SELN_DANRE
ID SELN_DANRE Reviewed; 557 AA.
AC Q3Y4E2; A9JT95; Q66L54; Q802F4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Selenoprotein N {ECO:0000303|PubMed:12915322};
DE Short=SePN {ECO:0000303|PubMed:12915322};
DE Short=SelN {ECO:0000250|UniProtKB:Q9NZV5};
GN Name=selenon {ECO:0000250|UniProtKB:Q9NZV5};
GN Synonyms=sepn {ECO:0000303|PubMed:12915322},
GN sepn1 {ECO:0000303|PubMed:17123513};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AB;
RA Jurynec M.J., Howard M.T., Grunwald D.J.;
RT "Zebrafish selenoprotein N.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-557, AND DEVELOPMENTAL STAGE.
RX PubMed=12915322; DOI=10.1016/s1567-133x(03)00054-1;
RA Thisse C., Degrave A., Kryukov G.V., Gladyshev V.N., Obrecht-Pflumio S.,
RA Krol A., Thisse B., Lescure A.;
RT "Spatial and temporal expression patterns of selenoprotein genes during
RT embryogenesis in zebrafish.";
RL Gene Expr. Patterns 3:525-532(2003).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17123513; DOI=10.1016/j.yexcr.2006.10.005;
RA Deniziak M., Thisse C., Rederstorff M., Hindelang C., Thisse B.,
RA Lescure A.;
RT "Loss of selenoprotein N function causes disruption of muscle architecture
RT in the zebrafish embryo.";
RL Exp. Cell Res. 313:156-167(2007).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RYR3.
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).
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 (By
CC similarity). Acts as a modulator of ryanodine receptor (RyR) activity:
CC protects RyR from oxidation due to increased oxidative stress, or
CC directly controls the RyR redox state, regulating the RyR-mediated
CC calcium mobilization required for normal muscle development and
CC differentiation (PubMed:18713863). Plays an important role in muscle
CC development and differentiation during early development. Required for
CC development of the slow muscle fiber lineage (PubMed:18713863).
CC Required for the correct organization and attachment of the myofibrils,
CC as well as for the continuity and integrity of the connective tissue
CC that forms the myoseptum (PubMed:17123513).
CC {ECO:0000250|UniProtKB:Q9NZV5, ECO:0000269|PubMed:17123513,
CC ECO:0000269|PubMed:18713863}.
CC -!- SUBUNIT: Interacts with ryr3. {ECO:0000269|PubMed:18713863}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9NZV5}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the anteroposterior axis and the
CC notochord at 5 hours post-fertilization (hpf). Expressed in the eye
CC inner cell layer of the retina at 48 hpf (PubMed:12915322). In the
CC embryo expressed at high levels in the notochord, the tailbud, the
CC presomitic mesoderm and the emerging somites. As the notochord and
CC somitic muscle differentiate overtly, expression in these tissues is
CC greatly reduced (PubMed:18713863). {ECO:0000269|PubMed:12915322,
CC ECO:0000269|PubMed:18713863}.
CC -!- DISRUPTION PHENOTYPE: Emrbyos show disruption of muscle architecture
CC and greatly reduced motility. Embryonic muscle tissue display
CC disorganization of the sarcomere and myofiber attachment defects
CC (PubMed:17123513). Embryos show a defect in the generation and
CC development of slow muscle fibers and a decrease in the expression of
CC myogenic lineage genes in slow muscle cell precursors
CC (PubMed:18713863). {ECO:0000269|PubMed:17123513,
CC ECO:0000269|PubMed:18713863}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO65271.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ160295; AAZ80054.1; -; mRNA.
DR EMBL; BC078430; AAH78430.1; -; mRNA.
DR EMBL; BC155254; AAI55255.1; -; mRNA.
DR EMBL; AY221262; AAO65271.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001004294.4; NM_001004294.4.
DR DIP; DIP-46265N; -.
DR STRING; 7955.ENSDARP00000119529; -.
DR PaxDb; Q3Y4E2; -.
DR GeneID; 352914; -.
DR KEGG; dre:352914; -.
DR CTD; 57190; -.
DR ZFIN; ZDB-GENE-030327-7; selenon.
DR eggNOG; ENOG502QREI; Eukaryota.
DR InParanoid; Q3Y4E2; -.
DR OrthoDB; 817333at2759; -.
DR PhylomeDB; Q3Y4E2; -.
DR PRO; PR:Q3Y4E2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0055074; P:calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:UniProtKB.
DR GO; GO:0055001; P:muscle cell development; IMP:UniProtKB.
DR GO; GO:0060537; P:muscle tissue development; IMP:UniProtKB.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IMP:UniProtKB.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:ZFIN.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Membrane; Oxidoreductase;
KW Reference proteome; Selenocysteine; Transmembrane; Transmembrane helix.
FT CHAIN 1..557
FT /note="Selenoprotein N"
FT /id="PRO_0000318633"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 430
FT /note="Selenocysteine"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 28
FT /note="G -> A (in Ref. 2; AAH78430)"
FT /evidence="ECO:0000305"
FT CONFLICT 29
FT /note="R -> C (in Ref. 2; AAH78430)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="G -> S (in Ref. 2; AAH78430)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="V -> F (in Ref. 2; AAH78430)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="D -> N (in Ref. 2; AAH78430)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="S -> P (in Ref. 2; AAH78430)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="P -> S (in Ref. 2; AAI55255)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="H -> R (in Ref. 2; AAI55255)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="D -> Y (in Ref. 2; AAH78430)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="S -> L (in Ref. 1; AAZ80054)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="R -> K (in Ref. 1; AAZ80054)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="S -> L (in Ref. 1; AAZ80054)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="V -> L (in Ref. 3; AAO65271)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 62624 MW; CBCC9CB45C74B46B CRC64;
MAADVDKTPA GEQKDDHEDR GTPSSRRGRS RFTQISSLFI IAAIPVIGVC IKYYLDIQFV
KRHEAGLKAL GADGLFFFSS LDTDHDLYLS PEEFKPIAEK LTGVAPPPEY EEEIPHDPNG
ETLTLHAKMQ PLLLESMTKS KDGFLGVSHS SLSGLRSWKR PAISSSTFYA SQFKVFLPPS
GKSAVGDTWW IIPSELNIFT GYLPNNRFHP PTPRGKEVLI HSLLSMFHPR PFVKSRFAPQ
GAVACIRATS DFYYDIVFRI HAEFQLNDVP DFPFWFTPGQ FAGHIILSKD ASHVRDFHIY
VPNDKTLNVD MEWLYGASET SNMEVDIGYL PQMELGAEGP STPSVIYDEQ GNMIDSRGEG
GEPIQFVFEE IVWSEELRRE EASRRLEVTM YPFKKVPYLP FSEAFSRASA EKKLVHSILL
WGALDDQSCU GSGRTLRETV LESSPVLALL NQSFISSWSL VKELEDLQGD VKNVELSEKA
RLHLEKYTFP VQMMVVLPNG TVVHHINANN FLDQTSMKPE DEGPGLSFSA GFEDPSTSTY
IRFLQEGLEK AKPYLES
