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Entry version 75 (26 Feb 2020)
Sequence version 1 (03 May 2011)
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Protein

Ryanodine receptor 1

Gene

Ryr1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium channel that mediates the release of Ca2+ from the sarcoplasmic reticulum into the cytoplasm and thereby plays a key role in triggering muscle contraction following depolarization of T-tubules (PubMed:11316255). Repeated very high-level exercise increases the open probability of the channel and leads to Ca2+ leaking into the cytoplasm (By similarity). Can also mediate the release of Ca2+ from intracellular stores in neurons, and may thereby promote prolonged Ca2+ 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).By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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. Channel activity is regulated by calmodulin (CALM) (By similarity). The calcium release is activated by increased cytoplasmic calcium levels, by nitric oxyde (NO), caffeine and ATP (PubMed:11316255). Channel activity is inhibited by magnesium ions, possibly by competition for calcium binding sites (PubMed:11316255).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi3896CalciumBy similarity1
Metal bindingi3970CalciumBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei4714CaffeineBy similarity1
Metal bindingi4999Calcium; via carbonyl oxygenBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi4214 – 4218ATPBy similarity5
Nucleotide bindingi4952 – 4957ATPBy similarity6
Nucleotide bindingi4977 – 4983ATPBy similarity7

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCalcium channel, Calmodulin-binding, Developmental protein, Ion channel, Ligand-gated ion channel, Receptor
Biological processCalcium transport, Ion transport, Transport
LigandATP-binding, Calcium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-2672351 Stimuli-sensing channels
R-RNO-5578775 Ion homeostasis

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Ryanodine receptor 1
Short name:
RYR-1
Short name:
RyR1
Alternative name(s):
Skeletal muscle calcium release channel
Skeletal muscle ryanodine receptor
Skeletal muscle-type ryanodine receptor
Type 1 ryanodine receptor
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ryr1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
1586637 Ryr1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 4556CytoplasmicBy similarityAdd BLAST4556
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei4557 – 4577Helical; Name=1By similarityAdd BLAST21
Topological domaini4578 – 4638LumenalBy similarityAdd BLAST61
Transmembranei4639 – 4659Helical; Name=2By similarityAdd BLAST21
Topological domaini4660 – 4777CytoplasmicBy similarityAdd BLAST118
Transmembranei4778 – 4800Helical; Name=3By similarityAdd BLAST23
Topological domaini4801LumenalBy similarity1
Transmembranei4802 – 4818Helical; Name=4By similarityAdd BLAST17
Topological domaini4819 – 4833CytoplasmicBy similarityAdd BLAST15
Transmembranei4834 – 4854Helical; Name=5By similarityAdd BLAST21
Topological domaini4855 – 4877LumenalBy similarityAdd BLAST23
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei4878 – 4897Pore-formingBy similarityAdd BLAST20
Topological domaini4898 – 4917LumenalBy similarityAdd BLAST20
Transmembranei4918 – 4938Helical; Name=6By similarityAdd BLAST21
Topological domaini4939 – 5035CytoplasmicBy similarityAdd BLAST97

Keywords - Cellular componenti

Membrane, Sarcoplasmic reticulum

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004155671 – 5035Ryanodine receptor 1Add BLAST5035

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1338PhosphoserineCombined sources1
Modified residuei2344PhosphoserineCombined sources1
Modified residuei2840PhosphoserineCombined sources1
Modified residuei3634S-nitrosocysteineBy similarity1
Modified residuei4464PhosphothreonineCombined sources1
Modified residuei4468PhosphoserineCombined sources1
Modified residuei4861PhosphotyrosineBy similarity1
Modified residuei4864PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Channel activity is modulated by phosphorylation. Phosphorylation at Ser-2840 may increase channel activity. Repeated very high-level exercise increases phosphorylation at Ser-2840.By similarity
Activated by reversible S-nitrosylation (By similarity). Repeated very high-level exercise increases S-nitrosylation (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
F1LMY4

PRoteomics IDEntifications database

More...
PRIDEi
F1LMY4

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
F1LMY4

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
F1LMY4

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
F1LMY4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in skeletal muscle (at protein level) (PubMed:11316255). Detected in myometrium smooth muscle (PubMed:10444400).2 Publications

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotetramer. Can also form heterotetramers with RYR2 (By similarity).

Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1). Repeated very high-level exercise decreases interaction with PDE4D and protein phosphatase 1 (PP1) (By similarity).

Interacts with CALM; CALM with bound calcium inhibits the RYR1 channel activity (By similarity).

Interacts with S100A1 (By similarity).

Interacts with FKBP1A; this stabilizes the closed conformation of the channel.

Interacts with CACNA1S; interaction with CACNA1S is important for activation of the RYR1 channel.

Interacts with CACNB1.

Interacts with TRDN and ASPH; these interactions stimulate RYR1 channel activity.

Interacts with SELENON (By similarity).

Interacts with scorpion calcins (AC P0DPT1; AC P0DM30; AC A0A1L4BJ42; AC P59868; AC P60254; AC B8QG00; AC L0GBR1; AC P60252; AC P60253) (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
F1LMY4

Protein interaction database and analysis system

More...
IntActi
F1LMY4, 3 interactors

Molecular INTeraction database

More...
MINTi
F1LMY4

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000027893

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini99 – 154MIR 1PROSITE-ProRule annotationAdd BLAST56
Domaini161 – 206MIR 2PROSITE-ProRule annotationAdd BLAST46
Domaini212 – 266MIR 3PROSITE-ProRule annotationAdd BLAST55
Domaini272 – 329MIR 4PROSITE-ProRule annotationAdd BLAST58
Domaini337 – 394MIR 5PROSITE-ProRule annotationAdd BLAST58
Domaini583 – 799B30.2/SPRY 1PROSITE-ProRule annotationAdd BLAST217
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati843 – 9561Add BLAST114
Repeati957 – 10702Add BLAST114
Domaini1015 – 1209B30.2/SPRY 2PROSITE-ProRule annotationAdd BLAST195
Repeati1345 – 13603; truncatedAdd BLAST16
Domaini1358 – 1571B30.2/SPRY 3PROSITE-ProRule annotationAdd BLAST214
Repeati1373 – 13884; truncatedAdd BLAST16
Repeati2723 – 28425Add BLAST120
Repeati2843 – 29566Add BLAST114
Domaini4078 – 4106EF-handPROSITE-ProRule annotationAdd BLAST29

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni671 – 682Interaction with FKBP1ABy similarityAdd BLAST12
Regioni843 – 29566 X approximate repeatsAdd BLAST2114
Regioni3613 – 3642Interaction with CALMBy similarityAdd BLAST30

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi4892 – 4898Selectivity filterBy similarity7

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1867 – 2087Glu-richAdd BLAST221
Compositional biasi3681 – 3760Glu-richAdd BLAST80
Compositional biasi4459 – 4525Pro-richAdd BLAST67

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The calcium release channel activity resides in the C-terminal region while the remaining part of the protein constitutes the 'foot' structure spanning the junctional gap between the sarcoplasmic reticulum (SR) and the T-tubule. Pore opening is mediated via the cytoplasmic calcium-binding domains that mediate a small rotation of the channel-forming transmembrane regions that then leads to channel opening.By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2243 Eukaryota
ENOG410YCNW LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
F1LMY4

TreeFam database of animal gene trees

More...
TreeFami
TF315244

Family and domain databases

Conserved Domains Database

More...
CDDi
cd12877 SPRY1_RyR, 1 hit
cd12878 SPRY2_RyR, 1 hit
cd12879 SPRY3_RyR, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001870 B30.2/SPRY
IPR013320 ConA-like_dom_sf
IPR011992 EF-hand-dom_pair
IPR014821 Ins145_P3_rcpt
IPR005821 Ion_trans_dom
IPR036300 MIR_dom_sf
IPR016093 MIR_motif
IPR013662 RIH_assoc-dom
IPR000699 RIH_dom
IPR013333 Ryan_recept
IPR003032 Ryanodine_rcpt
IPR009460 Ryanrecept_TM4-6
IPR035910 RyR/IP3R_RIH_dom_sf
IPR033215 RyR1
IPR035761 SPRY1_RyR
IPR035764 SPRY2_RyR
IPR035762 SPRY3_RyR
IPR003877 SPRY_dom

The PANTHER Classification System

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PANTHERi
PTHR13715:SF15 PTHR13715:SF15, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
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

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00795 RYANODINER

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00472 MIR, 4 hits
SM00449 SPRY, 3 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF100909 SSF100909, 2 hits
SSF47473 SSF47473, 1 hit
SSF49899 SSF49899, 3 hits
SSF82109 SSF82109, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50188 B302_SPRY, 3 hits
PS50919 MIR, 5 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

F1LMY4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGDGGGEGED EVQFLRTDDE VVLQCSATVL KEQLKLCLAA EGFGNRLCFL
60 70 80 90 100
EPTSNAQNVP PDLAICCFIL EQSLSVRALQ EMLANTVEAG VESSQGGGHR
110 120 130 140 150
TLLYGHAILL RHAHSRMYLS CLTTSRSMTD KLAFDVGLQE DATGEACWWT
160 170 180 190 200
MHPASKQRSE GEKVRVGDDL ILVSVSSERY LHLSTASGEL QVDASFMQTL
210 220 230 240 250
WNMNPICSCC EEGFVTGGHV LRLFHGHMDE CLTISPSDSD DQRRLVYYEG
260 270 280 290 300
GPVCTHARSL WRLEPLRISW SGSHLRWGQP LRIRHVTTGR YLALTEDQGL
310 320 330 340 350
VVVDASKAHT KATSFCFRIS KEKLDVAPKR DVEGMGPPEI KYGESLCFVQ
360 370 380 390 400
HVASGLWLTY AAPDPKALRL GVLKKKAMLH QEGHMDDALS LTRCQQEESQ
410 420 430 440 450
AARMIYSTAG LYNQFIKGLD SFSGKPRGSG PPAGSALPIE GVILSLQDLI
460 470 480 490 500
GYFEPPSEEL QHEEKQTKLR SLRNRQSLFQ EEGMLSLVLN CIDRLNVYTT
510 520 530 540 550
AAHFAEFAGE EAAESWKEIV NLLYELLASL IRGNRTNCAL FSTNLDWLVS
560 570 580 590 600
KLDRLEASSG ILEVLYCVLI ESPEVLNIIQ ENHIKSIISL LDKHGRNHKV
610 620 630 640 650
LDVLCSLCVC NGVAVRSNQD LITENLLPGR ELLLQTNLIN YVTSIRPNIF
660 670 680 690 700
VGRAEGSTQY GKWYFEVMVD EVAPFLTAQA THLRVGWALS EGYSPYPGGG
710 720 730 740 750
EGWGGNGVGD DLYSYGFDGL HLWTGHVARP VTSPGQHLLG PEDVVSCCLD
760 770 780 790 800
LSVPSISFRI NGCPVQGVFE SFNLDGLFFP VVSFSAGIKV RFLLGGRHGE
810 820 830 840 850
FKFLPPPGYA PCHEAVLPRE RLHLQPIKEY RREGPRGPHL VGPSRCLSHL
860 870 880 890 900
DFVPCPVDTI QIVLPPHLER IREKLAENIH ELWALTRIEQ GWTYGPVRDD
910 920 930 940 950
NKRLHPCLVD FHSLPEPERN YNLQMSGETL KTLLALGCHV GMADEKAEDN
960 970 980 990 1000
LKKTKLPKTY MMNNGYKPAP LDLSHVRLTP AQTTLVDRLA ENGHNVWARD
1010 1020 1030 1040 1050
RVAQGWSYSA VQDIPARRNP RLVPYRLLDE ATKRSNRDSL CQAVRTLLGY
1060 1070 1080 1090 1100
GYNIEPPDQE PSQVDSQSRG DRARIFRAEK SYAVQSGRWY FEFEAVTTGR
1110 1120 1130 1140 1150
ELGWARPELR PDVELGADDL AYVFNGHRGQ RWHLGSEPFG RPWQSGDVVG
1160 1170 1180 1190 1200
CMIDLTENTI IFTLNGEVLM SDSGSETAFR EIEIGDGFLP VCSLGPGQVG
1210 1220 1230 1240 1250
HLNLGQDVSS LRFFAICGLQ EGFEPFAINM QRPVTTWFSK SLPQFEPVPL
1260 1270 1280 1290 1300
EHPHYEVARM DGTVDTPPCL RLTHRTWGSQ NSLVEMLFLR LSLPVQFHQH
1310 1320 1330 1340 1350
FRCTAGATPL ASPGLQPPAE DEARAAEPDT DYENLRRSAG GWGEAEAGKD
1360 1370 1380 1390 1400
GTAKEGTPGG AAQPGVEAQP ARAENEKDAT TEKNKKRGFL FKAKKVAMMT
1410 1420 1430 1440 1450
QPPSTPALPR LPRDVVPADN RDDPEIILNT TTYYYSVRVF AGQEPSCVWV
1460 1470 1480 1490 1500
GWVTPDYHQH DMSFDLSKVR AVTVTMGDEQ GNVHSSLKCS NCYMVWGGDF
1510 1520 1530 1540 1550
VSPGQQGRIS HTDLVIGCLV DLATGLMTFT ANGKESNTFF QVEPNTKLFP
1560 1570 1580 1590 1600
AVFVLPTHQN VVQFDLRPGA NIMPLSAAMF LSERKNPAPQ CPPRLEVQML
1610 1620 1630 1640 1650
MPVSWSRMPN HFLHVDTRRA GERLGWAVQC QEPLMMMALH IPEENSEPYI
1660 1670 1680 1690 1700
HLKRAQLDPR DLRDYRDTKF DSESSDSDQT PQPGCYHVDQ AQLLHALEDA
1710 1720 1730 1740 1750
HLPGPLRAGY YDLLISIHLE SACRSRRSML SEYIVPLTEE TRAITLFPPG
1760 1770 1780 1790 1800
RSAEDGPRRH GLPGVGVTTS LRPPHHFSPP CFVVALPAAG AAEAPARLSP
1810 1820 1830 1840 1850
AIPLEALRDK ALRMLGEAVR DGGQHARDPV GGSVEFQFVP VLKLVSTLLV
1860 1870 1880 1890 1900
MGVFSDEDVK QILKMIEPEV FTEEEEVEEE EEEEEEDEEE KEEDEEEEAH
1910 1920 1930 1940 1950
EKEDEEKEEA EEAAEEEKEE LEEGLLQMKL PESVKLQMCH LLEYFCDQEL
1960 1970 1980 1990 2000
QHRVESLAAF AERYVDKLQS NQRGRYGLLM KAFTMSAAET ARRTREFRSP
2010 2020 2030 2040 2050
PQEQINMLLQ FKNGADEEDC PLPEEIREDL VNFHQDLLAH CGIQLEGEEE
2060 2070 2080 2090 2100
EPEEESTLGS RLMSLLEKVR LVKKKEEKPE EEPAAEEHKP QSLQELVSHT
2110 2120 2130 2140 2150
VVRWAQEDFV QSPELVRAMF SLLHRQYDGL GELLRALPRA YTISLSSVED
2160 2170 2180 2190 2200
TMSLLECLGQ IRSLLIVQMG PQEENLMIQS IGNIMNNKVF YQHPNLMRAL
2210 2220 2230 2240 2250
GMHETVMEVM VNVLGGGESK EIRFPKMVTS CCRFLCYFCR ISRQNQRSMF
2260 2270 2280 2290 2300
DHLSYLLENS GIGLGMQGST PLDVAAASVI DNNELALALQ EQDLEKVVSY
2310 2320 2330 2340 2350
LAGCGLQSCP MLLAKGYPDI GWNPCGGERY LDFLRFAVFV NGESVEENAN
2360 2370 2380 2390 2400
VVVRLLIRKP ECFGPALRGE GGSGLLAAIE EAIRISEDPA RDGPGVRRDR
2410 2420 2430 2440 2450
RREHFGEEPP EENRVHLGHA IMSFYAALID LLGRCAPEMH LIQAGKGEAL
2460 2470 2480 2490 2500
RIRAILRSLV PLDDLVGIIS LPLQIPTLGK DGALVQPKMS ASFVPDHKAS
2510 2520 2530 2540 2550
MVLFLDRVYG IENQDFLLHV LDVGFLPDMR AAASLDTATF SRRWALALTR
2560 2570 2580 2590 2600
YLCAVLPLIT KCAPLLRGTE HRAIMVDSML HTVYRLSRGR SLTKAQRDVI
2610 2620 2630 2640 2650
EDCLMALCRY IRPSMLQHLL RRLVFDVPIL NEFAKMPLKL LTNHYERCWK
2660 2670 2680 2690 2700
YYCLPTGWAN FGVTSEEELH LTRKLFWGIF DSLAHKKYDQ ELYRIAMPCL
2710 2720 2730 2740 2750
CAIAGALPPD YVDASYSSKT EKKATVDAEG NFDPRPVETL NVIIPEKLDS
2760 2770 2780 2790 2800
FINKFAEYAH EKWAFDKIQN NWSYGENIDE ELKTHPMLRP YKTFSEKDKE
2810 2820 2830 2840 2850
IYRWPIKESL KAMIAWEWTV EKAREGEEEK TEKKKTRKIS QTAQTYDPRE
2860 2870 2880 2890 2900
GYNPQPPDLS VVTLSRELQA MAEQLAENYH NTWGRKKKQE LEAKGGGSHP
2910 2920 2930 2940 2950
LLVPYDTLTA KEKARDREKA QELLKFLQMN GYAVTRHGKD MELDTSSIEK
2960 2970 2980 2990 3000
RFAFGFLQQL LRWMDISQEF IAHLEAVVSS GRVEKSPHEQ EIKFFAKILL
3010 3020 3030 3040 3050
PLINQYFTNH CLYFLSTPAK VLGSGGHASN KEKEMITSLF CKLAALVRHR
3060 3070 3080 3090 3100
VSLFGTDAPA VVNCLHILAR SLDARTVMKS GPEIVKAGLR SFFESASEDI
3110 3120 3130 3140 3150
EKMVENLRLG KVSQARTQVK GVGQNLTYTT VALLPVLTTL FQHIAQHQFG
3160 3170 3180 3190 3200
DDVILDDVQV SCYRTLCSIY SLGTTRNPYV EKLRPALGEC LARLAAAMPV
3210 3220 3230 3240 3250
AFLEPELNEY NACSVYTTKS PRERAILGLP NSVEEMCPDI PVLERLMAEI
3260 3270 3280 3290 3300
GGLAESGARY TEMPHVIEIT LPMLCSYLPR WWERGPEAPP PALPAGAPPP
3310 3320 3330 3340 3350
CTAVTSDHLN SLLGNILRII VNNLGIDEAS WMKRLAVFAQ PIVSRARPEL
3360 3370 3380 3390 3400
LRSHFIPTIG RLRKRAGKVV AEEEQLRLEA KAEAEEGELL VRDEFSVLCR
3410 3420 3430 3440 3450
DLYALYPLLI RYVDNNRSAW PRLPPSPSSS FSLPSPSELG RWLMKDHGHQ
3460 3470 3480 3490 3500
LYEESFTVPL ILDNAAFPLA RNQSRAIGCA GVVRSGGSDQ ERTKKKRRGD
3510 3520 3530 3540 3550
RYSVQTSLIV ATLKKMLPIG LNMCAPTDQD LIVLAKARYA LKDTDEEVRE
3560 3570 3580 3590 3600
FLQNNLNLQG KVEGSPSLRW QMALYRGVPG REEDADDPEK IVRRVQEVSA
3610 3620 3630 3640 3650
VLYHLDQTEH PYKSKKAVWH KLLSKQRRRA VVACFRMTPL YNLPTHRACN
3660 3670 3680 3690 3700
MFLESYKASW ILTEDHSFED RMIDDLSKAG EQEEEEEEVE EKKPDPLHQL
3710 3720 3730 3740 3750
VLHFSRTALT EKSKLDEDYL YMAYADIMAK SCHLEEGGEN VEEGGEEEEV
3760 3770 3780 3790 3800
EVSFEEKEME KQRLLYQQSR LHNRGAAEMV LQMISACKGE TGAMVSSTLK
3810 3820 3830 3840 3850
LGISILNGGN AEVQQKMLDY LKDKKEVGFF QSIQALMQTC RWPHKTLSQR
3860 3870 3880 3890 3900
EGQEERVMKV QTSGTLVIIN RQNGEKVMAD DEFTQDLFRF LQLLCEGHNN
3910 3920 3930 3940 3950
DFQNYLRTQT GNTTTINIII CTVDYLLRLQ ESISDFYWYY SGKDVIEEQG
3960 3970 3980 3990 4000
KRNFSKAMSV AKQVFNSLTE YIQGPCTGNQ QSLAHSRLWD AVVGFLHVFA
4010 4020 4030 4040 4050
HMMMKLAQDS SQIELLKELL DLQKDMVVML LSLLEGNVVN GMIARQMVDM
4060 4070 4080 4090 4100
LVESSSNVEM ILKFFDMFLK LKDIVGSEAF QDYVTDPRGL ISKKDFQKAM
4110 4120 4130 4140 4150
DSQKQFTGPE IQFLLSCSEA DENEMINCEE FANRFQEPAR DIGFNVAVLL
4160 4170 4180 4190 4200
TNLSEHVPHD PRLRNFLELA ESILDYFRPY LGRIEIMGAS RRIERIYFEI
4210 4220 4230 4240 4250
SETNRAQWEM PQVKESKRQF IFDVVNEGGE SEKMELFVSF CEDTIFEMQI
4260 4270 4280 4290 4300
AAQISEPEGE PEEDDDEGAE EAEEGAAGPD GSGSAAAAGV WTWLATAAGR
4310 4320 4330 4340 4350
TLRGLSYRSL RRRVRRLRRL TAREAATAVA VLLWAMVARA GGAGAGAAAG
4360 4370 4380 4390 4400
VLRLLWGSLF GGGLVDSAKK VTVTELLAGM PDPTGDEVHG QQPSGAGSDA
4410 4420 4430 4440 4450
EGEGQGEGEG DAAEGVGDEE VAADQAGTGG ADRTVAVADG SPFRPEGAGG
4460 4470 4480 4490 4500
LGDMGDTTPV EPPTPEGSPI LKRKLGVDGE EEEPQPEPEP EPEPEPEKAD
4510 4520 4530 4540 4550
TENGEKEVPE PPPEPPKKAP PPPPPKKEEA GGAGLEEFWG ELEVQRVKFL
4560 4570 4580 4590 4600
NYLSRNFYTL RFLALFLAFA INFILLFYKV SDSPPGEDDI EGSGAGDMSG
4610 4620 4630 4640 4650
AGSGDGSGWG SRASEEVEGD EDENMVYYFL EESTGYMEPA LRCLSLLHTL
4660 4670 4680 4690 4700
VAFLCIIGYN CLKVPLVIFK REKELARKLE FDGLYITEQP EDDDVKGQWD
4710 4720 4730 4740 4750
RLVLNTPSFP SNYWDKFVKR KVLDKHGDIF GRERIAELLG MDLASLEITA
4760 4770 4780 4790 4800
HNERKPDPPP GLLTWIMSID VKYQIWKFGV IFTDNSFLYL GWYMVMSLLG
4810 4820 4830 4840 4850
HYNNFFFAAH LLDIAMGVKT LRTILSSVTH NGKQLVMTVG LLAVVVYLYT
4860 4870 4880 4890 4900
VVAFNFFRKF YNKSEDEDEP DMKCDDMMTC YLFHMYVGVR AGGGIGDEIE
4910 4920 4930 4940 4950
DPAGDEYELY RVVFDITFFF FVIVILLAII QGLIIDAFGE LRDQQEQVKE
4960 4970 4980 4990 5000
DMETKCFICG IGSDYFDTTP HGFETHTLEE HNLANYMFFL MYLINKDETE
5010 5020 5030
HTGQESYVWK MYQERCWDFF PAGDCFRKQY EDQLG
Length:5,035
Mass (Da):565,483
Last modified:May 3, 2011 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i51705805EDCAF5CB
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K5J1A0A0G2K5J1_RAT
Ryanodine receptor 1
Ryr1
5,012Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
V9GZ83V9GZ83_RAT
Ryanodine receptor 1
Ryr1
3,903Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti673A → V in AAD48899 (PubMed:10444400).Curated1
Sequence conflicti4728D → H in AAD31270 (Ref. 3) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF112256 mRNA Translation: AAD48899.1
AF130879 mRNA Translation: AAD31270.1
AF011788 mRNA Translation: AAB65756.1

Genome annotation databases

UCSC genome browser

More...
UCSCi
RGD:620313 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF112256 mRNA Translation: AAD48899.1
AF130879 mRNA Translation: AAD31270.1
AF011788 mRNA Translation: AAB65756.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

CORUMiF1LMY4
IntActiF1LMY4, 3 interactors
MINTiF1LMY4
STRINGi10116.ENSRNOP00000027893

PTM databases

CarbonylDBiF1LMY4
iPTMnetiF1LMY4
PhosphoSitePlusiF1LMY4

Proteomic databases

PaxDbiF1LMY4
PRIDEiF1LMY4

Genome annotation databases

UCSCiRGD:620313 rat

Organism-specific databases

RGDi1586637 Ryr1

Phylogenomic databases

eggNOGiKOG2243 Eukaryota
ENOG410YCNW LUCA
InParanoidiF1LMY4
TreeFamiTF315244

Enzyme and pathway databases

ReactomeiR-RNO-2672351 Stimuli-sensing channels
R-RNO-5578775 Ion homeostasis

Miscellaneous databases

Protein Ontology

More...
PROi
PR:F1LMY4

Family and domain databases

CDDicd12877 SPRY1_RyR, 1 hit
cd12878 SPRY2_RyR, 1 hit
cd12879 SPRY3_RyR, 1 hit
InterProiView protein in InterPro
IPR001870 B30.2/SPRY
IPR013320 ConA-like_dom_sf
IPR011992 EF-hand-dom_pair
IPR014821 Ins145_P3_rcpt
IPR005821 Ion_trans_dom
IPR036300 MIR_dom_sf
IPR016093 MIR_motif
IPR013662 RIH_assoc-dom
IPR000699 RIH_dom
IPR013333 Ryan_recept
IPR003032 Ryanodine_rcpt
IPR009460 Ryanrecept_TM4-6
IPR035910 RyR/IP3R_RIH_dom_sf
IPR033215 RyR1
IPR035761 SPRY1_RyR
IPR035764 SPRY2_RyR
IPR035762 SPRY3_RyR
IPR003877 SPRY_dom
PANTHERiPTHR13715:SF15 PTHR13715:SF15, 1 hit
PfamiView protein in Pfam
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
PRINTSiPR00795 RYANODINER
SMARTiView protein in SMART
SM00472 MIR, 4 hits
SM00449 SPRY, 3 hits
SUPFAMiSSF100909 SSF100909, 2 hits
SSF47473 SSF47473, 1 hit
SSF49899 SSF49899, 3 hits
SSF82109 SSF82109, 2 hits
PROSITEiView protein in PROSITE
PS50188 B302_SPRY, 3 hits
PS50919 MIR, 5 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRYR1_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: F1LMY4
Secondary accession number(s): O35208, Q9R1G1, Q9R272
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 22, 2012
Last sequence update: May 3, 2011
Last modified: February 26, 2020
This is version 75 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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