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A2AGL3 (RYR3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ryr3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length4863 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Plays a role in cellular calcium signaling. Contributes to cellular calcium ion homeostasis. Isoform 2 lacks a predicted transmembrane segment and does not form functional calcium channels by itself; however, it can form tetramers with isoforms that contain the full complement of transmembrane segments and modulate their activity. Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Subunit structure

Homotetramer. Isoform 2 can form tetramers with isoform 1. Heterotetramer with RYR2. Interacts with FKBP1A. Interacts with CALM By similarity. Ref.6

Subcellular location

Sarcoplasmic reticulum membrane; Multi-pass membrane protein Probable. Membrane; Multi-pass membrane protein. Microsome membrane; 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. Ref.8

Tissue specificity

Detected in hippocampus, cerebellum, striatum, frontal brain cortex and parietal brain cortex. Detected in skeletal muscle, diaphragm muscle and myometrium (at protein level). Detected in egg cells. Detected in heart, diaphragm, stomach, spleen, ovary, testis germ cells, brain and cerebellum. Detected in cerebral artery smooth muscle cells. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11

Domain

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

Disruption phenotype

No apparent phenotype. Mice are born at the expected Mendelian rate and are fertile. They appear normal, except for increased locomotor activity and decreased social contact duration in social interaction tests. Ref.2 Ref.12

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.

Sequence similarities

Belongs to the ryanodine receptor (TC 1.A.3.1) family. RYR3 subfamily. [View classification]

Contains 3 B30.2/SPRY domains.

Contains 5 MIR domains.

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
Sarcoplasmic reticulum
   Coding sequence diversityAlternative splicing
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Calmodulin-binding
   Molecular functionCalcium channel
Ion channel
Ligand-gated ion channel
Receptor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium ion transmembrane transport

Inferred from sequence or structural similarity. Source: UniProtKB

cellular calcium ion homeostasis

Inferred from mutant phenotype PubMed 9384575. Source: MGI

cellular response to ATP

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to caffeine

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to calcium ion

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to magnesium ion

Inferred from sequence or structural similarity. Source: UniProtKB

protein homotetramerization

Inferred from sequence or structural similarity. Source: UniProtKB

striated muscle contraction

Inferred from mutant phenotype PubMed 9384575. Source: MGI

   Cellular_componentintegral component of membrane

Inferred from sequence or structural similarity. Source: UniProtKB

junctional membrane complex

Inferred from direct assay PubMed 10444070. Source: MGI

sarcoplasmic reticulum membrane

Inferred from direct assay PubMed 14592808. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

ryanodine-sensitive calcium-release channel activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: A2AGL3-1)

Also known as: RYR3L;

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.
Isoform 2 (identifier: A2AGL3-2)

Also known as: RYR3S;

The sequence of this isoform differs from the canonical sequence as follows:
     4397-4425: Missing.
Note: Lacks a predicted transmembrane segment and is not expected to form functional calcium channels.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 48634863Ryanodine receptor 3
PRO_0000415648

Regions

Topological domain1 – 41794179Cytoplasmic Potential
Transmembrane4180 – 420021Helical; Potential
Transmembrane4403 – 442321Helical; Potential
Transmembrane4478 – 449821Helical; Potential
Transmembrane4603 – 462321Helical; Potential
Transmembrane4626 – 464621Helical; Potential
Transmembrane4665 – 468521Helical; Potential
Intramembrane4716 – 472510Pore-forming; By similarity
Transmembrane4746 – 476621Helical; Potential
Topological domain4767 – 486397Cytoplasmic Potential
Domain100 – 15556MIR 1
Domain162 – 20746MIR 2
Domain215 – 26955MIR 3
Domain275 – 33359MIR 4
Domain343 – 40058MIR 5
Domain585 – 796212B30.2/SPRY 1
Repeat840 – 9531141
Repeat954 – 10681152
Domain1012 – 1208197B30.2/SPRY 2
Domain1254 – 1466213B30.2/SPRY 3
Repeat2587 – 27051193
Repeat2706 – 28181134
Region840 – 281819794 X approximate repeats
Region2320 – 233314Interaction with FKBP1A By similarity
Region3462 – 349130Interaction with CALM By similarity

Sites

Site38761Important for activation by Ca(2+) By similarity

Natural variations

Alternative sequence4397 – 442529Missing in isoform 2.
VSP_042304

Experimental info

Sequence conflict41691S → I in AAF21940. Ref.3
Sequence conflict42141E → Q in AAF21940. Ref.3
Sequence conflict44271T → A in AAF21940. Ref.3
Sequence conflict44501E → V in BAE21181. Ref.4
Sequence conflict44571F → L in CAA58786. Ref.5
Sequence conflict44691T → N in CAA58786. Ref.5
Sequence conflict46021H → N in AAA64957. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (RYR3L) [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: D2B086935E99D40B

FASTA4,863551,328
        10         20         30         40         50         60 
MAEAGEGGED EIQFLRTEDE VVLQCIANIH KEQRKFCLAA EGLGNRLCFL EPTSEAKYIP 

        70         80         90        100        110        120 
PDLCVCNFVL EQSLSVRALQ EMLANTVENG GEGAAQGGGH RTLLYGHAIL LRHSFSGMYL 

       130        140        150        160        170        180 
TCLTTSRSQT DKLAFDVGLR EHATGEACWW TIHPASKQRS EGEKVRIGDD LILVSVSSER 

       190        200        210        220        230        240 
YLHLSISNGS IQVDASFMQT LWNVHPTCSG SSIEEGYLLG GHVVRLFHGH DECLTIPSTD 

       250        260        270        280        290        300 
QNDSQHRRVF YEAGGAGTRA RSLWRVEPLR ISWSGSNIRW GQAFRLRHLT TGHYLALTED 

       310        320        330        340        350        360 
QGLLLQDRGK SDTKSTAFSF RASKEIKEKL DSSHKRDMEG MGVPEIKYGD SVCFVQHVAS 

       370        380        390        400        410        420 
GLWVTYKAQD AKTSRLGPLK RKVILHQEGH MDDGLTLQRC QQEESQAARI IRNTTALFSQ 

       430        440        450        460        470        480 
FVSGNNRTTA PVALPTEEVL QTLQDLIAYF QPPEDEMQHE DKQNKLRSLK NRQNLFKEEG 

       490        500        510        520        530        540 
MLALVLNCID RLNIYNSVAH FAGIVREESG MAWKEILNLL YKLLAALIRG NRNNCAQFSN 

       550        560        570        580        590        600 
NLDWLISKLD RLESSSGILE VLHCILIESP EALNLIAEGH IKSIISLLDK HGRNHKVLDV 

       610        620        630        640        650        660 
LCSLCLCNGV AVRANQNLIC DNLLPRRNLL LQTRLINDVT SIRPNIFLGV AEGSPQYKKW 

       670        680        690        700        710        720 
YFELIIDQVE PFLTAEPTHL RVGWASSSGY APYPGGGEGW GGNGVGDDLY SYGFDGLHLW 

       730        740        750        760        770        780 
SGRIPRAVAS INQHLLKSDD VVSCCLDLGV PSISFRINGQ PVQGMFENFN TDGLFFPVMS 

       790        800        810        820        830        840 
FSAGVKVRFL MGGRHGEFKF LPPSGYAPCY EALLPKEKMR LEPVKEYKRD ADGVRDLLGT 

       850        860        870        880        890        900 
TQFLSQASFI PCPIDTSQVV LPLHLEKIRD RLAENIHELW GMNKIELGWT YGKVRDDNKR 

       910        920        930        940        950        960 
QHPCLVEFSK LPETEKNYNL QMSTETLKTL LALGCHIAHV NPAAEEDLKK VKLPKNYMMS 

       970        980        990       1000       1010       1020 
NGYKPAPLDL SDVKLLPPQE ILVDKLAENA HNVWAKDRIK QGWTYGIQQD LKNKRNPRLV 

      1030       1040       1050       1060       1070       1080 
PYALLDERTK KSNRDSLREA VRTFVGYGYN IEPSDQELAD PTVEKVSIDK IRFFRVERSY 

      1090       1100       1110       1120       1130       1140 
AVKSGKWYFE FEVVTGGDMR VGWARPGCRP DIELGADDQA FVFEGSRGQR WHQGSGYFGR 

      1150       1160       1170       1180       1190       1200 
TWQPGDVVGC MINLDDASMV FTLNGELLIT NKGSELAFAD YEIENGFVPI CSLGLSQIGR 

      1210       1220       1230       1240       1250       1260 
MNLGTDASTF KFYTMCGLQE GFEPFAVNMN RDVAVWFSKR LPTFVNVPKD HPHIEVVRID 

      1270       1280       1290       1300       1310       1320 
GTMDSPPCLK VTHKTFGTQN SNANMIYCRL SMPVECHSSF SHSPCLDSEA FQKRKQMQEI 

      1330       1340       1350       1360       1370       1380 
LSHTTTQCYY AIRIFAGQDP SCVWVGWVTP DYHLYSEKFD LNKNCTVTVT LGDERGRVHE 

      1390       1400       1410       1420       1430       1440 
SVKRSNCYMV WGGDIVASSQ RSSRSNVDLE IGCLLDLAMG MLSFSANGKE LGTCYQVEPN 

      1450       1460       1470       1480       1490       1500 
TKVFPAVFLQ PTSTSLFQFE LGKLKNAMPL SAAIFKSEEK NPTPQCPPRL DVQTIQPVLW 

      1510       1520       1530       1540       1550       1560 
SRMPSSFLKV ETERVSERHG WVVQCLEPLQ MMALHIPEEN RCVDILELCE QEDLMQFHYH 

      1570       1580       1590       1600       1610       1620 
TLRLYSAVCA LGNSRVASAL CSHVDLSQLF YAIDNKYLPG LLRSGFYDLL ISIHLANAKE 

      1630       1640       1650       1660       1670       1680 
RKLMMKNEYI IPITSATRNI RLYPDESKRH GLPGVGLRTC LKPGFRFSTP CFVVTSEDHQ 

      1690       1700       1710       1720       1730       1740 
KQSPEIPLQI LKTKALSMLT EAVHCSGAHI RDPVGGSVEF QFVPVLKLIG TLLVMGVFDD 

      1750       1760       1770       1780       1790       1800 
DDVRQILLLI DPSVFGEHSG ETEEGVEKEV THAEEKAVEA GEKACKEAPV KGLLQTRLPE 

      1810       1820       1830       1840       1850       1860 
SVKLQMCELL SYLCDCELQH RVEAIVAFGD IYVSKLQANQ KFRYNELMQA LNMSAALTAR 

      1870       1880       1890       1900       1910       1920 
KTREFRSPPQ EQINMLLNFH LGENCPCPEE IREELYDFHE DLLVHCGVPL EEEEEEEEDT 

      1930       1940       1950       1960       1970       1980 
SWTGKLCALV YKIKGPPKPE KEQPTEEEKP YPTTLKELVS QTMIRWAQEN QIQDAELVRM 

      1990       2000       2010       2020       2030       2040 
MFNLLRRQYD SIGELLQALR KTYTISQASV NDTINLLAAL GQIRSLLSVR MGREEELLMI 

      2050       2060       2070       2080       2090       2100 
NGLGDIMNNK VFYQHPNLMR VLGMHETVME VMVNVLGTEK SQIAFPKMVA SCCRFLCYFC 

      2110       2120       2130       2140       2150       2160 
RISRQNQKAM FEHLSYLLEN SSVGLASPSM RGSTPLDVAA SSVMDNNELA LGLEEPDLEK 

      2170       2180       2190       2200       2210       2220 
VVTYLAGCGL QSCPMLLARG YPDVGWNPIE GERYLSFLRF AVFVNSESVE ENASVVVKLL 

      2230       2240       2250       2260       2270       2280 
IRRPECFGPA LRGEGGNGLL AAMQGAIKIS ENPALDLPSQ GYKTEVTQDD GEEEEIVHMG 

      2290       2300       2310       2320       2330       2340 
NAIMSFYSAL IDLLGRCAPE MHLIQTGKGE AIRIRSILRS LVPTEDLVGI ISIPLKLPSL 

      2350       2360       2370       2380       2390       2400 
NKDGSVSEPD MAANFCPDHK APMVLFLDRV YGIKDQTFLL HLLEVGFLPD LRASASLDTV 

      2410       2420       2430       2440       2450       2460 
SLSTTEAALA LNRYLCSAVL PLLTRCAPLF SGTEHCTSLI DSTLQTIYRL SKGRSLTKAQ 

      2470       2480       2490       2500       2510       2520 
RDTIEECLLA ICNHLRPSML QQLLRRLVFD VPQLSEYCKM PLKLLTNHYE QCWKYYCLPS 

      2530       2540       2550       2560       2570       2580 
GWGSYGLAVE EELHLTEKLF WGIFDSLSHK KYDLDLFRMA LPCLSAIAGA LPPDYLDTRI 

      2590       2600       2610       2620       2630       2640 
TATLEKQVSV DADGNFDPKP INTMNFSLPE KLEYIVTKYA EHSHDKWACD KSHSGWKYGI 

      2650       2660       2670       2680       2690       2700 
SLDENVKTHP LIRPFKTLTE KEKEIYRWPA RESLKTMLAV GWTVERTKEG EALVQQRENE 

      2710       2720       2730       2740       2750       2760 
KLRCVSQTNQ GNSYSPAPLD LSNVVLSREL QGMVEVVAEN YHNIWAKKKK LELESKGGGS 

      2770       2780       2790       2800       2810       2820 
HPLLVPYDTL TAKEKFRDRE KAQDLFKFLQ VNGILVSRGM KDLELDASSM EKRFAYKFLK 

      2830       2840       2850       2860       2870       2880 
KILKYVDAAQ EFIAHLEAIV SSGKTEKSPH DQEIKFFAKV LLPLVDQYFT NHRLYFLSSP 

      2890       2900       2910       2920       2930       2940 
LKPLSSSGYA SHKEKEMVAS LFCKLAALVR HRISLFGSDS TTMVSCLHIL AQTLDTRTVM 

      2950       2960       2970       2980       2990       3000 
KSGSELVKAG LRAFFENAAE DLEKTSENLK LGKFTHSRTQ IKGVSQNINY TTVALLPILT 

      3010       3020       3030       3040       3050       3060 
SIFEHIAQHQ FGVDLLLSDV QVSCYHILCS LYSLGTGKNI YVERQRPALG ECLASLAAAI 

      3070       3080       3090       3100       3110       3120 
PVAFLEPSLN RHNPLSVFNT KTPRERSILG MPDKVEDMCP DIPQLEGLMK EINDLAESGA 

      3130       3140       3150       3160       3170       3180 
RYTEMPHVIE VILPMLCNYL SYWWERGPEN LPPSTGPCCT KVTSEHLSLI LGNILKIINN 

      3190       3200       3210       3220       3230       3240 
NLGIDEASWM KRIAVYAQPI ISKARPDLLR SHFIPTLEKL KKKAVKTVQE EEQLKTDGKG 

      3250       3260       3270       3280       3290       3300 
DTQEAELLIL DEFAVLCRDL YAFYPMLIRY VDNNRSNWLK SPDPDSDQLF RMVAEVFILW 

      3310       3320       3330       3340       3350       3360 
CKSHNFKREE QNFVIQNEIN NLAFLTGDSK SKMSKSGGQD QERKKTKRRG DLYSIQTSLI 

      3370       3380       3390       3400       3410       3420 
VAALKKMLPI GLNMCTPGDQ ELISLAKSRY SCRDTDEEVK EHLRNNLHLQ EKSDDPAVKW 

      3430       3440       3450       3460       3470       3480 
QLNLYKDVLR NDEPSNPEKT VERVQSISAA LFHLEQVEQP LRSKKAVWHK LLSKQRKRAV 

      3490       3500       3510       3520       3530       3540 
VACFRMAPLY NLPRHRSINL FLHGYQRFWI ETEAHFFEEK LVQDLAKSPR VEDEEEEETE 

      3550       3560       3570       3580       3590       3600 
RQPDPLHQII LHFSRNALTE RSKLEDDPLY TSYSSMMAKS CQSGEDEEEE EDKEKTFEEK 

      3610       3620       3630       3640       3650       3660 
EMEKQKTLYQ QARLHERGAA EMVLQMISAS KGEMSPMVVE TLKLGIAILN GGNAGVQQKM 

      3670       3680       3690       3700       3710       3720 
LDYLKEKKDA GFFQSLSGLM QSCSVLDLNA FERQNKAEGL GMVTEEGTLI VRERGEKVLQ 

      3730       3740       3750       3760       3770       3780 
NDEFTQDLFR FLQLLCEGHN SDFQNFLRTQ MGNTTTVNII ISTVDYLLRL QESISDFYWY 

      3790       3800       3810       3820       3830       3840 
YSGKDIIDES GQHNFSKALA VTKQIFNSLT EYIQGPCIGN QQSLAHSRLW DAVVGFLHVF 

      3850       3860       3870       3880       3890       3900 
ANMQMKLSQD SSQIELLKEL LDLLQDMVVM LLSLLEGNVV NGTIGKQMVD TLVESSTNVE 

      3910       3920       3930       3940       3950       3960 
MILKFFDMFL KLKDLTSSDT FKEYDPDGKG IISRKEFQKA MEGLKQYTQS EIDFLLSCTE 

      3970       3980       3990       4000       4010       4020 
ADENDMFNYV DFVERFHEPA KDIGFNVAVL LTNLSEHMPN DSRLKSLLDP AESVLNYFEP 

      4030       4040       4050       4060       4070       4080 
YLGRIEIMGG AKKIERVYFE ISESSRTQWE KPQVKESKRQ FIFDVVNEGG EQEKMELFVN 

      4090       4100       4110       4120       4130       4140 
FCEDTIFEMQ LASQISESDS TDRPEEEEEE DEDSAYSIET EGEEEEKSFE SASAFTMACV 

      4150       4160       4170       4180       4190       4200 
SVKRNVTKFL KRATLKNLRK QYRNVKKMSA KELVKVFFSF FWMLFVGLFQ LLFTIFGGIF 

      4210       4220       4230       4240       4250       4260 
QILWNTVFGG GLVEGAKNIR VTKILGDMPD PTQFGIHDDV IETDRAEVTE PGVTTELVHF 

      4270       4280       4290       4300       4310       4320 
VKGEAGDTDI MSDLFGIHSK KEGGLKQGPE VGLGDLSEII GKDEPPTLES TVRKKRKAQA 

      4330       4340       4350       4360       4370       4380 
AEMKAVHEAE GKAESEKADM EDREKEDKIK EEGQTDYLWA DVTVKKTRRR GQKAEKPEAF 

      4390       4400       4410       4420       4430       4440 
MANFFKGLEI YQTKLLHYLA RNFYNLRFLA LFVAFAINFI LLFYKVTEEP LEEETEDVAN 

      4450       4460       4470       4480       4490       4500 
LWNSFNDDDE EEAMVFFVLQ ESTGYMAPTL RALAIVHTII SLVCVVGYYC LKVPLVVFKR 

      4510       4520       4530       4540       4550       4560 
EKEIARKLEF DGLYITEQPS EDDIKGQWDR LVINTPSFPN NYWDKFVKRK VINKYGDLYG 

      4570       4580       4590       4600       4610       4620 
AERIAELLGL DKNALDFSPV EEAKAEAASL VSWLSSIDMK YHIWKLGVVF TDNSFLYLAW 

      4630       4640       4650       4660       4670       4680 
YTTMSVLGHY NNFFFAAHLL DIAMGFKTLR TILSSVTHNG KQLVLTVGLL AVVVYLYTVV 

      4690       4700       4710       4720       4730       4740 
AFNFFRKFYN KSEDDDEPDM KCDDMMTCYL FHMYVGVRAG GGIGDEIEDP AGDPYEMYRI 

      4750       4760       4770       4780       4790       4800 
VFDITFFFFV IVILLAIIQG LIIDAFGELR DQQEQVREDM ETKCFICGIG NDYFDTTPHG 

      4810       4820       4830       4840       4850       4860 
FETHTLQEHN LANYLFFLMY LINKDETEHT GQESYVWKMY QERCWDFFPA GDCFRKQYED 


QLG 

« Hide

Isoform 2 (RYR3S) [UniParc].

Checksum: ED773D40A48B773A
Show »

FASTA4,834547,747

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"Generation and characterization of mutant mice lacking ryanodine receptor type 3."
Takeshima H., Ikemoto T., Nishi M., Nishiyama N., Shimuta M., Sugitani Y., Kuno J., Saito I., Saito H., Endo M., Iino M., Noda T.
J. Biol. Chem. 271:19649-19652(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-67, FUNCTION, DISRUPTION PHENOTYPE.
Tissue: Brain.
[3]"Calcium-induced calcium release dependent on ryanodine receptor type 3 (RyR3) modulates both neuronal excitability and transmitter release."
Chameau P., Van de Vrede Y., Lucas-Meunier E., Fossier P., Denizot J.-P., Shimahara T., Tauc L., Baux G.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4088-4541 (ISOFORM 1).
Strain: Swiss.
Tissue: Brain.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4220-4863 (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Skin.
[5]"The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues."
Giannini G., Conti A., Mammarella S., Scrobogna M., Sorrentino V.
J. Cell Biol. 128:893-904(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4405-4692 (ISOFORM 1), TISSUE SPECIFICITY.
Strain: BALB/c.
Tissue: Brain.
[6]"Regulation of mouse egg activation: presence of ryanodine receptors and effects of microinjected ryanodine and cyclic ADP ribose on uninseminated and inseminated eggs."
Ayabe T., Kopf G.S., Schultz R.M.
Development 121:2233-2244(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4598-4841, SUBUNIT, TISSUE SPECIFICITY.
Tissue: Egg.
[7]"Ca(2+)-induced Ca2+ release in myocytes from dyspedic mice lacking the type-1 ryanodine receptor."
Takeshima H., Yamazawa T., Ikemoto T., Takekura H., Nishi M., Noda T., Iino M.
EMBO J. 14:2999-3006(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4741-4863, FUNCTION, TISSUE SPECIFICITY.
Strain: C57BL/6J.
Tissue: Brain.
[8]"Functional properties of the ryanodine receptor type 3 (RyR3) Ca2+ release channel."
Sonnleitner A., Conti A., Bertocchini F., Schindler H., Sorrentino V.
EMBO J. 17:2790-2798(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]"Regulation of calcium sparks and spontaneous transient outward currents by RyR3 in arterial vascular smooth muscle cells."
Lohn M., Jessner W., Furstenau M., Wellner M., Sorrentino V., Haller H., Luft F.C., Gollasch M.
Circ. Res. 89:1051-1057(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[10]"RyR3 amplifies RyR1-mediated Ca(2+)-induced Ca(2+) release in neonatal mammalian skeletal muscle."
Yang D., Pan Z., Takeshima H., Wu C., Nagaraj R.Y., Ma J., Cheng H.
J. Biol. Chem. 276:40210-40214(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Role of RYR3 splice variants in calcium signaling in mouse nonpregnant and pregnant myometrium."
Dabertrand F., Fritz N., Mironneau J., Macrez N., Morel J.L.
Am. J. Physiol. 293:C848-C854(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION OF ISOFORM 2, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[12]"Comprehensive behavioral phenotyping of ryanodine receptor type 3 (RyR3) knockout mice: decreased social contact duration in two social interaction tests."
Matsuo N., Tanda K., Nakanishi K., Yamasaki N., Toyama K., Takao K., Takeshima H., Miyakawa T.
Front. Behav. Neurosci. 3:3-3(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[13]"Ryanodine receptor studies using genetically engineered mice."
Kushnir A., Betzenhauser M.J., Marks A.R.
FEBS Lett. 584:1956-1965(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL929348 Genomic DNA. No translation available.
AL672250 expand/collapse EMBL AC list , AL691423, AL732316, BX649564 Genomic DNA. Translation: CAM15357.1.
AL691423 expand/collapse EMBL AC list , AL672250, AL732316, BX649564 Genomic DNA. Translation: CAM17843.1.
AL732316 expand/collapse EMBL AC list , AL672250, AL691423, BX649564 Genomic DNA. Translation: CAM22353.1.
BX649564 expand/collapse EMBL AC list , AL672250, AL691423, AL732316 Genomic DNA. Translation: CAM23489.1.
D84237 mRNA. Translation: BAA12286.1.
AF111166 mRNA. Translation: AAF21940.1.
AK132464 mRNA. Translation: BAE21181.1.
X83934 mRNA. Translation: CAA58786.1.
U23756 mRNA. Translation: AAA64957.1.
D38218 mRNA. Translation: BAA07393.1.
PIRI48743.
S56107.
UniGeneMm.436657.

3D structure databases

ProteinModelPortalA2AGL3.
SMRA2AGL3. Positions 13-532, 2596-2798, 3462-3488.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2365.

Proteomic databases

PaxDbA2AGL3.
PRIDEA2AGL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000080673; ENSMUSP00000079503; ENSMUSG00000057378. [A2AGL3-1]

Organism-specific databases

MGIMGI:99684. Ryr3.

Phylogenomic databases

eggNOGNOG247670.
GeneTreeENSGT00690000101961.
HOGENOMHOG000231428.
HOVERGENHBG006699.
OrthoDBEOG71K622.
PhylomeDBA2AGL3.

Gene expression databases

ArrayExpressA2AGL3.
BgeeA2AGL3.
GenevestigatorA2AGL3.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.25.10.30. 1 hit.
InterProIPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl_sf.
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.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]
PANTHERPTHR13715. PTHR13715. 1 hit.
PfamPF08709. 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]
PRINTSPR00795. RYANODINER.
SMARTSM00472. MIR. 4 hits.
SM00449. SPRY. 3 hits.
[Graphical view]
SUPFAMSSF100909. SSF100909. 2 hits.
SSF49899. SSF49899. 3 hits.
SSF82109. SSF82109. 2 hits.
PROSITEPS50188. B302_SPRY. 3 hits.
PS50919. MIR. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRYR3. mouse.
PROA2AGL3.
SOURCESearch...

Entry information

Entry nameRYR3_MOUSE
AccessionPrimary (citable) accession number: A2AGL3
Secondary accession number(s): P70184 expand/collapse secondary AC list , P70185, Q3V1H0, Q4JFC4, Q60836, Q62175, Q62198, Q9QY91
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot