Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 41 (02 Jun 2021)
Sequence version 1 (23 Sep 2008)
Previous versions | rss
Add a publicationFeedback
Protein

GATA-type transcription factor SRE1

Gene

SRE1

Organism
Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

GATA-type transcription repressor that regulates iron- acquisition genes through specific binding the GATA sequence element 5'-(G/A)ATC(T/A)GATAA-3' of target promoters in an iron- and zinc-dependent manner (PubMed:18549241, PubMed:22117028).

Regulation occurs via direct binding of iron ions (PubMed:18549241).

Iron acquisition regulation is critical for survival under both iron-limiting conditions (to acquire essential iron) and iron-replete conditions (to limit iron toxicity) (PubMed:22117028).

SRE1 targets include genes encoding a number of key iron-regulated factors such as those involved in siderophore biosynthesis, presumed ferric reductase activity, iron-responsive transcriptional regulation, oxidative stress response, as well as genes encoding a number of putative oxidoreductases, metabolic and mitochondrial enzymes, superoxide dismutase, and genes previously identified as induced during nitrosative stress (PubMed:22117028).

2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri128 – 152GATA-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri291 – 315GATA-type 2PROSITE-ProRule annotationAdd BLAST25

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
GATA-type transcription factor SRE11 Publication
Alternative name(s):
Siderophore uptake regulator SRE11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:SRE11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiAjellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri5037 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeHistoplasma

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Impairs the repression of siderophore biosynthesis and utilization genes in the presence of abundant iron and thus produces siderophores even under iron-replete conditions (PubMed:22117028).1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi128C → A in gzf1; decreases both the number of zinc and iron ions bound and the ability to bind DNA; when associated with A-131. 1 Publication1
Mutagenesisi131C → A in gzf1; decreases both the number of zinc and iron ions bound and the ability to bind DNA; when associated with A-128. 1 Publication1
Mutagenesisi219C → A in crr1; decreases both the number of iron ions bound and the ability to bind DNA; when associated with A-225. 1 Publication1
Mutagenesisi225C → A in crr1; decreases both the number of iron ions bound and the ability to bind DNA; when associated with A-219. 1 Publication1
Mutagenesisi234C → A in crr2; decreases both the number of iron ions bound and the ability to bind DNA; when associated with A-237. 1 Publication1
Mutagenesisi237C → A in crr2; decreases both the number of iron ions bound and the ability to bind DNA; when associated with A-234. 1 Publication1
Mutagenesisi291C → A in gzf2; decreases both the number of zinc and iron ions bound and the ability to bind DNA; when associated with A-294. 1 Publication1
Mutagenesisi294C → A in gzf2; decreases both the number of zinc and iron ions bound and the ability to bind DNA; when associated with A-291. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004444031 – 630GATA-type transcription factor SRE1Add BLAST630

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Constitutively expressed in high-iron medium, whereas expression is reduced approximately 2.5-fold when an iron chelator, such as deferoxamine, is added to the growth medium (PubMed:18549241).1 Publication

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
B4XXY3

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 139DisorderedSequence analysisAdd BLAST139
Regioni162 – 203DisorderedSequence analysisAdd BLAST42
Regioni219 – 237Cystein-rich region (CRR)By similarityAdd BLAST19
Regioni256 – 283DisorderedSequence analysisAdd BLAST28
Regioni339 – 609DisorderedSequence analysisAdd BLAST271

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili595 – 630Sequence analysisAdd BLAST36

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi62 – 85Polar residuesSequence analysisAdd BLAST24
Compositional biasi102 – 137Polar residuesSequence analysisAdd BLAST36
Compositional biasi167 – 203Polar residuesSequence analysisAdd BLAST37
Compositional biasi348 – 364Polar residuesSequence analysisAdd BLAST17
Compositional biasi412 – 450Polar residuesSequence analysisAdd BLAST39
Compositional biasi467 – 483Polar residuesSequence analysisAdd BLAST17
Compositional biasi495 – 517Polar residuesSequence analysisAdd BLAST23
Compositional biasi539 – 564Polar residuesSequence analysisAdd BLAST26

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The conserved cystein-rich region (CRR) localized between the zinc fingers is also involved in DNA-binding and transcription repressor activity (By similarity).By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri128 – 152GATA-type 1PROSITE-ProRule annotationAdd BLAST25
Zinc fingeri291 – 315GATA-type 2PROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00202, ZnF_GATA, 2 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.50.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039355, Transcription_factor_GATA
IPR000679, Znf_GATA
IPR013088, Znf_NHR/GATA

The PANTHER Classification System

More...
PANTHERi
PTHR10071, PTHR10071, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00320, GATA, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00619, GATAZNFINGER

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00401, ZnF_GATA, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00344, GATA_ZN_FINGER_1, 2 hits
PS50114, GATA_ZN_FINGER_2, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

B4XXY3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTGLLASRLR AEGARSPTKG TDIPMRQPSA EDLDAAHQLV SSARGGRDNV
60 70 80 90 100
MNFRSDRQEM TGKALDNTQG DGSRNMDSQL QNGHKAPVEQ RAGESPPESG
110 120 130 140 150
ANPIDHPTSS KKSPKAQSKE QAFTGHSCSN CGTKRTPLWR RSPTGATICN
160 170 180 190 200
ACGLYLKARN TDRPTHRSRS LLTPYGSSSA QTLDKSRSST SPTNDGNDPR
210 220 230 240 250
LTDTWSNYAV KECTPSGSCP GGGSCNGTGG AEGCDGCPAY NNRVYKSAAR
260 270 280 290 300
NAMALHTPRT SPQVSTQGGP GSTEGDAGSS NPETMTLHIA CQNCQTTVTP
310 320 330 340 350
LWRRDENGHP ICNACGLYHK LHGAYRPPTM KKSIIKRRKR VVPAMREQSP
360 370 380 390 400
PSATQSSNGS VSPEASPAAL AHNHDSHRQY QNVEHGNGHP PPHTRPLYSH
410 420 430 440 450
AYHAPPPADF TGYTSNVISL PHHPPSTSQQ LRPYDNNHNN GETTNTHRAP
460 470 480 490 500
MPALHNPKKR TISESSIEDS QRPQASQILT HIPQINPPTP PSSSSASFPN
510 520 530 540 550
NNPGRFNSIS SLLNHPGEAA TVTAHDRDDS RVDPALSSAV APRTQQPQQE
560 570 580 590 600
HQHASAGSHS PPRFSPSLSP APPSTTAVPV GGGSGSGAAA VAGVVDHRDA
610 620 630
KAERRARLQR EAQDMREALK AKERELALLE
Length:630
Mass (Da):67,308
Last modified:September 23, 2008 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i1F6DF731B1254B64
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
EU220030 Genomic DNA Translation: ABY66603.1

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU220030 Genomic DNA Translation: ABY66603.1

3D structure databases

SMRiB4XXY3
ModBaseiSearch...

Family and domain databases

CDDicd00202, ZnF_GATA, 2 hits
Gene3Di3.30.50.10, 2 hits
InterProiView protein in InterPro
IPR039355, Transcription_factor_GATA
IPR000679, Znf_GATA
IPR013088, Znf_NHR/GATA
PANTHERiPTHR10071, PTHR10071, 1 hit
PfamiView protein in Pfam
PF00320, GATA, 2 hits
PRINTSiPR00619, GATAZNFINGER
SMARTiView protein in SMART
SM00401, ZnF_GATA, 2 hits
PROSITEiView protein in PROSITE
PS00344, GATA_ZN_FINGER_1, 2 hits
PS50114, GATA_ZN_FINGER_2, 2 hits

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSREA_AJECA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: B4XXY3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2018
Last sequence update: September 23, 2008
Last modified: June 2, 2021
This is version 41 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again