SEPP1_RAT
ID SEPP1_RAT Reviewed; 385 AA.
AC P25236;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Selenoprotein P {ECO:0000303|PubMed:2037562};
DE Short=SeP;
DE Contains:
DE RecName: Full=Selenoprotein Se-P10;
DE Contains:
DE RecName: Full=Selenoprotein Se-P6;
DE Contains:
DE RecName: Full=Selenoprotein Se-P2;
DE Contains:
DE RecName: Full=Selenoprotein Se-P1;
DE Flags: Precursor;
GN Name=Selenop {ECO:0000312|RGD:3660};
GN Synonyms=Selp {ECO:0000312|RGD:3660}, Sepp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-41; 267-287 AND 316-327,
RP AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=2037562; DOI=10.1016/s0021-9258(18)99185-4;
RA Hill K.E., Lloyd R.S., Yang J.-G., Read R., Burk R.F.;
RT "The cDNA for rat selenoprotein P contains 10 TGA codons in the open
RT reading frame.";
RL J. Biol. Chem. 266:10050-10053(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=7637580; DOI=10.1016/0169-328x(94)00007-2;
RA Saijoh K., Saito N., Lee M.J., Fujii M., Kobayashi T., Sumino K.;
RT "Molecular cloning of cDNA encoding a bovine selenoprotein P-like protein
RT containing 12 selenocysteines and a (His-Pro) rich domain insertion, and
RT its regional expression.";
RL Brain Res. Mol. Brain Res. 30:301-311(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [4]
RP CHARACTERIZATION OF ISOFORMS.
RX PubMed=11821412; DOI=10.1074/jbc.m111462200;
RA Ma S., Hill K.E., Caprioli R.M., Burk R.F.;
RT "Mass spectrometric characterization of full-length rat selenoprotein P and
RT three isoforms shortened at the C-terminus. Evidence that three UGA codons
RT in the mRNA open reading frame have alternative functions of specifying
RT selenocysteine insertion or translation termination.";
RL J. Biol. Chem. 277:12749-12754(2002).
RN [5]
RP GLYCOSYLATION AT ASN-83; ASN-174; ASN-188 AND THR-365, LACK OF
RP GLYCOSYLATION AT ASN-370 AND ASN-375, AND DISULFIDE BONDS.
RX PubMed=12911312; DOI=10.1021/bi0346300;
RA Ma S., Hill K.E., Burk R.F., Caprioli R.M.;
RT "Mass spectrometric identification of N- and O-glycosylation sites of full-
RT length rat selenoprotein P and determination of selenide-sulfide and
RT disulfide linkages in the shortest isoform.";
RL Biochemistry 42:9703-9711(2003).
RN [6]
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).
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:2037562}.
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: Widely expressed, mainly by the liver. Secreted in
CC plasma.
CC -!- DOMAIN: The C-terminus is not required for endocytic uptake in the
CC proximal tubule epithelium. {ECO:0000250|UniProtKB:P70274}.
CC -!- PTM: Isoform Se-P1 contains several disulfide bridges and a selenide-
CC sulfide bond between Sec-59 and Cys-62. These bonds are speculated to
CC serve as redox-active pairs.
CC -!- PTM: Phosphorylation sites are present in the extracellular medium.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Plasma contains 4 isoforms, which are named isoforms Se-
CC P10, Se-P6, Se-P2 and Se-P1, according to the number of selenocysteines
CC they contain. All isoforms arise from the same mRNA. The 3 shortened
CC isoforms terminated at the opal stop codons at positions 264, 282, 371,
CC when selenocysteine has not been inserted.
CC -!- SIMILARITY: Belongs to the selenoprotein P family. {ECO:0000305}.
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DR EMBL; M63574; AAA42129.2; -; mRNA.
DR EMBL; D25221; BAA04950.2; -; mRNA.
DR EMBL; BC072539; AAH72539.1; -; mRNA.
DR PIR; A40380; OMRTSP.
DR RefSeq; NP_001077380.1; NM_001083911.1.
DR RefSeq; NP_062065.2; NM_019192.2.
DR GlyGen; P25236; 4 sites.
DR iPTMnet; P25236; -.
DR PhosphoSitePlus; P25236; -.
DR Ensembl; ENSRNOT00000086590; ENSRNOP00000069020; ENSRNOG00000053086.
DR GeneID; 29360; -.
DR KEGG; rno:29360; -.
DR CTD; 6414; -.
DR RGD; 3660; Selenop.
DR GeneTree; ENSGT00510000049326; -.
DR InParanoid; P25236; -.
DR OrthoDB; 1197628at2759; -.
DR PhylomeDB; P25236; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR PRO; PR:P25236; -.
DR Proteomes; UP000002494; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0008430; F:selenium binding; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0040008; P:regulation of growth; ISO:RGD.
DR GO; GO:0010269; P:response to selenium ion; IEP:RGD.
DR GO; GO:0001887; P:selenium compound metabolic process; ISO:RGD.
DR GO; GO:0019953; P:sexual reproduction; ISO:RGD.
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; Disulfide bond; Glycoprotein; Phosphoprotein;
KW Reference proteome; Secreted; Selenium; Selenocysteine; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2037562"
FT CHAIN 20..385
FT /note="Selenoprotein Se-P10"
FT /id="PRO_0000022316"
FT CHAIN 20..370
FT /note="Selenoprotein Se-P6"
FT /id="PRO_0000022317"
FT CHAIN 20..281
FT /note="Selenoprotein Se-P2"
FT /id="PRO_0000022318"
FT CHAIN 20..263
FT /note="Selenoprotein Se-P1"
FT /id="PRO_0000022319"
FT REGION 196..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..257
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 370
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:12911312"
FT SITE 375
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:12911312"
FT NON_STD 59
FT /note="Selenocysteine"
FT NON_STD 264
FT /note="Selenocysteine"
FT NON_STD 282
FT /note="Selenocysteine"
FT NON_STD 323
FT /note="Selenocysteine"
FT NON_STD 335
FT /note="Selenocysteine"
FT NON_STD 357
FT /note="Selenocysteine"
FT NON_STD 371
FT /note="Selenocysteine"
FT NON_STD 373
FT /note="Selenocysteine"
FT NON_STD 380
FT /note="Selenocysteine"
FT NON_STD 382
FT /note="Selenocysteine"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49908"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12911312"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12911312"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12911312"
FT CARBOHYD 365
FT /note="O-linked (Hex...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:12911312"
FT DISULFID 168..186
FT /note="In isoform Se-P1"
FT /evidence="ECO:0000269|PubMed:12911312"
FT DISULFID 172..175
FT /note="In isoform Se-P1"
FT /evidence="ECO:0000269|PubMed:12911312"
FT CROSSLNK 59..62
FT /note="Cysteinyl-selenocysteine (Sec-Cys); in isoform Se-
FT P1"
SQ SEQUENCE 385 AA; 43083 MW; CF638BA2B6959170 CRC64;
MWRSLGLALA LCLLPYGGAE SQGQSPACKQ APPWNIGDQN PMLNSEGTVT VVALLQASUY
LCLLQASRLE DLRIKLENQG YFNISYIVVN HQGSPSQLKH AHLKKQVSDH IAVYRQDEHQ
TDVWTLLNGN KDDFLIYDRC GRLVYHLGLP YSFLTFPYVE EAIKIAYCEK RCGNCSFTSL
EDEAFCKNVS SATASKTTEP SEEHNHHKHH DKHGHEHLGS SKPSENQQPG ALDVETSLPP
SGLHHHHHHH KHKGQHRQGH LESUDMGASE GLQLSLAQRK LURRGCINQL LCKLSEESGA
ATSSCCCHCR HLIFEKSGSA ITUQCAENLP SLCSUQGLFA EEKVIESCQC RSPPAAUHSQ
HVSPTEASPN USUNNKTKKU KUNLN
