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A2AGL3

- RYR3_MOUSE

UniProt

A2AGL3 - RYR3_MOUSE

Protein

Ryanodine receptor 3

Gene

Ryr3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 62 (01 Oct 2014)
      Sequence version 1 (05 Feb 2008)
      Previous versions | rss
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    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. 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.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei3876 – 38761Important for activation by Ca(2+)By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. calcium ion transmembrane transport Source: UniProtKB
    2. cellular calcium ion homeostasis Source: MGI
    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. protein homotetramerization Source: UniProtKB
    8. striated muscle contraction Source: MGI

    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_196640. 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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:99684. Ryr3.

    Subcellular locationi

    Sarcoplasmic reticulum membrane 1 Publication; Multi-pass membrane protein 1 Publication. Membrane 1 Publication; Multi-pass membrane protein 1 Publication. 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: MGI
    3. sarcoplasmic reticulum membrane Source: MGI

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome, Sarcoplasmic reticulum

    Pathology & Biotechi

    Disruption phenotypei

    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.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 48634863Ryanodine receptor 3PRO_0000415648Add
    BLAST

    Proteomic databases

    PaxDbiA2AGL3.
    PRIDEiA2AGL3.

    Expressioni

    Tissue specificityi

    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.6 Publications

    Gene expression databases

    ArrayExpressiA2AGL3.
    BgeeiA2AGL3.
    GenevestigatoriA2AGL3.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliA2AGL3.
    SMRiA2AGL3. Positions 13-532, 2596-2798, 3462-3488.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 41794179CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini4767 – 486397CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei4716 – 472510Pore-formingBy similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4180 – 420021HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4403 – 442321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4478 – 449821HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4603 – 462321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4626 – 464621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4665 – 468521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei4746 – 476621HelicalSequence 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
    Repeati2587 – 27051193Add
    BLAST
    Repeati2706 – 28181134Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni840 – 281819794 X approximate repeatsAdd
    BLAST
    Regioni2320 – 233314Interaction with FKBP1ABy similarityAdd
    BLAST
    Regioni3462 – 349130Interaction 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.
    GeneTreeiENSGT00690000101961.
    HOGENOMiHOG000231428.
    HOVERGENiHBG006699.
    OrthoDBiEOG71K622.
    PhylomeDBiA2AGL3.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    1.25.10.30. 1 hit.
    InterProiIPR001870. 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]
    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. 2 hits.
    SSF49899. SSF49899. 3 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. Align

    Isoform 1 (identifier: A2AGL3-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAEAGEGGED EIQFLRTEDE VVLQCIANIH KEQRKFCLAA EGLGNRLCFL     50
    EPTSEAKYIP PDLCVCNFVL EQSLSVRALQ EMLANTVENG GEGAAQGGGH 100
    RTLLYGHAIL LRHSFSGMYL TCLTTSRSQT DKLAFDVGLR EHATGEACWW 150
    TIHPASKQRS EGEKVRIGDD LILVSVSSER YLHLSISNGS IQVDASFMQT 200
    LWNVHPTCSG SSIEEGYLLG GHVVRLFHGH DECLTIPSTD QNDSQHRRVF 250
    YEAGGAGTRA RSLWRVEPLR ISWSGSNIRW GQAFRLRHLT TGHYLALTED 300
    QGLLLQDRGK SDTKSTAFSF RASKEIKEKL DSSHKRDMEG MGVPEIKYGD 350
    SVCFVQHVAS GLWVTYKAQD AKTSRLGPLK RKVILHQEGH MDDGLTLQRC 400
    QQEESQAARI IRNTTALFSQ FVSGNNRTTA PVALPTEEVL QTLQDLIAYF 450
    QPPEDEMQHE DKQNKLRSLK NRQNLFKEEG MLALVLNCID RLNIYNSVAH 500
    FAGIVREESG MAWKEILNLL YKLLAALIRG NRNNCAQFSN NLDWLISKLD 550
    RLESSSGILE VLHCILIESP EALNLIAEGH IKSIISLLDK HGRNHKVLDV 600
    LCSLCLCNGV AVRANQNLIC DNLLPRRNLL LQTRLINDVT SIRPNIFLGV 650
    AEGSPQYKKW YFELIIDQVE PFLTAEPTHL RVGWASSSGY APYPGGGEGW 700
    GGNGVGDDLY SYGFDGLHLW SGRIPRAVAS INQHLLKSDD VVSCCLDLGV 750
    PSISFRINGQ PVQGMFENFN TDGLFFPVMS FSAGVKVRFL MGGRHGEFKF 800
    LPPSGYAPCY EALLPKEKMR LEPVKEYKRD ADGVRDLLGT TQFLSQASFI 850
    PCPIDTSQVV LPLHLEKIRD RLAENIHELW GMNKIELGWT YGKVRDDNKR 900
    QHPCLVEFSK LPETEKNYNL QMSTETLKTL LALGCHIAHV NPAAEEDLKK 950
    VKLPKNYMMS NGYKPAPLDL SDVKLLPPQE ILVDKLAENA HNVWAKDRIK 1000
    QGWTYGIQQD LKNKRNPRLV PYALLDERTK KSNRDSLREA VRTFVGYGYN 1050
    IEPSDQELAD PTVEKVSIDK IRFFRVERSY AVKSGKWYFE FEVVTGGDMR 1100
    VGWARPGCRP DIELGADDQA FVFEGSRGQR WHQGSGYFGR TWQPGDVVGC 1150
    MINLDDASMV FTLNGELLIT NKGSELAFAD YEIENGFVPI CSLGLSQIGR 1200
    MNLGTDASTF KFYTMCGLQE GFEPFAVNMN RDVAVWFSKR LPTFVNVPKD 1250
    HPHIEVVRID GTMDSPPCLK VTHKTFGTQN SNANMIYCRL SMPVECHSSF 1300
    SHSPCLDSEA FQKRKQMQEI LSHTTTQCYY AIRIFAGQDP SCVWVGWVTP 1350
    DYHLYSEKFD LNKNCTVTVT LGDERGRVHE SVKRSNCYMV WGGDIVASSQ 1400
    RSSRSNVDLE IGCLLDLAMG MLSFSANGKE LGTCYQVEPN TKVFPAVFLQ 1450
    PTSTSLFQFE LGKLKNAMPL SAAIFKSEEK NPTPQCPPRL DVQTIQPVLW 1500
    SRMPSSFLKV ETERVSERHG WVVQCLEPLQ MMALHIPEEN RCVDILELCE 1550
    QEDLMQFHYH TLRLYSAVCA LGNSRVASAL CSHVDLSQLF YAIDNKYLPG 1600
    LLRSGFYDLL ISIHLANAKE RKLMMKNEYI IPITSATRNI RLYPDESKRH 1650
    GLPGVGLRTC LKPGFRFSTP CFVVTSEDHQ KQSPEIPLQI LKTKALSMLT 1700
    EAVHCSGAHI RDPVGGSVEF QFVPVLKLIG TLLVMGVFDD DDVRQILLLI 1750
    DPSVFGEHSG ETEEGVEKEV THAEEKAVEA GEKACKEAPV KGLLQTRLPE 1800
    SVKLQMCELL SYLCDCELQH RVEAIVAFGD IYVSKLQANQ KFRYNELMQA 1850
    LNMSAALTAR KTREFRSPPQ EQINMLLNFH LGENCPCPEE IREELYDFHE 1900
    DLLVHCGVPL EEEEEEEEDT SWTGKLCALV YKIKGPPKPE KEQPTEEEKP 1950
    YPTTLKELVS QTMIRWAQEN QIQDAELVRM MFNLLRRQYD SIGELLQALR 2000
    KTYTISQASV NDTINLLAAL GQIRSLLSVR MGREEELLMI NGLGDIMNNK 2050
    VFYQHPNLMR VLGMHETVME VMVNVLGTEK SQIAFPKMVA SCCRFLCYFC 2100
    RISRQNQKAM FEHLSYLLEN SSVGLASPSM RGSTPLDVAA SSVMDNNELA 2150
    LGLEEPDLEK VVTYLAGCGL QSCPMLLARG YPDVGWNPIE GERYLSFLRF 2200
    AVFVNSESVE ENASVVVKLL IRRPECFGPA LRGEGGNGLL AAMQGAIKIS 2250
    ENPALDLPSQ GYKTEVTQDD GEEEEIVHMG NAIMSFYSAL IDLLGRCAPE 2300
    MHLIQTGKGE AIRIRSILRS LVPTEDLVGI ISIPLKLPSL NKDGSVSEPD 2350
    MAANFCPDHK APMVLFLDRV YGIKDQTFLL HLLEVGFLPD LRASASLDTV 2400
    SLSTTEAALA LNRYLCSAVL PLLTRCAPLF SGTEHCTSLI DSTLQTIYRL 2450
    SKGRSLTKAQ RDTIEECLLA ICNHLRPSML QQLLRRLVFD VPQLSEYCKM 2500
    PLKLLTNHYE QCWKYYCLPS GWGSYGLAVE EELHLTEKLF WGIFDSLSHK 2550
    KYDLDLFRMA LPCLSAIAGA LPPDYLDTRI TATLEKQVSV DADGNFDPKP 2600
    INTMNFSLPE KLEYIVTKYA EHSHDKWACD KSHSGWKYGI SLDENVKTHP 2650
    LIRPFKTLTE KEKEIYRWPA RESLKTMLAV GWTVERTKEG EALVQQRENE 2700
    KLRCVSQTNQ GNSYSPAPLD LSNVVLSREL QGMVEVVAEN YHNIWAKKKK 2750
    LELESKGGGS HPLLVPYDTL TAKEKFRDRE KAQDLFKFLQ VNGILVSRGM 2800
    KDLELDASSM EKRFAYKFLK KILKYVDAAQ EFIAHLEAIV SSGKTEKSPH 2850
    DQEIKFFAKV LLPLVDQYFT NHRLYFLSSP LKPLSSSGYA SHKEKEMVAS 2900
    LFCKLAALVR HRISLFGSDS TTMVSCLHIL AQTLDTRTVM KSGSELVKAG 2950
    LRAFFENAAE DLEKTSENLK LGKFTHSRTQ IKGVSQNINY TTVALLPILT 3000
    SIFEHIAQHQ FGVDLLLSDV QVSCYHILCS LYSLGTGKNI YVERQRPALG 3050
    ECLASLAAAI PVAFLEPSLN RHNPLSVFNT KTPRERSILG MPDKVEDMCP 3100
    DIPQLEGLMK EINDLAESGA RYTEMPHVIE VILPMLCNYL SYWWERGPEN 3150
    LPPSTGPCCT KVTSEHLSLI LGNILKIINN NLGIDEASWM KRIAVYAQPI 3200
    ISKARPDLLR SHFIPTLEKL KKKAVKTVQE EEQLKTDGKG DTQEAELLIL 3250
    DEFAVLCRDL YAFYPMLIRY VDNNRSNWLK SPDPDSDQLF RMVAEVFILW 3300
    CKSHNFKREE QNFVIQNEIN NLAFLTGDSK SKMSKSGGQD QERKKTKRRG 3350
    DLYSIQTSLI VAALKKMLPI GLNMCTPGDQ ELISLAKSRY SCRDTDEEVK 3400
    EHLRNNLHLQ EKSDDPAVKW QLNLYKDVLR NDEPSNPEKT VERVQSISAA 3450
    LFHLEQVEQP LRSKKAVWHK LLSKQRKRAV VACFRMAPLY NLPRHRSINL 3500
    FLHGYQRFWI ETEAHFFEEK LVQDLAKSPR VEDEEEEETE RQPDPLHQII 3550
    LHFSRNALTE RSKLEDDPLY TSYSSMMAKS CQSGEDEEEE EDKEKTFEEK 3600
    EMEKQKTLYQ QARLHERGAA EMVLQMISAS KGEMSPMVVE TLKLGIAILN 3650
    GGNAGVQQKM LDYLKEKKDA GFFQSLSGLM QSCSVLDLNA FERQNKAEGL 3700
    GMVTEEGTLI VRERGEKVLQ NDEFTQDLFR FLQLLCEGHN SDFQNFLRTQ 3750
    MGNTTTVNII ISTVDYLLRL QESISDFYWY YSGKDIIDES GQHNFSKALA 3800
    VTKQIFNSLT EYIQGPCIGN QQSLAHSRLW DAVVGFLHVF ANMQMKLSQD 3850
    SSQIELLKEL LDLLQDMVVM LLSLLEGNVV NGTIGKQMVD TLVESSTNVE 3900
    MILKFFDMFL KLKDLTSSDT FKEYDPDGKG IISRKEFQKA MEGLKQYTQS 3950
    EIDFLLSCTE ADENDMFNYV DFVERFHEPA KDIGFNVAVL LTNLSEHMPN 4000
    DSRLKSLLDP AESVLNYFEP YLGRIEIMGG AKKIERVYFE ISESSRTQWE 4050
    KPQVKESKRQ FIFDVVNEGG EQEKMELFVN FCEDTIFEMQ LASQISESDS 4100
    TDRPEEEEEE DEDSAYSIET EGEEEEKSFE SASAFTMACV SVKRNVTKFL 4150
    KRATLKNLRK QYRNVKKMSA KELVKVFFSF FWMLFVGLFQ LLFTIFGGIF 4200
    QILWNTVFGG GLVEGAKNIR VTKILGDMPD PTQFGIHDDV IETDRAEVTE 4250
    PGVTTELVHF VKGEAGDTDI MSDLFGIHSK KEGGLKQGPE VGLGDLSEII 4300
    GKDEPPTLES TVRKKRKAQA AEMKAVHEAE GKAESEKADM EDREKEDKIK 4350
    EEGQTDYLWA DVTVKKTRRR GQKAEKPEAF MANFFKGLEI YQTKLLHYLA 4400
    RNFYNLRFLA LFVAFAINFI LLFYKVTEEP LEEETEDVAN LWNSFNDDDE 4450
    EEAMVFFVLQ ESTGYMAPTL RALAIVHTII SLVCVVGYYC LKVPLVVFKR 4500
    EKEIARKLEF DGLYITEQPS EDDIKGQWDR LVINTPSFPN NYWDKFVKRK 4550
    VINKYGDLYG AERIAELLGL DKNALDFSPV EEAKAEAASL VSWLSSIDMK 4600
    YHIWKLGVVF TDNSFLYLAW YTTMSVLGHY NNFFFAAHLL DIAMGFKTLR 4650
    TILSSVTHNG KQLVLTVGLL AVVVYLYTVV AFNFFRKFYN KSEDDDEPDM 4700
    KCDDMMTCYL FHMYVGVRAG GGIGDEIEDP AGDPYEMYRI VFDITFFFFV 4750
    IVILLAIIQG LIIDAFGELR DQQEQVREDM ETKCFICGIG NDYFDTTPHG 4800
    FETHTLQEHN LANYLFFLMY LINKDETEHT GQESYVWKMY QERCWDFFPA 4850
    GDCFRKQYED QLG 4863
    Length:4,863
    Mass (Da):551,328
    Last modified:February 5, 2008 - v1
    Checksum:iD2B086935E99D40B
    GO
    Isoform 2 (identifier: A2AGL3-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:4,834
    Mass (Da):547,747
    Checksum:iED773D40A48B773A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4169 – 41691S → I in AAF21940. 1 PublicationCurated
    Sequence conflicti4214 – 42141E → Q in AAF21940. 1 PublicationCurated
    Sequence conflicti4427 – 44271T → A in AAF21940. 1 PublicationCurated
    Sequence conflicti4450 – 44501E → V in BAE21181. (PubMed:16141072)Curated
    Sequence conflicti4457 – 44571F → L in CAA58786. (PubMed:7876312)Curated
    Sequence conflicti4469 – 44691T → N in CAA58786. (PubMed:7876312)Curated
    Sequence conflicti4602 – 46021H → N in AAA64957. (PubMed:7635066)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei4397 – 442529Missing in isoform 2. 1 PublicationVSP_042304Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL929348 Genomic DNA. No translation available.
    AL672250
    , AL691423, AL732316, BX649564 Genomic DNA. Translation: CAM15357.1.
    AL691423
    , AL672250, AL732316, BX649564 Genomic DNA. Translation: CAM17843.1.
    AL732316
    , AL672250, AL691423, BX649564 Genomic DNA. Translation: CAM22353.1.
    BX649564
    , 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.
    PIRiI48743.
    S56107.
    UniGeneiMm.436657.

    Genome annotation databases

    EnsembliENSMUST00000080673; ENSMUSP00000079503; ENSMUSG00000057378. [A2AGL3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL929348 Genomic DNA. No translation available.
    AL672250
    , AL691423 , AL732316 , BX649564 Genomic DNA. Translation: CAM15357.1 .
    AL691423
    , AL672250 , AL732316 , BX649564 Genomic DNA. Translation: CAM17843.1 .
    AL732316
    , AL672250 , AL691423 , BX649564 Genomic DNA. Translation: CAM22353.1 .
    BX649564
    , 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 .
    PIRi I48743.
    S56107.
    UniGenei Mm.436657.

    3D structure databases

    ProteinModelPortali A2AGL3.
    SMRi A2AGL3. Positions 13-532, 2596-2798, 3462-3488.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL2365.

    Proteomic databases

    PaxDbi A2AGL3.
    PRIDEi A2AGL3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000080673 ; ENSMUSP00000079503 ; ENSMUSG00000057378 . [A2AGL3-1 ]

    Organism-specific databases

    MGIi MGI:99684. Ryr3.

    Phylogenomic databases

    eggNOGi NOG247670.
    GeneTreei ENSGT00690000101961.
    HOGENOMi HOG000231428.
    HOVERGENi HBG006699.
    OrthoDBi EOG71K622.
    PhylomeDBi A2AGL3.

    Enzyme and pathway databases

    Reactomei REACT_196640. Stimuli-sensing channels.

    Miscellaneous databases

    ChiTaRSi RYR3. mouse.
    PROi A2AGL3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi A2AGL3.
    Bgeei A2AGL3.
    Genevestigatori A2AGL3.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.25.10.30. 1 hit.
    InterProi IPR001870. 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 ]
    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. 2 hits.
    SSF49899. SSF49899. 3 hits.
    SSF82109. SSF82109. 2 hits.
    PROSITEi PS50188. B302_SPRY. 3 hits.
    PS50919. MIR. 5 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. 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.
      , 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.

    Entry informationi

    Entry nameiRYR3_MOUSE
    AccessioniPrimary (citable) accession number: A2AGL3
    Secondary accession number(s): P70184
    , P70185, Q3V1H0, Q4JFC4, Q60836, Q62175, Q62198, Q9QY91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2012
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 62 of the entry and version 1 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 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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3