SEPP1_BOVIN
ID SEPP1_BOVIN Reviewed; 402 AA.
AC P49907; O19003; Q9N2H6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Selenoprotein P {ECO:0000305};
DE Short=SeP;
DE AltName: Full=Selenoprotein P-like protein {ECO:0000303|PubMed:7637580};
DE Flags: Precursor;
GN Name=SELENOP {ECO:0000250|UniProtKB:P49908};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SELENOCYSTEINE AT SEC-59; SEC-297; SEC-307;
RP SEC-338; SEC-350; SEC-363; SEC-365; SEC-372; SEC-388; SEC-390; SEC-397 AND
RP SEC-399, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Cerebellum;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9358058; DOI=10.1016/s0378-1119(97)00369-7;
RA Fujii M., Saijoh K., Kobayashi T., Fujii S., Lee M.J., Sumino K.;
RT "Analysis of bovine selenoprotein P-like protein gene and availability of
RT metal responsive element (MRE) located in its promoter.";
RL Gene 199:211-217(1997).
RN [3]
RP SEQUENCE REVISION TO 59; 297; 307; 338; 350; 363; 365; 372; 388; 390; 397
RP AND 399.
RA Saijoh K.;
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hara S., Imura N., Shoji Y.;
RT "Bovine endothelial selenoprotein P.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Constitutes a major selenium pool in the brain and may play
CC an important role in developing and/or modulating the morphology of
CC neurons and/or glial cells. {ECO:0000269|PubMed:7637580}.
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 -!- TISSUE SPECIFICITY: Brain and kidney. Most prominently expressed in the
CC cerebellar cortex, hippocampus and olfactory bulb.
CC {ECO:0000269|PubMed:7637580}.
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; D25220; BAA04949.2; -; mRNA.
DR EMBL; D88033; BAA23414.2; -; Genomic_DNA.
DR EMBL; AB032826; BAA84781.1; -; mRNA.
DR RefSeq; NP_776884.2; NM_174459.3.
DR PRIDE; P49907; -.
DR Ensembl; ENSBTAT00000084253; ENSBTAP00000057403; ENSBTAG00000054085.
DR GeneID; 282066; -.
DR KEGG; bta:282066; -.
DR CTD; 6414; -.
DR VEuPathDB; HostDB:ENSBTAG00000054085; -.
DR VGNC; VGNC:109401; SELENOP.
DR GeneTree; ENSGT00510000049326; -.
DR InParanoid; P49907; -.
DR OMA; XSXKNKA; -.
DR OrthoDB; 1197628at2759; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000054085; Expressed in liver and 104 other tissues.
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; 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; Repeat; Secreted;
KW Selenium; Selenocysteine; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..402
FT /note="Selenoprotein P"
FT /id="PRO_0000022312"
FT REPEAT 204..205
FT /note="1"
FT REPEAT 206..207
FT /note="2"
FT REPEAT 208..209
FT /note="3"
FT REPEAT 210..211
FT /note="4"
FT REPEAT 212..213
FT /note="5"
FT REPEAT 214..215
FT /note="6"
FT REPEAT 216..217
FT /note="7"
FT REPEAT 218..219
FT /note="8"
FT REPEAT 220..221
FT /note="9"
FT REPEAT 222..223
FT /note="10"
FT REPEAT 224..225
FT /note="11"
FT REPEAT 226..227
FT /note="12"
FT REPEAT 228..229
FT /note="13"
FT REGION 196..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..229
FT /note="13 X 2 AA tandem repeats of H-[PHS]"
FT REGION 366..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..229
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 59
FT /note="Selenocysteine"
FT NON_STD 297
FT /note="Selenocysteine"
FT NON_STD 307
FT /note="Selenocysteine"
FT NON_STD 338
FT /note="Selenocysteine"
FT NON_STD 350
FT /note="Selenocysteine"
FT NON_STD 363
FT /note="Selenocysteine"
FT NON_STD 365
FT /note="Selenocysteine"
FT NON_STD 372
FT /note="Selenocysteine"
FT NON_STD 388
FT /note="Selenocysteine"
FT NON_STD 390
FT /note="Selenocysteine"
FT NON_STD 397
FT /note="Selenocysteine"
FT NON_STD 399
FT /note="Selenocysteine"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49908"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CONFLICT 178..181
FT /note="KALE -> SRPQ (in Ref. 1; BAA04949)"
FT /evidence="ECO:0000305"
FT CONFLICT 211..226
FT /note="Missing (in Ref. 4; BAA84781)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="P -> T (in Ref. 1; BAA04949)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="V -> L (in Ref. 1; BAA04949)"
FT /evidence="ECO:0000305"
FT CONFLICT 312
FT /note="D -> Y (in Ref. 1; BAA04949)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 402 AA; 45488 MW; 5C16C132DA59516C CRC64;
MWRGLGLALA LCLLLTGGTE SQGQSSYCKQ PPPWSIKDQD PMLNSYGSVT VVALLQASUY
LCILQASRLE DLRVKLEKEG YSNISYVVVN HQGISSRLKY VHLKNKVSEH IPVYQQEENQ
PDVWTLLNGN KDDFLIYDRC GRLVYHLGLP YSFLTFTYVE DSIKTVYCED KCGNCSLKAL
EDEDVCKNVF LATKEKTAEA SQRHHHPHPH SHPHPHPHPH PHPHPHPHHG HQLHENAHLS
ESPKPDTPDT PENPPPSGLH HHHHRHKGPQ RQGHSDNCDT PVGSESLQPS LPQKKLURKR
CINQLLUQFP KDSESALSSC CCHCRHLVFE KTGSAITUQC TEKLPSLCSU QGLLAEENVI
ESUQURLPPA AUQAAGQQLN PTEASTKUSU KNKAKMUKUP SN
