ID   SEPP1_PONAB             Reviewed;         381 AA.
AC   Q5R8W9;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 58.
DE   RecName: Full=Selenoprotein P {ECO:0000250|UniProtKB:P49908};
DE            Short=SeP;
DE   Flags: Precursor;
GN   Name=SELENOP {ECO:0000250|UniProtKB:P49908};
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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. May supply selenium to tissues such as brain and
CC       testis (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P70274}.
CC       Note=Passes from plasma into the glomerular filtrate where it is
CC       removed by endocytosis mediated by LRP2 in the proximal tubule
CC       epithelium. {ECO:0000250|UniProtKB:P70274}.
CC   -!- DOMAIN: The C-terminus is not required for endocytic uptake in the
CC       proximal tubule epithelium. {ECO:0000250|UniProtKB:P70274}.
CC   -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the selenoprotein P family. {ECO:0000305}.
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DR   EMBL; CR859629; CAH91791.1; -; mRNA.
DR   RefSeq; NP_001127462.1; NM_001133990.1.
DR   STRING; 9601.ENSPPYP00000023549; -.
DR   GeneID; 100174535; -.
DR   KEGG; pon:100174535; -.
DR   CTD; 6414; -.
DR   eggNOG; ENOG502QWRU; Eukaryota.
DR   InParanoid; Q5R8W9; -.
DR   OrthoDB; 1197628at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008430; F:selenium binding; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Glycoprotein; Phosphoprotein; Reference proteome; Secreted; Selenium;
KW   Selenocysteine; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000250"
FT   CHAIN           20..381
FT                   /note="Selenoprotein P"
FT                   /id="PRO_0000022315"
FT   REGION          197..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_STD         59
FT                   /note="Selenocysteine"
FT   NON_STD         318
FT                   /note="Selenocysteine"
FT   NON_STD         330
FT                   /note="Selenocysteine"
FT   NON_STD         345
FT                   /note="Selenocysteine"
FT   NON_STD         352
FT                   /note="Selenocysteine"
FT   NON_STD         367
FT                   /note="Selenocysteine"
FT   NON_STD         369
FT                   /note="Selenocysteine"
FT   NON_STD         376
FT                   /note="Selenocysteine"
FT   NON_STD         378
FT                   /note="Selenocysteine"
FT   MOD_RES         266
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P49908"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        128
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   381 AA;  43174 MW;  5CDC8567D9B69CBB CRC64;
     MWRSLGLALA LCLLPLGGTE SQDQSSLCKQ PPAWSIRDQG PMLNSNGSVT VVALLQASUY
     LCILQASKLE DLRVKLKKEG YSNISHIVVN HQGISSRLKY THLKNKVSEH IPVYQQEENQ
     TDVWTLLNGS KDDFLIYDRC GRLVYHLGLP FSFLTFPYVE EAVKIAYCEK KCGYCSLTTL
     KDEDFCKSVS LATVDKTVEA PSPHYHHEHH HNHRHQHLGS SELSENQQPG APDAPTHPAP
     PGLHHHHKHK GQHRQGHPEN RDMPGSEDIQ DLQKKLCRKR CINQLLCKLP KDSELAPRSC
     CCHCRHLIFE KTGSAITUQC KENLPSLCSU QGLRAEENIT ESCQURLPPP AUQISQQLIP
     TEASTSURUK NQAKKUEUPS N