ID   TEF_HUMAN               Reviewed;         303 AA.
AC   Q10587; Q15729; Q7Z3J7; Q8IU94; Q96TG4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 3.
DT   07-JUL-2009, entry version 80.
DE   RecName: Full=Thyrotroph embryonic factor;
GN   Name=TEF; Synonyms=KIAA1655;
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].
RX   MEDLINE=95137580; PubMed=7835883; DOI=10.1006/geno.1994.1510;
RA   Khatib Z.A., Inaba T., Valentine M., Look A.T.;
RT   "Chromosomal localization and cDNA cloning of the human DBP and TEF
RT   genes.";
RL   Genomics 23:344-351(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96219638; PubMed=8639829;
RA   Hunger S.P., Li S., Fall M.Z., Naumovski L., Cleary M.L.;
RT   "The proto-oncogene HLF and the related basic leucine zipper protein
RT   TEF display highly similar DNA-binding and transcriptional regulatory
RT   properties.";
RL   Blood 87:4607-4617(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA   Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA   Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA   Beare D.M., Dunham I.;
RT   "A genome annotation-driven approach to cloning the human ORFeome.";
RL   Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
RA   Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
RA   Korn B., Zuo D., Hu Y., LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=20057165; PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA   Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA   Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA   Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA   Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA   Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA   Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA   Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA   Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA   Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA   Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA   Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA   Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA   Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA   Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA   Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA   Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA   Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA   Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA   Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA   Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA   Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA   Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA   Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA   Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA   Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA   Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA   Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA   Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA   Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA   Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA   Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA   O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA   Khan A.S., Lane L., Tilahun Y., Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 164-303.
RC   TISSUE=Retina;
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., Blocker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K.,
RA   Ottenwalder 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).
CC   -!- FUNCTION: Transcription factor that binds to and transactivates
CC       the TSHB promoter. Binds to a minimal DNA-binding sequence 5'-
CC       [TC][AG][AG]TTA[TC][AG]-3'.
CC   -!- SUBUNIT: Binds DNA as a homodimer or a heterodimer. Can form a
CC       heterodimer with DBP.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- INDUCTION: Accumulates according to a robust circadian rhythm (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the bZIP family. PAR subfamily.
CC   -!- SIMILARITY: Contains 1 bZIP domain.
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DR   EMBL; U06935; AAA81373.1; ALT_INIT; mRNA.
DR   EMBL; U44059; AAB06497.1; -; mRNA.
DR   EMBL; CR456592; CAG30478.1; -; mRNA.
DR   EMBL; CR541827; CAG46626.1; -; mRNA.
DR   EMBL; AL035659; CAI23516.1; -; Genomic_DNA.
DR   EMBL; BC039258; AAH39258.1; -; mRNA.
DR   EMBL; BC042476; AAH42476.1; -; mRNA.
DR   EMBL; BX537848; CAD97856.1; -; mRNA.
DR   IPI; IPI00216670; -.
DR   PIR; G02360; G02360.
DR   RefSeq; NP_001138870.1; -.
DR   RefSeq; NP_003207.1; -.
DR   UniGene; Hs.181159; -.
DR   PhosphoSite; Q10587; -.
DR   PRIDE; Q10587; -.
DR   Ensembl; ENSG00000167074; Homo sapiens.
DR   GeneID; 7008; -.
DR   KEGG; hsa:7008; -.
DR   UCSC; uc003azy.1; human.
DR   GeneCards; GC22P040102; -.
DR   H-InvDB; HIX0016516; -.
DR   HGNC; HGNC:11722; TEF.
DR   MIM; 188595; gene.
DR   PharmGKB; PA36439; -.
DR   HOGENOM; Q10587; -.
DR   HOVERGEN; Q10587; -.
DR   OMA; Q10587; WSEKKAD.
DR   NextBio; 27374; -.
DR   ArrayExpress; Q10587; -.
DR   Bgee; Q10587; -.
DR   CleanEx; HS_TEF; -.
DR   GermOnline; ENSG00000167074; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0003702; F:RNA polymerase II transcription factor acti...; TAS:ProtInc.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0003700; F:transcription factor activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription from RNA polyme...; TAS:ProtInc.
DR   GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR011700; bZIP_2.
DR   InterPro; IPR004827; TF_bZIP.
DR   Pfam; PF07716; bZIP_2; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   PROSITE; PS00036; BZIP_BASIC; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Activator; Biological rhythms; Complete proteome; DNA-binding;
KW   Nucleus; Transcription; Transcription regulation.
FT   CHAIN         1    303       Thyrotroph embryonic factor.
FT                                /FTId=PRO_0000076512.
FT   DOMAIN      268    282       Leucine-zipper.
FT   DNA_BIND    239    257       Basic motif.
FT   COMPBIAS    166    217       Pro-rich (proline/acidic region (PAR)).
FT   CONFLICT     54     54       K -> E (in Ref. 1; AAA81373).
SQ   SEQUENCE   303 AA;  33248 MW;  4A87B7BFA7248C6F CRC64;
     MSDAGGGKKP PVDPQAGPGP GPGRAAGERG LSGSFPLVLK KLMENPPREA RLDKEKGKEK
     LEEDEAAAAS TMAVSASLMP PIWDKTIPYD GESFHLEYMD LDEFLLENGI PASPTHLAHN
     LLLPVAELEG KESASSSTAS PPSSSTAIFQ PSETVSSTES SLEKERETPS PIDPNCVEVD
     VNFNPDPADL VLSSVPGGEL FNPRKHKFAE EDLKPQPMIK KAKKVFVPDE QKDEKYWTRR
     KKNNVAAKRS RDARRLKENQ ITIRAAFLEK ENTALRTEVA ELRKEVGKCK TIVSKYETKY
     GPL
//