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Q15413

- RYR3_HUMAN

UniProt

Q15413 - RYR3_HUMAN

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Protein

Ryanodine receptor 3

Gene

RYR3

Organism
Homo sapiens (Human)
Status
Reviewed - 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 in muscle and thereby plays a role in triggering muscle contraction. May regulate Ca2+ release by other calcium channels. Calcium channel that mediates Ca2+-induced Ca2+ release from the endoplasmic reticulum in non-muscle cells. Contributes to cellular calcium ion homeostasis (By similarity). Plays a role in cellular calcium signaling.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei3883 – 38831Important for activation by Ca(2+)By similarity

GO - Molecular functioni

  1. calcium-induced calcium release activity Source: Ensembl
  2. calcium ion binding Source: InterPro
  3. calcium-release channel activity Source: UniProtKB
  4. ryanodine-sensitive calcium-release channel activity Source: UniProtKB

GO - Biological processi

  1. calcium ion transmembrane transport Source: UniProtKB
  2. calcium ion transport Source: UniProtKB
  3. cellular response to ATP Source: UniProtKB
  4. cellular response to caffeine Source: UniProtKB
  5. cellular response to calcium ion Source: UniProtKB
  6. cellular response to magnesium ion Source: UniProtKB
  7. ion transmembrane transport Source: Reactome
  8. negative regulation of cytosolic calcium ion concentration Source: Ensembl
  9. protein homotetramerization Source: UniProtKB
  10. striated muscle contraction Source: Ensembl
  11. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Ligand-gated ion channel, Receptor

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_160189. Stimuli-sensing channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Ryanodine receptor 3
Short name:
RYR-3
Short name:
RyR3
Alternative name(s):
Brain ryanodine receptor-calcium release channel
Brain-type ryanodine receptor
Type 3 ryanodine receptor
Gene namesi
Name:RYR3
Synonyms:HBRR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:10485. RYR3.

Subcellular locationi

Sarcoplasmic reticulum membrane Curated; Multi-pass membrane protein Curated. Membrane Curated; Multi-pass membrane protein Curated. Microsome membrane By similarity; Multi-pass membrane protein By similarity
Note: The number of predicted transmembrane domains varies between orthologs, but both N-terminus and C-terminus seem to be cytoplasmic.By similarity

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB
  2. junctional membrane complex Source: Ensembl
  3. perinuclear region of cytoplasm Source: Ensembl
  4. sarcoplasmic reticulum membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Microsome, Sarcoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34897.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 48704870Ryanodine receptor 3PRO_0000219363Add
BLAST

Proteomic databases

PaxDbiQ15413.
PRIDEiQ15413.

PTM databases

PhosphoSiteiQ15413.

Expressioni

Tissue specificityi

Brain, skeletal muscle, placenta and possibly liver and kidney. In brain, highest levels are found in the cerebellum, hippocampus, caudate nucleus and amygdala, with lower levels in the corpus callosum, substantia nigra and thalamus.2 Publications

Gene expression databases

BgeeiQ15413.
CleanExiHS_RYR3.
GenevestigatoriQ15413.

Organism-specific databases

HPAiCAB006887.

Interactioni

Subunit structurei

Homotetramer. Heterotetramer with RYR2. Interacts with CALM (By similarity). Interacts with FKBP1A.By similarity1 Publication

Protein-protein interaction databases

BioGridi112175. 7 interactions.
IntActiQ15413. 2 interactions.
STRINGi9606.ENSP00000373884.

Structurei

Secondary structure

1
4870
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2612 – 263524
Turni2646 – 26494
Helixi2657 – 26593
Helixi2662 – 268120
Beta strandi2685 – 26884
Helixi2695 – 270410
Helixi2723 – 27253
Helixi2730 – 275728
Helixi2769 – 27713
Helixi2774 – 279219
Turni2793 – 27953
Beta strandi2796 – 27994

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ERVX-ray1.75A2597-2800[»]
ProteinModelPortaliQ15413.
SMRiQ15413. Positions 13-530, 3469-3495.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 41864186CytoplasmicBy similarityAdd
BLAST
Topological domaini4774 – 487097CytoplasmicBy similarityAdd
BLAST

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei4723 – 473210Pore-formingBy similarity

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4187 – 420721HelicalSequence AnalysisAdd
BLAST
Transmembranei4410 – 443021HelicalSequence AnalysisAdd
BLAST
Transmembranei4485 – 450521HelicalSequence AnalysisAdd
BLAST
Transmembranei4610 – 463021HelicalSequence AnalysisAdd
BLAST
Transmembranei4633 – 465321HelicalSequence AnalysisAdd
BLAST
Transmembranei4672 – 469221HelicalSequence AnalysisAdd
BLAST
Transmembranei4753 – 477321HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini100 – 15556MIR 1PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 20746MIR 2PROSITE-ProRule annotationAdd
BLAST
Domaini215 – 26955MIR 3PROSITE-ProRule annotationAdd
BLAST
Domaini275 – 33359MIR 4PROSITE-ProRule annotationAdd
BLAST
Domaini343 – 40058MIR 5PROSITE-ProRule annotationAdd
BLAST
Domaini585 – 796212B30.2/SPRY 1PROSITE-ProRule annotationAdd
BLAST
Repeati840 – 9531141Add
BLAST
Repeati954 – 10681152Add
BLAST
Domaini1012 – 1208197B30.2/SPRY 2PROSITE-ProRule annotationAdd
BLAST
Domaini1254 – 1466213B30.2/SPRY 3PROSITE-ProRule annotationAdd
BLAST
Repeati2589 – 27071193Add
BLAST
Repeati2708 – 28201134Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni840 – 282019814 X approximate repeatsAdd
BLAST
Regioni2322 – 233514Interaction with FKBP1AAdd
BLAST
Regioni3469 – 349830Interaction 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

eggNOGiNOG247670.
GeneTreeiENSGT00760000119152.
HOGENOMiHOG000231428.
HOVERGENiHBG006699.
InParanoidiQ15413.
KOiK04963.
OMAiIDQVDPF.
OrthoDBiEOG71K622.
PhylomeDBiQ15413.
TreeFamiTF315244.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR001870. 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. 1 hit.
PfamiPF08709. 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. 1 hit.
SSF48371. SSF48371. 10 hits.
SSF49899. SSF49899. 3 hits.
SSF82109. SSF82109. 2 hits.
PROSITEiPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15413-1) [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.

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        10         20         30         40         50
MAEGGEGGED EIQFLRTEDE VVLQCIATIH KEQRKFCLAA EGLGNRLCFL
60 70 80 90 100
EPTSEAKYIP PDLCVCNFVL EQSLSVRALQ EMLANTGENG GEGAAQGGGH
110 120 130 140 150
RTLLYGHAVL LRHSFSGMYL TCLTTSRSQT DKLAFDVGLR EHATGEACWW
160 170 180 190 200
TIHPASKQRS EGEKVRIGDD LILVSVSSER YLHLSVSNGN IQVDASFMQT
210 220 230 240 250
LWNVHPTCSG SSIEEGYLLG GHVVRLFHGH DECLTIPSTD QNDSQHRRIF
260 270 280 290 300
YEAGGAGTRA RSLWRVEPLR ISWSGSNIRW GQAFRLRHLT TGHYLALTED
310 320 330 340 350
QGLILQDRAK SDTKSTAFSF RASKELKEKL DSSHKRDIEG MGVPEIKYGD
360 370 380 390 400
SVCFVQHIAS GLWVTYKAQD AKTSRLGPLK RKVILHQEGH MDDGLTLQRC
410 420 430 440 450
QREESQAARI IRNTTALFSQ FVSGNNRTAA PITLPIEEVL QTLQDLIAYF
460 470 480 490 500
QPPEEEMRHE DKQNKLRSLK NRQNLFKEEG MLALVLNCID RLNVYNSVAH
510 520 530 540 550
FAGIAREESG MAWKEILNLL YKLLAALIRG NRNNCAQFSN NLDWLISKLD
560 570 580 590 600
RLESSSGILE VLHCILTESP EALNLIAEGH IKSIISLLDK HGRNHKVLDI
610 620 630 640 650
LCSLCLCNGV AVRANQNLIC DNLLPRRNLL LQTRLINDVT SIRPNIFLGV
660 670 680 690 700
AEGSAQYKKW YFELIIDQVD PFLTAEPTHL RVGWASSSGY APYPGGGEGW
710 720 730 740 750
GGNGVGDDLY SYGFDGLHLW SGRIPRAVAS INQHLLRSDD VVSCCLDLGV
760 770 780 790 800
PSISFRINGQ PVQGMFENFN TDGLFFPVMS FSAGVKVRFL MGGRHGEFKF
810 820 830 840 850
LPPSGYAPCY EALLPKEKMR LEPVKEYKRD ADGIRDLLGT TQFLSQASFI
860 870 880 890 900
PCPVDTSQVI LPPHLEKIRD RLAENIHELW GMNKIELGWT FGKIRDDNKR
910 920 930 940 950
QHPCLVEFSK LPETEKNYNL QMSTETLKTL LALGCHIAHV NPAAEEDLKK
960 970 980 990 1000
VKLPKNYMMS NGYKPAPLDL SDVKLLPPQE ILVDKLAENA HNVWAKDRIK
1010 1020 1030 1040 1050
QGWTYGIQQD LKNKRNPRLV PYALLDERTK KSNRDSLREA VRTFVGYGYN
1060 1070 1080 1090 1100
IEPSDQELAD SAVEKVSIDK IRFFRVERSY AVRSGKWYFE FEVVTGGDMR
1110 1120 1130 1140 1150
VGWARPGCRP DVELGADDQA FVFEGNRGQR WHQGSGYFGR TWQPGDVVGC
1160 1170 1180 1190 1200
MINLDDASMI FTLNGELLIT NKGSELAFAD YEIENGFVPI CCLGLSQIGR
1210 1220 1230 1240 1250
MNLGTDASTF KFYTMCGLQE GFEPFAVNMN RDVAMWFSKR LPTFVNVPKD
1260 1270 1280 1290 1300
HPHIEVMRID GTMDSPPCLK VTHKTFGTQN SNADMIYCRL SMPVECHSSF
1310 1320 1330 1340 1350
SHSPCLDSEA FQKRKQMQEI LSHTTTQCYY AIRIFAGQDP SCVWVGWVTP
1360 1370 1380 1390 1400
DYHLYSEKFD LNKNCTVTVT LGDERGRVHE SVKRSNCYMV WGGDIVASSQ
1410 1420 1430 1440 1450
RSNRSNVDLE IGCLVDLAMG MLSFSANGKE LGTCYQVEPN TKVFPAVFLQ
1460 1470 1480 1490 1500
PTSTSLFQFE LGKLKNAMPL SAAIFRSEEK NPVPQCPPRL DVQTIQPVLW
1510 1520 1530 1540 1550
SRMPNSFLKV ETERVSERHG WVVQCLEPLQ MMALHIPEEN RCVDILELCE
1560 1570 1580 1590 1600
QEDLMRFHYH TLRLYSAVCA LGNSRVAYAL CSHVDLSQLF YAIDNKYLPG
1610 1620 1630 1640 1650
LLRSGFYDLL ISIHLASAKE RKLMMKNEYI IPITSTTRNI RLFPDESKRH
1660 1670 1680 1690 1700
GLPGVGLRTC LKPGFRFSTP CFVVTGEDHQ KQSPEIPLES LRTKALSMLT
1710 1720 1730 1740 1750
EAVQCSGAHI RDPVGGSVEF QFVPVLKLIG TLLVMGVFDD DDVRQILLLI
1760 1770 1780 1790 1800
DPSVFGEHSA GTEEGAEKEE VTQVEEKAVE AGEKAGKEAP VKGLLQTRLP
1810 1820 1830 1840 1850
ESVKLQMCEL LSYLCDCELQ HRVEAIVAFG DIYVSKLQAN QKFRYNELMQ
1860 1870 1880 1890 1900
ALNMSAALTA RKTKEFRSPP QEQINMLLNF QLGENCPCPE EIREELYDFH
1910 1920 1930 1940 1950
EDLLLHCGVP LEEEEEEEED TSWTGKLCAL VYKIKGPPKP EKEQPTEEEE
1960 1970 1980 1990 2000
RCPTTLKELI SQTMICWAQE DQIQDSELVR MMFNLLRRQY DSIGELLQAL
2010 2020 2030 2040 2050
RKTYTISHTS VSDTINLLAA LGQIRSLLSV RMGKEEELLM INGLGDIMNN
2060 2070 2080 2090 2100
KVFYQHPNLM RVLGMHETVM EVMVNVLGTE KSQIAFPKMV ASCCRFLCYF
2110 2120 2130 2140 2150
CRISRQNQKA MFEHLSYLLE NSSVGLASPS MRGSTPLDVA ASSVMDNNEL
2160 2170 2180 2190 2200
ALSLEEPDLE KVVTYLAGCG LQSCPMLLAK GYPDVGWNPI EGERYLSFLR
2210 2220 2230 2240 2250
FAVFVNSESV EENASVVVKL LIRRPECFGP ALRGEGGNGL LAAMQGAIKI
2260 2270 2280 2290 2300
SENPALDLPS QGYKREVSTG DDEEEEEIVH MGNAIMSFYS ALIDLLGRCA
2310 2320 2330 2340 2350
PEMHLIQTGK GEAIRIRSIL RSLVPTEDLV GIISIPLKLP SLNKDGSVSE
2360 2370 2380 2390 2400
PDMAANFCPD HKAPMVLFLD RVYGIKDQTF LLHLLEVGFL PDLRASASLD
2410 2420 2430 2440 2450
TVSLSTTEAA LALNRYICSA VLPLLTRCAP LFAGTEHCTS LIDSTLQTIY
2460 2470 2480 2490 2500
RLSKGRSLTK AQRDTIEECL LAICNHLRPS MLQQLLRRLV FDVPQLNEYC
2510 2520 2530 2540 2550
KMPLKLLTNH YEQCWKYYCL PSGWGSYGLA VEEELHLTEK LFWGIFDSLS
2560 2570 2580 2590 2600
HKKYDPDLFR MALPCLSAIA GALPPDYLDT RITATLEKQI SVDADGNFDP
2610 2620 2630 2640 2650
KPINTMNFSL PEKLEYIVTK YAEHSHDKWA CDKSQSGWKY GISLDENVKT
2660 2670 2680 2690 2700
HPLIRPFKTL TEKEKEIYRW PARESLKTML AVGWTVERTK EGEALVQQRE
2710 2720 2730 2740 2750
NEKLRSVSQA NQGNSYSPAP LDLSNVVLSR ELQGMVEVVA ENYHNIWAKK
2760 2770 2780 2790 2800
KKLELESKGG GSHPLLVPYD TLTAKEKFKD REKAQDLFKF LQVNGIIVSR
2810 2820 2830 2840 2850
GMKDMELDAS SMEKRFAYKF LKKILKYVDS AQEFIAHLEA IVSSGKTEKS
2860 2870 2880 2890 2900
PRDQEIKFFA KVLLPLVDQY FTSHCLYFLS SPLKPLSSSG YASHKEKEMV
2910 2920 2930 2940 2950
AGLFCKLAAL VRHRISLFGS DSTTMVSCLH ILAQTLDTRT VMKSGSELVK
2960 2970 2980 2990 3000
AGLRAFFENA AEDLEKTSEN LKLGKFTHSR TQIKGVSQNI NYTTVALLPI
3010 3020 3030 3040 3050
LTSIFEHVTQ HQFGMDLLLG DVQISCYHIL CSLYSLGTGK NIYVERQRPA
3060 3070 3080 3090 3100
LGECLASLAA AIPVAFLEPT LNRYNPLSVF NTKTPRERSI LGMPDTVEDM
3110 3120 3130 3140 3150
CPDIPQLEGL MKEINDLAES GARYTEMPHV IEVILPMLCN YLSYWWERGP
3160 3170 3180 3190 3200
ENLPPSTGPC CTKVTSEHLS LILGNILKII NNNLGIDEAS WMKRIAVYAQ
3210 3220 3230 3240 3250
PIISKARPDL LRSHFIPTLE KLKKKAVKTV QEEEQLKADG KGDTQEAELL
3260 3270 3280 3290 3300
ILDEFAVLCR DLYAFYPMLI RYVDNNRSNW LKSPDADSDQ LFRMVAEVFI
3310 3320 3330 3340 3350
LWCKSHNFKR EEQNFVIQNE INNLAFLTGD SKSKMSKAMQ VKSGGQDQER
3360 3370 3380 3390 3400
KKTKRRGDLY SIQTSLIVAA LKKMLPIGLN MCTPGDQELI SLAKSRYSHR
3410 3420 3430 3440 3450
DTDEEVREHL RNNLHLQEKS DDPAVKWQLN LYKDVLKSEE PFNPEKTVER
3460 3470 3480 3490 3500
VQRISAAVFH LEQVEQPLRS KKAVWHKLLS KQRKRAVVAC FRMAPLYNLP
3510 3520 3530 3540 3550
RHRSINLFLH GYQRFWIETE EYSFEEKLVQ DLAKSPKVEE EEEEETEKQP
3560 3570 3580 3590 3600
DPLHQIILYF SRNALTERSK LEDDPLYTSY SSMMAKSCQS GEDEEEDEDK
3610 3620 3630 3640 3650
EKTFEEKEME KQKTLYQQAR LHERGAAEMV LQMISASKGE MSPMVVETLK
3660 3670 3680 3690 3700
LGIAILNGGN AGVQQKMLDY LKEKKDAGFF QSLSGLMQSC SVLDLNAFER
3710 3720 3730 3740 3750
QNKAEGLGMV TEEGTLIVRE RGEKVLQNDE FTRDLFRFLQ LLCEGHNSDF
3760 3770 3780 3790 3800
QNFLRTQMGN TTTVNVIIST VDYLLRLQES ISDFYWYYSG KDIIDESGQH
3810 3820 3830 3840 3850
NFSKALAVTK QIFNSLTEYI QGPCIGNQQS LAHSRLWDAV VGFLHVFANM
3860 3870 3880 3890 3900
QMKLSQDSSQ IELLKELLDL LQDMVVMLLS LLEGNVVNGT IGKQMVDTLV
3910 3920 3930 3940 3950
ESSTNVEMIL KFFDMFLKLK DLTSSDTFKE YDPDGKGIIS KKEFQKAMEG
3960 3970 3980 3990 4000
QKQYTQSEID FLLSCAEADE NDMFNYVDFV DRFHEPAKDI GFNVAVLLTN
4010 4020 4030 4040 4050
LSEHMPNDSR LKCLLDPAES VLNYFEPYLG RIEIMGGAKK IERVYFEISE
4060 4070 4080 4090 4100
SSRTQWEKPQ VKESKRQFIF DVVNEGGEQE KMELFVNFCE DTIFEMQLAS
4110 4120 4130 4140 4150
QISESDSADR PEEEEEDEDS SYVLEIAGEE EEDGSLEPAS AFAMACASVK
4160 4170 4180 4190 4200
RNVTDFLKRA TLKNLRKQYR NVKKMTAKEL VKVLFSFFWM LFVGLFQLLF
4210 4220 4230 4240 4250
TILGGIFQIL WSTVFGGGLV EGAKNIRVTK ILGDMPDPTQ FGIHDDTMEA
4260 4270 4280 4290 4300
ERAEVMEPGI TTELVHFIKG EKGDTDIMSD LFGLHPKKEG SLKHGPEVGL
4310 4320 4330 4340 4350
GDLSEIIGKD EPPTLESTVQ KKRKAQAAEM KAANEAEGKV ESEKADMEDG
4360 4370 4380 4390 4400
EKEDKDKEEE QAEYLWTEVT KKKKRRCGQK VEKPEAFTAN FFKGLEIYQT
4410 4420 4430 4440 4450
KLLHYLARNF YNLRFLALFV AFAINFILLF YKVTEEPLEE ETEDVANLWN
4460 4470 4480 4490 4500
SFNDEEEEEA MVFFVLQEST GYMAPTLRAL AIIHTIISLV CVVGYYCLKV
4510 4520 4530 4540 4550
PLVVFKREKE IARKLEFDGL YITEQPSEDD IKGQWDRLVI NTPSFPNNYW
4560 4570 4580 4590 4600
DKFVKRKVIN KYGDLYGAER IAELLGLDKN ALDFSPVEET KAEAASLVSW
4610 4620 4630 4640 4650
LSSIDMKYHI WKLGVVFTDN SFLYLAWYTT MSVLGHYNNF FFAAHLLDIA
4660 4670 4680 4690 4700
MGFKTLRTIL SSVTHNGKQL VLTVGLLAVV VYLYTVVAFN FFRKFYNKSE
4710 4720 4730 4740 4750
DDDEPDMKCD DMMTCYLFHM YVGVRAGGGI GDEIEDPAGD PYEMYRIVFD
4760 4770 4780 4790 4800
ITFFFFVIVI LLAIIQGLII DAFGELRDQQ EQVREDMETK CFICGIGNDY
4810 4820 4830 4840 4850
FDTTPHGFET HTLQEHNLAN YLFFLMYLIN KDETEHTGQE SYVWKMYQER
4860 4870
CWDFFPAGDC FRKQYEDQLG
Length:4,870
Mass (Da):552,042
Last modified:March 8, 2011 - v3
Checksum:iB953487A89FD480F
GO
Isoform 2 (identifier: Q15413-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3337-3341: Missing.

Show »
Length:4,865
Mass (Da):551,484
Checksum:i1967DCA6B019C276
GO
Isoform 3 (identifier: Q15413-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3857-3859: DSS → GMW
     3860-4870: Missing.

Show »
Length:3,859
Mass (Da):435,934
Checksum:i637F449F56BDEB60
GO

Sequence cautioni

The sequence BAA23795.1 differs from that shown. Reason: Frameshift at positions 742 and 766.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti932 – 9321A → T in BAA23795. (PubMed:9395096)Curated
Sequence conflicti1081 – 10811A → P in BAA23795. (PubMed:9395096)Curated
Sequence conflicti1336 – 13361A → G in BAA23795. (PubMed:9395096)Curated
Sequence conflicti1480 – 14801K → E in BAA23795. (PubMed:9395096)Curated
Sequence conflicti1641 – 16411R → C in BAA23795. (PubMed:9395096)Curated
Sequence conflicti1641 – 16411R → C in CAA04798. (PubMed:9515741)Curated
Sequence conflicti2270 – 22701G → E in BAA23795. (PubMed:9395096)Curated
Sequence conflicti2270 – 22701G → E in CAA04798. (PubMed:9515741)Curated
Sequence conflicti2355 – 23551A → G in BAA23795. (PubMed:9395096)Curated
Sequence conflicti2433 – 24331A → G in BAA23795. (PubMed:9395096)Curated
Sequence conflicti2546 – 25461F → I in BAA23795. (PubMed:9395096)Curated
Sequence conflicti2580 – 25801T → S in BAA23795. (PubMed:9395096)Curated
Sequence conflicti2817 – 28171A → G in BAA23795. (PubMed:9395096)Curated
Sequence conflicti3684 – 36841S → P in BAA23795. (PubMed:9395096)Curated
Sequence conflicti3698 – 36981F → S in BAA23795. (PubMed:9395096)Curated
Sequence conflicti4026 – 40261E → G in BAA23795. (PubMed:9395096)Curated
Sequence conflicti4083 – 40831E → G in BAA23795. (PubMed:9395096)Curated
Sequence conflicti4537 – 45371R → P in BAA23795. (PubMed:9395096)Curated
Sequence conflicti4604 – 46041I → L in BAA23795. (PubMed:9395096)Curated
Sequence conflicti4709 – 47091C → R in CAA52326. (PubMed:8276408)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti261 – 2611R → S.1 Publication
VAR_024077
Natural varianti358 – 3581I → T.
Corresponds to variant rs2304380 [ dbSNP | Ensembl ].
VAR_057166
Natural varianti494 – 4941V → I.1 Publication
Corresponds to variant rs2077268 [ dbSNP | Ensembl ].
VAR_024078
Natural varianti693 – 6931Y → C.1 Publication
VAR_011404
Natural varianti731 – 7311I → V.1 Publication
Corresponds to variant rs2229116 [ dbSNP | Ensembl ].
VAR_011405
Natural varianti1380 – 13801E → G.1 Publication
VAR_011406
Natural varianti2268 – 22681Missing.1 Publication
VAR_011407

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3337 – 33415Missing in isoform 2. 1 PublicationVSP_005954
Alternative sequencei3857 – 38593DSS → GMW in isoform 3. CuratedVSP_005955
Alternative sequencei3860 – 48701011Missing in isoform 3. CuratedVSP_005956Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB001025 mRNA. Translation: BAA23795.1. Frameshift.
AJ001515 mRNA. Translation: CAA04798.1.
AC010809 Genomic DNA. No translation available.
AC011938 Genomic DNA. No translation available.
AC055874 Genomic DNA. No translation available.
AC067793 Genomic DNA. No translation available.
AC087638 Genomic DNA. No translation available.
AJ002512 mRNA. Translation: CAA05503.1.
X74269 mRNA. Translation: CAA52326.1.
X74270 Genomic DNA. Translation: CAA52327.1.
CCDSiCCDS45210.1. [Q15413-1]
CCDS58351.1. [Q15413-2]
PIRiS37537.
S66631.
RefSeqiNP_001027.3. NM_001036.4. [Q15413-1]
NP_001230925.1. NM_001243996.2. [Q15413-2]
UniGeneiHs.709373.

Genome annotation databases

EnsembliENST00000389232; ENSP00000373884; ENSG00000198838. [Q15413-1]
ENST00000415757; ENSP00000399610; ENSG00000198838. [Q15413-2]
GeneIDi6263.
KEGGihsa:6263.
UCSCiuc001zhi.3. human. [Q15413-1]
uc010bar.3. human. [Q15413-2]

Polymorphism databases

DMDMi325511382.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Ryanodine receptor entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB001025 mRNA. Translation: BAA23795.1 . Frameshift.
AJ001515 mRNA. Translation: CAA04798.1 .
AC010809 Genomic DNA. No translation available.
AC011938 Genomic DNA. No translation available.
AC055874 Genomic DNA. No translation available.
AC067793 Genomic DNA. No translation available.
AC087638 Genomic DNA. No translation available.
AJ002512 mRNA. Translation: CAA05503.1 .
X74269 mRNA. Translation: CAA52326.1 .
X74270 Genomic DNA. Translation: CAA52327.1 .
CCDSi CCDS45210.1. [Q15413-1 ]
CCDS58351.1. [Q15413-2 ]
PIRi S37537.
S66631.
RefSeqi NP_001027.3. NM_001036.4. [Q15413-1 ]
NP_001230925.1. NM_001243996.2. [Q15413-2 ]
UniGenei Hs.709373.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4ERV X-ray 1.75 A 2597-2800 [» ]
ProteinModelPortali Q15413.
SMRi Q15413. Positions 13-530, 3469-3495.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112175. 7 interactions.
IntActi Q15413. 2 interactions.
STRINGi 9606.ENSP00000373884.

Chemistry

BindingDBi Q15413.
ChEMBLi CHEMBL2062.
GuidetoPHARMACOLOGYi 749.

PTM databases

PhosphoSitei Q15413.

Polymorphism databases

DMDMi 325511382.

Proteomic databases

PaxDbi Q15413.
PRIDEi Q15413.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000389232 ; ENSP00000373884 ; ENSG00000198838 . [Q15413-1 ]
ENST00000415757 ; ENSP00000399610 ; ENSG00000198838 . [Q15413-2 ]
GeneIDi 6263.
KEGGi hsa:6263.
UCSCi uc001zhi.3. human. [Q15413-1 ]
uc010bar.3. human. [Q15413-2 ]

Organism-specific databases

CTDi 6263.
GeneCardsi GC15P033603.
H-InvDB HIX0038065.
HGNCi HGNC:10485. RYR3.
HPAi CAB006887.
MIMi 180903. gene.
neXtProti NX_Q15413.
PharmGKBi PA34897.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG247670.
GeneTreei ENSGT00760000119152.
HOGENOMi HOG000231428.
HOVERGENi HBG006699.
InParanoidi Q15413.
KOi K04963.
OMAi IDQVDPF.
OrthoDBi EOG71K622.
PhylomeDBi Q15413.
TreeFami TF315244.

Enzyme and pathway databases

Reactomei REACT_160189. Stimuli-sensing channels.

Miscellaneous databases

GeneWikii RYR3.
GenomeRNAii 6263.
NextBioi 24329.
PROi Q15413.
SOURCEi Search...

Gene expression databases

Bgeei Q15413.
CleanExi HS_RYR3.
Genevestigatori Q15413.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProi IPR016024. ARM-type_fold.
IPR001870. 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 ]
PANTHERi PTHR13715. PTHR13715. 1 hit.
Pfami 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 ]
PRINTSi PR00795. RYANODINER.
SMARTi SM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view ]
SUPFAMi SSF100909. SSF100909. 1 hit.
SSF48371. SSF48371. 10 hits.
SSF49899. SSF49899. 3 hits.
SSF82109. SSF82109. 2 hits.
PROSITEi PS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a human brain ryanodine receptor."
    Nakashima Y., Nishimura S., Maeda A., Barsoumian E.L., Hakamata Y., Nakai J., Allen P.D., Imoto K., Kita T.
    FEBS Lett. 417:157-162(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "cDNA cloning and sequencing of the human ryanodine receptor type 3 (RYR3) reveals a novel alternative splice site in the RYR3 gene."
    Leeb T., Brenig B.
    FEBS Lett. 423:367-370(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, VARIANTS SER-261; ILE-494; CYS-693; VAL-731; GLY-1380 AND SER-2268 DEL.
    Tissue: Fetal brain.
  3. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Partial cloning and differential expression of ryanodine receptor/calcium-release channel genes in human tissues including the hippocampus and cerebellum."
    Martin C., Chapman K.E., Seckl J.R., Ashley R.H.
    Neuroscience 85:205-216(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 520-660, TISSUE SPECIFICITY.
    Tissue: Skeletal muscle.
  5. "Involvement of the brain type of ryanodine receptor in T-cell proliferation."
    Hakamata Y., Nishimura S., Nakai J., Nakashima Y., Kita T., Imoto K.
    FEBS Lett. 352:206-210(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3943-4870.
    Tissue: T-cell.
  6. "Localization of a novel ryanodine receptor gene (RYR3) to human chromosome 15q14-q15 by in situ hybridization."
    Sorrentino V., Giannini G., Malzac P., Mattei M.-G.
    Genomics 18:163-165(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 4644-4842.
    Tissue: Cervix carcinoma and Hepatoma.
  7. "Isolation and partial cloning of ryanodine-sensitive Ca2+ release channel protein isoforms from human myometrial smooth muscle."
    Lynn S., Morgan J.M., Lamb H.K., Meissner G., Gillespie J.I.
    FEBS Lett. 372:6-12(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4652-4803.
    Tissue: Myometrium.
  8. "Knock-down of the type 3 ryanodine receptor impairs sustained Ca2+ signaling via the T cell receptor/CD3 complex."
    Schwarzmann N., Kunerth S., Weber K., Mayr G.W., Guse A.H.
    J. Biol. Chem. 277:50636-50642(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Characterization of the binding sites for the interactions between FKBP12 and intracellular calcium release channels."
    Wen H., Kang S., Song Y., Song Y., Yang H.J., Kim M.H., Park S.
    Arch. Biochem. Biophys. 517:37-42(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FKBP1A.

Entry informationi

Entry nameiRYR3_HUMAN
AccessioniPrimary (citable) accession number: Q15413
Secondary accession number(s): O15175, Q15412
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: March 8, 2011
Last modified: October 29, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Channel activity is modulated by the alkaloid ryanodine that binds to the open calcium-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 elevated cytoplasmic calcium levels in the micromolar range, by caffeine and adenine nucleotides, such as AMP and ATP. Inhibited by Mg2+ and ruthenium red (By similarity).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3