Swiss-Prot entry
ID NR2E1_HUMAN STANDARD; PRT; 385 AA.
AC Q9Y466;
DT 16-OCT-2001 (Rel. 40, Created)
DT 16-OCT-2001 (Rel. 40, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Orphan nuclear receptor NR2E1 (Nuclear receptor TLX) (Tailless
DE homolog) (Tll) (hTll).
GN Name=NR2E1; Synonyms=TLX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Fetal brain;
RX MEDLINE=98292492; PubMed=9628820 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1006/geno.1998.5270;
RA Jackson A., Panayiotidis P., Foroni L.;
RT "The human homologue of the Drosophila tailless gene (TLX):
RT characterization and mapping to a region of common deletion in human
RT lymphoid leukemia on chromosome 6q21.";
RL Genomics 50:34-43(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Brain;
RX MEDLINE=20528616; PubMed=11073974 [NCBI, ExPASy, EBI, Israel, Japan];
RX DOI=10.1128/MCB.20.23.8731-8739.2000;
RA Kobayashi M., Yu R.T., Yasuda K., Umesono K.;
RT "Cell-type-specific regulation of the retinoic acid receptor mediated
RT by the orphan nuclear receptor TLX.";
RL Mol. Cell. Biol. 20:8731-8739(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RA Hua F., Wu J., Zhang B., Peng X., Yuan J., Qiang B.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE.
RA Mashreghi-Mohammadi M.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX MEDLINE=22388257; PubMed=12477932 [NCBI, ExPASy, EBI, Israel, Japan]; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC -!- FUNCTION: Orphan receptor that binds DNA as a monomer to hormone
CC response elements (HRE) containing an extended core motif half-
CC site sequence 5'-AAGGTCA-3' in which the 5' flanking nucleotides
CC participate in determining receptor specificity. May be required
CC for brain development. May be involved in the regulation of
CC retinal development (By similarity).
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Nuclear (By similarity).
CC -!- TISSUE SPECIFICITY: Brain specific. Present in all brain sections
CC tested, highest levels in the caudate nucleus and hippocampus,
CC weakest levels in the thalamus.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily.
CC -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; Y13276; CAA73725.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF220532; AAG31945.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF411525; AAL05871.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AL078596; CAB75626.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; BC028031; AAH28031.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P03372; 1HCQ. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR TRANSFAC; T04808; -.
DR Ensembl; ENSG00000112333; Homo_sapiens
DR Genew; HGNC:7973; NR2E1.
DR CleanEx; HGNC:7973; NR2E1.
DR MIM; 603849; -. [NCBI / EBI]
DR GeneCards; NR2E1.
DR GeneLynx; NR2E1.
DR GenAtlas; NR2E1.
DR SOURCE; NR2E1.
DR GO; GO:0003707; F:steroid hormone receptor activity; TAS.
DR GO; GO:0007399; P:neurogenesis; TAS.
DR InterPro; IPR000536; Hrmon_recept_lig.
DR InterPro; IPR000003; RtnoidX_receptor.
DR InterPro; IPR001723; Stdhrmn_receptor.
DR InterPro; IPR008946; Str_ncl_receptor.
DR InterPro; IPR001628; Znf_C4steroid.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR00545; RETINOIDXR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR ProDom; PD000035; Znf_C4steroid; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR CMR; Q9Y466.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q9Y466.
DR ProtoNet; Q9Y466.
DR ProtoMap; Q9Y466.
DR PRESAGE; Q9Y466.
DR DIP; Q9Y466.
DR ModBase; Q9Y466.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Activator; Developmental protein; DNA-binding; Nuclear protein;
KW Receptor; Repressor; Transcription; Transcription regulation;
KW Zinc-finger.
FT DNA_BIND 13 90 Nuclear receptor-type.
FT ZN_FING 16 36 C4-type.
FT ZN_FING 52 78 C4-type.
FT DOMAIN 187 354 Ligand-binding (By similarity).
FT DOMAIN 343 347 Poly-Leu.
SQ SEQUENCE 385 AA; 42589 MW; 39181A42A2FB79C2 CRC64;
MSKPAGSTSR ILDIPCKVCG DRSSGKHYGV YACDGCSGFF KRSIRRNRTY VCKSGNQGGC
PVDKTHRNQC RACRLKKCLE VNMNKDAVQH ERGPRTSTIR KQVALYFRGH KEENGAAAHF
PSAALPAPAF FTAVTQLEPH GLELAAVSTT PERQTLVSLA QPTPKYPHEV NGTPMYLYEV
ATESVCESAA RLLFMSIKWA KSVPAFSTLS LQDQLMLLED AWRELFVLGI AQWAIPVDAN
TLLAVSGMNG DNTDSQKLNK IISEIQALQE VVARFRQLRL DATEFACLKC IVTFKAVPTH
SGSELRSFRN AAAIAALQDE AQLTLNSYIH TRYPTQPCRF GKLLLLLPAL RSISPSTIEE
VFFKKTIGNV PITRLLSDMY KSSDI
//