SEP15_MOUSE
ID SEP15_MOUSE Reviewed; 162 AA.
AC Q9ERR7; Q3TXW1; Q544W8; Q8VE40;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Selenoprotein F {ECO:0000250|UniProtKB:O60613};
DE AltName: Full=15 kDa selenoprotein {ECO:0000303|PubMed:10945981};
DE Flags: Precursor;
GN Name=Selenof {ECO:0000312|MGI:MGI:1927947};
GN Synonyms=Sep15 {ECO:0000312|MGI:MGI:1927947};
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].
RX PubMed=10945981; DOI=10.1074/jbc.m004014200;
RA Kumaraswamy E., Malykh A., Korotkov K.V., Kozyavkin S., Hu Y., Kwon S.Y.,
RA Moustafa M.E., Carlson B.A., Berry M.J., Lee B.J., Hatfield D.L.,
RA Diamond A.M., Gladyshev V.N.;
RT "Structure-expression relationships of the 15-kDa selenoprotein gene.
RT Possible role of the protein in cancer etiology.";
RL J. Biol. Chem. 275:35540-35547(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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=FVB/N-3; TISSUE=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 INTERACTION WITH UGGT1.
RX PubMed=11278576; DOI=10.1074/jbc.m009861200;
RA Korotkov K.V., Kumaraswamy E., Zhou Y., Hatfield D.L., Gladyshev V.N.;
RT "Association between the 15-kDa selenoprotein and UDP-glucose:glycoprotein
RT glucosyltransferase in the endoplasmic reticulum of mammalian cells.";
RL J. Biol. Chem. 276:15330-15336(2001).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May be involved in redox reactions associated with the
CC formation of disulfide bonds (By similarity). May contribute to the
CC quality control of protein folding in the endoplasmic reticulum. May
CC regulate protein folding by enhancing the catalytic activity of
CC UGGT1/UGCGL1 and UGGT2/UGCGL2 (By similarity).
CC {ECO:0000250|UniProtKB:O60613, ECO:0000250|UniProtKB:Q923V8}.
CC -!- SUBUNIT: Forms a tight complex with UGGT1/UGCGL1 (PubMed:11278576).
CC Interacts with UGGT2/UGCGL2 (By similarity). Interacts with RDH11 (By
CC similarity). {ECO:0000250|UniProtKB:O60613,
CC ECO:0000269|PubMed:11278576}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250}.
CC Note=The association with UGGT1/UGCGL1 is essential for its retention
CC in the endoplasmic reticulum. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the selenoprotein M/F family. {ECO:0000305}.
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DR EMBL; AF288740; AAG31765.1; -; mRNA.
DR EMBL; AK020419; BAC55255.1; -; mRNA.
DR EMBL; AK159085; BAE34803.1; -; mRNA.
DR EMBL; AK159353; BAE35012.1; -; mRNA.
DR EMBL; BC019792; AAH19792.2; -; mRNA.
DR CCDS; CCDS17884.1; -.
DR RefSeq; NP_444332.1; NM_053102.2.
DR BioGRID; 220234; 4.
DR IntAct; Q9ERR7; 1.
DR STRING; 10090.ENSMUSP00000046910; -.
DR iPTMnet; Q9ERR7; -.
DR PhosphoSitePlus; Q9ERR7; -.
DR EPD; Q9ERR7; -.
DR jPOST; Q9ERR7; -.
DR MaxQB; Q9ERR7; -.
DR PaxDb; Q9ERR7; -.
DR PeptideAtlas; Q9ERR7; -.
DR PRIDE; Q9ERR7; -.
DR ProteomicsDB; 256779; -.
DR GeneID; 93684; -.
DR KEGG; mmu:93684; -.
DR UCSC; uc008rpr.1; mouse.
DR CTD; 9403; -.
DR MGI; MGI:1927947; Selenof.
DR eggNOG; KOG3384; Eukaryota.
DR InParanoid; Q9ERR7; -.
DR OrthoDB; 1405992at2759; -.
DR PhylomeDB; Q9ERR7; -.
DR TreeFam; TF315117; -.
DR BioGRID-ORCS; 93684; 0 hits in 46 CRISPR screens.
DR ChiTaRS; Sep15; mouse.
DR PRO; PR:Q9ERR7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9ERR7; protein.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008430; F:selenium binding; ISO:MGI.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; ISO:MGI.
DR GO; GO:0051084; P:'de novo' post-translational protein folding; TAS:UniProtKB.
DR GO; GO:0035092; P:sperm DNA condensation; ISO:MGI.
DR Gene3D; 3.40.30.50; -; 1.
DR InterPro; IPR038219; Sep15/SelM_sf.
DR InterPro; IPR039992; Sep15_SelM.
DR InterPro; IPR014912; Sep15_SelM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR13077; PTHR13077; 1.
DR Pfam; PF08806; Sep15_SelM; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Reference proteome; Selenocysteine; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..162
FT /note="Selenoprotein F"
FT /id="PRO_0000022308"
FT NON_STD 93
FT /note="Selenocysteine"
FT CONFLICT 26
FT /note="V -> A (in Ref. 1; AAG31765 and 2; BAE35012/
FT BAC55255)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="F -> L (in Ref. 3; AAH19792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 162 AA; 17806 MW; 6EFF88F68C81903C CRC64;
MAAGQGGWLR PALGLRLLLA TAFQAVSALG AEFASEACRE LGFSSNLLCS SCDLLGQFNL
LPLDPVCRGC CQEEAQFETK KLYAGAILEV CGUKLGRFPQ VQAFVRSDKP KLFRGLQIKY
VRGSDPVLKL LDDNGNIAEE LSILKWNTDS VEEFLSEKLE RI
