Full text data of SEP15
SEP15
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
15 kDa selenoprotein; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
15 kDa selenoprotein; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O60613
ID SEP15_HUMAN Reviewed; 162 AA.
AC O60613; Q4GZG7; Q8WU00; Q9BS64; Q9GZW0; Q9NR01;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 26-FEB-2008, sequence version 3.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=15 kDa selenoprotein;
DE Flags: Precursor;
GN Name=SEP15;
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 [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 98-106;
RP 123-127 AND 146-158, 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,
RT characterization, and cDNA sequence.";
RL J. Biol. Chem. 273:8910-8915(1998).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [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).
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).
CC -!- SUBUNIT: Forms a tight complex with UGGT1/UGCGL1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=The
CC association with UGGT1/UGCGL1 is essential for its retention in
CC 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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Higher levels in prostate and thyroid gland.
CC -!- PTM: The N-terminus is blocked.
CC -!- MASS SPECTROMETRY: Mass=14870; Method=Electrospray; Range=26-162;
CC Source=PubMed:9535873;
CC -!- MASS SPECTROMETRY: Mass=14830; Method=MALDI; Range=26-162;
CC Source=PubMed:9535873;
CC -!- SIMILARITY: Belongs to the selenoprotein M/SEP15 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05294.3; Type=Erroneous initiation;
CC Sequence=AAH16359.3; Type=Erroneous initiation;
CC Sequence=AAH21697.3; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SEP15ID42260ch1p22.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF051894; AAC15478.1; -; mRNA.
DR EMBL; AF288991; AAG31556.1; -; mRNA.
DR EMBL; AF288992; AAG31557.1; -; Genomic_DNA.
DR EMBL; AF267982; AAF78966.1; -; Genomic_DNA.
DR EMBL; AL833575; CAJ18323.1; -; mRNA.
DR EMBL; AL121989; CAC04186.1; -; Genomic_DNA.
DR EMBL; BC005294; AAH05294.3; ALT_INIT; mRNA.
DR EMBL; BC016359; AAH16359.3; ALT_INIT; mRNA.
DR EMBL; BC021697; AAH21697.3; ALT_INIT; mRNA.
DR RefSeq; NP_004252.2; NM_004261.3.
DR RefSeq; NP_976086.1; NM_203341.1.
DR UniGene; Hs.362728; -.
DR ProteinModelPortal; O60613; -.
DR SMR; O60613; 74-161.
DR IntAct; O60613; 3.
DR PhosphoSite; O60613; -.
DR PaxDb; O60613; -.
DR PRIDE; O60613; -.
DR DNASU; 9403; -.
DR GeneID; 9403; -.
DR KEGG; hsa:9403; -.
DR UCSC; uc021oph.1; human.
DR CTD; 9403; -.
DR GeneCards; GC01M087328; -.
DR MIM; 606254; gene.
DR neXtProt; NX_O60613; -.
DR eggNOG; NOG243434; -.
DR HOGENOM; HOG000238561; -.
DR HOVERGEN; HBG108472; -.
DR InParanoid; O60613; -.
DR OMA; VCTCKFG; -.
DR PhylomeDB; O60613; -.
DR GeneWiki; SEP15; -.
DR GenomeRNAi; 9403; -.
DR NextBio; 35227; -.
DR PRO; PR:O60613; -.
DR ArrayExpress; O60613; -.
DR Genevestigator; O60613; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0008430; F:selenium binding; IDA:UniProtKB.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:UniProtKB.
DR InterPro; IPR014912; Sep15_SelM.
DR InterPro; IPR012336; Thioredoxin-like_fold.
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 28 Potential.
FT CHAIN 29 162 15 kDa selenoprotein.
FT /FTId=PRO_0000022307.
FT NON_STD 93 93 Selenocysteine.
FT VAR_SEQ 103 121 AFVRSDKPKLFRGLQIKYV -> VCPWFRPCIKAFGRQWEH
FT C (in isoform 2).
FT /FTId=VSP_014695.
FT VAR_SEQ 122 162 Missing (in isoform 2).
FT /FTId=VSP_014696.
SQ SEQUENCE 162 AA; 17790 MW; 55E382B423AA731E CRC64;
MAAGPSGCLV PAFGLRLLLA TVLQAVSAFG AEFSSEACRE LGFSSNLLCS SCDLLGQFNL
LQLDPDCRGC CQEEAQFETK KLYAGAILEV CGUKLGRFPQ VQAFVRSDKP KLFRGLQIKY
VRGSDPVLKL LDDNGNIAEE LSILKWNTDS VEEFLSEKLE RI
//
ID SEP15_HUMAN Reviewed; 162 AA.
AC O60613; Q4GZG7; Q8WU00; Q9BS64; Q9GZW0; Q9NR01;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
read moreDT 26-FEB-2008, sequence version 3.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=15 kDa selenoprotein;
DE Flags: Precursor;
GN Name=SEP15;
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 [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 98-106;
RP 123-127 AND 146-158, 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,
RT characterization, and cDNA sequence.";
RL J. Biol. Chem. 273:8910-8915(1998).
RN [2]
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 [3]
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 [4]
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 [5]
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 [6]
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 [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).
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).
CC -!- SUBUNIT: Forms a tight complex with UGGT1/UGCGL1 (By similarity).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen. Note=The
CC association with UGGT1/UGCGL1 is essential for its retention in
CC 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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Higher levels in prostate and thyroid gland.
CC -!- PTM: The N-terminus is blocked.
CC -!- MASS SPECTROMETRY: Mass=14870; Method=Electrospray; Range=26-162;
CC Source=PubMed:9535873;
CC -!- MASS SPECTROMETRY: Mass=14830; Method=MALDI; Range=26-162;
CC Source=PubMed:9535873;
CC -!- SIMILARITY: Belongs to the selenoprotein M/SEP15 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05294.3; Type=Erroneous initiation;
CC Sequence=AAH16359.3; Type=Erroneous initiation;
CC Sequence=AAH21697.3; Type=Erroneous initiation;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SEP15ID42260ch1p22.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF051894; AAC15478.1; -; mRNA.
DR EMBL; AF288991; AAG31556.1; -; mRNA.
DR EMBL; AF288992; AAG31557.1; -; Genomic_DNA.
DR EMBL; AF267982; AAF78966.1; -; Genomic_DNA.
DR EMBL; AL833575; CAJ18323.1; -; mRNA.
DR EMBL; AL121989; CAC04186.1; -; Genomic_DNA.
DR EMBL; BC005294; AAH05294.3; ALT_INIT; mRNA.
DR EMBL; BC016359; AAH16359.3; ALT_INIT; mRNA.
DR EMBL; BC021697; AAH21697.3; ALT_INIT; mRNA.
DR RefSeq; NP_004252.2; NM_004261.3.
DR RefSeq; NP_976086.1; NM_203341.1.
DR UniGene; Hs.362728; -.
DR ProteinModelPortal; O60613; -.
DR SMR; O60613; 74-161.
DR IntAct; O60613; 3.
DR PhosphoSite; O60613; -.
DR PaxDb; O60613; -.
DR PRIDE; O60613; -.
DR DNASU; 9403; -.
DR GeneID; 9403; -.
DR KEGG; hsa:9403; -.
DR UCSC; uc021oph.1; human.
DR CTD; 9403; -.
DR GeneCards; GC01M087328; -.
DR MIM; 606254; gene.
DR neXtProt; NX_O60613; -.
DR eggNOG; NOG243434; -.
DR HOGENOM; HOG000238561; -.
DR HOVERGEN; HBG108472; -.
DR InParanoid; O60613; -.
DR OMA; VCTCKFG; -.
DR PhylomeDB; O60613; -.
DR GeneWiki; SEP15; -.
DR GenomeRNAi; 9403; -.
DR NextBio; 35227; -.
DR PRO; PR:O60613; -.
DR ArrayExpress; O60613; -.
DR Genevestigator; O60613; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB.
DR GO; GO:0008430; F:selenium binding; IDA:UniProtKB.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:UniProtKB.
DR InterPro; IPR014912; Sep15_SelM.
DR InterPro; IPR012336; Thioredoxin-like_fold.
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 28 Potential.
FT CHAIN 29 162 15 kDa selenoprotein.
FT /FTId=PRO_0000022307.
FT NON_STD 93 93 Selenocysteine.
FT VAR_SEQ 103 121 AFVRSDKPKLFRGLQIKYV -> VCPWFRPCIKAFGRQWEH
FT C (in isoform 2).
FT /FTId=VSP_014695.
FT VAR_SEQ 122 162 Missing (in isoform 2).
FT /FTId=VSP_014696.
SQ SEQUENCE 162 AA; 17790 MW; 55E382B423AA731E CRC64;
MAAGPSGCLV PAFGLRLLLA TVLQAVSAFG AEFSSEACRE LGFSSNLLCS SCDLLGQFNL
LQLDPDCRGC CQEEAQFETK KLYAGAILEV CGUKLGRFPQ VQAFVRSDKP KLFRGLQIKY
VRGSDPVLKL LDDNGNIAEE LSILKWNTDS VEEFLSEKLE RI
//
MIM
606254
*RECORD*
*FIELD* NO
606254
*FIELD* TI
*606254 SELENOPROTEIN, 15-KD
;;SEP15
*FIELD* TX
Nutritional and biochemical studies have implicated selenium in
read moreimmunologic and other biologic processes. In mammals, selenium is found
not as a cofactor but as a selenocysteine residue, sometimes termed the
twenty-first amino acid, encoded by UGA. In order for the UGA codon to
be translated correctly, rather than as a stop codon, a stem-loop
structure called a selenocysteine insertion sequence, or SECIS, element
in the 3-prime untranslated region (UTR) of selenoprotein mRNA is
essential.
CLONING
By culturing a T-cell line in the presence of selenium, SDS-PAGE
analysis, biochemical purification of a 15-kD protein, micropeptide
sequence analysis, and EST database searching, Gladyshev et al. (1998)
obtained a cDNA encoding SEP15. The deduced 162-amino acid protein has
an N-terminal signal peptide. SEP15 mRNA contains a SECIS element in its
3-prime UTR.
Using Northern blot analysis, Kumaraswamy et al. (2000) detected high
expression of a 1.3-kb SEP15 transcript in prostate, liver, brain,
kidney, and testis; expression was low in skeletal muscle, mammary
gland, and trachea. They noted that selenium supplementation trials had
shown reduced cancer incidence in prostate and liver, where SEP15 was
highly expressed.
MOLECULAR GENETICS
Kumaraswamy et al. (2000) found that an A-to-G polymorphism at position
1125 in the SECIS of SEP15 results in increased responses to selenium in
terms of luciferase activity.
GENE STRUCTURE
Kumaraswamy et al. (2000) determined that the SEP15 gene contains 5
exons, with the TGA codon for sec located in exon 3, and spans 51 kb.
MAPPING
By analysis of ESTs corresponding to the SEP15 gene, Gladyshev et al.
(1998) mapped the SEP15 gene to 1p31, a region frequently deleted or
altered in cancer.
*FIELD* RF
1. Gladyshev, V. N.; Jeang, K.-T.; Wootton, J. C.; Hatfield, D. L.
: A new human selenium-containing protein: purification, characterization,
and cDNA sequence. J. Biol. Chem. 273: 8910-8915, 1998.
2. Kumaraswamy, E.; Malykh, A.; Korotkov, K. V.; Kozyavkin, S.; Hu,
Y.; Kwon, S. Y.; Moustafa, M. E.; Carlson, B. A.; Berry, M. J.; Lee,
B. J.; Hatfield, D. L.; Diamond, A. M.; Gladyshev, V. N.: Structure-expression
relationships of the 15-kDa selenoprotein gene: possible role of the
protein in cancer etiology. J. Biol. Chem. 275: 35540-35547, 2000.
*FIELD* CD
Paul J. Converse: 9/6/2001
*FIELD* ED
wwang: 07/29/2009
mgross: 9/6/2001
*RECORD*
*FIELD* NO
606254
*FIELD* TI
*606254 SELENOPROTEIN, 15-KD
;;SEP15
*FIELD* TX
Nutritional and biochemical studies have implicated selenium in
read moreimmunologic and other biologic processes. In mammals, selenium is found
not as a cofactor but as a selenocysteine residue, sometimes termed the
twenty-first amino acid, encoded by UGA. In order for the UGA codon to
be translated correctly, rather than as a stop codon, a stem-loop
structure called a selenocysteine insertion sequence, or SECIS, element
in the 3-prime untranslated region (UTR) of selenoprotein mRNA is
essential.
CLONING
By culturing a T-cell line in the presence of selenium, SDS-PAGE
analysis, biochemical purification of a 15-kD protein, micropeptide
sequence analysis, and EST database searching, Gladyshev et al. (1998)
obtained a cDNA encoding SEP15. The deduced 162-amino acid protein has
an N-terminal signal peptide. SEP15 mRNA contains a SECIS element in its
3-prime UTR.
Using Northern blot analysis, Kumaraswamy et al. (2000) detected high
expression of a 1.3-kb SEP15 transcript in prostate, liver, brain,
kidney, and testis; expression was low in skeletal muscle, mammary
gland, and trachea. They noted that selenium supplementation trials had
shown reduced cancer incidence in prostate and liver, where SEP15 was
highly expressed.
MOLECULAR GENETICS
Kumaraswamy et al. (2000) found that an A-to-G polymorphism at position
1125 in the SECIS of SEP15 results in increased responses to selenium in
terms of luciferase activity.
GENE STRUCTURE
Kumaraswamy et al. (2000) determined that the SEP15 gene contains 5
exons, with the TGA codon for sec located in exon 3, and spans 51 kb.
MAPPING
By analysis of ESTs corresponding to the SEP15 gene, Gladyshev et al.
(1998) mapped the SEP15 gene to 1p31, a region frequently deleted or
altered in cancer.
*FIELD* RF
1. Gladyshev, V. N.; Jeang, K.-T.; Wootton, J. C.; Hatfield, D. L.
: A new human selenium-containing protein: purification, characterization,
and cDNA sequence. J. Biol. Chem. 273: 8910-8915, 1998.
2. Kumaraswamy, E.; Malykh, A.; Korotkov, K. V.; Kozyavkin, S.; Hu,
Y.; Kwon, S. Y.; Moustafa, M. E.; Carlson, B. A.; Berry, M. J.; Lee,
B. J.; Hatfield, D. L.; Diamond, A. M.; Gladyshev, V. N.: Structure-expression
relationships of the 15-kDa selenoprotein gene: possible role of the
protein in cancer etiology. J. Biol. Chem. 275: 35540-35547, 2000.
*FIELD* CD
Paul J. Converse: 9/6/2001
*FIELD* ED
wwang: 07/29/2009
mgross: 9/6/2001