SEP15_HUMAN
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 03-AUG-2022, entry version 182.
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, ECO:0000312|HGNC:HGNC:17705};
GN Synonyms=SEP15 {ECO:0000303|PubMed:11278576};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., 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 [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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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 project:
RT 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 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, characterization,
RT 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-glucose:glycoprotein
RT glucosyltransferase in the endoplasmic reticulum 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., Buerckstuemmer T.,
RA 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., Ayoub D.,
RA 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., Bruford E.A.,
RA Burk R.F., Carlson B.A., Castellano S., Chavatte L., Conrad M.,
RA Copeland P.R., Diamond A.M., Driscoll D.M., Ferreiro A., Flohe L.,
RA Green F.R., Guigo R., Handy D.E., Hatfield D.L., Hesketh J., Hoffmann P.R.,
RA Holmgren A., Hondal R.J., Howard M.T., Huang K., Kim H.Y., Kim I.Y.,
RA Koehrle J., Krol A., Kryukov G.V., Lee B.J., Lee B.C., Lei X.G., Liu Q.,
RA Lescure A., Lobanov A.V., Loscalzo J., Maiorino M., Mariotti M.,
RA Sandeep Prabhu K., Rayman M.P., Rozovsky S., Salinas G., Schmidt E.E.,
RA Schomburg L., Schweizer U., Simonovic M., Sunde R.A., Tsuji P.A.,
RA Tweedie S., Ursini F., Whanger P.D., Zhang Y.;
RT "Selenoprotein gene nomenclature.";
RL J. Biol. Chem. 291:24036-24040(2016).
RN [11]
RP FUNCTION, INTERACTION WITH UGGT1 AND UGGT2, AND MUTAGENESIS OF SEC-96.
RX PubMed=24415556; DOI=10.1093/glycob/cwt163;
RA Takeda Y., Seko A., Hachisu M., Daikoku S., Izumi M., Koizumi A.,
RA Fujikawa K., Kajihara Y., Ito Y.;
RT "Both isoforms of human UDP-glucose:glycoprotein glucosyltransferase are
RT enzymatically active.";
RL Glycobiology 24:344-350(2014).
RN [12]
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 dehydrogenase 11
RT (RDH11) implied a role of SELENOF in vitamin A metabolism.";
RL Nutr. Metab. 15:7-7(2018).
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
CC (PubMed:24415556). May regulate protein folding by enhancing the
CC catalytic activity of UGGT1/UGCGL1 and UGGT2/UGCGL2 (PubMed:24415556).
CC {ECO:0000250|UniProtKB:Q923V8, ECO:0000269|PubMed:24415556}.
CC -!- SUBUNIT: Forms a tight complex with UGGT1/UGCGL1 (PubMed:24415556).
CC Interacts with UGGT2/UGCGL2 (PubMed:24415556). Interacts with RDH11
CC (PubMed:29410696). {ECO:0000269|PubMed:24415556,
CC ECO:0000269|PubMed:29410696}.
CC -!- INTERACTION:
CC O60613; Q8TC12: RDH11; NbExp=5; IntAct=EBI-1052797, EBI-2823756;
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 -!- 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 -!- 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;
CC Evidence={ECO:0000269|PubMed:9535873};
CC -!- MASS SPECTROMETRY: Mass=14830; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:9535873};
CC -!- SIMILARITY: Belongs to the selenoprotein M/F family. {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=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF78966.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG31556.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG31557.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAJ18323.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC 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 BioGRID; 114800; 59.
DR IntAct; O60613; 19.
DR MINT; O60613; -.
DR STRING; 9606.ENSP00000328729; -.
DR PhosphoSitePlus; O60613; -.
DR SwissPalm; O60613; -.
DR BioMuta; SELENOF; -.
DR EPD; O60613; -.
DR jPOST; O60613; -.
DR MassIVE; O60613; -.
DR PaxDb; O60613; -.
DR PeptideAtlas; O60613; -.
DR PRIDE; O60613; -.
DR ProteomicsDB; 49486; -. [O60613-1]
DR ProteomicsDB; 49487; -. [O60613-2]
DR Antibodypedia; 46916; 33 antibodies from 11 providers.
DR DNASU; 9403; -.
DR Ensembl; ENST00000331835.10; ENSP00000328729.6; ENSG00000183291.18. [O60613-1]
DR Ensembl; ENST00000370554.5; ENSP00000359585.2; ENSG00000183291.18. [O60613-2]
DR GeneID; 9403; -.
DR KEGG; hsa:9403; -.
DR MANE-Select; ENST00000331835.10; ENSP00000328729.6; NM_004261.5; NP_004252.2.
DR CTD; 9403; -.
DR DisGeNET; 9403; -.
DR GeneCards; SELENOF; -.
DR HGNC; HGNC:17705; SELENOF.
DR HPA; ENSG00000183291; Low tissue specificity.
DR MIM; 606254; gene.
DR neXtProt; NX_O60613; -.
DR OpenTargets; ENSG00000183291; -.
DR VEuPathDB; HostDB:ENSG00000183291; -.
DR eggNOG; KOG3384; Eukaryota.
DR GeneTree; ENSGT00940000154284; -.
DR InParanoid; O60613; -.
DR OMA; FPQVQFV; -.
DR OrthoDB; 1393196at2759; -.
DR PhylomeDB; O60613; -.
DR PathwayCommons; O60613; -.
DR SignaLink; O60613; -.
DR SIGNOR; O60613; -.
DR BioGRID-ORCS; 9403; 9 hits in 212 CRISPR screens.
DR ChiTaRS; SELENOF; human.
DR GeneWiki; SEP15; -.
DR GenomeRNAi; 9403; -.
DR Pharos; O60613; Tbio.
DR PRO; PR:O60613; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60613; protein.
DR Bgee; ENSG00000183291; Expressed in islet of Langerhans and 207 other tissues.
DR ExpressionAtlas; O60613; baseline and differential.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008430; F:selenium binding; IEA:Ensembl.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:Ensembl.
DR GO; GO:0051084; P:'de novo' post-translational protein folding; TAS:UniProtKB.
DR GO; GO:0035092; P:sperm DNA condensation; IEA:Ensembl.
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; Direct protein sequencing; Endoplasmic reticulum;
KW Reference proteome; Selenocysteine; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..165
FT /note="Selenoprotein F"
FT /id="PRO_0000022307"
FT NON_STD 96
FT /note="Selenocysteine"
FT VAR_SEQ 106..124
FT /note="AFVRSDKPKLFRGLQIKYV -> VCPWFRPCIKAFGRQWEHC (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014695"
FT VAR_SEQ 125..165
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014696"
FT MUTAGEN 96
FT /note="U->C: Does not affect protein folding and binding to
FT UGGT1 or UGGT2."
FT /evidence="ECO:0000269|PubMed:24415556"
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
