SELN_HUMAN
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 03-AUG-2022, entry version 172.
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, ECO:0000312|HGNC:HGNC:15999};
GN Synonyms=SELN {ECO:0000303|PubMed:27645994},
GN SEPN1 {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 RSMD1
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 CFTD, AND VARIANT CFTD 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 RSMD1 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 RSMD1 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 RSMD1 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 RSMD1 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 RSMD1 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: Rigid spine muscular dystrophy 1 (RSMD1) [MIM:602771]: A
CC neuromuscular disorder characterized by poor axial muscle strength,
CC scoliosis and neck weakness, and a variable degree of spinal rigidity.
CC Early ventilatory insufficiency can lead to death by respiratory
CC failure. {ECO:0000269|PubMed:11528383, ECO:0000269|PubMed:12192640,
CC ECO:0000269|PubMed:15122708, ECO:0000269|PubMed:15668457,
CC ECO:0000269|PubMed:18713863, ECO:0000269|PubMed:19067361}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Myopathy, congenital, with fiber-type disproportion (CFTD)
CC [MIM:255310]: A genetically heterogeneous disorder in which there is
CC relative hypotrophy of type 1 muscle fibers compared to type 2 fibers
CC on skeletal muscle biopsy. However, these findings are not specific and
CC can be found in many different myopathic and neuropathic conditions.
CC {ECO:0000269|PubMed:16365872}. 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; 92.
DR IntAct; Q9NZV5; 18.
DR MINT; Q9NZV5; -.
DR STRING; 9606.ENSP00000355141; -.
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; Q9NZV5; -.
DR PeptideAtlas; Q9NZV5; -.
DR PRIDE; Q9NZV5; -.
DR ProteomicsDB; 83517; -. [Q9NZV5-1]
DR ProteomicsDB; 83518; -. [Q9NZV5-2]
DR Antibodypedia; 56475; 144 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 CTD; 57190; -.
DR DisGeNET; 57190; -.
DR GeneCards; SELENON; -.
DR HGNC; HGNC:15999; SELENON.
DR HPA; ENSG00000162430; Low tissue specificity.
DR MalaCards; SELENON; -.
DR MIM; 255310; phenotype.
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; FEEITWQ; -.
DR OrthoDB; 929408at2759; -.
DR PhylomeDB; Q9NZV5; -.
DR TreeFam; TF329622; -.
DR PathwayCommons; Q9NZV5; -.
DR SignaLink; Q9NZV5; -.
DR BioGRID-ORCS; 57190; 6 hits in 1074 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 173 other tissues.
DR ExpressionAtlas; Q9NZV5; baseline and differential.
DR Genevisible; Q9NZV5; HS.
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 PROSITE; PS50222; EF_HAND_2; 1.
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 RSMD1; dbSNP:rs121908182)"
FT /evidence="ECO:0000269|PubMed:11528383"
FT /id="VAR_019635"
FT VARIANT 293
FT /note="H -> R (in RSMD1; 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 RSMD1 and CFTD; 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 RSMD1; dbSNP:rs749911126)"
FT /evidence="ECO:0000269|PubMed:12192640"
FT /id="VAR_019638"
FT VARIANT 453
FT /note="W -> S (in RSMD1; dbSNP:rs121908186)"
FT /evidence="ECO:0000269|PubMed:12192640"
FT /id="VAR_019639"
FT VARIANT 462
FT /note="U -> G (in RSMD1; dbSNP:rs121908187)"
FT /evidence="ECO:0000269|PubMed:12192640"
FT /id="VAR_019640"
FT VARIANT 463
FT /note="G -> V (in RSMD1)"
FT /evidence="ECO:0000269|PubMed:19067361"
FT /id="VAR_058462"
FT VARIANT 466
FT /note="R -> Q (in RSMD1; 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 RSMD1; dbSNP:rs779162837)"
FT /evidence="ECO:0000269|PubMed:19067361"
FT /id="VAR_058463"
FT VARIANT 469
FT /note="R -> W (in RSMD1; 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
