ID   SEP15_RAT               Reviewed;         162 AA.
AC   Q923V8;
DT   31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 3.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Selenoprotein F {ECO:0000250|UniProtKB:O60613};
DE   AltName: Full=15 kDa selenoprotein {ECO:0000303|PubMed:11278576};
DE   Flags: Precursor;
GN   Name=Selenof {ECO:0000250|UniProtKB:O60613};
GN   Synonyms=Sep15 {ECO:0000312|RGD:621291};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Roethlein D., Kyriakopoulos A., Behne D.;
RT   "A 15 kDa-selenoprotein in several tissues of the rat.";
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
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   [3]
RP   FUNCTION, INTERACTION WITH UGGT1, AND SUBCELLULAR LOCATION.
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   [4]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15659830; DOI=10.1196/annals.1329.057;
RA   Kyriakopoulos A., Bukalis K., Roethlein D., Hoppe B., Graebert A.,
RA   Behne D.;
RT   "Prevention against oxidative stress of eukaryotic cell membranes by
RT   selenium compounds of the rat.";
RL   Ann. N. Y. Acad. Sci. 1030:458-461(2004).
CC   -!- FUNCTION: May be involved in redox reactions associated with the
CC       formation of disulfide bonds (PubMed:15659830). May contribute to the
CC       quality control of protein folding in the endoplasmic reticulum
CC       (PubMed:11278576). May regulate protein folding by enhancing the
CC       catalytic activity of UGGT1/UGCGL1 and UGGT2/UGCGL2 (By similarity).
CC       {ECO:0000250|UniProtKB:O60613, ECO:0000269|PubMed:11278576,
CC       ECO:0000269|PubMed:15659830}.
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
CC       {ECO:0000269|PubMed:11278576}. Note=The association with UGGT1/UGCGL1
CC       is essential for its retention in the endoplasmic reticulum.
CC   -!- TISSUE SPECIFICITY: Highest levels in prostate, lower levels in brain,
CC       lung, thyroid gland, and large intestine.
CC       {ECO:0000269|PubMed:15659830}.
CC   -!- SIMILARITY: Belongs to the selenoprotein M/F family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF390544; AAK73100.1; -; mRNA.
DR   EMBL; BC060547; AAH60547.1; -; mRNA.
DR   RefSeq; NP_579831.2; NM_133297.2.
DR   CORUM; Q923V8; -.
DR   IntAct; Q923V8; 1.
DR   jPOST; Q923V8; -.
DR   PRIDE; Q923V8; -.
DR   Ensembl; ENSRNOT00000083750; ENSRNOP00000075579; ENSRNOG00000055257.
DR   GeneID; 113922; -.
DR   KEGG; rno:113922; -.
DR   CTD; 9403; -.
DR   RGD; 621291; Selenof.
DR   GeneTree; ENSGT00940000154284; -.
DR   InParanoid; Q923V8; -.
DR   OrthoDB; 1405992at2759; -.
DR   PhylomeDB; Q923V8; -.
DR   TreeFam; TF315117; -.
DR   PRO; PR:Q923V8; -.
DR   Proteomes; UP000002494; Chromosome 2.
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; IDA:UniProtKB.
DR   GO; GO:0008379; F:thioredoxin peroxidase activity; IDA:RGD.
DR   GO; GO:0051084; P:'de novo' post-translational protein folding; TAS:UniProtKB.
DR   GO; GO:0035092; P:sperm DNA condensation; IMP:RGD.
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_0000022310"
FT   NON_STD         93
FT                   /note="Selenocysteine"
SQ   SEQUENCE   162 AA;  17822 MW;  604590968C81885C CRC64;
     MAAGQGGWLR PALGLRLLLA TAFQAVSALG AEFSSEACRE LGFSSNLLCS SCDLLGQFNL
     LPLDPVCRGC CQEEAQFETK KLYAGAILEV CGUKLGRFPQ VQAFVRSDKP KLFRGLQIKY
     VRGSDPVLKL LDDNGNIAEE LSILKWNTDS VEEFLSEKLE RI