationi

Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2809 and Ser-2815 increases the open probability of the calcium channel. Phosphorylation is increased in failing heart, leading to calcium leaks and increased cytoplasmic Ca2+ levels.1 Publication
Phosphorylation at Ser-2031 by PKA enhances the response to lumenal calcium.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP30957.

PTM databases

iPTMnetiP30957.

Expressioni

Tissue specificityi

Heart and brain.

Interactioni

Subunit structurei

Homotetramer. Can also form heterotetramers with RYR1 and RYR3. 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. 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 SEPN1 (PubMed:18713863).By similarity1 Publication

Protein-protein interaction databases

IntActiP30957. 1 interaction.
MINTiMINT-8146741.
STRINGi9986.ENSOCUP00000016860.

Structurei

3D structure databases

ProteinModelPortaliP30957.
SMRiP30957. Positions 3582-3608.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini110 – 16556MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini172 – 21746MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini225 – 28056MIR 3PROSITE-ProRule annotationAdd
BLAST
Domaini286 – 34560MIR 4PROSITE-ProRule annotationAdd
BLAST
Domaini351 – 40858MIR 5PROSITE-ProRule annotationAdd
BLAST
Domaini599 – 809211B30.2/SPRY 1PROSITE-ProRule annotationAdd
BLAST
Repeati853 – 9661141Add
BLAST
Repeati967 – 10801142Add
BLAST
Domaini1025 – 1222198B30.2/SPRY 2PROSITE-ProRule annotationAdd
BLAST
Domaini1357 – 1562206B30.2/SPRY 3PROSITE-ProRule annotationAdd
BLAST
Repeati2693 – 28111193Add
BLAST
Repeati2813 – 29261144Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni853 – 292620744 X approximate repeatsAdd
BLAST
Regioni3582 – 361130Interaction with CALMBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili4413 – 444634Sequence analysisAdd
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

Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2243. Eukaryota.
ENOG410YCNW. LUCA.
HOGENOMiHOG000231428.
HOVERGENiHBG006699.
InParanoidiP30957.

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]

Sequencei

Sequence statusi: Complete.

P30957-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADGGEGEDE IQFLRTDDEV VLQCTATIHK EQQKLCLAAE GFGNRLCFLE
60 70 80 90 100
STSNSKNVPP DLSICTFVLE QSLLVRALQE MLANTVEKSE GQVDVEKWKF
110 120 130 140 150
MMKTAQGGGH RTLLYGHAIL LRHSYSGMYL CCLSTSRSST DKLAFDVGLQ
160 170 180 190 200
EDTTGEACWW TIHPASKQRS EGEKVRVGDD LILVSVSSER YLHLSYGNGS
210 220 230 240 250
LHVDAAFQQT LWSVAPISSG SEAAQGYLIG GDVLRLLHGH MDECLTVPSG
260 270 280 290 300
EHGEEQRRTV HYEGGAVSVH ARSLWRLETL RVAWSGSHIR WGQPFRLRHV
310 320 330 340 350
TTGKYLSLME DKNLLLMDKE KADVKSTAFT FRSSKEKLDG GVRKEVDGMG
360 370 380 390 400
TSEIKYGDSI CYIQHVDTGL WLTYQSVDVK SVRMGSIQRK AIMHHEGHMD
410 420 430 440 450
DGLNLSRSQH EESRTARVIR STVFLFNRFI RGLDALSKKA KASSVDLPIE
460 470 480 490 500
SVSLSLQDLI GYFHPPDEHL EHEDKQNRLR ALKNRQNLFQ EEGMINLVLE
510 520 530 540 550
CIDRLHVYSS AAHFADVAGR EAGESWKSIL NSLYELLAAL IRGNRKNCAQ
560 570 580 590 600
FSGSLDWLIS RLERLEASSG ILEVLHCVLV ESPEALNIIK EGHIKSIISL
610 620 630 640 650
LDKHGRNHKV LDVLCSLCVC HGVAVRSNQH LICDNLLPGR DLLLQTRLVN
660 670 680 690 700
HVSSMRPNIF LGVSEGSAQY KKWYYELMVD HTEPFVTAEA THLRVGWAST
710 720 730 740 750
EGYSPYPGGG EEWGGNGVGD DLFSYGFDGL HLWSGCIART VSSPNQHLLR
760 770 780 790 800
TDDVISCCLD LSAPSISFRI NGQPVQGMFE NFNIDGLFFP VVSFSAGIKV
810 820 830 840 850
RFLLGGRHGE FKFLPPPGYA PCYEAVLPKE KLKVEHSREY KQERTYTRDL
860 870 880 890 900
LGPTVSLTQA AFTPIPVDTS QIVLPPHLER IREKLAENIH ELWVMNKIEL
910 920 930 940 950
GWQYGPVRDD NKRQHPCLVE FSKLPEQERN YNLQMSLETL KTLLALGCHV
960 970 980 990 1000
GISDEHAEEK VKKMKLPKNY QLTSGYKPAP MDLSFIKLTP SQEAMVDKLA
1010 1020 1030 1040 1050
ENAHNVWARD RIRQGWTYGI QQDVKNRRNP RLVPYTLLDD RTKKSNKDSL
1060 1070 1080 1090 1100
REAVRTLLGY GYNLEAPDQD HAARAEVCSG TGERFRIFRA EKTYAVKAGR
1110 1120 1130 1140 1150
WYFEFEAVTS GDMRVGWSRP GCQPDQELGS DERAFAFDGF KAQRWHQGNE
1160 1170 1180 1190 1200
HYGRSWQAGD VVGCMVDMNE HTMMFTLNGE ILLDDSGSEL AFKDFDVGDG
1210 1220 1230 1240 1250
FIPVCSLGVA QVGRMNFGKD VSTLKYFTIC GLQEGYEPFA VNTNRDITMW
1260 1270 1280 1290 1300
LSKRLPQFLQ VPSNHEHIEV TRIDGTIDSS PCLKVTQKSF GSQNSNTDIM
1310 1320 1330 1340 1350
FYRLSMPIEC AEVFSKTVPG GLPGAGLFGP KNDLEDYDAD SDFEVLMKTA
1360 1370 1380 1390 1400
HGHLVPDRVD KDKETTKAEF NNHKDYAQEK PSRLKQRFLL RRTKPDYSTS
1410 1420 1430 1440 1450
HSARLTEDVL ADDRDDYDFL MQTSTYYYSV RIFPGQEPAN VWVGWITSDF
1460 1470 1480 1490 1500
HQYDTGFDLD RVRTVTVTLG DEKGKVHESI KRSNCYMVCA GESMSPGQGR
1510 1520 1530 1540 1550
NNNGLEIGCV VDAASGLLTF IANGKELSTY YQVEPSTKLF PAVFAQATSP
1560 1570 1580 1590 1600
NVFQFELGRI KNVMPLSAGL FKSEHKNPVP QCPPRLHVQF LSHVLWSRMP
1610 1620 1630 1640 1650
NQFLKVDVSR ISERQGWLVQ CLDPLQFMSL HIPEENRSVD ILELTEQEEL
1660 1670 1680 1690 1700
LKFHYHTLRL YSAVCALGNH RVAHALCSHV DEPQLLYAIE NKYMPGLLRT
1710 1720 1730 1740 1750
GYYDLLIDIH LSSYATARLM MNNEFIVPMT EETKSITLFP DENKKHGLPG
1760 1770 1780 1790 1800
IGLSTSLRPR MQFSSPSFVS INNECYQYSP EFPLDILKAK TIQMLTEAVK
1810 1820 1830 1840 1850
EGSLHGRDPV GGTTEFLFVP LIKLFYTLLI MGIFHNEDLR HILQLIEPSV
1860 1870 1880 1890 1900
FKDAATPEEE GDTLEEEPSV EDTKLEGAGE EEAKVGKRPK EGLLQMKLPE
1910 1920 1930 1940 1950
PVKLQMCLLL QYLCDCQVRH RIEAIVAFSD DFVAKLQDNQ RFRYNEVMQA
1960 1970 1980 1990 2000
LNMSAALTAR KTKEFRSPPQ EQINMLLNFK DDKSECPCPE EIRDQLLDFH
2010 2020 2030 2040 2050
EDLMTHCGIE LDEDGSLDGN SDLTIRGRLL SLVEKVTYLK KKQTEKPVES
2060 2070 2080 2090 2100
DSRKSSTLQQ LISETMVRWA QESVIEDPEL VRAMFVLLHR QYDGIGGLVR
2110 2120 2130 2140 2150
ALPKTYTING VSVEDTINLL ASLGQIRSLL SVRMGKEEEK LMIRGLGDIM
2160 2170 2180 2190 2200
NNKVFYQHPN LMRALGMHET VMEVMVNVLG GGESKEITFP KMVANCCRFL
2210 2220 2230 2240 2250
CYFCRISRQN QKAMFDHLSY LLENSSVGLA SPAMRGSTPL DVAAASVMDN
2260 2270 2280 2290 2300
NELALALREP DLEKVVVRYL AGCGLQSCQM LVSKGYPDIG WNPVEGERYL
2310 2320 2330 2340 2350
DFLRFAVFCN GESVEENANV VVRLLIRRPE CFGPALRGEG GNGLLAAMEE
2360 2370 2380 2390 2400
AIKIAEDPSR DGPSPTSGSS KTLDTEEEED DTIHMGNAIM TFYAALIDLL
2410 2420 2430 2440 2450
GRCAPEMHLI HAGKGEAIRI RSILRSLIPL GDLVGVISIA FQMPTIAKDG
2460 2470 2480 2490 2500
NVVEPDMSAG FCPDHKAAMV LFLDRVYGIE VQDFLLHLLE VGFLPDLRAA
2510 2520 2530 2540 2550
ASLDTAALSA TDMALALNRY LCTAVLPLLT RCAPLFAGTE HHASLIDSLL
2560 2570 2580 2590 2600
HTVYRLSKGC SLTKAQRDSI EVCLLSICGQ LRPSMMQHLL RRLVFDVPLL
2610 2620 2630 2640 2650
NEHAKMPLKL LTNHYERCWK YYCLPGGWGN FGAASEEELH LSRKLFWGIF
2660 2670 2680 2690 2700
DALSQKKYEQ ELFKLALPCL SAVAGALPPD YMESNYVSMM EKQSSMDSEG
2710 2720 2730 2740 2750
NFNPQPVDTS NIIIPEKLEY FINKYAEHSH DKWSMDKLAN GWIYGEIYSD
2760 2770 2780 2790 2800
SSKIQPLMKP YKLLSEKEKE IYRWPIKESL KTMLAWGWRI ERTREGDSMA
2810 2820 2830 2840 2850
LYNRTRRISQ TSQVSVDAAH GYSPRAIDMS NVTLSRDLHA MAEMMAENYH
2860 2870 2880 2890 2900
NIWAKKKKLE LESKGGGNHP LLVPYDTLTA KEKAKDREKA QDILKFLQIN
2910 2920 2930 2940 2950
GYAVSRGFKD LELDTPSIEK RFAYSFLQQL IRYVDEAHQY ILEFDGGSRS
2960 2970 2980 2990 3000
KGEHFPYEQE IKFFAKVVLP LIDQYFKNHR LYFLSAASRP LCSGGHASNK
3010 3020 3030 3040 3050
EKEMVTSLFC KLGVLVRHRI SLFGNDATSI VNCLHILGQT LDARTVMKTG
3060 3070 3080 3090 3100
LESVKSALRA FLDNAAEDLE KTMENLKQGQ FTHTRNQPRG VTQIINYTTV
3110 3120 3130 3140 3150
ALLPMLSSLF EHIGQHQFGE DLILEDVQVS CYRILTSLYA LGTSKSIYVE
3160 3170 3180 3190 3200
RQRSALGECL AAFAGAFPVA FLETHLNKHN IYSIYNTKSS RERAALSLPA
3210 3220 3230 3240 3250
NVEDVCPNIP SLEKLMEEIV ELAESGIRYT QMPHVMEVIL PMLCSYMSRW
3260 3270 3280 3290 3300
WEHGPESNPG RAEMCCTALN SEHMNTLLGN ILKIIYNNLG IDEGAWMKRL
3310 3320 3330 3340 3350
AVFSQPIINK VKPQLLKTHF LPLMEKLKKK AAMVVSEEDH LKAEARGDMS
3360 3370 3380 3390 3400
EAELLILDEF TTLARDLYAF YPLLIRFVDY NRAKWLKEPT PEAEELFRMV
3410 3420 3430 3440 3450
AEVFIYWSKS HNFKREEQNF VVQNEINNMS FLITDTKSKM SKAAVSDQER
3460 3470 3480 3490 3500
KKMKRKGDRY SMQTSLIVAA LKRLLPIGLN ICAPGDQELI ALAKNRFSLK
3510 3520 3530 3540 3550
ATEDEVRDII RNNIHLQGKL EDPAIRWQMA LYKDLPNRTE ETSDPEKTVE
3560 3570 3580 3590 3600
RVLDIANVLF HLEQKSKFIG RRYYNLVEHP QRSKKAVWHK LLSKQRKRAV
3610 3620 3630 3640 3650
VACFRMAPLY NLPRHRAVNL FLQGYEKSWI ETEEHYFEDK LIEDLAKPGA
3660 3670 3680 3690 3700
EPPEEDEVTK RVDPLHQLIL LFSRTALTEK CKLEEDFLYM AYADIMAKSC
3710 3720 3730 3740 3750
HDEEDDDGEE EVKSFEEKEM EKQKLLYQQA RLHDRGAAEM VLQTISASKG
3760 3770 3780 3790 3800
ETGPMVAATL KLGIAILNGG NSTVQQKMLD YLKEKKDVGF FQSLAGLMQS
3810 3820 3830 3840 3850
CSVLDLNAFE RQNKAEGLGM VTEEGSGEKV LQDDEFTCDL FRFLQLLCEG
3860 3870 3880 3890 3900
HNSDFQNYLR TQTGNNTTVN IIISTVDYLL RVQESISDFY WYYSGKDVID
3910 3920 3930 3940 3950
EQGQRNFSKA IQVAKQVFNT LTEYIQGPCT GNQQSLAHSR LWDAVVGFLH
3960 3970 3980 3990 4000
VFAHMQMKLS QDSSQIELLK ELMDLQKDMV VMLLSMLEGN VVNGTIGKQM
4010 4020 4030 4040 4050
VDMLVESSNN VEMILKFFDM FLKLKDLTSS DTFKEYDPDG KGIISKRDFH
4060 4070 4080 4090 4100
KAMESHKHYT QSETEFLLSC AETDENETLD YEEFVKRFHE PAKDIGFNVA
4110 4120 4130 4140 4150
VLLTNLSEHM PNDTRLQTFL ELAESVLNYF QPFLGRIEIM GSAKRIERVY
4160 4170 4180 4190 4200
FEISESSRTQ WEKPQVKESK RQFIFDVVNE GGEKEKMELF VNFCEDTIFE
4210 4220 4230 4240 4250
MQLAAQISES DLNERSANKE ESEKERPEEQ GPKMGFFSVL TVRSALFALR
4260 4270 4280 4290 4300
YNILTLMRML SLKSLKKQMK KMKKMTVKDM VTAFFSSYWS IFMTLLHFVA
4310 4320 4330 4340 4350
SVFRGFFRIV CSLLLGGSLV EGAKKIKVAE LLANMPDPTQ DEVRGDGEEG
4360 4370 4380 4390 4400
ERKPMETTLP SEDLTDLKEL TEESDLLSDI FGLDLKREGG QYKLIPHNPN
4410 4420 4430 4440 4450
AGLSDLMSNP VLIPEEQEKF QEQKTKEEEK EEKEETKSEP EKAEGEDGEK
4460 4470 4480 4490 4500
EEKVKEDKGK QKLRQLHTHR YGEPEVPESA FWKKIIAYQQ KLLNYLARNF
4510 4520 4530 4540 4550
YNMRMLALFV AFAINFILLF YKVSTSSVVE GKELPSRSTS ENAKVTTSLD
4560 4570 4580 4590 4600
SSSHRIIAVH YVLEESSGYM EPTLRILAIL HTVISFFCII GYYCLKVPLV
4610 4620 4630 4640 4650
IFKREKEVAR KLEFDGLYIT EQPSEDDIKG QWDRLVINTQ SFPNNYWDKF
4660 4670 4680 4690 4700
VKRKVMDKYG EFYGRDRISE LLGMDKAALD FSDAREKKKP KKDSSLSAVL
4710 4720 4730 4740 4750
NSIDVKYQMW KLGVVFTDNS FLYLAWYMTM SILGHYNNFF FAAHLLDIAM
4760 4770 4780 4790 4800
GFKTLRTILS SVTHNGKQLV LTVGLLAVVV YLYTVVAFNF FRKFYNKSED
4810 4820 4830 4840 4850
GDTPDMKCDD MLTCYMFHMY VGVRAGGGIG DEIEDPAGDE YEIYRIIFDI
4860 4870 4880 4890 4900
TFFFFVIVIL LAIIQGLIID AFGELRDQQE QVKEDMETKC FICGIGNDYF
4910 4920 4930 4940 4950
DTVPHGFETH TLQEHNLANY LFFLMYLINK DETEHTGQES YVWKMYQERC
4960
WEFFPAGDCF RKQYEDQLN
Length:4,969
Mass (Da):565,073
Last modified:October 5, 2010 - v3
Checksum:iFF6E0684B974BB4D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59743 mRNA. Translation: AAA31179.1.
PIRiA37113.
UniGeneiOcu.1832.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M59743 mRNA. Translation: AAA31179.1.
PIRiA37113.
UniGeneiOcu.1832.

3D structure databases

ProteinModelPortaliP30957.
SMRiP30957. Positions 3582-3608.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP30957. 1 interaction.
MINTiMINT-8146741.
STRINGi9986.ENSOCUP00000016860.

PTM databases

iPTMnetiP30957.

Proteomic databases

PRIDEiP30957.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG2243. Eukaryota.
ENOG410YCNW. LUCA.
HOGENOMiHOG000231428.
HOVERGENiHBG006699.
InParanoidiP30957.

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...

Entry informationi

Entry nameiRYR2_RABIT
AccessioniPrimary (citable) accession number: P30957
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 5, 2010
Last modified: July 6, 2016
This is version 130 of the entry and version 3 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 and maintains the channel in an open conformation. Channel activity is regulated by calmodulin (CALM). The calcium release channel is activated by calcium ions and ATP. Channel activity is inhibited by magnesium ions (By similarity).By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.