ID   SELM_DANRE              Reviewed;         151 AA.
AC   Q802G7; Q5XJC8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Selenoprotein M {ECO:0000303|PubMed:12915322};
DE            Short=SePM {ECO:0000303|PubMed:12915322};
DE            Short=SelM;
DE   Flags: Precursor;
GN   Name=Selenom {ECO:0000250|UniProtKB:Q8WWX9};
GN   Synonyms=selm, sepm {ECO:0000303|PubMed:12915322};
GN   ORFNames=zgc:103431 {ECO:0000312|EMBL:AAH83376.1};
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], AND TISSUE SPECIFICITY.
RC   TISSUE=Embryo;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May function as a thiol-disulfide oxidoreductase that
CC       participates in disulfide bond formation. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: During early embryogenesis, abundantly expressed
CC       within the notochord and anterior somites. At later stages, accumulates
CC       within the axial fin fold, dorsal spinal cord neurons, then in lateral
CC       line neuromasts. {ECO:0000269|PubMed:12915322}.
CC   -!- SIMILARITY: Belongs to the selenoprotein M/F family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH83376.1; Type=Erroneous termination; Note=Truncated C-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; AY216584; AAO86698.1; -; mRNA.
DR   EMBL; BC083376; AAH83376.1; ALT_SEQ; mRNA.
DR   STRING; 7955.ENSDARP00000119889; -.
DR   PaxDb; Q802G7; -.
DR   ZFIN; ZDB-GENE-030410-4; selenom.
DR   eggNOG; ENOG502S29K; Eukaryota.
DR   InParanoid; Q802G7; -.
DR   PhylomeDB; Q802G7; -.
DR   PRO; PR:Q802G7; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   Gene3D; 3.40.30.50; -; 1.
DR   InterPro; IPR038219; Sep15/SelM_sf.
DR   InterPro; IPR039992; Sep15_SelM.
DR   InterPro; IPR014912; Sep15_SelM_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR13077; PTHR13077; 1.
DR   Pfam; PF08806; Sep15_SelM; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome; Selenocysteine; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..151
FT                   /note="Selenoprotein M"
FT                   /id="PRO_0000318607"
FT   REGION          109..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..124
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        35
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        38
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   NON_STD         38
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        35..38
FT                   /note="Cysteinyl-selenocysteine (Cys-Sec)"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        88
FT                   /note="S -> F (in Ref. 2; AAH83376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        108
FT                   /note="G -> D (in Ref. 2; AAH83376)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130..135
FT                   /note="SRLSSA -> GRQSST (in Ref. 2; AAH83376)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   151 AA;  17172 MW;  60B4B22DAA6E6866 CRC64;
     MWPLIFTALL PSVILTYEVN IEKLSGLARA RVETCGGUQL NRMREVKAFV TQDIPLYHNL
     VMKHIPGADP ELVLLNHYYE ELDRIPLSEM TRAEINKLLA ELGFYKKGHP EDQVPEEFRF
     SPAKDSPFES RLSSAAAPET TEPSDSQHTD L