SELN_MOUSE
ID SELN_MOUSE Reviewed; 557 AA.
AC D3Z2R5;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2016, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Selenoprotein N {ECO:0000303|PubMed:21131290};
DE Short=SelN {ECO:0000303|PubMed:21131290};
DE Flags: Precursor;
GN Name=Selenon {ECO:0000312|MGI:MGI:2151208};
GN Synonyms=Seln {ECO:0000303|PubMed:21131290},
GN Sepn1 {ECO:0000312|MGI:MGI:2151208};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=21858002; DOI=10.1371/journal.pone.0023094;
RA Rederstorff M., Castets P., Arbogast S., Laine J., Vassilopoulos S.,
RA Beuvin M., Dubourg O., Vignaud A., Ferry A., Krol A., Allamand V.,
RA Guicheney P., Ferreiro A., Lescure A.;
RT "Increased muscle stress-sensitivity induced by selenoprotein N
RT inactivation in mouse: a mammalian model for SEPN1-related myopathy.";
RL PLoS ONE 6:E23094-E23094(2011).
RN [4]
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).
CC -!- FUNCTION: Plays an important role in cell protection against oxidative
CC stress and in the regulation of redox-related calcium homeostasis.
CC Regulates the calcium level of the ER by protecting the calcium pump
CC ATP2A2 against the oxidoreductase ERO1A-mediated oxidative damage.
CC Within the ER, ERO1A activity increases the concentration of H(2)O(2),
CC which attacks the luminal thiols in ATP2A2 and thus leads to cysteinyl
CC sulfenic acid formation (-SOH) and SEPN1 reduces the SOH back to free
CC thiol (-SH), thus restoring ATP2A2 activity (PubMed:25452428). Acts as
CC a modulator of ryanodine receptor (RyR) activity: protects RyR from
CC oxidation due to increased oxidative stress, or directly controls the
CC RyR redox state, regulating the RyR-mediated calcium mobilization
CC required for normal muscle development and differentiation (By
CC similarity). Essential for muscle regeneration and satellite cell
CC maintenance in skeletal muscle (PubMed:21131290).
CC {ECO:0000250|UniProtKB:Q9NZV5, ECO:0000269|PubMed:21131290,
CC ECO:0000269|PubMed:25452428}.
CC -!- SUBUNIT: Interacts with RYR1, RYR2 and RYR3.
CC {ECO:0000250|UniProtKB:Q9NZV5}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NZV5}.
CC -!- DOMAIN: The N-terminus (first 61 amino acids) contains an endoplasmic
CC reticulum addressing and retention targeting signal.
CC {ECO:0000250|UniProtKB:Q9NZV5}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9NZV5}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show only subtle alterations in the
CC muscle morphology, ultrastructure and contractility. They display
CC increased muscle stress-sensitivity to physical exercise when performed
CC under stress conditions such as a forced swimming test. Under these
CC conditions, they develop muscle atrophy, predominantly affecting trunk
CC muscles and leading to severe kyphosis (PubMed:21858002). The number of
CC satellite cells in uninjured adult muscle is reduced. After one single
CC cardiotoxin-induced injury, a correct restoration of the muscle fibers
CC is seen in skeletal muscle, whereas after two successive injuries,
CC regeneration is completely abolished (PubMed:21131290).
CC {ECO:0000269|PubMed:21131290, ECO:0000269|PubMed:21858002}.
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DR EMBL; AL669982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38917.1; -.
DR RefSeq; NP_083376.2; NM_029100.2.
DR IntAct; D3Z2R5; 1.
DR STRING; 10090.ENSMUSP00000060026; -.
DR GlyGen; D3Z2R5; 3 sites.
DR iPTMnet; D3Z2R5; -.
DR PhosphoSitePlus; D3Z2R5; -.
DR EPD; D3Z2R5; -.
DR jPOST; D3Z2R5; -.
DR PaxDb; D3Z2R5; -.
DR PeptideAtlas; D3Z2R5; -.
DR PRIDE; D3Z2R5; -.
DR ProteomicsDB; 257117; -.
DR Ensembl; ENSMUST00000060435; ENSMUSP00000060026; ENSMUSG00000050989.
DR GeneID; 74777; -.
DR KEGG; mmu:74777; -.
DR UCSC; uc008vfk.1; mouse.
DR CTD; 57190; -.
DR MGI; MGI:2151208; Selenon.
DR VEuPathDB; HostDB:ENSMUSG00000050989; -.
DR eggNOG; ENOG502QREI; Eukaryota.
DR GeneTree; ENSGT00390000005972; -.
DR HOGENOM; CLU_042746_1_0_1; -.
DR InParanoid; D3Z2R5; -.
DR OMA; FEEITWQ; -.
DR OrthoDB; 817333at2759; -.
DR PhylomeDB; D3Z2R5; -.
DR TreeFam; TF329622; -.
DR BioGRID-ORCS; 74777; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Selenon; mouse.
DR PRO; PR:D3Z2R5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; D3Z2R5; protein.
DR Bgee; ENSMUSG00000050989; Expressed in granulocyte and 225 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO: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; ISS:UniProtKB.
DR GO; GO:0071313; P:cellular response to caffeine; IMP:MGI.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:MGI.
DR GO; GO:0048286; P:lung alveolus development; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0033555; P:multicellular organismal response to stress; IMP:MGI.
DR GO; GO:1902884; P:positive regulation of response to oxidative stress; ISS:UniProtKB.
DR GO; GO:0014858; P:positive regulation of skeletal muscle cell proliferation; IDA:MGI.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0003016; P:respiratory system process; IMP:MGI.
DR GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; IMP:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR GO; GO:0014816; P:skeletal muscle satellite cell differentiation; IMP:MGI.
DR GO; GO:0014834; P:skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration; IMP:UniProtKB.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:MGI.
DR InterPro; IPR002048; EF_hand_dom.
DR PROSITE; PS50222; EF_HAND_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Oxidoreductase;
KW Reference proteome; Repeat; Selenocysteine; Signal.
FT SIGNAL 1..42
FT /evidence="ECO:0000255"
FT CHAIN 43..557
FT /note="Selenoprotein N"
FT /id="PRO_0000436040"
FT DOMAIN 67..102
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 428
FT /note="Selenocysteine"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 557 AA; 62492 MW; D085928963DE8257 CRC64;
MGQARPAARR PHSPDPGAQP APPRRRARAL ALLGALLAAA AAVAAARACA LLADAQAAAR
QESALKVLGT DGLFLFSSLD TDQDMYISPE EFKPIAEKLT GSVPVANYEE EELPHDPSEE
TLTIEARFQP LLMETMTKSK DGFLGVSRLA LSGLRNWTTA ASPSAAFAAR HFRPFLPPPG
QELGQPWWII PGELSVFTGY LSNNRFYPPP PKGKEVIIHR LLSMFHPRPF VKTRFAPQGT
VACLTAISDS YYTVMFRIHA EFQLSEPPDF PFWFSPGQFT GHIILSKDAT HIRDFRLFVP
NHRSLNVDME WLYGASETSN MEVDIGYVPQ MELEAVGPSV PSVILDEDGN MIDSRLPSGE
PLQFVFEEIK WHQELSWEEA ARRLEVAMYP FKKVNYLPFT EAFDRARAEK KLVHSILLWG
ALDDQSCUGS GRTLRETVLE SPPILTLLNE SFISTWSLVK ELEDLQTQQE NPLHRQLAGL
HLEKYSFPVE MMICLPNGTV VHHINANYFL DITSMKPEDM ENNNVFSFSS SFEDPSTATY
MQFLREGLRR GLPLLQP
