SELS_RAT
ID SELS_RAT Reviewed; 190 AA.
AC Q8VHV8; Q6PCV8;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Selenoprotein S {ECO:0000250|UniProtKB:Q9BQE4};
DE Short=SelS {ECO:0000250|UniProtKB:Q9BQE4};
DE AltName: Full=Sg2 {ECO:0000312|EMBL:AAL59556.1};
GN Name=Selenos {ECO:0000312|RGD:628897};
GN Synonyms=Vimp {ECO:0000312|RGD:628897};
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].
RC TISSUE=Testis;
RA Lou L., Zhang Y., Jia M.;
RT "Screening genes associated with spermatogenesis.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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).
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). Interacts with
CC CCDC47 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9BCZ4,
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=AAH59111.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL59556.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF367467; AAL59556.1; ALT_SEQ; mRNA.
DR EMBL; BC059111; AAH59111.1; ALT_SEQ; mRNA.
DR RefSeq; NP_775143.2; NM_173120.2.
DR STRING; 10116.ENSRNOP00000016916; -.
DR PaxDb; Q8VHV8; -.
DR PRIDE; Q8VHV8; -.
DR GeneID; 286900; -.
DR KEGG; rno:286900; -.
DR UCSC; RGD:628897; rat.
DR CTD; 55829; -.
DR RGD; 628897; Selenos.
DR eggNOG; ENOG502RXYU; Eukaryota.
DR InParanoid; Q8VHV8; -.
DR OrthoDB; 1489479at2759; -.
DR PhylomeDB; Q8VHV8; -.
DR TreeFam; TF329454; -.
DR PRO; PR:Q8VHV8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005881; C:cytoplasmic microtubule; ISS:UniProtKB.
DR GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:RGD.
DR GO; GO:0036502; C:Derlin-1-VIMP complex; ISO:RGD.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0034362; C:low-density lipoprotein particle; ISO:RGD.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; ISO:RGD.
DR GO; GO:0016209; F:antioxidant activity; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:RGD.
DR GO; GO:0045454; P:cell redox homeostasis; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:RGD.
DR GO; GO:0006983; P:ER overload response; ISO:RGD.
DR GO; GO:0002865; P:negative regulation of acute inflammatory response to antigenic stimulus; ISO:RGD.
DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; ISO:RGD.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; ISO:RGD.
DR GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; ISO:RGD.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0080164; P:regulation of nitric oxide metabolic process; ISO:RGD.
DR GO; GO:0009749; P:response to glucose; ISO:RGD.
DR GO; GO:0051775; P:response to redox state; ISO:RGD.
DR GO; GO:0030970; P:retrograde protein transport, ER to cytosol; ISO:RGD.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISO:RGD.
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; Reference proteome;
KW Selenocysteine; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..190
FT /note="Selenoprotein S"
FT /id="PRO_0000097674"
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 95..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 189
FT /note="Selenocysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 8
FT /note="M -> L (in Ref. 2; AAH59111)"
FT /evidence="ECO:0000305"
FT CONFLICT 104
FT /note="Q -> L (in Ref. 2; AAH59111)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 190 AA; 21385 MW; A2872A4F93677FD5 CRC64;
MDRGEEPMSA RPALETESLR FLHVTVGSLL ASYGWYILFS CVLLYIVIQK LSLRLRALRQ
RQLDQAEAVL EPDVVVKRQE ALAAARLRMQ EDLNAQVEKH KEKQRQLEEE KRRQKIEMWD
SMQEGRSYKR NSGRPQEEDG PGPSTSSVIP KGKSDKKPLR GGGYNPLTGE GGGTCSWRPG
RRGPSSGGUS
