ID   SEP15_HUMAN             Reviewed;         165 AA.
AC   O60613; A0A0B4J1S4; Q4GZG7; Q8WU00; Q9BS64; Q9GZW0; Q9NR01;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   28-MAR-2018, sequence version 4.
DT   13-FEB-2019, entry version 163.
DE   RecName: Full=Selenoprotein F {ECO:0000303|PubMed:27645994};
DE   AltName: Full=15 kDa selenoprotein {ECO:0000303|PubMed:9535873};
DE   Flags: Precursor;
GN   Name=SELENOF {ECO:0000303|PubMed:27645994,
GN   ECO:0000312|HGNC:HGNC:17705};
GN   Synonyms=SEP15 {ECO:0000303|PubMed:11278576};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX   PubMed=10945981; DOI=10.1074/jbc.M004014200;
RA   Kumaraswamy E., Malykh A., Korotkov K.V., Kozyavkin S., Hu Y.,
RA   Kwon S.Y., Moustafa M.E., Carlson B.A., Berry M.J., Lee B.J.,
RA   Hatfield D.L., 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 [GENOMIC DNA].
RA   Ryu M., Moon E.;
RT   "The human 15-kDa selenoprotein gene: characterisation of the genomic
RT   structure and functional analysis of the promoter.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Endometrium;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Bone marrow, and Kidney;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 3-165 (ISOFORM 1), PROTEIN SEQUENCE OF
RP   101-109; 126-130 AND 149-161, TISSUE SPECIFICITY, AND MASS
RP   SPECTROMETRY.
RX   PubMed=9535873; DOI=10.1074/jbc.273.15.8910;
RA   Gladyshev V.N., Jeang K.-T., Wootton J.C., Hatfield D.L.;
RT   "A new human selenium-containing protein. Purification,
RT   characterization, and cDNA sequence.";
RL   J. Biol. Chem. 273:8910-8915(1998).
RN   [7]
RP   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-
RT   glucose:glycoprotein glucosyltransferase in the endoplasmic reticulum
RT   of mammalian cells.";
RL   J. Biol. Chem. 276:15330-15336(2001).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [10]
RP   NOMENCLATURE.
RX   PubMed=27645994; DOI=10.1074/jbc.M116.756155;
RA   Gladyshev V.N., Arner E.S., Berry M.J., Brigelius-Flohe R.,
RA   Bruford E.A., Burk R.F., Carlson B.A., Castellano S., Chavatte L.,
RA   Conrad M., Copeland P.R., Diamond A.M., Driscoll D.M., Ferreiro A.,
RA   Flohe L., Green F.R., Guigo R., Handy D.E., Hatfield D.L., Hesketh J.,
RA   Hoffmann P.R., Holmgren A., Hondal R.J., Howard M.T., Huang K.,
RA   Kim H.Y., Kim I.Y., Koehrle J., Krol A., Kryukov G.V., Lee B.J.,
RA   Lee B.C., Lei X.G., Liu Q., Lescure A., Lobanov A.V., Loscalzo J.,
RA   Maiorino M., Mariotti M., Sandeep Prabhu K., Rayman M.P., Rozovsky S.,
RA   Salinas G., Schmidt E.E., Schomburg L., Schweizer U., Simonovic M.,
RA   Sunde R.A., Tsuji P.A., Tweedie S., Ursini F., Whanger P.D., Zhang Y.;
RT   "Selenoprotein gene nomenclature.";
RL   J. Biol. Chem. 291:24036-24040(2016).
RN   [11]
RP   INTERACTION WITH RDH11.
RX   PubMed=29410696; DOI=10.1186/s12986-017-0235-x;
RA   Tian J., Liu J., Li J., Zheng J., Chen L., Wang Y., Liu Q., Ni J.;
RT   "The interaction of selenoprotein F (SELENOF) with retinol
RT   dehydrogenase 11 (RDH11) implied a role of SELENOF in vitamin A
RT   metabolism.";
RL   Nutr. Metab. 15:7-7(2018).
CC   -!- FUNCTION: May be involved in redox reactions associated with the
CC       formation of disulfide bonds. May contribute to the quality
CC       control of protein folding in the endoplasmic reticulum (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a tight complex with UGGT1/UGCGL1. Interacts with
CC       RDH11 (PubMed:29410696). {ECO:0000250,
CC       ECO:0000269|PubMed:29410696}.
CC   -!- INTERACTION:
CC       Q8TC12:RDH11; NbExp=5; IntAct=EBI-1052797, EBI-2823756;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC       {ECO:0000269|PubMed:11278576}. Note=The association with
CC       UGGT1/UGCGL1 is essential for its retention in the endoplasmic
CC       reticulum.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O60613-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O60613-2; Sequence=VSP_014695, VSP_014696;
CC         Note=No experimental confirmation available.;
CC   -!- TISSUE SPECIFICITY: Higher levels in prostate and thyroid gland.
CC       {ECO:0000269|PubMed:9535873}.
CC   -!- PTM: The N-terminus is blocked.
CC   -!- MASS SPECTROMETRY: Mass=14870; Method=Electrospray; Range=29-165;
CC       Evidence={ECO:0000269|PubMed:9535873};
CC   -!- MASS SPECTROMETRY: Mass=14830; Method=MALDI; Range=29-165;
CC       Evidence={ECO:0000269|PubMed:9535873};
CC   -!- SIMILARITY: Belongs to the selenoprotein M/F family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC15478.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAF78966.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAG31556.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAG31557.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=CAJ18323.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/SEP15ID42260ch1p22.html";
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DR   EMBL; AF288991; AAG31556.1; ALT_INIT; mRNA.
DR   EMBL; AF288992; AAG31557.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AF267982; AAF78966.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL833575; CAJ18323.1; ALT_INIT; mRNA.
DR   EMBL; AL121989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005294; AAH05294.3; -; mRNA.
DR   EMBL; BC016359; AAH16359.3; -; mRNA.
DR   EMBL; BC021697; AAH21697.3; -; mRNA.
DR   EMBL; AF051894; AAC15478.1; ALT_INIT; mRNA.
DR   CCDS; CCDS76177.1; -. [O60613-2]
DR   CCDS; CCDS76178.1; -. [O60613-1]
DR   RefSeq; NP_004252.2; NM_004261.4. [O60613-1]
DR   RefSeq; NP_976086.1; NM_203341.2. [O60613-2]
DR   UniGene; Hs.362728; -.
DR   ProteinModelPortal; O60613; -.
DR   BioGrid; 114800; 28.
DR   IntAct; O60613; 12.
DR   MINT; O60613; -.
DR   STRING; 9606.ENSP00000328729; -.
DR   iPTMnet; O60613; -.
DR   PhosphoSitePlus; O60613; -.
DR   SwissPalm; O60613; -.
DR   BioMuta; SELENOF; -.
DR   EPD; O60613; -.
DR   jPOST; O60613; -.
DR   PaxDb; O60613; -.
DR   PeptideAtlas; O60613; -.
DR   PRIDE; O60613; -.
DR   ProteomicsDB; 49486; -.
DR   ProteomicsDB; 49487; -. [O60613-2]
DR   DNASU; 9403; -.
DR   Ensembl; ENST00000331835; ENSP00000328729; ENSG00000183291. [O60613-1]
DR   Ensembl; ENST00000370554; ENSP00000359585; ENSG00000183291. [O60613-2]
DR   GeneID; 9403; -.
DR   KEGG; hsa:9403; -.
DR   CTD; 9403; -.
DR   DisGeNET; 9403; -.
DR   EuPathDB; HostDB:ENSG00000183291.15; -.
DR   GeneCards; SELENOF; -.
DR   HGNC; HGNC:17705; SELENOF.
DR   HPA; HPA054937; -.
DR   MIM; 606254; gene.
DR   neXtProt; NX_O60613; -.
DR   OpenTargets; ENSG00000183291; -.
DR   eggNOG; KOG3384; Eukaryota.
DR   eggNOG; ENOG4111MSS; LUCA.
DR   GeneTree; ENSGT00940000154284; -.
DR   HOGENOM; HOG000238561; -.
DR   HOVERGEN; HBG108472; -.
DR   InParanoid; O60613; -.
DR   OMA; VCTCKFG; -.
DR   OrthoDB; 1393196at2759; -.
DR   PhylomeDB; O60613; -.
DR   ChiTaRS; SELENOF; human.
DR   GeneWiki; SEP15; -.
DR   GenomeRNAi; 9403; -.
DR   PRO; PR:O60613; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000183291; Expressed in 237 organ(s), highest expression level in palpebral conjunctiva.
DR   ExpressionAtlas; O60613; baseline and differential.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR   GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:UniProtKB.
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   Alternative splicing; Complete proteome; Direct protein sequencing;
KW   Endoplasmic reticulum; Reference proteome; Selenocysteine; Signal.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   CHAIN        32    165       Selenoprotein F.
FT                                /FTId=PRO_0000022307.
FT   NON_STD      96     96       Selenocysteine.
FT   VAR_SEQ     106    124       AFVRSDKPKLFRGLQIKYV -> VCPWFRPCIKAFGRQWEH
FT                                C (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_014695.
FT   VAR_SEQ     125    165       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_014696.
SQ   SEQUENCE   165 AA;  18092 MW;  E20C44FAB97AD336 CRC64;
     MVAMAAGPSG CLVPAFGLRL LLATVLQAVS AFGAEFSSEA CRELGFSSNL LCSSCDLLGQ
     FNLLQLDPDC RGCCQEEAQF ETKKLYAGAI LEVCGUKLGR FPQVQAFVRS DKPKLFRGLQ
     IKYVRGSDPV LKLLDDNGNI AEELSILKWN TDSVEEFLSE KLERI
//