SELK_MOUSE
ID SELK_MOUSE Reviewed; 94 AA.
AC Q9JLJ1; Q8CI00;
DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Selenoprotein K {ECO:0000303|PubMed:21849499};
DE Short=SelK {ECO:0000303|PubMed:21849499};
GN Name=Selenok {ECO:0000312|MGI:MGI:1931466};
GN Synonyms=Selk {ECO:0000303|PubMed:21849499};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Thymic epithelium;
RA Xie L.P., Chen W.F.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Pancreas, Small intestine, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Mammary gland, and Mammary tumor;
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).
RN [4]
RP TISSUE SPECIFICITY, AND CLEAVAGE BY CAPN2.
RX PubMed=21849499; DOI=10.1074/jbc.m111.265520;
RA Huang Z., Hoffmann F.W., Norton R.L., Hashimoto A.C., Hoffmann P.R.;
RT "Selenoprotein K is a novel target of m-calpain, and cleavage is regulated
RT by Toll-like receptor-induced calpastatin in macrophages.";
RL J. Biol. Chem. 286:34830-34838(2011).
RN [5]
RP INTERACTION WITH DERL1; DERL2 AND DERL3.
RX PubMed=22016385; DOI=10.1074/jbc.m111.310920;
RA Shchedrina V.A., Everley R.A., Zhang Y., Gygi S.P., Hatfield D.L.,
RA Gladyshev V.N.;
RT "Selenoprotein K binds multiprotein complexes and is involved in the
RT regulation of endoplasmic reticulum homeostasis.";
RL J. Biol. Chem. 286:42937-42948(2011).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=21220695; DOI=10.4049/jimmunol.1002878;
RA Verma S., Hoffmann F.W., Kumar M., Huang Z., Roe K., Nguyen-Wu E.,
RA Hashimoto A.S., Hoffmann P.R.;
RT "Selenoprotein K knockout mice exhibit deficient calcium flux in immune
RT cells and impaired immune responses.";
RL J. Immunol. 186:2127-2137(2011).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23444136; DOI=10.1189/jlb.1212647;
RA Meiler S., Baumer Y., Huang Z., Hoffmann F.W., Fredericks G.J., Rose A.H.,
RA Norton R.L., Hoffmann P.R., Boisvert W.A.;
RT "Selenoprotein K is required for palmitoylation of CD36 in macrophages:
RT implications in foam cell formation and atherogenesis.";
RL J. Leukoc. Biol. 93:771-780(2013).
RN [8]
RP FUNCTION, AND INTERACTION WITH ZDHHC6.
RX PubMed=25368151; DOI=10.1073/pnas.1417176111;
RA Fredericks G.J., Hoffmann F.W., Rose A.H., Osterheld H.J., Hess F.M.,
RA Mercier F., Hoffmann P.R.;
RT "Stable expression and function of the inositol 1,4,5-triphosphate receptor
RT requires palmitoylation by a DHHC6/selenoprotein K complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:16478-16483(2014).
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
CC (PubMed:21220695). Involved in endoplasmic reticulum-associated
CC degradation (ERAD) of soluble glycosylated proteins (By similarity).
CC Required for palmitoylation and cell surface expression of CD36 and
CC involved in macrophage uptake of low-density lipoprotein and in foam
CC cell formation (PubMed:23444136). Together with ZDHHC6, required for
CC palmitoylation of ITPR1 in immune cells, leading to regulate ITPR1
CC stability and function (PubMed:25368151). Plays a role in protection of
CC cells from ER stress-induced apoptosis (By similarity). Protects cells
CC from oxidative stress when overexpressed in cardiomyocytes (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y6D0,
CC ECO:0000269|PubMed:21220695, ECO:0000269|PubMed:23444136,
CC ECO:0000269|PubMed:25368151}.
CC -!- SUBUNIT: Interacts with DERL1, DERL2, DERL3 and SELENOS
CC (PubMed:22016385). The SELENOK-SELENOS complex interacts with VCP (By
CC similarity). Interacts with ZDHHC6 (PubMed:25368151).
CC {ECO:0000250|UniProtKB:Q9Y6D0, ECO:0000269|PubMed:22016385}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21220695}; 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:0000269|PubMed:21220695}.
CC -!- TISSUE SPECIFICITY: High expression in spleen and intestine (at protein
CC level). Expressed in a range of immune cells including T and B-cells
CC and also in myeloid cells including macrophages, neutrophils and
CC dendritic cells (at protein level). {ECO:0000269|PubMed:21220695,
CC ECO:0000269|PubMed:21849499}.
CC -!- INDUCTION: By increased dietary selenium. Expression is significantly
CC decreased by a low selenium diet. {ECO:0000269|PubMed:21220695}.
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. {ECO:0000269|PubMed:21849499}.
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 -!- DISRUPTION PHENOTYPE: Normal growth, fertility and immune system
CC development. Reduced receptor-mediated Ca(2+) flux in T-cells,
CC neutrophils and macrophages. Reduced T-cell proliferation and reduced
CC T-cell and neutrophil migration. Decreased viral clearance and
CC increased mortality following infection with West Nile virus. Bone
CC marrow-derived macrophages from knockout mice display decreased uptake
CC of acetylated or oxidized low-density lipoprotein, reduced foam cell
CC formation and decreased palmitoylation and cell surface expression of
CC CD36. {ECO:0000269|PubMed:21220695, ECO:0000269|PubMed:23444136}.
CC -!- SIMILARITY: Belongs to the selenoprotein K family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF27311.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF170920; AAF27311.1; ALT_SEQ; mRNA.
DR EMBL; AK003206; BAB22642.2; -; mRNA.
DR EMBL; AK006674; BAB24699.2; -; mRNA.
DR EMBL; AK007523; BAB25088.2; -; mRNA.
DR EMBL; AK008419; BAB25657.2; -; mRNA.
DR EMBL; BC038049; AAH38049.3; -; mRNA.
DR EMBL; BC096044; AAH96044.1; -; mRNA.
DR EMBL; BC096677; AAH96677.2; -; mRNA.
DR CCDS; CCDS36844.1; -.
DR RefSeq; NP_064363.2; NM_019979.2.
DR BioGRID; 219813; 1.
DR STRING; 10090.ENSMUSP00000107887; -.
DR iPTMnet; Q9JLJ1; -.
DR PhosphoSitePlus; Q9JLJ1; -.
DR EPD; Q9JLJ1; -.
DR MaxQB; Q9JLJ1; -.
DR PaxDb; Q9JLJ1; -.
DR PeptideAtlas; Q9JLJ1; -.
DR PRIDE; Q9JLJ1; -.
DR ProteomicsDB; 256769; -.
DR Antibodypedia; 1553; 86 antibodies from 21 providers.
DR DNASU; 80795; -.
DR Ensembl; ENSMUST00000112268; ENSMUSP00000107887; ENSMUSG00000042682.
DR GeneID; 80795; -.
DR KEGG; mmu:80795; -.
DR UCSC; uc007sul.1; mouse.
DR CTD; 58515; -.
DR MGI; MGI:1931466; Selenok.
DR VEuPathDB; HostDB:ENSMUSG00000042682; -.
DR eggNOG; ENOG502S3PW; Eukaryota.
DR GeneTree; ENSGT00390000016119; -.
DR HOGENOM; CLU_182590_0_1_1; -.
DR InParanoid; Q9JLJ1; -.
DR OMA; FWGIADF; -.
DR OrthoDB; 1566291at2759; -.
DR PhylomeDB; Q9JLJ1; -.
DR TreeFam; TF328380; -.
DR BioGRID-ORCS; 80795; 8 hits in 41 CRISPR screens.
DR ChiTaRS; Selk; mouse.
DR PRO; PR:Q9JLJ1; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q9JLJ1; protein.
DR Bgee; ENSMUSG00000042682; Expressed in embryonic brain and 249 other tissues.
DR ExpressionAtlas; Q9JLJ1; baseline and differential.
DR Genevisible; Q9JLJ1; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:MGI.
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:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; IMP:MGI.
DR GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; IBA:GO_Central.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:MGI.
DR GO; GO:0010742; P:macrophage derived foam cell differentiation; IMP:MGI.
DR GO; GO:1990266; P:neutrophil migration; IMP:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:UniProtKB.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IMP:UniProtKB.
DR GO; GO:1902624; P:positive regulation of neutrophil migration; IMP:MGI.
DR GO; GO:2000406; P:positive regulation of T cell migration; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:UniProtKB.
DR GO; GO:0018345; P:protein palmitoylation; IDA:UniProtKB.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IMP:UniProtKB.
DR GO; GO:0051223; P:regulation of protein transport; IMP:MGI.
DR GO; GO:0045728; P:respiratory burst after phagocytosis; IMP:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISO:MGI.
DR GO; GO:0072678; P:T cell migration; IMP:MGI.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR InterPro; IPR024491; Se_SelK/SelG.
DR PANTHER; PTHR16875; PTHR16875; 1.
DR Pfam; PF10961; SelK_SelG; 1.
PE 1: Evidence at protein level;
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_0000097670"
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 50..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 81..82
FT /note="Cleavage; by CAPN2"
FT NON_STD 92
FT /note="Selenocysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 94 AA; 10642 MW; 840B51DC9CF7B8F2 CRC64;
MVYISNGQVL DSRNQSPWRV SFLTDFFWGI AEFVVFFFKT LLQQDVKKRR GYGSSSDSRY
DDGRGPPGNP PRRMGRISHL RGPSPPPMAG GUGR
