ID   SELPB_DANRE             Reviewed;         265 AA.
AC   Q98SV0;
DT   11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Selenoprotein Pb;
DE            Short=zSelPb;
DE   Flags: Precursor;
GN   Name=sepp1b;
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:AAG53689.1};
RN   [1] {ECO:0000312|EMBL:AAG53689.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
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).
CC   -!- FUNCTION: Might be responsible for some of the extracellular
CC       antioxidant defense properties of selenium.
CC       {ECO:0000250|UniProtKB:P49908}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P49908}.
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DR   EMBL; AF322072; AAG53689.1; -; mRNA.
DR   STRING; 7955.ENSDARP00000100393; -.
DR   PaxDb; Q98SV0; -.
DR   PRIDE; Q98SV0; -.
DR   ZFIN; ZDB-GENE-030311-2; selenop2.
DR   eggNOG; ENOG502RY36; Eukaryota.
DR   InParanoid; Q98SV0; -.
DR   PhylomeDB; Q98SV0; -.
DR   PRO; PR:Q98SV0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0008430; F:selenium binding; IBA:GO_Central.
DR   GO; GO:0001887; P:selenium compound metabolic process; IBA:GO_Central.
DR   InterPro; IPR007671; Selenoprotein-P_N.
DR   InterPro; IPR037941; SeP.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR10105; PTHR10105; 1.
DR   Pfam; PF04592; SelP_N; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Reference proteome; Secreted; Selenocysteine; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..265
FT                   /note="Selenoprotein Pb"
FT                   /id="PRO_0000022301"
FT   REGION          187..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..234
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..258
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_STD         64
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000303|PubMed:11168591"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        184
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   265 AA;  30040 MW;  D858FC5CD7EDEB13 CRC64;
     MQALWPLLLS ALPALLGASS LFVEKESNGS RICKPAPQWE IDGKTPMKEL LGNVVVVALL
     KASUHFCLTQ AARLGDLRDK LANGGLTNIS FMVVNEQDSQ SRAMYWELKR RTAQDIPVYQ
     QSPLQNDVWE ILEGDKDDFL VYDRCGYLTF HIVLPFSFLH YPYIEAAIRA TYHKNMCNCS
     LNANFSISES SDSTKNDPAG ENNQRPNSTE PVTAAHHHHH QQHEPHHHHH NPYPNSHKKS
     GDSDVTGKPK EPPHHSHQEH VHNHR