SELS_PIG
ID SELS_PIG Reviewed; 190 AA.
AC F1SR90; D9DBG2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Selenoprotein S {ECO:0000303|PubMed:21116851};
DE Short=SelS {ECO:0000303|PubMed:21116851};
GN Name=SELENOS {ECO:0000250|UniProtKB:Q9BQE4};
GN Synonyms=SELS {ECO:0000303|PubMed:21116851};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ADJ67513.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Guanxi bama miniature pig {ECO:0000269|PubMed:21116851};
RC TISSUE=Liver {ECO:0000312|EMBL:ADJ67513.1};
RX PubMed=21116851; DOI=10.1007/s11033-010-0551-y;
RA Zhang N., Jing W., Cheng J., Cui W., Mu Y., Li K., Lei X.;
RT "Molecular characterization and NF-kappaB-regulated transcription of
RT selenoprotein S from the Bama mini-pig.";
RL Mol. Biol. Rep. 38:4281-4286(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Landrace;
RG Swine Genome Sequencing Consortium.;
RL Submitted (NOV-2009) 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|UniProtKB:Q9BQE4}.
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: Cytoplasm {ECO:0000269|PubMed:21116851}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9BQE4}; Single-
CC pass membrane protein {ECO:0000250|UniProtKB:Q9BQE4}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highest expression in liver
CC and lung, with lower levels detected in spleen, kidney, brain, lymph
CC nodes, small intestine, stomach and heart. Very low expression detected
CC in longissimus dorsi. {ECO:0000269|PubMed:21116851}.
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:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CU467921; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; GU983865; ADJ67513.1; -; mRNA.
DR EMBL; CU467921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001157585.1; NM_001164113.1.
DR STRING; 9823.ENSSSCP00000005198; -.
DR PaxDb; F1SR90; -.
DR PeptideAtlas; F1SR90; -.
DR PRIDE; F1SR90; -.
DR Ensembl; ENSSSCT00000005328; ENSSSCP00000005198; ENSSSCG00000004826.
DR Ensembl; ENSSSCT00005033810; ENSSSCP00005020637; ENSSSCG00005021369.
DR Ensembl; ENSSSCT00015009328; ENSSSCP00015003719; ENSSSCG00015007042.
DR Ensembl; ENSSSCT00025047518; ENSSSCP00025020357; ENSSSCG00025034862.
DR Ensembl; ENSSSCT00030083765; ENSSSCP00030038485; ENSSSCG00030060018.
DR Ensembl; ENSSSCT00035076131; ENSSSCP00035031074; ENSSSCG00035056945.
DR Ensembl; ENSSSCT00040099309; ENSSSCP00040044466; ENSSSCG00040072172.
DR Ensembl; ENSSSCT00050043302; ENSSSCP00050017883; ENSSSCG00050032250.
DR Ensembl; ENSSSCT00055011141; ENSSSCP00055008794; ENSSSCG00055005728.
DR Ensembl; ENSSSCT00060067522; ENSSSCP00060028949; ENSSSCG00060049719.
DR Ensembl; ENSSSCT00065016715; ENSSSCP00065006839; ENSSSCG00065012554.
DR Ensembl; ENSSSCT00070032817; ENSSSCP00070027391; ENSSSCG00070016664.
DR GeneID; 100151836; -.
DR KEGG; ssc:100151836; -.
DR CTD; 55829; -.
DR VGNC; VGNC:98308; SELENOS.
DR eggNOG; ENOG502RXYU; Eukaryota.
DR GeneTree; ENSGT00390000015688; -.
DR HOGENOM; CLU_117238_0_0_1; -.
DR InParanoid; F1SR90; -.
DR OMA; LSLYGWY; -.
DR OrthoDB; 1489479at2759; -.
DR Proteomes; UP000008227; Chromosome 1.
DR Proteomes; UP000314985; Chromosome 1.
DR Bgee; ENSSSCG00000004826; Expressed in duodenum and 45 other tissues.
DR Genevisible; F1SR90; SS.
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_0000411969"
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 121..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 189
FT /note="Selenocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQE4"
FT MOD_RES 140
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQE4"
SQ SEQUENCE 190 AA; 21279 MW; 3727B7CA0243DF37 CRC64;
MEQDGDQLSA RPALETEGLR FLHVTVGSLL ATYGWYIVFC CILLYVVFQK LSTRLRALRQ
RHLDGAAAAL EPDVVVKRQE ALAAARLKMQ EELNAQVEKH KEKLRQLEEE KRRQKIERWD
SVQEGRSYRG DARKRQEEDS PGPSTSSVIP KRKSDKKPLR GGGYNPLSGE GGGACSWRPG
RRGPSSGGUG
