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Database: UniProt
Entry: A4II20
LinkDB: A4II20
Original site: A4II20 
ID   EGR1_XENTR              Reviewed;         498 AA.
AC   A4II20; Q6F2L9;
DT   13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 2.
DT   30-NOV-2016, entry version 63.
DE   RecName: Full=Early growth response protein 1 {ECO:0000250|UniProtKB:P08046};
DE            Short=EGR-1 {ECO:0000250|UniProtKB:P08046};
GN   Name=egr1 {ECO:0000312|EMBL:AAI35807.1};
GN   Synonyms=egr {ECO:0000303|Ref.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAT71995.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Qin S., Dors M., Johnson E., Bloom S., Hood L., Rowen L.;
RT   "Sequence of Xenopus tropicalis development genes.";
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|EMBL:AAT71995.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole {ECO:0000312|EMBL:AAI35807.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcriptional regulator. Recognizes and binds to the
CC       DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region
CC       of target genes (By similarity). Binds double-stranded target DNA,
CC       irrespective of the cytosine methylation status (By similarity).
CC       Regulates the transcription of numerous target genes, and thereby
CC       plays an important role in regulating the response to growth
CC       factors, DNA damage, and ischemia. Plays a role in the regulation
CC       of cell survival, proliferation and cell death. Mediates responses
CC       to ischemia and hypoxia; regulates the expression of proteins that
CC       are involved in inflammatory processes (By similarity).
CC       {ECO:0000250|UniProtKB:P08046, ECO:0000250|UniProtKB:P18146}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18146}.
CC       Cytoplasm {ECO:0000250|UniProtKB:P18146}.
CC   -!- DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3'
CC       via its C2H2-type zinc fingers. The first, most N-terminal zinc
CC       finger binds to the 3'-GCG motif, the middle zinc finger interacts
CC       with the central TGG motif, and the C-terminal zinc finger binds
CC       to the 5'-GCG motif. Binds double-stranded target DNA,
CC       irrespective of the cytosine methylation status. Has reduced
CC       affinity for target DNA where the cytosines have been oxidized to
CC       5-hydroxymethylcytosine. Does not bind target DNA where the
CC       cytosines have been oxidized to 5-formylcytosine or 5-
CC       carboxylcytosine. {ECO:0000250|UniProtKB:P18146}.
CC   -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein
CC       family. {ECO:0000255}.
CC   -!- SIMILARITY: Contains 3 C2H2-type zinc fingers.
CC       {ECO:0000255|PROSITE-ProRule:PRU00042}.
DR   EMBL; AC146894; AAT71995.1; -; Genomic_DNA.
DR   EMBL; BC135806; AAI35807.1; -; mRNA.
DR   RefSeq; NP_001090830.1; NM_001097361.1.
DR   UniGene; Str.39717; -.
DR   ProteinModelPortal; A4II20; -.
DR   STRING; 8364.ENSXETP00000047681; -.
DR   PaxDb; A4II20; -.
DR   Ensembl; ENSXETT00000047681; ENSXETP00000047681; ENSXETG00000006697.
DR   GeneID; 100038164; -.
DR   KEGG; xtr:100038164; -.
DR   CTD; 1958; -.
DR   Xenbase; XB-GENE-853412; egr1.
DR   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00550000074455; -.
DR   HOGENOM; HOG000036856; -.
DR   InParanoid; A4II20; -.
DR   KO; K09203; -.
DR   OMA; GEEHEND; -.
DR   OrthoDB; EOG091G06VX; -.
DR   TreeFam; TF318980; -.
DR   Proteomes; UP000008143; Unassembled WGS sequence.
DR   Bgee; ENSXETG00000006697; -.
DR   ExpressionAtlas; A4II20; differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0010385; F:double-stranded methylated DNA binding; ISS:UniProtKB.
DR   GO; GO:0044729; F:hemi-methylated DNA-binding; ISS:UniProtKB.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IEA:Ensembl.
DR   GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; -; 3.
DR   InterPro; IPR021839; DUF3432.
DR   InterPro; IPR021849; DUF3446.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   InterPro; IPR013087; Znf_C2H2/integrase_DNA-bd.
DR   Pfam; PF11914; DUF3432; 1.
DR   Pfam; PF11928; DUF3446; 1.
DR   SMART; SM00355; ZnF_C2H2; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE   2: Evidence at transcript level;
KW   Activator; Complete proteome; Cytoplasm; DNA-binding; Metal-binding;
KW   Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN         1    498       Early growth response protein 1.
FT                                /FTId=PRO_0000386429.
FT   ZN_FING     307    331       C2H2-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     337    359       C2H2-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   ZN_FING     365    387       C2H2-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00042}.
FT   COMPBIAS    139    183       Ser-rich. {ECO:0000255}.
FT   COMPBIAS    402    491       Ser-rich. {ECO:0000255}.
FT   SITE        305    305       Interaction with DNA.
FT                                {ECO:0000250|UniProtKB:P18146}.
FT   SITE        316    316       Interaction with DNA.
FT                                {ECO:0000250|UniProtKB:P08046}.
FT   SITE        320    320       Interaction with DNA.
FT                                {ECO:0000250|UniProtKB:P08046}.
FT   SITE        326    326       Interaction with DNA.
FT                                {ECO:0000250|UniProtKB:P18146}.
FT   SITE        344    344       Interaction with DNA.
FT                                {ECO:0000250|UniProtKB:P08046}.
FT   SITE        348    348       Interaction with DNA.
FT                                {ECO:0000250|UniProtKB:P18146}.
FT   SITE        372    372       Interaction with DNA.
FT                                {ECO:0000250|UniProtKB:P18146}.
FT   SITE        376    376       Interaction with DNA.
FT                                {ECO:0000250|UniProtKB:P18146}.
FT   SITE        382    382       Interaction with DNA.
FT                                {ECO:0000250|UniProtKB:P18146}.
FT   CONFLICT    148    148       P -> PS (in Ref. 2; AAI35807).
FT                                {ECO:0000305}.
SQ   SEQUENCE   498 AA;  53997 MW;  F0A812624C004C74 CRC64;
     MAAAKTDMLV SPLQISDPFS SFPHSPTMDN YPKLEEMMLL NPGAPQFLGA AVPEGSGFNS
     PVEGSEQFDH LAADAFSDMS LSGEKAVIES SYANQSARLP SLTYTGRFSL EPAPNSSNTL
     WPEPLFSLVS GLVGMANASP SSAPSSSPSS SSSSSQSPPL SCSVQSNDSS PIYSAAPTFP
     NSSPELFPDQ SPQPFQNAST ASIPYPPPAY PVSKTTFQVP MIPDYLFPQQ QGDVSLVSAD
     QKPFQAMESR TQQPSLTPLS TIKAFATQTS QDLKTINSTY QSQIIKPSRM RKYPNRPSKT
     PPHERPYACP VESCDRRFSR SDELTRHIRI HTGQKPFQCR ICMRNFSRSD HLTTHIRTHT
     GEKPFACDIC GRKFARSDER KRHTKIHLRQ KDKKADKATP VSVASPVSSY SPSASTSYPS
     PVPTSYSSPV SSAYPSPVHS SFPSPTTAVT YPSVTSTFQT HGITSFPSSI VTNSFSSPVS
     SALSDMSITY SPRTIEIC
//
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