SEPP1_HUMAN
ID SEPP1_HUMAN Reviewed; 381 AA.
AC P49908; Q6PD59; Q6PI43; Q6PI87; Q6PJF9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Selenoprotein P {ECO:0000303|PubMed:27645994};
DE Short=SeP;
DE Flags: Precursor;
GN Name=SELENOP {ECO:0000303|PubMed:27645994, ECO:0000312|HGNC:HGNC:10751};
GN Synonyms=SELP {ECO:0000312|HGNC:HGNC:10751}, SEPP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart, and Liver;
RX PubMed=8421687; DOI=10.1073/pnas.90.2.537;
RA Hill K.E., Lloyd R.S., Burk R.F.;
RT "Conserved nucleotide sequences in the open reading frame and 3'
RT untranslated region of selenoprotein P mRNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:537-541(1993).
RN [2]
RP SEQUENCE REVISION TO 59; 300; 318; 330; 345; 352; 367; 369; 376 AND 378.
RA Hill K.E.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-112; THR-234; GLN-278;
RP PRO-314 AND CYS-368.
RG NIEHS SNPs program;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-234.
RC TISSUE=Bone marrow, Brain, Liver, and PNS;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PARTIAL PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RX PubMed=8142465; DOI=10.1016/0167-4838(94)90014-0;
RA Aakesson B., Bellew T., Burk R.F.;
RT "Purification of selenoprotein P from human plasma.";
RL Biochim. Biophys. Acta 1204:243-249(1994).
RN [7]
RP CHARACTERIZATION.
RX PubMed=9735174; DOI=10.1006/abbi.1998.0809;
RA Mostert V., Lombeck I., Abel J.;
RT "A novel method for the purification of selenoprotein P from human
RT plasma.";
RL Arch. Biochem. Biophys. 357:326-330(1998).
RN [8]
RP CHARACTERIZATION.
RX PubMed=10775431; DOI=10.1006/abbi.2000.1735;
RA Mostert V.;
RT "Selenoprotein P: properties, functions, and regulation.";
RL Arch. Biochem. Biophys. 376:433-438(2000).
RN [9]
RP REVIEW.
RX PubMed=7931697; DOI=10.1093/jn/124.10.1891;
RA Burk R.F., Hill K.E.;
RT "Selenoprotein P. A selenium-rich extracellular glycoprotein.";
RL J. Nutr. 124:1891-1897(1994).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83; ASN-119 AND ASN-128.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [11]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-83 AND ASN-119.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [12]
RP GLYCOSYLATION AT ASN-83.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP NOMENCLATURE.
RX PubMed=27645994; DOI=10.1074/jbc.m116.756155;
RA Gladyshev V.N., Arner E.S., Berry M.J., Brigelius-Flohe R., Bruford E.A.,
RA Burk R.F., Carlson B.A., Castellano S., Chavatte L., Conrad M.,
RA Copeland P.R., Diamond A.M., Driscoll D.M., Ferreiro A., Flohe L.,
RA Green F.R., Guigo R., Handy D.E., Hatfield D.L., Hesketh J., Hoffmann P.R.,
RA Holmgren A., Hondal R.J., Howard M.T., Huang K., Kim H.Y., Kim I.Y.,
RA Koehrle J., Krol A., Kryukov G.V., Lee B.J., Lee B.C., Lei X.G., Liu Q.,
RA Lescure A., Lobanov A.V., Loscalzo J., Maiorino M., Mariotti M.,
RA Sandeep Prabhu K., Rayman M.P., Rozovsky S., Salinas G., Schmidt E.E.,
RA Schomburg L., Schweizer U., Simonovic M., Sunde R.A., Tsuji P.A.,
RA Tweedie S., Ursini F., Whanger P.D., Zhang Y.;
RT "Selenoprotein gene nomenclature.";
RL J. Biol. Chem. 291:24036-24040(2016).
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.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8142465}.
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 -!- TISSUE SPECIFICITY: Made in the liver and heart and secreted into the
CC plasma. It is also found in the kidney.
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 -!- SIMILARITY: Belongs to the selenoprotein P family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/sepp1/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SEPP1ID46513ch5p12.html";
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; Z11793; CAA77836.2; -; mRNA.
DR EMBL; DQ022288; AAY26400.1; -; Genomic_DNA.
DR EMBL; AC008945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005244; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC015875; AAH15875.1; -; mRNA.
DR EMBL; BC040075; AAH40075.1; -; mRNA.
DR EMBL; BC046152; AAH46152.1; -; mRNA.
DR EMBL; BC058919; AAH58919.1; -; mRNA.
DR CCDS; CCDS43311.1; -.
DR PIR; A47327; A47327.
DR RefSeq; NP_001078955.1; NM_001085486.2.
DR RefSeq; NP_001087195.1; NM_001093726.2.
DR RefSeq; NP_005401.3; NM_005410.3.
DR BioGRID; 112313; 5.
DR IntAct; P49908; 16.
DR STRING; 9606.ENSP00000420939; -.
DR DrugBank; DB11127; Selenious acid.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR GlyConnect; 1729; 10 N-Linked glycans (3 sites).
DR GlyGen; P49908; 7 sites, 14 N-linked glycans (3 sites), 3 O-linked glycans (1 site).
DR iPTMnet; P49908; -.
DR PhosphoSitePlus; P49908; -.
DR BioMuta; SELENOP; -.
DR DMDM; 172046864; -.
DR jPOST; P49908; -.
DR MassIVE; P49908; -.
DR PaxDb; P49908; -.
DR PeptideAtlas; P49908; -.
DR PRIDE; P49908; -.
DR ProteomicsDB; 56176; -.
DR Antibodypedia; 43718; 163 antibodies from 21 providers.
DR DNASU; 6414; -.
DR Ensembl; ENST00000506577.5; ENSP00000425915.1; ENSG00000250722.6.
DR Ensembl; ENST00000511224.5; ENSP00000427671.1; ENSG00000250722.6.
DR Ensembl; ENST00000514985.6; ENSP00000420939.1; ENSG00000250722.6.
DR GeneID; 6414; -.
DR KEGG; hsa:6414; -.
DR MANE-Select; ENST00000514985.6; ENSP00000420939.1; NM_005410.4; NP_005401.3.
DR UCSC; uc011cpt.3; human.
DR CTD; 6414; -.
DR DisGeNET; 6414; -.
DR GeneCards; SELENOP; -.
DR HGNC; HGNC:10751; SELENOP.
DR HPA; ENSG00000250722; Group enriched (intestine, liver).
DR MIM; 601484; gene.
DR neXtProt; NX_P49908; -.
DR OpenTargets; ENSG00000250722; -.
DR PharmGKB; PA35672; -.
DR VEuPathDB; HostDB:ENSG00000250722; -.
DR eggNOG; ENOG502QWRU; Eukaryota.
DR GeneTree; ENSGT00510000049326; -.
DR InParanoid; P49908; -.
DR OMA; XSXKNKA; -.
DR OrthoDB; 1197628at2759; -.
DR PhylomeDB; P49908; -.
DR TreeFam; TF333425; -.
DR PathwayCommons; P49908; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; P49908; -.
DR BioGRID-ORCS; 6414; 8 hits in 1074 CRISPR screens.
DR ChiTaRS; SELENOP; human.
DR GeneWiki; SEPP1; -.
DR GenomeRNAi; 6414; -.
DR Pharos; P49908; Tbio.
DR PRO; PR:P49908; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P49908; protein.
DR Bgee; ENSG00000250722; Expressed in jejunal mucosa and 205 other tissues.
DR ExpressionAtlas; P49908; baseline and differential.
DR Genevisible; P49908; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0031089; C:platelet dense granule lumen; TAS:Reactome.
DR GO; GO:0008430; F:selenium binding; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0040008; P:regulation of growth; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR GO; GO:0001887; P:selenium compound metabolic process; IBA:GO_Central.
DR GO; GO:0019953; P:sexual reproduction; IEA:Ensembl.
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 Direct protein sequencing; Glycoprotein; Phosphoprotein;
KW Reference proteome; Secreted; Selenium; Selenocysteine; Signal.
FT SIGNAL 1..19
FT CHAIN 20..381
FT /note="Selenoprotein P"
FT /id="PRO_0000022313"
FT REGION 197..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 59
FT /note="Selenocysteine"
FT NON_STD 300
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:0007744|PubMed:24275569"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 112
FT /note="P -> S (in dbSNP:rs28919895)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_023256"
FT VARIANT 234
FT /note="A -> T (in dbSNP:rs3877899)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_023257"
FT VARIANT 278
FT /note="R -> Q (in dbSNP:rs28919923)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_023258"
FT VARIANT 314
FT /note="S -> P (in dbSNP:rs28919925)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_023259"
FT VARIANT 368
FT /note="R -> C (in dbSNP:rs28919926)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_023260"
FT CONFLICT 64..65
FT /note="LQ -> IE (in Ref. 1; CAA77836)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="K -> E (in Ref. 5; AAH15875)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="L -> F (in Ref. 5; AAH46152)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 43174 MW; 00872B8030840B02 CRC64;
MWRSLGLALA LCLLPSGGTE SQDQSSLCKQ PPAWSIRDQD PMLNSNGSVT VVALLQASUY
LCILQASKLE DLRVKLKKEG YSNISYIVVN HQGISSRLKY THLKNKVSEH IPVYQQEENQ
TDVWTLLNGS KDDFLIYDRC GRLVYHLGLP FSFLTFPYVE EAIKIAYCEK KCGNCSLTTL
KDEDFCKRVS LATVDKTVET PSPHYHHEHH HNHGHQHLGS SELSENQQPG APNAPTHPAP
PGLHHHHKHK GQHRQGHPEN RDMPASEDLQ DLQKKLCRKR CINQLLCKLP TDSELAPRSU
CCHCRHLIFE KTGSAITUQC KENLPSLCSU QGLRAEENIT ESCQURLPPA AUQISQQLIP
TEASASURUK NQAKKUEUPS N
