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SELPA_DANRE
ID   SELPA_DANRE             Reviewed;         367 AA.
AC   Q98SV1;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Selenoprotein Pa;
DE            Short=zSelPa;
DE   Flags: Precursor;
GN   Name=sepp1a;
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 {ECO:0000312|EMBL:AAG53688.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX   PubMed=11168591; DOI=10.1046/j.1365-2443.2000.00392.x;
RA   Kryukov G.V., Gladyshev V.N.;
RT   "Selenium metabolism in zebrafish: multiplicity of selenoprotein genes and
RT   expression of a protein containing 17 selenocysteine residues.";
RL   Genes Cells 5:1049-1060(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retina;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Might be responsible for some of the extracellular
CC       antioxidant defense properties of selenium or might be involved in the
CC       transport of selenium. {ECO:0000250|UniProtKB:P49908}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11168591}.
CC   -!- SIMILARITY: Belongs to the selenoprotein P family. {ECO:0000305}.
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DR   EMBL; AF322071; AAG53688.1; -; mRNA.
DR   EMBL; BC059656; AAH59656.1; -; mRNA.
DR   STRING; 7955.ENSDARP00000116562; -.
DR   PaxDb; Q98SV1; -.
DR   ZFIN; ZDB-GENE-030311-1; selenop.
DR   eggNOG; ENOG502QWRU; Eukaryota.
DR   InParanoid; Q98SV1; -.
DR   PhylomeDB; Q98SV1; -.
DR   Reactome; R-DRE-114608; Platelet degranulation.
DR   PRO; PR:Q98SV1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0008430; F:selenium binding; IBA:GO_Central.
DR   GO; GO:0001887; P:selenium compound metabolic process; IDA:ZFIN.
DR   InterPro; IPR007671; Selenoprotein-P_N.
DR   InterPro; IPR007672; SelP_C.
DR   InterPro; IPR037941; SeP.
DR   PANTHER; PTHR10105; PTHR10105; 1.
DR   Pfam; PF04593; SelP_C; 1.
DR   Pfam; PF04592; SelP_N; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Reference proteome; Secreted; Selenium; Selenocysteine;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..367
FT                   /note="Selenoprotein Pa"
FT                   /id="PRO_0000022300"
FT   REGION          191..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          306..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..236
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_STD         59
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         267
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         273
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         279
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         290
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         292
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         294
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         310
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         320
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         322
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         336
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         338
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         346
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         353
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         355
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         362
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   NON_STD         364
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   367 AA;  41968 MW;  5CFF2C2D5DA39097 CRC64;
     MWKALSLTLA LCLLVGCSAE SETEGARCKL PPEWKVGDVE PMKNALGQVT VVAYLQASUL
     FCLEQASKLN DLLLKLENQG YPNIAYMVVN NREERSQRLH HLLQERLLNI TLYAQDLSQP
     DAWQAVNAEK DDILVYDRCG RLTYHLSLPY TILSHPHVEE AIKHTYCDRI CGECSLESSA
     QLEECKKATE EVNKPVEEEP RQDHGHHEHG HHEHQGEAER HRHGHHHPHH HHHHHRGQQQ
     VDVDQQVLSQ VDFGQVAVET PMMKRPUAKH SRUKVQYSUQ QGADSPVASU CUHURQLFGG
     EGNGRVAGLU HCDEPLPASU PUQGLKEQDN HIKETUQURP APPAEUELSQ PTUVUPAGDA
     TUGURKK
 
 
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