SEPP1_MOUSE
ID SEPP1_MOUSE Reviewed; 380 AA.
AC P70274; Q3TJ31; Q3TXG8; Q6PKE7; Q80T08; Q80UF3; Q9Z2T7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Selenoprotein P {ECO:0000303|PubMed:9288402};
DE Short=SeP;
DE AltName: Full=Plasma selenoprotein P;
DE Flags: Precursor;
GN Name=Selenop {ECO:0000312|MGI:MGI:894288};
GN Synonyms=Selp {ECO:0000312|MGI:MGI:894288}, Sepp1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Swiss Webster / NIH;
RX PubMed=9288402; DOI=10.1002/biof.5520060302;
RA Steinert P., Ahrens M., Gross G., Flohe L.;
RT "cDNA and deduced polypeptide sequence of a mouse selenoprotein P.";
RL BioFactors 6:311-319(1997).
RN [2]
RP SEQUENCE REVISION TO 59; 259; 277; 318; 330; 352; 366; 368; 375 AND 377.
RA Steinert P.;
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129;
RX PubMed=9687017; DOI=10.1515/bchm.1998.379.6.683;
RA Steinert P., Bachner D., Flohe L.;
RT "Analysis of the mouse selenoprotein P gene.";
RL Biol. Chem. 379:683-691(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Amnion, Kidney, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=18174160; DOI=10.1074/jbc.m709945200;
RA Olson G.E., Winfrey V.P., Hill K.E., Burk R.F.;
RT "Megalin mediates selenoprotein P uptake by kidney proximal tubule
RT epithelial cells.";
RL J. Biol. Chem. 283:6854-6860(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity). May supply selenium to tissues
CC such as brain and testis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18174160}.
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:0000269|PubMed:18174160}.
CC -!- TISSUE SPECIFICITY: In the kidney, expressed in the cortex with no
CC expression observed in the medulla (at protein level)
CC (PubMed:18174160). Expressed by the liver and secreted in plasma
CC (PubMed:9687017). {ECO:0000269|PubMed:18174160,
CC ECO:0000269|PubMed:9687017}.
CC -!- DOMAIN: The C-terminus is not required for endocytic uptake in the
CC proximal tubule epithelium. {ECO:0000269|PubMed:18174160}.
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; X99807; CAA68140.2; -; mRNA.
DR EMBL; AF021345; AAD01684.1; -; Genomic_DNA.
DR EMBL; AK002450; BAC55246.3; -; mRNA.
DR EMBL; AK077265; BAC55264.3; -; mRNA.
DR EMBL; AK146774; BAE27423.1; -; mRNA.
DR EMBL; AK148623; BAE28626.1; -; mRNA.
DR EMBL; AK159269; BAE34948.1; -; mRNA.
DR EMBL; AK159524; BAE35153.1; -; mRNA.
DR EMBL; AK159894; BAE35460.1; -; mRNA.
DR EMBL; AK159911; BAE35474.1; -; mRNA.
DR EMBL; AK159935; BAE35495.1; -; mRNA.
DR EMBL; AK167611; BAE39664.1; -; mRNA.
DR EMBL; AK168463; BAE40359.1; -; mRNA.
DR EMBL; AK168583; BAE40452.1; -; mRNA.
DR EMBL; AK168631; BAE40491.1; -; mRNA.
DR EMBL; AK168747; BAE40587.1; -; mRNA.
DR EMBL; AK168926; BAE40739.1; -; mRNA.
DR EMBL; AK169011; BAE40808.1; -; mRNA.
DR EMBL; AK169158; BAE40937.1; -; mRNA.
DR EMBL; AK169362; BAE41111.1; -; mRNA.
DR EMBL; BC001991; AAH01991.2; -; mRNA.
DR CCDS; CCDS27357.1; -.
DR PIR; T10442; T10442.
DR RefSeq; NP_001036078.1; NM_001042613.2.
DR RefSeq; NP_001036079.1; NM_001042614.2.
DR RefSeq; NP_033181.3; NM_009155.4.
DR BioGRID; 203178; 6.
DR STRING; 10090.ENSMUSP00000124305; -.
DR TCDB; 9.B.88.1.1; the putative selenoprotein p hydrogen selenide uptake protein (selp) family.
DR GlyGen; P70274; 5 sites.
DR PhosphoSitePlus; P70274; -.
DR CPTAC; non-CPTAC-3746; -.
DR MaxQB; P70274; -.
DR PaxDb; P70274; -.
DR PeptideAtlas; P70274; -.
DR PRIDE; P70274; -.
DR ProteomicsDB; 256962; -.
DR Antibodypedia; 43718; 163 antibodies from 21 providers.
DR DNASU; 20363; -.
DR Ensembl; ENSMUST00000082424; ENSMUSP00000081004; ENSMUSG00000064373.
DR Ensembl; ENSMUST00000159216; ENSMUSP00000124305; ENSMUSG00000064373.
DR GeneID; 20363; -.
DR KEGG; mmu:20363; -.
DR UCSC; uc007vby.1; mouse.
DR CTD; 6414; -.
DR MGI; MGI:894288; Selenop.
DR VEuPathDB; HostDB:ENSMUSG00000064373; -.
DR eggNOG; ENOG502QWRU; Eukaryota.
DR GeneTree; ENSGT00510000049326; -.
DR HOGENOM; CLU_064314_1_0_1; -.
DR InParanoid; P70274; -.
DR OMA; XSXKNKA; -.
DR OrthoDB; 1197628at2759; -.
DR PhylomeDB; P70274; -.
DR TreeFam; TF333425; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 20363; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Sepp1; mouse.
DR PRO; PR:P70274; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P70274; protein.
DR Bgee; ENSMUSG00000064373; Expressed in stroma of bone marrow and 256 other tissues.
DR ExpressionAtlas; P70274; baseline and differential.
DR Genevisible; P70274; MM.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0008430; F:selenium binding; IDA:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0040008; P:regulation of growth; IMP:MGI.
DR GO; GO:0010269; P:response to selenium ion; IEA:Ensembl.
DR GO; GO:0001887; P:selenium compound metabolic process; IDA:MGI.
DR GO; GO:0019953; P:sexual reproduction; IMP:MGI.
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; Phosphoprotein; Reference proteome; Secreted; Selenium;
KW Selenocysteine; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..380
FT /note="Selenoprotein P"
FT /id="PRO_0000022314"
FT REGION 196..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 59
FT /note="Selenocysteine"
FT NON_STD 259
FT /note="Selenocysteine"
FT NON_STD 277
FT /note="Selenocysteine"
FT NON_STD 318
FT /note="Selenocysteine"
FT NON_STD 330
FT /note="Selenocysteine"
FT NON_STD 352
FT /note="Selenocysteine"
FT NON_STD 366
FT /note="Selenocysteine"
FT NON_STD 368
FT /note="Selenocysteine"
FT NON_STD 375
FT /note="Selenocysteine"
FT NON_STD 377
FT /note="Selenocysteine"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49908"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 184
FT /note="D -> Y (in Ref. 3; BAC55264)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="T -> N (in Ref. 2; AAD01684 and 4; AAH01991)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="A -> V (in Ref. 2; AAD01684)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="A -> V (in Ref. 2; AAD01684)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="S -> R (in Ref. 3; BAE34948)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="I -> V (in Ref. 3; BAC55264)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="A -> C (in Ref. 4; AAH01991)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 380 AA; 42706 MW; 0972BF4993CC208D CRC64;
MWRSLGLALA LCLLPYGGAE SQGQSSACYK APEWYIGDQN PMLNSEGKVT VVALLQASUY
LCLLQASRLE DLRIKLESQG YFNISYIVVN HQGSPSQLKH SHLKKQVSEH IAVYRQEEDG
IDVWTLLNGN KDDFLIYDRC GRLVYHLGLP YSFLTFPYVE EAIKIAYCEE RCGNCNLTSL
EDEDFCKTVT SATANKTAEP SEAHSHHKHH NKHGQEHLGS SKPSENQQPG PSETTLPPSG
LHHHHRHRGQ HRQGHLESUD TTASEGLHLS LAQRKLURRG CINQLLCKLS KESEAAPSSC
CCHCRHLIFE KSGSAIAUQC AENLPSLCSU QGLFAEEKVT ESCQCRSPPA AUQNQPMNPM
EANPNUSUDN QTRKUKUHSN
