Full text data of EEFSEC
EEFSEC
(SELB)
[Confidence: low (only semi-automatic identification from reviews)]
Selenocysteine-specific elongation factor (Elongation factor sec; Eukaryotic elongation factor, selenocysteine-tRNA-specific)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Selenocysteine-specific elongation factor (Elongation factor sec; Eukaryotic elongation factor, selenocysteine-tRNA-specific)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P57772
ID SELB_HUMAN Reviewed; 596 AA.
AC P57772;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-SEP-2009, sequence version 4.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Selenocysteine-specific elongation factor;
DE AltName: Full=Elongation factor sec;
DE AltName: Full=Eukaryotic elongation factor, selenocysteine-tRNA-specific;
GN Name=EEFSEC; Synonyms=SELB;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-596.
RX PubMed=10970870; DOI=10.1093/emboj/19.17.4796;
RA Fagegaltier D., Hubert N., Yamada K., Mizutani T., Carbon P., Krol A.;
RT "Characterization of mSelB, a novel mammalian elongation factor for
RT selenoprotein translation.";
RL EMBO J. 19:4796-4805(2000).
RN [3]
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: Translation factor necessary for the incorporation of
CC selenocysteine into proteins. It probably replaces EF-Tu for the
CC insertion of selenocysteine directed by the UGA codon. SelB binds
CC GTP and GDP.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). Nucleus (Potential).
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC SelB subfamily.
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; AL449214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL449210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL449217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF268872; AAG13375.1; -; mRNA.
DR RefSeq; NP_068756.2; NM_021937.3.
DR UniGene; Hs.477498; -.
DR ProteinModelPortal; P57772; -.
DR SMR; P57772; 7-340.
DR IntAct; P57772; 1.
DR STRING; 9606.ENSP00000254730; -.
DR PhosphoSite; P57772; -.
DR DMDM; 259016384; -.
DR PaxDb; P57772; -.
DR PRIDE; P57772; -.
DR DNASU; 60678; -.
DR Ensembl; ENST00000254730; ENSP00000254730; ENSG00000132394.
DR GeneID; 60678; -.
DR KEGG; hsa:60678; -.
DR UCSC; uc003eki.3; human.
DR CTD; 60678; -.
DR GeneCards; GC03P127872; -.
DR H-InvDB; HIX0003649; -.
DR HGNC; HGNC:24614; EEFSEC.
DR HPA; HPA035795; -.
DR MIM; 607695; gene.
DR neXtProt; NX_P57772; -.
DR PharmGKB; PA142671916; -.
DR eggNOG; COG3276; -.
DR HOGENOM; HOG000247007; -.
DR HOVERGEN; HBG017788; -.
DR InParanoid; P57772; -.
DR OMA; DHCFSIR; -.
DR OrthoDB; EOG75B858; -.
DR PhylomeDB; P57772; -.
DR ChiTaRS; EEFSEC; human.
DR GenomeRNAi; 60678; -.
DR NextBio; 65496; -.
DR PRO; PR:P57772; -.
DR ArrayExpress; P57772; -.
DR Bgee; P57772; -.
DR CleanEx; HS_EEFSEC; -.
DR Genevestigator; P57772; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; NAS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:Ensembl.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:Ensembl.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00301; EFACTOR_GTP; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Nucleus; Polymorphism; Protein biosynthesis; Reference proteome.
FT CHAIN 1 596 Selenocysteine-specific elongation
FT factor.
FT /FTId=PRO_0000091478.
FT NP_BIND 14 21 GTP (Potential).
FT NP_BIND 92 96 GTP (Potential).
FT NP_BIND 146 150 GTP (Potential).
FT MOTIF 547 553 Nuclear localization signal (Potential).
FT VARIANT 435 435 A -> V (in dbSNP:rs34326479).
FT /FTId=VAR_055712.
FT CONFLICT 577 577 L -> F (in Ref. 2; AAG13375).
SQ SEQUENCE 596 AA; 65305 MW; C92C43E3F250F686 CRC64;
MAGRRVNVNV GVLGHIDSGK TALARALSTT ASTAAFDKQP QSRERGITLD LGFSCFSVPL
PARLRSSLPE FQAAPEAEPE PGEPLLQVTL VDCPGHASLI RTIIGGAQII DLMMLVIDVT
KGMQTQSAEC LVIGQIACQK LVVVLNKIDL LPEGKRQAAI DKMTKKMQKT LENTKFRGAP
IIPVAAKPGG PEAPETEAPQ GIPELIELLT SQISIPTRDP SGPFLMSVDH CFSIKGQGTV
MTGTILSGSI SLGDSVEIPA LKVVKKVKSM QMFHMPITSA MQGDRLGICV TQFDPKLLER
GLVCAPESLH TVHAALISVE KIPYFRGPLQ TKAKFHITVG HETVMGRLMF FSPAPDNFDQ
EPILDSFNFS QEYLFQEQYL SKDLTPAVTD NDEADKKAGQ ATEGHCPRQQ WALVEFEKPV
TCPRLCLVIG SRLDADIHTN TCRLAFHGIL LHGLEDRNYA DSFLPRLKVY KLKHKHGLVE
RAMDDYSVIG RSLFKKETNI QLFVGLKVHL STGELGIIDS AFGQSGKFKI HIPGGLSPES
KKILTPALKK RARAGRGEAT RQEESAERSE PSQHVVLSLT FKRYVFDTHK RMVQSP
//
ID SELB_HUMAN Reviewed; 596 AA.
AC P57772;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 22-SEP-2009, sequence version 4.
DT 22-JAN-2014, entry version 103.
DE RecName: Full=Selenocysteine-specific elongation factor;
DE AltName: Full=Elongation factor sec;
DE AltName: Full=Eukaryotic elongation factor, selenocysteine-tRNA-specific;
GN Name=EEFSEC; Synonyms=SELB;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 71-596.
RX PubMed=10970870; DOI=10.1093/emboj/19.17.4796;
RA Fagegaltier D., Hubert N., Yamada K., Mizutani T., Carbon P., Krol A.;
RT "Characterization of mSelB, a novel mammalian elongation factor for
RT selenoprotein translation.";
RL EMBO J. 19:4796-4805(2000).
RN [3]
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: Translation factor necessary for the incorporation of
CC selenocysteine into proteins. It probably replaces EF-Tu for the
CC insertion of selenocysteine directed by the UGA codon. SelB binds
CC GTP and GDP.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential). Nucleus (Potential).
CC -!- SIMILARITY: Belongs to the GTP-binding elongation factor family.
CC SelB subfamily.
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; AL449214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL449210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL449217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF268872; AAG13375.1; -; mRNA.
DR RefSeq; NP_068756.2; NM_021937.3.
DR UniGene; Hs.477498; -.
DR ProteinModelPortal; P57772; -.
DR SMR; P57772; 7-340.
DR IntAct; P57772; 1.
DR STRING; 9606.ENSP00000254730; -.
DR PhosphoSite; P57772; -.
DR DMDM; 259016384; -.
DR PaxDb; P57772; -.
DR PRIDE; P57772; -.
DR DNASU; 60678; -.
DR Ensembl; ENST00000254730; ENSP00000254730; ENSG00000132394.
DR GeneID; 60678; -.
DR KEGG; hsa:60678; -.
DR UCSC; uc003eki.3; human.
DR CTD; 60678; -.
DR GeneCards; GC03P127872; -.
DR H-InvDB; HIX0003649; -.
DR HGNC; HGNC:24614; EEFSEC.
DR HPA; HPA035795; -.
DR MIM; 607695; gene.
DR neXtProt; NX_P57772; -.
DR PharmGKB; PA142671916; -.
DR eggNOG; COG3276; -.
DR HOGENOM; HOG000247007; -.
DR HOVERGEN; HBG017788; -.
DR InParanoid; P57772; -.
DR OMA; DHCFSIR; -.
DR OrthoDB; EOG75B858; -.
DR PhylomeDB; P57772; -.
DR ChiTaRS; EEFSEC; human.
DR GenomeRNAi; 60678; -.
DR NextBio; 65496; -.
DR PRO; PR:P57772; -.
DR ArrayExpress; P57772; -.
DR Bgee; P57772; -.
DR CleanEx; HS_EEFSEC; -.
DR Genevestigator; P57772; -.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR GO; GO:0003746; F:translation elongation factor activity; NAS:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:Ensembl.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:Ensembl.
DR InterPro; IPR000795; EF_GTP-bd_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009000; Transl_B-barrel.
DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00301; EFACTOR_GTP; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding;
KW Nucleus; Polymorphism; Protein biosynthesis; Reference proteome.
FT CHAIN 1 596 Selenocysteine-specific elongation
FT factor.
FT /FTId=PRO_0000091478.
FT NP_BIND 14 21 GTP (Potential).
FT NP_BIND 92 96 GTP (Potential).
FT NP_BIND 146 150 GTP (Potential).
FT MOTIF 547 553 Nuclear localization signal (Potential).
FT VARIANT 435 435 A -> V (in dbSNP:rs34326479).
FT /FTId=VAR_055712.
FT CONFLICT 577 577 L -> F (in Ref. 2; AAG13375).
SQ SEQUENCE 596 AA; 65305 MW; C92C43E3F250F686 CRC64;
MAGRRVNVNV GVLGHIDSGK TALARALSTT ASTAAFDKQP QSRERGITLD LGFSCFSVPL
PARLRSSLPE FQAAPEAEPE PGEPLLQVTL VDCPGHASLI RTIIGGAQII DLMMLVIDVT
KGMQTQSAEC LVIGQIACQK LVVVLNKIDL LPEGKRQAAI DKMTKKMQKT LENTKFRGAP
IIPVAAKPGG PEAPETEAPQ GIPELIELLT SQISIPTRDP SGPFLMSVDH CFSIKGQGTV
MTGTILSGSI SLGDSVEIPA LKVVKKVKSM QMFHMPITSA MQGDRLGICV TQFDPKLLER
GLVCAPESLH TVHAALISVE KIPYFRGPLQ TKAKFHITVG HETVMGRLMF FSPAPDNFDQ
EPILDSFNFS QEYLFQEQYL SKDLTPAVTD NDEADKKAGQ ATEGHCPRQQ WALVEFEKPV
TCPRLCLVIG SRLDADIHTN TCRLAFHGIL LHGLEDRNYA DSFLPRLKVY KLKHKHGLVE
RAMDDYSVIG RSLFKKETNI QLFVGLKVHL STGELGIIDS AFGQSGKFKI HIPGGLSPES
KKILTPALKK RARAGRGEAT RQEESAERSE PSQHVVLSLT FKRYVFDTHK RMVQSP
//
MIM
607695
*RECORD*
*FIELD* NO
607695
*FIELD* TI
*607695 EUKARYOTIC ELONGATION FACTOR, SELENOCYSTEINE-tRNA-SPECIFIC; EEFSEC
;;SELENOPROTEIN TRANSLATION FACTOR SELB; SELB;;
read moreEFSEC
*FIELD* TX
CLONING
Decoding of UGA selenocysteine (sec) codons in eubacteria is mediated by
the specialized elongation factor SelB, which conveys the charged
tRNA(sec) to the A site of the ribosome, through binding to the sec
insertion sequence (SECIS) mRNA hairpin. By searching an EST database
for SelB homologs, followed by 5-prime RACE and screening a HeLa cell
cDNA library, Fagegaltier et al. (2000) obtained a partial human cDNA
encoding SELB. Using the partial human sequence for further EST database
searching, they identified a full-length cDNA encoding mouse SelB. The
deduced 583-amino acid mouse SelB protein and the partial 526-amino acid
human SELB protein share 88% amino acid identity.
GENE FUNCTION
Fagegaltier et al. (2000) determined that the putative mouse SelB
protein binds GTP, recognizes sec-tRNA(sec) in vitro and in vivo, and is
required for efficient selenoprotein translation in vivo. In contrast to
the eubacterial SelB, recombinant mouse SelB alone was unable to bind
specifically the eukaryotic SECIS RNA hairpin. However, complementation
with HeLa cell extracts led to the formation of a SECIS-dependent
complex containing mouse SelB and at least another factor. Fagegaltier
et al. (2000) concluded that the role carried out by a single elongation
factor in eubacterial selenoprotein translation is devoted to 2 or more
specialized proteins in eukaryotes.
Zavacki et al. (2003) stated that eukaryotes employ 2 distinct factors
for decoding UGA sec codons. The first, SECIS-binding protein-2 (SBP2;
607693), binds the SECIS element in the 3-prime untranslated region of
the mRNA and recruits the second protein, SELB. Using coprecipitation
studies, they identified the C-terminal 64 amino acids of mouse SelB as
sufficient for interaction with mouse Sbp2. Selenocysteyl-tRNA was
required for this interaction; the 2 factors did not coprecipitate in
its absence. Selenocysteyl-tRNA stabilized the C-terminal domain of
SelB. Zavacki et al. (2003) concluded that the coupling effect is
critical to preventing nonproductive decoding attempts and hence forms a
basis for effective selenoprotein synthesis.
*FIELD* RF
1. Fagegaltier, D.; Hubert, N.; Yamada, K.; Mizutani, T.; Carbon,
P.; Krol, A.: Characterization of mSelB, a novel mammalian elongation
factor for selenoprotein translation. EMBO J. 19: 4796-4805, 2000.
2. Zavacki, A. M.; Mansell, J. B.; Chung, M.; Klimovitsky, B.; Harney,
J. W.; Berry, M. J.: Coupled tRNA(Sec)-dependent assembly of the
selenocysteine decoding apparatus. Molec. Cell 11: 773-781, 2003.
*FIELD* CD
Stylianos E. Antonarakis: 4/18/2003
*FIELD* ED
carol: 12/29/2011
mgross: 4/18/2003
*RECORD*
*FIELD* NO
607695
*FIELD* TI
*607695 EUKARYOTIC ELONGATION FACTOR, SELENOCYSTEINE-tRNA-SPECIFIC; EEFSEC
;;SELENOPROTEIN TRANSLATION FACTOR SELB; SELB;;
read moreEFSEC
*FIELD* TX
CLONING
Decoding of UGA selenocysteine (sec) codons in eubacteria is mediated by
the specialized elongation factor SelB, which conveys the charged
tRNA(sec) to the A site of the ribosome, through binding to the sec
insertion sequence (SECIS) mRNA hairpin. By searching an EST database
for SelB homologs, followed by 5-prime RACE and screening a HeLa cell
cDNA library, Fagegaltier et al. (2000) obtained a partial human cDNA
encoding SELB. Using the partial human sequence for further EST database
searching, they identified a full-length cDNA encoding mouse SelB. The
deduced 583-amino acid mouse SelB protein and the partial 526-amino acid
human SELB protein share 88% amino acid identity.
GENE FUNCTION
Fagegaltier et al. (2000) determined that the putative mouse SelB
protein binds GTP, recognizes sec-tRNA(sec) in vitro and in vivo, and is
required for efficient selenoprotein translation in vivo. In contrast to
the eubacterial SelB, recombinant mouse SelB alone was unable to bind
specifically the eukaryotic SECIS RNA hairpin. However, complementation
with HeLa cell extracts led to the formation of a SECIS-dependent
complex containing mouse SelB and at least another factor. Fagegaltier
et al. (2000) concluded that the role carried out by a single elongation
factor in eubacterial selenoprotein translation is devoted to 2 or more
specialized proteins in eukaryotes.
Zavacki et al. (2003) stated that eukaryotes employ 2 distinct factors
for decoding UGA sec codons. The first, SECIS-binding protein-2 (SBP2;
607693), binds the SECIS element in the 3-prime untranslated region of
the mRNA and recruits the second protein, SELB. Using coprecipitation
studies, they identified the C-terminal 64 amino acids of mouse SelB as
sufficient for interaction with mouse Sbp2. Selenocysteyl-tRNA was
required for this interaction; the 2 factors did not coprecipitate in
its absence. Selenocysteyl-tRNA stabilized the C-terminal domain of
SelB. Zavacki et al. (2003) concluded that the coupling effect is
critical to preventing nonproductive decoding attempts and hence forms a
basis for effective selenoprotein synthesis.
*FIELD* RF
1. Fagegaltier, D.; Hubert, N.; Yamada, K.; Mizutani, T.; Carbon,
P.; Krol, A.: Characterization of mSelB, a novel mammalian elongation
factor for selenoprotein translation. EMBO J. 19: 4796-4805, 2000.
2. Zavacki, A. M.; Mansell, J. B.; Chung, M.; Klimovitsky, B.; Harney,
J. W.; Berry, M. J.: Coupled tRNA(Sec)-dependent assembly of the
selenocysteine decoding apparatus. Molec. Cell 11: 773-781, 2003.
*FIELD* CD
Stylianos E. Antonarakis: 4/18/2003
*FIELD* ED
carol: 12/29/2011
mgross: 4/18/2003