EGR1A_XENLA
ID EGR1A_XENLA Reviewed; 497 AA.
AC Q6GQH4; Q9I831;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Early growth response protein 1-A;
DE Short=EGR-1-A;
DE Short=Xegr-1 {ECO:0000303|PubMed:9687509};
GN Name=egr1-a; Synonyms=egr1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAF66986.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RX PubMed=9687509; DOI=10.1093/emboj/17.15.4414;
RA Panitz F., Krain B., Hollemann T., Nordheim A., Pieler T.;
RT "The Spemann organizer-expressed zinc finger gene Xegr-1 responds to the
RT MAP kinase/Ets-SRF signal transduction pathway.";
RL EMBO J. 17:4414-4425(1998).
RN [2] {ECO:0000312|EMBL:AAH72770.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:AAH72770.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP INDUCTION.
RX PubMed=10610029;
RA Krain B., Nordheim A.;
RT "Artefactual gene induction during preparation of Xenopus laevis animal cap
RT explants.";
RL Int. J. Dev. Biol. 43:563-566(1999).
RN [4] {ECO:0000305}
RP INDUCTION.
RX PubMed=10096064; DOI=10.1016/s0925-4773(98)00194-4;
RA Chen Y., Hollemann T., Grunz H., Pieler T.;
RT "Characterization of the Ets-type protein ER81 in Xenopus embryos.";
RL Mech. Dev. 80:67-76(1999).
RN [5] {ECO:0000305}
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=10781937; DOI=10.1016/s0925-4773(00)00260-4;
RA Saka Y., Tada M., Smith J.C.;
RT "A screen for targets of the Xenopus T-box gene Xbra.";
RL Mech. Dev. 93:27-39(2000).
CC -!- FUNCTION: Transcriptional regulator. Recognizes and binds to the DNA
CC sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target
CC genes (By similarity). Binds double-stranded target DNA, irrespective
CC of the cytosine methylation status (By similarity). Regulates the
CC transcription of numerous target genes, and thereby plays an important
CC role in regulating the response to growth factors, DNA damage, and
CC ischemia. Plays a role in the regulation of cell survival,
CC proliferation and cell death. Mediates responses to ischemia and
CC hypoxia; regulates the expression of proteins that are involved in
CC inflammatory processes (By similarity). Plays a role in regulating the
CC expression of circadian clock genes (By similarity).
CC {ECO:0000250|UniProtKB:P08046, ECO:0000250|UniProtKB:P18146}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18146}. Cytoplasm
CC {ECO:0000250|UniProtKB:P18146}.
CC -!- TISSUE SPECIFICITY: Expressed in the presumptive mesoderm. In blastula
CC embryos, expressed in the dorsal marginal zone, and at the onset of
CC gastrulation expression is specific to the Spemann organizer. As
CC gastrulation proceeds, expressed in a ring around the yolk plug. This
CC expression is maintained in advanced gastrulae, with weak expression
CC also extending into the dorsal midline. By the neurula stage,
CC expression is excluded from the notochord. In late tailbud stages,
CC expressed in two spots in the anterior forebrain, which are connected
CC via a bridge of cells that also show expression.
CC {ECO:0000269|PubMed:10781937, ECO:0000269|PubMed:9687509}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed at a low level maternally, with expression strongly
CC increasing with the onset of gastrulation, then decreasing again in
CC later stages of embryonic development with expression undetectable
CC during neurulation. Expressed in adults. {ECO:0000269|PubMed:9687509}.
CC -!- INDUCTION: By dorsalizing and ventralizing growth factors during
CC mesoderm induction. Responds to the FGF-induced MAPK/Ets-serum response
CC factor (srf-elk1)-signaling pathway. Induced by activin and bmp4 acting
CC indirectly via an FGF-signaling pathway. Induced in response to wound-
CC induced activation of the MAPK pathway. Induced by both t/bra and
CC foxa4/pintallavis alone, with maximal activation requiring both
CC transcription factors. Induction by t/bra is indirect and probably
CC occurs via the FGF-signaling pathway, whereas induction by
CC foxa4/pintallavis may be direct. {ECO:0000269|PubMed:10096064,
CC ECO:0000269|PubMed:10610029, ECO:0000269|PubMed:10781937,
CC ECO:0000269|PubMed:9687509}.
CC -!- DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via
CC its C2H2-type zinc fingers. The first, most N-terminal zinc finger
CC binds to the 3'-GCG motif, the middle zinc finger interacts with the
CC central TGG motif, and the C-terminal zinc finger binds to the 5'-GCG
CC motif. Binds double-stranded target DNA, irrespective of the cytosine
CC methylation status. Has reduced affinity for target DNA where the
CC cytosines have been oxidized to 5-hydroxymethylcytosine. Does not bind
CC target DNA where the cytosines have been oxidized to 5-formylcytosine
CC or 5-carboxylcytosine. {ECO:0000250|UniProtKB:P18146}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000255}.
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DR EMBL; AF250345; AAF66986.1; -; mRNA.
DR EMBL; BC072770; AAH72770.1; -; mRNA.
DR RefSeq; NP_001083862.1; NM_001090393.1.
DR AlphaFoldDB; Q6GQH4; -.
DR SMR; Q6GQH4; -.
DR PRIDE; Q6GQH4; -.
DR DNASU; 399162; -.
DR GeneID; 399162; -.
DR KEGG; xla:399162; -.
DR CTD; 399162; -.
DR Xenbase; XB-GENE-853419; egr1.L.
DR OMA; QAMESRT; -.
DR OrthoDB; 1318335at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 399162; Expressed in brain and 17 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; 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:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR021839; EGR1_C.
DR InterPro; IPR021849; EGR_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF11914; DUF3432; 1.
DR Pfam; PF11928; DUF3446; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 2: Evidence at transcript level;
KW Activator; Biological rhythms; Cytoplasm; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..497
FT /note="Early growth response protein 1-A"
FT /id="PRO_0000386427"
FT ZN_FING 306..330
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 336..358
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 364..386
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 139..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 304
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 315
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 319
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 325
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 343
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P08046"
FT SITE 347
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 371
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 375
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT SITE 381
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT CONFLICT 447
FT /note="A -> G (in Ref. 1; AAF66986)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="C -> W (in Ref. 1; AAF66986)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 54142 MW; 794C1446864E53EB CRC64;
MAVAKTEMLV SPLQISDPFS SFPHSPTMDN YPKLEEMMLL NAGGPQFLGA SVPDGSGFNS
TVEGAEQFDH LTADAFSEMS LSSEKALVES SYANQTTRLP SLTYTGRFSL EPATNSSNTL
WPEPLFSLVS GLVGMANISP SSAPSSSPSS SSSSSSSQSP PLSCSVQSND SSPIYSAAPT
FPNSSSEIFP DHSPQPFQNA SIPYPPPAYP VSKTTFQVPM IPDYLFPQQQ GDVSLVSADQ
KPFQAMESRT QQPSLTPLST IKAYATHTSQ DLKTINSTYQ SQIIKPSRMR KYPNRPSKTP
PHERPYGCPV ESCDRRFSRS DELTRHIRIH TGQKPFQCRI CMRNFSRSDH LTTHIRTHTG
EKPFACDICG RKFARSDERK RHTKIHLRQK DKKADKATPV SVASPVSSYS PSASTSYPSP
VPTSYSSPVS SSYPSPVHSS FPSPTTAVTY PSVTSTFQTH GITSFPSSIM TNAFSSPMSS
ALSDMSLTYS PRTIEIC
