SELS_BOVIN
ID SELS_BOVIN Reviewed; 190 AA.
AC Q2KI76;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Selenoprotein S {ECO:0000250|UniProtKB:Q9BQE4};
DE Short=SelS {ECO:0000250|UniProtKB:Q9BQE4};
GN Name=SELENOS {ECO:0000250|UniProtKB:Q9BQE4};
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the degradation process of misfolded endoplasmic
CC reticulum (ER) luminal proteins. Participates in the transfer of
CC misfolded proteins from the ER to the cytosol, where they are destroyed
CC by the proteasome in a ubiquitin-dependent manner. Probably acts by
CC serving as a linker between DERL1, which mediates the
CC retrotranslocation of misfolded proteins into the cytosol, and the
CC ATPase complex VCP, which mediates the translocation and ubiquitination
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with DERL1 and (via VIM motif) with VCP, suggesting
CC that it forms a membrane complex with DERL1 that serves as a receptor
CC for VCP. Also interacts with DERL2, DERL3 and SELENOK. The SELENOK-
CC SELENOS complex interacts with VCP (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9BQE4}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Single-pass membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- PTM: Truncated SELENOS proteins produced by failed UGA/Sec decoding are
CC ubiquitinated by the CRL2(KLHDC2) and CRL2(KLHDC3) complexes, which
CC recognizes the glycine (Gly) at the C-terminus of truncated SELENOS
CC proteins. Truncated SELENOS proteins produced by failed UGA/Sec
CC decoding are also ubiquitinated by the CRL5(KLHDC1) complex.
CC {ECO:0000250|UniProtKB:Q9BQE4}.
CC -!- SIMILARITY: Belongs to the selenoprotein S family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI12741.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI12741.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC112740; AAI12741.1; ALT_INIT; mRNA.
DR RefSeq; NP_001039579.2; NM_001046114.3.
DR RefSeq; NP_001335155.1; NM_001348226.1.
DR STRING; 9913.ENSBTAP00000000842; -.
DR PaxDb; Q2KI76; -.
DR PRIDE; Q2KI76; -.
DR Ensembl; ENSBTAT00000000842; ENSBTAP00000000842; ENSBTAG00000000640.
DR GeneID; 512276; -.
DR KEGG; bta:512276; -.
DR CTD; 55829; -.
DR VEuPathDB; HostDB:ENSBTAG00000000640; -.
DR VGNC; VGNC:57162; SELENOS.
DR eggNOG; ENOG502RXYU; Eukaryota.
DR GeneTree; ENSGT00390000015688; -.
DR HOGENOM; CLU_117238_0_0_1; -.
DR InParanoid; Q2KI76; -.
DR OMA; LSLYGWY; -.
DR OrthoDB; 1489479at2759; -.
DR TreeFam; TF329454; -.
DR Proteomes; UP000009136; Chromosome 21.
DR Bgee; ENSBTAG00000000640; Expressed in spermatocyte and 106 other tissues.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IBA:GO_Central.
DR GO; GO:0036502; C:Derlin-1-VIMP complex; IBA:GO_Central.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0034362; C:low-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IEA:Ensembl.
DR GO; GO:0016209; F:antioxidant activity; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; IEA:Ensembl.
DR GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IBA:GO_Central.
DR GO; GO:0006983; P:ER overload response; IEA:Ensembl.
DR GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; IEA:Ensembl.
DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; IEA:Ensembl.
DR GO; GO:0080164; P:regulation of nitric oxide metabolic process; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0051775; P:response to redox state; IEA:Ensembl.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IBA:GO_Central.
DR InterPro; IPR009703; Selenoprotein_S.
DR PANTHER; PTHR28621; PTHR28621; 1.
DR Pfam; PF06936; Selenoprotein_S; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endoplasmic reticulum; Membrane; Phosphoprotein;
KW Reference proteome; Selenocysteine; Transmembrane; Transmembrane helix;
KW Ubl conjugation.
FT CHAIN 1..190
FT /note="Selenoprotein S"
FT /id="PRO_0000318650"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 78..90
FT /note="VCP/p97-interacting motif (VIM)"
FT /evidence="ECO:0000250|UniProtKB:Q9BQE4"
FT REGION 115..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 189
FT /note="Selenocysteine"
FT /evidence="ECO:0000250"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQE4"
SQ SEQUENCE 190 AA; 21385 MW; 8EF4185A31199B2A CRC64;
MERDGDQLSA RPTLETEGLR FLHVTVGSLL ATYGWYIVFS CILLYVVFQK LSTRLRALRQ
RHLDQAAAAL EPDIVVKRQE ALAAARLKMQ EELNAQVEKH KEKLRQLEEE KRRQKIEMWD
SMQEGKSYKG NTRKPQEEDS PGPSTSSVIP KRKSDRKPLR GGGYNPLSGE GGGTCSWRPG
RRGPSSGGUG
