ID SELK_MACFA Reviewed; 94 AA.
AC Q4R8M1;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Selenoprotein K {ECO:0000250|UniProtKB:Q9Y6D0};
DE Short=SelK {ECO:0000250|UniProtKB:Q9Y6D0};
GN Name=SELENOK {ECO:0000250|UniProtKB:Q9Y6D0};
GN Synonyms=SELK {ECO:0000250|UniProtKB:Q9Y6D0};
GN ORFNames=QtsA-12089 {ECO:0000312|EMBL:BAE00551.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) 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=BAE00551.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB168431; BAE00551.1; ALT_SEQ; mRNA.
DR SMR; Q4R8M1; -.
DR STRING; 9541.ENSMFAP00000020314; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0018345; P:protein palmitoylation; ISS:UniProtKB.
DR InterPro; IPR024491; Se_SelK/SelG.
DR PANTHER; PTHR16875; SELENOPROTEIN K; 1.
DR PANTHER; PTHR16875:SF0; SELENOPROTEIN K; 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_0000290203"
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; 10645 MW; D26F13E90BEC6807 CRC64;
MVYISNGQVL DSRSQSPWRL SLITDFFWGI AEFVVLFFKT LLQQDVKKRR SYGNSSDSRY
DDGRGPPGNP PRRMGRINHL RGPSPPPMAG GUGR
//
