RYR1
entrez
6261
canonical
uniprot
P21817
canonical
ensembl
ENSG00000196218
resolver
ensp
ENSP00000347667
resolver
ensp
ENSP00000352608
resolver
ensp
ENSP00000470927
resolver
ensp
ENSP00000508999
resolver
enst
ENST00000594335
resolver
enst
ENST00000689936
resolver
genesymbol
RYR1
resolver
genesymbol_syn
RYDR
resolver
hgnc
HGNC:10483
resolver
uniprot
A0A8I5KSR1
resolver
uniprot
M0R014
resolver
uniprot
Q16314
resolver
uniprot
Q16368
resolver
uniprot
Q9NPK1
resolver
uniprot
Q9P1U4
resolver
uniprot_entry
A0A8I5KSR1_HUMAN
resolver
uniprot_entry
M0R014_HUMAN
resolver
uniprot_entry
RYR1_HUMAN
resolver
uniprot_sec
Q16314
resolver
uniprot_sec
Q16368
resolver
uniprot_sec
Q9NPK1
resolver
uniprot_sec
Q9P1U4
resolver
activity_regulation
ACTIVITY REGULATION: The calcium release is activated by increased cytosolic calcium levels, by nitric oxyde (NO), caffeine and ATP (PubMed:16163667, PubMed:18268335). Channel activity is modulated by the alkaloid ryanodine that binds to the open Ca-release channel with high affinity. At low concentrations, ryanodine maintains the channel in an open conformation. High ryanodine concentrations inhibit channel activity (By similarity). Channel activity is regulated by calmodulin (CALM) (PubMed:18650434). Channel activity is inhibited by magnesium ions, possibly by competition for calcium binding sites (By similarity). {ECO:0000250|UniProtKB:P11716, ECO:0000269|PubMed:16163667, ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:18650434}.
uniprot
proteins
amino_acid_sequence
MGDAEGEDEVQFLRTDDEVVLQCSATVLKEQLKLCLAAEGFGNRLCFLEPTSNAQNVPPDLAICCFVLEQSLSVRALQEMLANTVEAGVESSQGGGHRTLLYGHAILLRHAHSRMYLSCLTTSRSMTDKLAFDVGLQEDATGEACWWTMHPASKQRSEGEKVRVGDDIILVSVSSERYLHLSTASGELQVDASFMQTLWNMNPICSRCEEGFVTGGHVLRLFHGHMDECLTISPADSDDQRRLVYYEGGAVCTHARSLWRLEPLRISWSGSHLRWGQPLRVRHVTTGQYLALTEDQGLVVVDASKAHTKATSFCFRISKEKLDVAPKRDVEGMGPPEIKYGESLCFVQHVASGLWLTYAAPDPKALRLGVLKKKAMLHQEGHMDDALSLTRCQQEESQAARMIHSTNGLYNQFIKSLDSFSGKPRGSGPPAGTALPIEGVILSLQDLIIYFEPPSEDLQHEEKQSKLRSLRNRQSLFQEEGMLSMVLNCIDRLNVYTTAAHFAEFAGEEAAESWKEIVNLLYELLASLIRGNRSNCALFSTNLDWLVSKLDRLEASSGILEVLYCVLIESPEVLNIIQENHIKSIISLLDKHGRNHKVLDVLCSLCVCNGVAVRSNQDLITENLLPGRELLLQTNLINYVTSIRPNIFVGRAEGTTQYSKWYFEVMVDEVTPFLTAQATHLRVGWALTEGYTPYPGAGEGWGGNGVGDDLYSYGFDGLHLWTGHVARPVTSPGQHLLAPEDVISCCLDLSVPSISFRINGCPVQGVFESFNLDGLFFPVVSFSAGVKVRFLLGGRHGEFKFLPPPGYAPCHEAVLPRERLHLEPIKEYRREGPRGPHLVGPSRCLSHTDFVPCPVDTVQIVLPPHLERIREKLAENIHELWALTRIEQGWTYGPVRDDNKRLHPCLVDFHSLPEPERNYNLQMSGETLKTLLALGCHVGMADEKAEDNLKKTKLPKTYMMSNGYKPAPLDLSHVRLTPAQTTLVDRLAENGHNVWARDRVGQGWSYSAVQDIPARRNPRLVPYRLLDEATKRSNRDSLCQAVRTLLGYGYNIEPPDQEPSQVENQSRCDRVRIFRAEKSYTVQSGRWYFEFEAVTTGEMRVGWARPELRPDVELGADELAYVFNGHRGQRWHLGSEPFGRPWQPGDVVGCMIDLTENTIIFTLNGEVLMSDSGSETAFREIEIGDGFLPVCSLGPGQVGHLNLGQDVSSLRFFAICGLQEGFEPFAINMQRPVTTWFSKGLPQFEPVPLEHPHYEVSRVDGTVDTPPCLRLTHRTWGSQNSLVEMLFLRLSLPVQFHQHFRCTAGATPLAPPGLQPPAEDEARAAEPDPDYENLRRSAGGWSEAENGKEGTAKEGAPGGTPQAGGEAQPARAENEKDATTEKNKKRGFLFKAKKVAMMTQPPATPTLPRLPHDVVPADNRDDPEIILNTTTYYYSVRVFAGQEPSCVWAGWVTPDYHQHDMSFDLSKVRVVTVTMGDEQGNVHSSLKCSNCYMVWGGDFVSPGQQGRISHTDLVIGCLVDLATGLMTFTANGKESNTFFQVEPNTKLFPAVFVLPTHQNVIQFELGKQKNIMPLSAAMFQSERKNPAPQCPPRLEMQMLMPVSWSRMPNHFLQVETRRAGERLGWAVQCQEPLTMMALHIPEENRCMDILELSERLDLQRFHSHTLRLYRAVCALGNNRVAHALCSHVDQAQLLHALEDAHLPGPLRAGYYDLLISIHLESACRSRRSMLSEYIVPLTPETRAITLFPPGRSTENGHPRHGLPGVGVTTSLRPPHHFSPPCFVAALPAAGAAEAPARLSPAIPLEALRDKALRMLGEAVRDGGQHARDPVGGSVEFQFVPVLKLVSTLLVMGIFGDEDVKQILKMIEPEVFTEEEEEEDEEEEGEEEDEEEKEEDEEETAQEKEDEEKEEEEAAEGEKEEGLEEGLLQMKLPESVKLQMCHLLEYFCDQELQHRVESLAAFAERYVDKLQANQRSRYGLLIKAFSMTAAETARRTREFRSPPQEQINMLLQFKDGTDEEDCPLPEEIRQDLLDFHQDLLAHCGIQLDGEEEEPEEETTLGSRLMSLLEKVRLVKKKEEKPEEERSAEESKPRSLQELVSHMVVRWAQEDFVQSPELVRAMFSLLHRQYDGLGELLRALPRAYTISPSSVEDTMSLLECLGQIRSLLIVQMGPQEENLMIQSIGNIMNNKVFYQHPNLMRALGMHETVMEVMVNVLGGGESKEIRFPKMVTSCCRFLCYFCRISRQNQRSMFDHLSYLLENSGIGLGMQGSTPLDVAAASVIDNNELALALQEQDLEKVVSYLAGCGLQSCPMLVAKGYPDIGWNPCGGERYLDFLRFAVFVNGESVEENANVVVRLLIRKPECFGPALRGEGGSGLLAAIEEAIRISEDPARDGPGIRRDRRREHFGEEPPEENRVHLGHAIMSFYAALIDLLGRCAPEMHLIQAGKGEALRIRAILRSLVPLEDLVGIISLPLQIPTLGKDGALVQPKMSASFVPDHKASMVLFLDRVYGIENQDFLLHVLDVGFLPDMRAAASLDTATFSTTEMALALNRYLCLAVLPLITKCAPLFAGTEHRAIMVDSMLHTVYRLSRGRSLTKAQRDVIEDCLMSLCRYIRPSMLQHLLRRLVFDVPILNEFAKMPLKLLTNHYERCWKYYCLPTGWANFGVTSEEELHLTRKLFWGIFDSLAHKKYDPELYRMAMPCLCAIAGALPPDYVDASYSSKAEKKATVDAEGNFDPRPVETLNVIIPEKLDSFINKFAEYTHEKWAFDKIQNNWSYGENIDEELKTHPMLRPYKTFSEKDKEIYRWPIKESLKAMIAWEWTIEKAREGEEEKTEKKKTRKISQSAQTYDPREGYNPQPPDLSAVTLSRELQAMAEQLAENYHNTWGRKKKQELEAKGGGTHPLLVPYDTLTAKEKARDREKAQELLKFLQMNGYAVTRGLKDMELDSSSIEKRFAFGFLQQLLRWMDISQEFIAHLEAVVSSGRVEKSPHEQEIKFFAKILLPLINQYFTNHCLYFLSTPAKVLGSGGHASNKEKEMITSLFCKLAALVRHRVSLFGTDAPAVVNCLHILARSLDARTVMKSGPEIVKAGLRSFFESASEDIEKMVENLRLGKVSQARTQVKGVGQNLTYTTVALLPVLTTLFQHIAQHQFGDDVILDDVQVSCYRTLCSIYSLGTTKNTYVEKLRPALGECLARLAAAMPVAFLEPQLNEYNACSVYTTKSPRERAILGLPNSVEEMCPDIPVLERLMADIGGLAESGARYTEMPHVIEITLPMLCSYLPRWWERGPEAPPSALPAGAPPPCTAVTSDHLNSLLGNILRIIVNNLGIDEASWMKRLAVFAQPIVSRARPELLQSHFIPTIGRLRKRAGKVVSEEEQLRLEAKAEAQEGELLVRDEFSVLCRDLYALYPLLIRYVDNNRAQWLTEPNPSAEELFRMVGEIFIYWSKSHNFKREEQNFVVQNEINNMSFLTADNKSKMAKAGDIQSGGSDQERTKKKRRGDRYSVQTSLIVATLKKMLPIGLNMCAPTDQDLITLAKTRYALKDTDEEVREFLHNNLHLQGKVEGSPSLRWQMALYRGVPGREEDADDPEKIVRRVQEVSAVLYYLDQTEHPYKSKKAVWHKLLSKQRRRAVVACFRMTPLYNLPTHRACNMFLESYKAAWILTEDHSFEDRMIDDLSKAGEQEEEEEEVEEKKPDPLHQLVLHFSRTALTEKSKLDEDYLYMAYADIMAKSCHLEEGGENGEAEEEVEVSFEEKQMEKQRLLYQQARLHTRGAAEMVLQMISACKGETGAMVSSTLKLGISILNGGNAEVQQKMLDYLKDKKEVGFFQSIQALMQTCSVLDLNAFERQNKAEGLGMVNEDGTVINRQNGEKVMADDEFTQDLFRFLQLLCEGHNNDFQNYLRTQTGNTTTINIIICTVDYLLRLQESISDFYWYYSGKDVIEEQGKRNFSKAMSVAKQVFNSLTEYIQGPCTGNQQSLAHSRLWDAVVGFLHVFAHMMMKLAQDSSQIELLKELLDLQKDMVVMLLSLLEGNVVNGMIARQMVDMLVESSSNVEMILKFFDMFLKLKDIVGSEAFQDYVTDPRGLISKKDFQKAMDSQKQFSGPEIQFLLSCSEADENEMINCEEFANRFQEPARDIGFNVAVLLTNLSEHVPHDPRLHNFLELAESILEYFRPYLGRIEIMGASRRIERIYFEISETNRAQWEMPQVKESKRQFIFDVVNEGGEAEKMELFVSFCEDTIFEMQIAAQISEPEGEPETDEDEGAGAAEAGAEGAEEGAAGLEGTAATAAAGATARVVAAAGRALRGLSYRSLRRRVRRLRRLTAREAATAVAALLWAAVTRAGAAGAGAAAGALGLLWGSLFGGGLVEGAKKVTVTELLAGMPDPTSDEVHGEQPAGPGGDADGEGASEGAGDAAEGAGDEEEAVHEAGPGGADGAVAVTDGGPFRPEGAGGLGDMGDTTPAEPPTPEGSPILKRKLGVDGVEEELPPEPEPEPEPELEPEKADAENGEKEEVPEPTPEPPKKQAPPSPPPKKEEAGGEFWGELEVQRVKFLNYLSRNFYTLRFLALFLAFAINFILLFYKVSDSPPGEDDMEGSAAGDVSGAGSGGSSGWGLGAGEEAEGDEDENMVYYFLEESTGYMEPALRCLSLLHTLVAFLCIIGYNCLKVPLVIFKREKELARKLEFDGLYITEQPEDDDVKGQWDRLVLNTPSFPSNYWDKFVKRKVLDKHGDIYGRERIAELLGMDLATLEITAHNERKPNPPPGLLTWLMSIDVKYQIWKFGVIFTDNSFLYLGWYMVMSLLGHYNNFFFAAHLLDIAMGVKTLRTILSSVTHNGKQLVMTVGLLAVVVYLYTVVAFNFFRKFYNKSEDEDEPDMKCDDMMTCYLFHMYVGVRAGGGIGDEIEDPAGDEYELYRVVFDITFFFFVIVILLAIIQGLIIDAFGELRDQQEQVKEDMETKCFICGIGSDYFDTTPHGFETHTLEEHNLANYMFFLMYLINKDETEHTGQESYVWKMYQERCWDFFPAGDCFRKQYEDQLS
uniprot
proteins
disease_involvement
DISEASE: Malignant hyperthermia 1 (MHS1) [MIM:145600]: Autosomal dominant pharmacogenetic disorder of skeletal muscle and is one of the main causes of death due to anesthesia. In susceptible people, an MH episode can be triggered by all commonly used inhalational anesthetics such as halothane and by depolarizing muscle relaxants such as succinylcholine. The clinical features of the myopathy are hyperthermia, accelerated muscle metabolism, contractures, metabolic acidosis, tachycardia and death, if not treated with the postsynaptic muscle relaxant, dantrolene. Susceptibility to MH can be determined with the 'in vitro' contracture test (IVCT): observing the magnitude of contractures induced in strips of muscle tissue by caffeine alone and halothane alone. Patients with normal response are MH normal (MHN), those with abnormal response to caffeine alone or halothane alone are MH equivocal (MHE(C) and MHE(H) respectively). {ECO:0000269|PubMed:10051009, ECO:0000269|PubMed:10484775, ECO:0000269|PubMed:10612851, ECO:0000269|PubMed:10823104, ECO:0000269|PubMed:10888602, ECO:0000269|PubMed:11241852, ECO:0000269|PubMed:11389482, ECO:0000269|PubMed:11525881, ECO:0000269|PubMed:11575529, ECO:0000269|PubMed:11928716, ECO:0000269|PubMed:12059893, ECO:0000269|PubMed:12066726, ECO:0000269|PubMed:12123492, ECO:0000269|PubMed:12208234, ECO:0000269|PubMed:12411788, ECO:0000269|PubMed:12709367, ECO:0000269|PubMed:12883402, ECO:0000269|PubMed:1354642, ECO:0000269|PubMed:14641996, ECO:0000269|PubMed:14732627, ECO:0000269|PubMed:14985404, ECO:0000269|PubMed:15221887, ECO:0000269|PubMed:15448513, ECO:0000269|PubMed:16163667, ECO:0000269|PubMed:1774074, ECO:0000269|PubMed:19191329, ECO:0000269|PubMed:19685112, ECO:0000269|PubMed:20142353, ECO:0000269|PubMed:20681998, ECO:0000269|PubMed:23558838, ECO:0000269|PubMed:24013571, ECO:0000269|PubMed:26115329, ECO:0000269|PubMed:26381711, ECO:0000269|PubMed:26631338, ECO:0000269|PubMed:27586648, ECO:0000269|PubMed:7751854, ECO:0000269|PubMed:7849712, ECO:0000269|PubMed:7881417, ECO:0000269|PubMed:8012359, ECO:0000269|PubMed:8220423, ECO:0000269|PubMed:9066328, ECO:0000269|PubMed:9138151, ECO:0000269|PubMed:9389851, ECO:0000269|PubMed:9450902, ECO:0000269|PubMed:9497245}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Congenital myopathy 1A, autosomal dominant, with susceptibility to malignant hyperthermia (CMYO1A) [MIM:117000]: An autosomal dominant myopathy characterized by hypotonia and proximal muscle weakness primarily affecting the lower limbs, beginning in infancy or early childhood. Some patients manifest later onset of symptoms. The clinical course of the disorder is usually slow or non-progressive in adulthood, and the severity of the symptoms is variable. Affected individuals typically show delayed motor development and usually achieve independent walking, although many have difficulty running or climbing stairs. Additional features often include mild facial weakness, joint laxity, shoulder girdle weakness, and skeletal manifestations, such as dislocation of the hips, foot deformities, scoliosis, and Achilles tendon contractures. Microscopic examination of affected skeletal muscle reveals a predominance of type I fibers containing amorphous-looking areas (cores) that do not stain with oxidative and phosphorylase histochemical techniques. Additional pathologic findings may also be observed on muscle biopsy. CMYO1A affected individuals are at risk for malignant hyperthermia, and both disorders may be present in the same family. {ECO:0000269|PubMed:10097181, ECO:0000269|PubMed:11113224, ECO:0000269|PubMed:11709545, ECO:0000269|PubMed:11741831, ECO:0000269|PubMed:12565913, ECO:0000269|PubMed:12566385, ECO:0000269|PubMed:12937085, ECO:0000269|PubMed:14670767, ECO:0000269|PubMed:14985404, ECO:0000269|PubMed:17204054, ECO:0000269|PubMed:17226826, ECO:0000269|PubMed:18312400, ECO:0000269|PubMed:20142353, ECO:0000269|PubMed:21674524, ECO:0000269|PubMed:23558838, ECO:0000269|PubMed:24561095, ECO:0000269|PubMed:26381711, ECO:0000269|PubMed:27234031, ECO:0000269|PubMed:27586648, ECO:0000269|PubMed:7829078, ECO:0000269|PubMed:8220422, ECO:0000269|PubMed:8220423, ECO:0000269|PubMed:9497245}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Congenital myopathy 1B, autosomal recessive (CMYO1B) [MIM:255320]: An autosomal recessive myopathy characterized by severe hypotonia and generalized muscle weakness and atrophy apparent soon after birth or in early childhood. Affected individuals show delayed motor development, proximal muscle weakness with axial and shoulder girdle involvement, difficulty walking or running, external ophthalmoplegia, and bulbar weakness often resulting in feeding difficulties and respiratory insufficiency. Disease severity is variable. Some affected individuals show symptoms in utero, including reduced fetal movements, polyhydramnios, and intrauterine growth restriction. Some patients have lethal fetal akinesia with death in utero. Muscle biopsy can show variable findings, including multiple and poorly circumscribed areas of sarcomere disorganization and mitochondria depletion (areas termed minicores). Typically, no dystrophic signs, such as muscle fiber necrosis or regeneration or significant endomysial fibrosis, are present. {ECO:0000269|PubMed:12112081, ECO:0000269|PubMed:12136074, ECO:0000269|PubMed:12719381, ECO:0000269|PubMed:12937085, ECO:0000269|PubMed:16380615, ECO:0000269|PubMed:17226826, ECO:0000269|PubMed:18253926, ECO:0000269|PubMed:20583297}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in RYR1 may be a cause of Samaritan myopathy, a congenital myopathy with benign course. Patients display severe hypotonia and respiratory distress at birth. Unlike other congenital myopathies, the health status constantly improves and patients are minimally affected at adulthood.; DISEASE: King-Denborough syndrome (KDS) [MIM:619542]: An autosomal dominant disorder characterized by the triad of dysmorphic features, congenital myopathy, and susceptibility to malignant hyperthermia. Variable expressivity has been reported in several cases. {ECO:0000269|PubMed:18765655, ECO:0000269|PubMed:21514828, ECO:0000269|PubMed:27918309}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytosol and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (PubMed:11741831, PubMed:16163667, PubMed:18268335, PubMed:18650434, PubMed:26115329). Repeated very high-level exercise increases the open probability of the channel and leads to Ca(2+) leaking into the cytoplasm (PubMed:18268335). Can also mediate the release of Ca(2+) from intracellular stores in neurons, and may thereby promote prolonged Ca(2+) signaling in the brain. Required for normal embryonic development of muscle fibers and skeletal muscle. Required for normal heart morphogenesis, skin development and ossification during embryogenesis (By similarity). {ECO:0000250|UniProtKB:E9PZQ0, ECO:0000269|PubMed:18268335, ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:26115329, ECO:0000305|PubMed:11741831, ECO:0000305|PubMed:16163667}.
uniprot
proteins
mass_dalton
565176
uniprot
proteins
mutagenesis
MUTAGEN 522; /note="Y->C: Increases calcium-induced calcium release activity."; /evidence="ECO:0000269|PubMed:26115329"; MUTAGEN 2508; /note="R->K: Increases sensitivity to caffeine and 4-chloro-m-cresol."; /evidence="ECO:0000269|PubMed:26381711"; MUTAGEN 2508; /note="R->S: Increases sensitivity to caffeine and 4-chloro-m-cresol."; /evidence="ECO:0000269|PubMed:26381711
uniprot
proteins
post_translational_modification
PTM: Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2843 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2843. {ECO:0000269|PubMed:18268335}.; PTM: Activated by reversible S-nitrosylation (By similarity). Repeated very high-level exercise increases S-nitrosylation (PubMed:18268335). {ECO:0000250|UniProtKB:P11716, ECO:0000269|PubMed:18268335}.
uniprot
proteins
protein_family
RYR1 subfamily
uniprot
proteins
protein_family
Ryanodine receptor (TC 1.A.3.1) family
uniprot
proteins
pubmed
10051009
uniprot
proteins
pubmed
10097181
uniprot
proteins
pubmed
10484775
uniprot
proteins
pubmed
10612851
uniprot
proteins
pubmed
10823104
uniprot
proteins
pubmed
10888602
uniprot
proteins
pubmed
11113224
uniprot
proteins
pubmed
11241852
uniprot
proteins
pubmed
11389482
uniprot
proteins
pubmed
11525881
uniprot
proteins
pubmed
11575529
uniprot
proteins
pubmed
11709545
uniprot
proteins
pubmed
11741831
uniprot
proteins
pubmed
11928716
uniprot
proteins
pubmed
12059893
uniprot
proteins
pubmed
12066726
uniprot
proteins
pubmed
12112081
uniprot
proteins
pubmed
12123492
uniprot
proteins
pubmed
12136074
uniprot
proteins
pubmed
12208234
uniprot
proteins
pubmed
12411788
uniprot
proteins
pubmed
12565913
uniprot
proteins
pubmed
12566385
uniprot
proteins
pubmed
12709367
uniprot
proteins
pubmed
12719381
uniprot
proteins
pubmed
12883402
uniprot
proteins
pubmed
12937085
uniprot
proteins
pubmed
1354642
uniprot
proteins
pubmed
14641996
uniprot
proteins
pubmed
14670767
uniprot
proteins
pubmed
14732627
uniprot
proteins
pubmed
14985404
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15221887
uniprot
proteins
pubmed
15448513
uniprot
proteins
pubmed
16163667
uniprot
proteins
pubmed
16380615
uniprot
proteins
pubmed
1639409
uniprot
proteins
pubmed
17204054
uniprot
proteins
pubmed
17226826
uniprot
proteins
pubmed
1774074
uniprot
proteins
pubmed
18253926
uniprot
proteins
pubmed
18268335
uniprot
proteins
pubmed
18312400
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18650434
uniprot
proteins
pubmed
18765655
uniprot
proteins
pubmed
19191329
uniprot
proteins
pubmed
19685112
uniprot
proteins
pubmed
20142353
uniprot
proteins
pubmed
20583297
uniprot
proteins
pubmed
20681998
uniprot
proteins
pubmed
20961976
uniprot
proteins
pubmed
21514828
uniprot
proteins
pubmed
21674524
uniprot
proteins
pubmed
22752422
uniprot
proteins
pubmed
2298749
uniprot
proteins
pubmed
23558838
uniprot
proteins
pubmed
24013571
uniprot
proteins
pubmed
24561095
uniprot
proteins
pubmed
26115329
uniprot
proteins
pubmed
26381711
uniprot
proteins
pubmed
26631338
uniprot
proteins
pubmed
27234031
uniprot
proteins
pubmed
27586648
uniprot
proteins
pubmed
27616680
uniprot
proteins
pubmed
27918309
uniprot
proteins
pubmed
7556644
uniprot
proteins
pubmed
7751854
uniprot
proteins
pubmed
7829078
uniprot
proteins
pubmed
7849712
uniprot
proteins
pubmed
7881417
uniprot
proteins
pubmed
8012359
uniprot
proteins
pubmed
8220422
uniprot
proteins
pubmed
8220423
uniprot
proteins
pubmed
8661021
uniprot
proteins
pubmed
9066328
uniprot
proteins
pubmed
9138151
uniprot
proteins
pubmed
9389851
uniprot
proteins
pubmed
9450902
uniprot
proteins
pubmed
9497245
uniprot
proteins
pubmed
9607712
uniprot
proteins
sequence_length
5038
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:7556644}; Multi-pass membrane protein {ECO:0000255}. Note=The number of predicted transmembrane domains varies between orthologs. Both N-terminus and C-terminus are cytoplasmic. {ECO:0000250|UniProtKB:P11716}.
uniprot
proteins
transmembrane_region
TRANSMEM 4560..4580; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P11716"; TRANSMEM 4642..4662; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P11716"; TRANSMEM 4781..4803; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P11716"; TRANSMEM 4805..4821; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P11716"; TRANSMEM 4837..4857; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P11716"; TRANSMEM 4921..4941; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P11716
uniprot
proteins