ID   SELK_PIG                Reviewed;          94 AA.
AC   Q2EN82;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   29-SEP-2021, entry version 57.
DE   RecName: Full=Selenoprotein K {ECO:0000250|UniProtKB:Q9Y6D0};
DE            Short=SelK {ECO:0000250|UniProtKB:Q9Y6D0};
GN   Name=SELENOK {ECO:0000250|UniProtKB:Q9Y6D0};
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]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chen C.H., Ding S.T.;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for Ca(2+) flux in immune cells and plays a role in
CC       T-cell proliferation and in T-cell and neutrophil migration (By
CC       similarity). Involved in endoplasmic reticulum-associated degradation
CC       (ERAD) of soluble glycosylated proteins (By similarity). Required for
CC       palmitoylation and cell surface expression of CD36 and involved in
CC       macrophage uptake of low-density lipoprotein and in foam cell formation
CC       (By similarity). Together with ZDHHC6, required for palmitoylation of
CC       ITPR1 in immune cells, leading to regulate ITPR1 stability and
CC       function. Plays a role in protection of cells from ER stress-induced
CC       apoptosis. Protects cells from oxidative stress when overexpressed in
CC       cardiomyocytes (By similarity). {ECO:0000250|UniProtKB:Q9JLJ1,
CC       ECO:0000250|UniProtKB:Q9Y6D0}.
CC   -!- SUBUNIT: Interacts with DERL1, DERL2, DERL3 and SELENOS. The SELENOK-
CC       SELENOS complex interacts with VCP. Interacts with ZDHHC6.
CC       {ECO:0000250|UniProtKB:Q9Y6D0}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9Y6D0}; Single-pass membrane protein
CC       {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q9Y6D0}; Single-
CC       pass membrane protein {ECO:0000255}. Note=Probably mainly localized in
CC       the ER. {ECO:0000250|UniProtKB:Q9Y6D0}.
CC   -!- PTM: Cleaved by CAPN2/m-calpain in resting macrophages but not in
CC       activated macrophages. Macrophage activation up-regulates expression of
CC       the calpain inhibitor CAST/calpastatin, resulting in inhibition of
CC       CAPN2 activity (By similarity). {ECO:0000250|UniProtKB:Q9JLJ1}.
CC   -!- PTM: Truncated SELENOK proteins produced by failed UGA/Sec decoding are
CC       ubiquitinated by the CRL2(KLHDC2) complex, which recognizes the
CC       diglycine (Gly-Gly) at the C-terminus of truncated SELENOK proteins.
CC       {ECO:0000250|UniProtKB:Q9Y6D0}.
CC   -!- SIMILARITY: Belongs to the selenoprotein K family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABD18450.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; DQ372075; ABD18450.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001038018.2; NM_001044553.1.
DR   STRING; 9823.ENSSSCP00000012212; -.
DR   PaxDb; Q2EN82; -.
DR   GeneID; 733604; -.
DR   KEGG; ssc:733604; -.
DR   CTD; 58515; -.
DR   eggNOG; ENOG502S3PW; Eukaryota.
DR   InParanoid; Q2EN82; -.
DR   OrthoDB; 1566291at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR   GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IBA:GO_Central.
DR   GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR   InterPro; IPR024491; Se_SelK/SelG.
DR   PANTHER; PTHR16875; PTHR16875; 1.
DR   Pfam; PF10961; SelK_SelG; 1.
PE   3: Inferred from homology;
KW   Calcium; Calcium transport; Cell membrane; Endoplasmic reticulum;
KW   Ion transport; Membrane; Reference proteome; Selenocysteine; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..94
FT                   /note="Selenoprotein K"
FT                   /id="PRO_0000290204"
FT   TRANSMEM        20..42
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          48..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            81..82
FT                   /note="Cleavage; by CAPN2"
FT                   /evidence="ECO:0000250"
FT   NON_STD         92
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   94 AA;  10619 MW;  7979C91BF013C3F3 CRC64;
     MVYISNGQAL DSRSQSPWRL SFITDFFWGI AEFVVLFFRT LLQQDVKKRR GYGGSSDSRY
     DDGRGPPGNP PRRMGRINHL RGPNPPPMAG GUGR