ID SELN_HUMAN Reviewed; 590 AA. AC Q9NZV5; A6NJG8; A8MQ64; Q6PI70; Q969F6; Q9NUI6; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2011, sequence version 5. DT 27-MAR-2024, entry version 181. DE RecName: Full=Selenoprotein N {ECO:0000303|PubMed:27645994}; DE Short=SelN {ECO:0000303|PubMed:27645994}; DE Flags: Precursor; GN Name=SELENON {ECO:0000303|PubMed:27645994, GN ECO:0000312|HGNC:HGNC:15999}; GN Synonyms=SELN {ECO:0000303|PubMed:27645994}, SEPN1 GN {ECO:0000303|PubMed:11528383, ECO:0000312|HGNC:HGNC:15999}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANTS CMYP3 RP GLU-273; ARG-293 AND GLN-466, VARIANTS TYR-142 AND LYS-502, AND TISSUE RP SPECIFICITY. RX PubMed=11528383; DOI=10.1038/ng713; RA Moghadaszadeh B., Petit N., Jaillard C., Brockington M., Roy S.Q., RA Merlini L., Romero N., Estournet B., Desguerre I., Chaigne D., Muntoni F., RA Topaloglu H., Guicheney P.; RT "Mutations in SEPN1 cause congenital muscular dystrophy with spinal RT rigidity and restrictive respiratory syndrome."; RL Nat. Genet. 29:17-18(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 86-590 (ISOFORM 2), AND VARIANT LYS-502. RX PubMed=10608886; DOI=10.1074/jbc.274.53.38147; RA Lescure A., Gautheret D., Carbon P., Krol A.; RT "Novel selenoproteins identified in silico and in vivo by using a conserved RT RNA structural motif."; RL J. Biol. Chem. 274:38147-38154(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 428-590 (ISOFORMS 1/2), AND RP VARIANT LYS-502. RC TISSUE=Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP SUBCELLULAR LOCATION (ISOFORM 2), TISSUE SPECIFICITY (ISOFORM 2), RP GLYCOSYLATION (ISOFORM 2), AND DOMAIN (ISOFORM 2). RX PubMed=12700173; DOI=10.1093/hmg/ddg115; RA Petit N., Lescure A., Rederstorff M., Krol A., Moghadaszadeh B., RA Wewer U.M., Guicheney P.; RT "Selenoprotein N: an endoplasmic reticulum glycoprotein with an early RT developmental expression pattern."; RL Hum. Mol. Genet. 12:1045-1053(2003). RN [6] RP INVOLVEMENT IN CMYP3, AND VARIANT CMYP3 SER-315. RX PubMed=16365872; DOI=10.1002/ana.20761; RA Clarke N.F., Kidson W., Quijano-Roy S., Estournet B., Ferreiro A., RA Guicheney P., Manson J.I., Kornberg A.J., Shield L.K., North K.N.; RT "SEPN1: associated with congenital fiber-type disproportion and insulin RT resistance."; RL Ann. Neurol. 59:546-552(2006). RN [7] RP FUNCTION (ISOFORM 2), INTERACTION WITH RYR1; RYR2 AND RYR3 (ISOFORM 2), AND RP CHARACTERIZATION OF VARIANT CMYP3 GLN-466. RX PubMed=18713863; DOI=10.1073/pnas.0806015105; RA Jurynec M.J., Xia R., Mackrill J.J., Gunther D., Crawford T., RA Flanigan K.M., Abramson J.J., Howard M.T., Grunwald D.J.; RT "Selenoprotein N is required for ryanodine receptor calcium release channel RT activity in human and zebrafish muscle."; RL Proc. Natl. Acad. Sci. U.S.A. 105:12485-12490(2008). RN [8] RP FUNCTION (ISOFORM 2). RX PubMed=19557870; DOI=10.1002/ana.21644; RA Arbogast S., Beuvin M., Fraysse B., Zhou H., Muntoni F., Ferreiro A.; RT "Oxidative stress in SEPN1-related myopathy: from pathophysiology to RT treatment."; RL Ann. Neurol. 65:677-686(2009). RN [9] RP REVIEW. RX PubMed=19769461; DOI=10.1089/ars.2009.2890; RA Arbogast S., Ferreiro A.; RT "Selenoproteins and protection against oxidative stress: selenoprotein N as RT a novel player at the crossroads of redox signaling and calcium RT homeostasis."; RL Antioxid. Redox Signal. 12:893-904(2010). RN [10] RP FUNCTION. RX PubMed=21131290; DOI=10.1093/hmg/ddq515; RA Castets P., Bertrand A.T., Beuvin M., Ferry A., Le Grand F., Castets M., RA Chazot G., Rederstorff M., Krol A., Lescure A., Romero N.B., Guicheney P., RA Allamand V.; RT "Satellite cell loss and impaired muscle regeneration in selenoprotein N RT deficiency."; RL Hum. Mol. Genet. 20:694-704(2011). RN [11] RP REVIEW. RX PubMed=22527882; DOI=10.1007/s00109-012-0896-x; RA Castets P., Lescure A., Guicheney P., Allamand V.; RT "Selenoprotein N in skeletal muscle: from diseases to function."; RL J. Mol. Med. 90:1095-1107(2012). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] RP FUNCTION. RX PubMed=25452428; DOI=10.1093/hmg/ddu602; RA Marino M., Stoilova T., Giorgi C., Bachi A., Cattaneo A., Auricchio A., RA Pinton P., Zito E.; RT "SEPN1, an endoplasmic reticulum-localized selenoprotein linked to skeletal RT muscle pathology, counteracts hyperoxidation by means of redox-regulating RT SERCA2 pump activity."; RL Hum. Mol. Genet. 24:1843-1855(2015). RN [14] RP NOMENCLATURE. RX PubMed=27645994; DOI=10.1074/jbc.m116.756155; RA Gladyshev V.N., Arner E.S., Berry M.J., Brigelius-Flohe R., Bruford E.A., RA Burk R.F., Carlson B.A., Castellano S., Chavatte L., Conrad M., RA Copeland P.R., Diamond A.M., Driscoll D.M., Ferreiro A., Flohe L., RA Green F.R., Guigo R., Handy D.E., Hatfield D.L., Hesketh J., Hoffmann P.R., RA Holmgren A., Hondal R.J., Howard M.T., Huang K., Kim H.Y., Kim I.Y., RA Koehrle J., Krol A., Kryukov G.V., Lee B.J., Lee B.C., Lei X.G., Liu Q., RA Lescure A., Lobanov A.V., Loscalzo J., Maiorino M., Mariotti M., RA Sandeep Prabhu K., Rayman M.P., Rozovsky S., Salinas G., Schmidt E.E., RA Schomburg L., Schweizer U., Simonovic M., Sunde R.A., Tsuji P.A., RA Tweedie S., Ursini F., Whanger P.D., Zhang Y.; RT "Selenoprotein gene nomenclature."; RL J. Biol. Chem. 291:24036-24040(2016). RN [15] RP VARIANTS CMYP3 ARG-293; SER-315; ILE-340; SER-453; GLY-462 AND GLN-466. RX PubMed=12192640; DOI=10.1086/342719; RA Ferreiro A., Quijano-Roy S., Pichereau C., Moghadaszadeh B., Goemans N., RA Boennemann C., Jungbluth H., Straub V., Villanova M., Leroy J.-P., RA Romero N.B., Martin J.-J., Muntoni F., Voit T., Estournet B., Richard P., RA Fardeau M., Guicheney P.; RT "Mutations of the selenoprotein N gene, which is implicated in rigid spine RT muscular dystrophy, cause the classical phenotype of multiminicore disease: RT reassessing the nosology of early-onset myopathies."; RL Am. J. Hum. Genet. 71:739-749(2002). RN [16] RP VARIANT CMYP3 SER-315. RX PubMed=15122708; DOI=10.1002/ana.20077; RA Ferreiro A., Ceuterick-de Groote C., Marks J.J., Goemans N., Schreiber G., RA Hanefeld F., Fardeau M., Martin J.-J., Goebel H.H., Richard P., RA Guicheney P., Bonnemann C.G.; RT "Desmin-related myopathy with Mallory body-like inclusions is caused by RT mutations of the selenoprotein N gene."; RL Ann. Neurol. 55:676-686(2004). RN [17] RP VARIANT CMYP3 SER-315. RX PubMed=15668457; DOI=10.1212/01.wnl.0000149755.85666.db; RA Venance S.L., Koopman W.J., Miskie B.A., Hegele R.A., Hahn A.F.; RT "Rigid spine muscular dystrophy due to SEPN1 mutation presenting as cor RT pulmonale."; RL Neurology 64:395-396(2005). RN [18] RP VARIANTS CMYP3 VAL-463; GLN-466; GLN-469 AND TRP-469. RX PubMed=19067361; DOI=10.1002/humu.20879; RA Maiti B., Arbogast S., Allamand V., Moyle M.W., Anderson C.B., Richard P., RA Guicheney P., Ferreiro A., Flanigan K.M., Howard M.T.; RT "A mutation in the SEPN1 selenocysteine redefinition element (SRE) reduces RT selenocysteine incorporation and leads to SEPN1-related myopathy."; RL Hum. Mutat. 30:411-416(2009). CC -!- FUNCTION: [Isoform 2]: Plays an important role in cell protection CC against oxidative stress and in the regulation of redox-related calcium CC homeostasis. Regulates the calcium level of the ER by protecting the CC calcium pump ATP2A2 against the oxidoreductase ERO1A-mediated oxidative CC damage. Within the ER, ERO1A activity increases the concentration of CC H(2)O(2), which attacks the luminal thiols in ATP2A2 and thus leads to CC cysteinyl sulfenic acid formation (-SOH) and SEPN1 reduces the SOH back CC to free thiol (-SH), thus restoring ATP2A2 activity (PubMed:25452428). CC Acts as a modulator of ryanodine receptor (RyR) activity: protects RyR CC from oxidation due to increased oxidative stress, or directly controls CC the RyR redox state, regulating the RyR-mediated calcium mobilization CC required for normal muscle development and differentiation CC (PubMed:19557870, PubMed:18713863). {ECO:0000269|PubMed:18713863, CC ECO:0000269|PubMed:19557870, ECO:0000269|PubMed:25452428}. CC -!- FUNCTION: Essential for muscle regeneration and satellite cell CC maintenance in skeletal muscle (PubMed:21131290). CC {ECO:0000269|PubMed:21131290}. CC -!- SUBUNIT: [Isoform 2]: Interacts with RYR1, RYR2 and RYR3 CC (PubMed:18713863). {ECO:0000269|PubMed:18713863}. CC -!- INTERACTION: CC Q9NZV5; P16333: NCK1; NbExp=2; IntAct=EBI-1751965, EBI-389883; CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:12700173}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NZV5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NZV5-2; Sequence=VSP_011372; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 2 are expressed in skeletal CC muscle, brain, lung and placenta. Isoform 2 is also expressed in heart, CC diaphragm and stomach. {ECO:0000269|PubMed:11528383, CC ECO:0000269|PubMed:12700173}. CC -!- DOMAIN: [Isoform 2]: The N-terminus (first 61 amino acids) contains an CC endoplasmic reticulum addressing and retention targeting signal. CC {ECO:0000269|PubMed:12700173}. CC -!- PTM: [Isoform 2]: N-glycosylated. {ECO:0000269|PubMed:12700173}. CC -!- DISEASE: Congenital myopathy 3 with rigid spine (CMYP3) [MIM:602771]: CC An autosomal recessive, slowly progressive muscular disorder apparent CC from birth or early childhood and characterized by hypotonia, proximal CC muscle weakness, poor axial muscle strength, scoliosis and neck CC weakness, and a variable degree of spinal rigidity. Most patients CC remain ambulatory. Early ventilatory insufficiency may lead to death by CC respiratory failure. Additional features may include facial muscle CC weakness, amyotrophy, joint contractures, distal hyperlaxity, pulmonary CC hypertension with secondary cardiac dysfunction, and insulin resistance CC in patients with a low BMI. Skeletal muscle biopsy typically shows CC multiminicores and other abnormal non-specific myopathic findings. CC {ECO:0000269|PubMed:11528383, ECO:0000269|PubMed:12192640, CC ECO:0000269|PubMed:15122708, ECO:0000269|PubMed:15668457, CC ECO:0000269|PubMed:16365872, ECO:0000269|PubMed:18713863, CC ECO:0000269|PubMed:19067361}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 1]: The UGA codons present in position 127 and CC 462 are either a selenocysteine or a real stop codon. CC -!- MISCELLANEOUS: [Isoform 2]: The UGA codon present in position 428 is CC either a selenocysteine or a real stop codon. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH15638.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH42154.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ306399; CAC83791.1; -; mRNA. DR EMBL; AJ306398; CAC83790.1; -; Genomic_DNA. DR EMBL; AL020996; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF166125; AAF21430.1; -; mRNA. DR EMBL; BC015638; AAH15638.1; ALT_INIT; mRNA. DR EMBL; BC042154; AAH42154.1; ALT_INIT; mRNA. DR CCDS; CCDS41282.1; -. [Q9NZV5-1] DR CCDS; CCDS41283.1; -. [Q9NZV5-2] DR RefSeq; NP_065184.2; NM_020451.2. [Q9NZV5-1] DR RefSeq; NP_996809.1; NM_206926.1. [Q9NZV5-2] DR BioGRID; 121439; 96. DR IntAct; Q9NZV5; 18. DR MINT; Q9NZV5; -. DR STRING; 9606.ENSP00000355141; -. DR GlyCosmos; Q9NZV5; 6 sites, 1 glycan. DR GlyGen; Q9NZV5; 6 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q9NZV5; -. DR PhosphoSitePlus; Q9NZV5; -. DR BioMuta; SELENON; -. DR DMDM; 317373588; -. DR EPD; Q9NZV5; -. DR jPOST; Q9NZV5; -. DR MassIVE; Q9NZV5; -. DR MaxQB; Q9NZV5; -. DR PaxDb; 9606-ENSP00000355141; -. DR PeptideAtlas; Q9NZV5; -. DR ProteomicsDB; 83517; -. [Q9NZV5-1] DR ProteomicsDB; 83518; -. [Q9NZV5-2] DR Pumba; Q9NZV5; -. DR Antibodypedia; 56475; 166 antibodies from 19 providers. DR DNASU; 57190; -. DR Ensembl; ENST00000361547.7; ENSP00000355141.2; ENSG00000162430.18. [Q9NZV5-1] DR Ensembl; ENST00000374315.1; ENSP00000363434.1; ENSG00000162430.18. [Q9NZV5-2] DR GeneID; 57190; -. DR KEGG; hsa:57190; -. DR MANE-Select; ENST00000361547.7; ENSP00000355141.2; NM_020451.3; NP_065184.2. DR UCSC; uc021ojk.2; human. [Q9NZV5-1] DR AGR; HGNC:15999; -. DR CTD; 57190; -. DR DisGeNET; 57190; -. DR GeneCards; SELENON; -. DR HGNC; HGNC:15999; SELENON. DR HPA; ENSG00000162430; Low tissue specificity. DR MalaCards; SELENON; -. DR MIM; 602771; phenotype. DR MIM; 606210; gene. DR neXtProt; NX_Q9NZV5; -. DR OpenTargets; ENSG00000162430; -. DR Orphanet; 324604; Classic multiminicore myopathy. DR Orphanet; 2020; Congenital fiber-type disproportion myopathy. DR Orphanet; 84132; Desmin-related myopathy with Mallory body-like inclusions. DR Orphanet; 97244; Rigid spine syndrome. DR PharmGKB; PA38079; -. DR VEuPathDB; HostDB:ENSG00000162430; -. DR eggNOG; ENOG502QREI; Eukaryota. DR GeneTree; ENSGT00390000005972; -. DR HOGENOM; CLU_042746_1_0_1; -. DR InParanoid; Q9NZV5; -. DR OMA; EITWQQE; -. DR OrthoDB; 4625592at2759; -. DR PhylomeDB; Q9NZV5; -. DR TreeFam; TF329622; -. DR PathwayCommons; Q9NZV5; -. DR SignaLink; Q9NZV5; -. DR BioGRID-ORCS; 57190; 6 hits in 1152 CRISPR screens. DR ChiTaRS; SELENON; human. DR GeneWiki; SEPN1; -. DR GenomeRNAi; 57190; -. DR Pharos; Q9NZV5; Tbio. DR PRO; PR:Q9NZV5; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9NZV5; Protein. DR Bgee; ENSG00000162430; Expressed in stromal cell of endometrium and 175 other cell types or tissues. DR ExpressionAtlas; Q9NZV5; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0055074; P:calcium ion homeostasis; IMP:UniProtKB. DR GO; GO:0071313; P:cellular response to caffeine; IEA:Ensembl. DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl. DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl. DR GO; GO:0007005; P:mitochondrion organization; IEA:Ensembl. DR GO; GO:0033555; P:multicellular organismal response to stress; IEA:Ensembl. DR GO; GO:1902884; P:positive regulation of response to oxidative stress; IMP:UniProtKB. DR GO; GO:0014858; P:positive regulation of skeletal muscle cell proliferation; IEA:Ensembl. DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:UniProtKB. DR GO; GO:0003016; P:respiratory system process; IEA:Ensembl. DR GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; IEA:Ensembl. DR GO; GO:0048741; P:skeletal muscle fiber development; IBA:GO_Central. DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IEA:Ensembl. DR GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; IEA:Ensembl. DR InterPro; IPR002048; EF_hand_dom. DR PANTHER; PTHR16213:SF78; SELENOPROTEIN N; 1. DR PANTHER; PTHR16213; UNCHARACTERIZED; 1. DR PROSITE; PS50222; EF_HAND_2; 1. DR Genevisible; Q9NZV5; HS. PE 1: Evidence at protein level; KW Alternative splicing; Desmin-related myopathy; Disease variant; KW Endoplasmic reticulum; Glycoprotein; Membrane; Myofibrillar myopathy; KW Oxidoreductase; Reference proteome; Selenocysteine; Signal. FT SIGNAL 1..43 FT /evidence="ECO:0000255" FT CHAIN 44..590 FT /note="Selenoprotein N" FT /id="PRO_0000022311" FT DOMAIN 67..102 FT /note="EF-hand" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 9..23 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_STD 127 FT /note="Selenocysteine" FT NON_STD 462 FT /note="Selenocysteine" FT CARBOHYD 126 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 190 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 483 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 505 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 531 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 102..135 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10608886" FT /id="VSP_011372" FT VARIANT 137 FT /note="T -> A (in dbSNP:rs35019869)" FT /id="VAR_038845" FT VARIANT 142 FT /note="C -> Y (in dbSNP:rs7349185)" FT /evidence="ECO:0000269|PubMed:11528383" FT /id="VAR_038846" FT VARIANT 273 FT /note="G -> E (in CMYP3; dbSNP:rs121908182)" FT /evidence="ECO:0000269|PubMed:11528383" FT /id="VAR_019635" FT VARIANT 293 FT /note="H -> R (in CMYP3; dbSNP:rs776738184)" FT /evidence="ECO:0000269|PubMed:11528383, FT ECO:0000269|PubMed:12192640" FT /id="VAR_019636" FT VARIANT 315 FT /note="G -> S (in CMYP3; dbSNP:rs121908188)" FT /evidence="ECO:0000269|PubMed:12192640, FT ECO:0000269|PubMed:15122708, ECO:0000269|PubMed:15668457, FT ECO:0000269|PubMed:16365872" FT /id="VAR_019637" FT VARIANT 340 FT /note="N -> I (in CMYP3; dbSNP:rs749911126)" FT /evidence="ECO:0000269|PubMed:12192640" FT /id="VAR_019638" FT VARIANT 453 FT /note="W -> S (in CMYP3; dbSNP:rs121908186)" FT /evidence="ECO:0000269|PubMed:12192640" FT /id="VAR_019639" FT VARIANT 462 FT /note="U -> G (in CMYP3; dbSNP:rs121908187)" FT /evidence="ECO:0000269|PubMed:12192640" FT /id="VAR_019640" FT VARIANT 463 FT /note="G -> V (in CMYP3)" FT /evidence="ECO:0000269|PubMed:19067361" FT /id="VAR_058462" FT VARIANT 466 FT /note="R -> Q (in CMYP3; decreased function in the FT regulation of ryanodine receptor activity; FT dbSNP:rs121908185)" FT /evidence="ECO:0000269|PubMed:11528383, FT ECO:0000269|PubMed:12192640, ECO:0000269|PubMed:18713863, FT ECO:0000269|PubMed:19067361" FT /id="VAR_019641" FT VARIANT 469 FT /note="R -> Q (in CMYP3; dbSNP:rs779162837)" FT /evidence="ECO:0000269|PubMed:19067361" FT /id="VAR_058463" FT VARIANT 469 FT /note="R -> W (in CMYP3; dbSNP:rs756927098)" FT /evidence="ECO:0000269|PubMed:19067361" FT /id="VAR_058464" FT VARIANT 502 FT /note="N -> K (in dbSNP:rs2294228)" FT /evidence="ECO:0000269|PubMed:10608886, FT ECO:0000269|PubMed:11528383, ECO:0000269|PubMed:15489334" FT /id="VAR_038847" FT CONFLICT 247 FT /note="G -> S (in Ref. 3; AAF21430)" FT /evidence="ECO:0000305" SQ SEQUENCE 590 AA; 65813 MW; D7D4D6331652C359 CRC64; MGRARPGQRG PPSPGPAAQP PAPPRRRARS LALLGALLAA AAAAAVRVCA RHAEAQAAAR QELALKTLGT DGLFLFSSLD TDGDMYISPE EFKPIAEKLT GSCSVTQTGV QWCSHSSLQP QLPWLNUSSC LSLLRSTPAA SCEEEELPPD PSEETLTIEA RFQPLLPETM TKSKDGFLGV SRLALSGLRN WTAAASPSAV FATRHFQPFL PPPGQELGEP WWIIPSELSM FTGYLSNNRF YPPPPKGKEV IIHRLLSMFH PRPFVKTRFA PQGAVACLTA ISDFYYTVMF RIHAEFQLSE PPDFPFWFSP AQFTGHIILS KDATHVRDFR LFVPNHRSLN VDMEWLYGAS ESSNMEVDIG YIPQMELEAT GPSVPSVILD EDGSMIDSHL PSGEPLQFVF EEIKWQQELS WEEAARRLEV AMYPFKKVSY LPFTEAFDRA KAENKLVHSI LLWGALDDQS CUGSGRTLRE TVLESSPILT LLNESFISTW SLVKELEELQ NNQENSSHQK LAGLHLEKYS FPVEMMICLP NGTVVHHINA NYFLDITSVK PEEIESNLFS FSSTFEDPST ATYMQFLKEG LRRGLPLLQP //