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O00910 (STATA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Signal transducer and activator of transcription A
Alternative name(s):
Dd-STATa
STAT5 homolog A
Gene names
Name:dstA
Synonyms:stat5, statA
ORF Names:DDB_G0281381
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length707 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor that binds to 5'-TTGAATTGA-3' elements in the promoter region of target genes. Functions as repressor of the ecmB gene. Regulates the differentiation of prestalk cells during development. Ref.1 Ref.5 Ref.6 Ref.7

Subunit structure

Monomer, in the absence of tyrosine phosphorylation. Homodimer, or heterodimer with another family member, when tyrosine phosphorylated. Ref.1 Ref.7

Subcellular location

Cytoplasm. Nucleus. Note: Cytoplasmic in growing cells. Translocated into the nucleus in response to cAMP-induced tyrosine phosphorylation. Nuclear at the tight mound stage and in the upper, prestalk region of tipped aggregates and in cells at the tip of the slug. Subject to crm1-dependent nuclear export. Ref.3 Ref.6

Developmental stage

Constitutively expressed with a slight increase during the tight mound stage (at protein level). Detected at very low levels in growing cells and aggregates up to the loose mound stage. Highly expressed in tipped aggregates and in the Mexican hat stage. Expressed at lower levels in early and late culminants and in fruiting bodies. Ref.1 Ref.3

Post-translational modification

Tyrosine phosphorylated in response to cAMP. Not tyrosine phosphorylated in growing cells. Tyrosine phosphorylation is first detected at the tight mound stage, continues throughout the slug stage and early culmination, and starts to decrease at mid-culmination. Barely detectable in fruiting bodies. Ref.1 Ref.3 Ref.4 Ref.6

Disruption phenotype

Cells are hypersensitive to the chlorinated hexaphenone DIF. They form slugs, but there is little or no stalk cell differentiation. After several days of developmental arrest very small spore masses appear that are supported by columns of apparently undifferentiated cells. Ref.5

Sequence similarities

Belongs to the transcription factor STAT family.

Contains 1 SH2 domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainCoiled coil
SH2 domain
   LigandDNA-binding
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processculmination involved in sorocarp development

Inferred from mutant phenotype Ref.5Ref.7. Source: dictyBase

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.5. Source: dictyBase

positive regulation of gene expression

Inferred from direct assay PubMed 15470642. Source: dictyBase

regulation of gene expression

Inferred from direct assay PubMed 15733068. Source: dictyBase

sorocarp development

Inferred from mutant phenotype PubMed 17659086. Source: dictyBase

sorocarp stalk cell differentiation

Inferred from mutant phenotype Ref.5. Source: dictyBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Inferred from direct assay Ref.3. Source: dictyBase

nucleus

Inferred from direct assay PubMed 11032815PubMed 12506009Ref.3. Source: dictyBase

   Molecular_functionDNA binding

Inferred from direct assay Ref.7Ref.1. Source: dictyBase

calcium ion binding

Inferred from electronic annotation. Source: InterPro

protein homodimerization activity

Inferred from direct assay Ref.7. Source: dictyBase

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 707707Signal transducer and activator of transcription A
PRO_0000328082

Regions

Domain583 – 686104SH2
DNA binding443 – 48745
Coiled coil242 – 356115 Ref.7
Compositional bias90 – 11122Poly-Gln
Compositional bias158 – 21356Poly-Asn
Compositional bias214 – 23623Poly-Gln

Sites

Site3801Interaction with DNA By similarity
Site5771Interaction with DNA By similarity

Amino acid modifications

Modified residue7021Phosphotyrosine Ref.3

Experimental info

Mutagenesis4431K → D: Loss of DNA binding. Ref.7
Mutagenesis449 – 4502RK → DD: About 3-fold reduced DNA binding.
Mutagenesis4841N → A: Loss of DNA binding. Ref.7

Secondary structure

.................................................................... 707
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00910 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 9803388BD324D7B6

FASTA70779,792
        10         20         30         40         50         60 
MSSAEFSMDD FEDTFDSNAT ISTKDLFEGS DRLPLNQSIN TTIQNLYLPN GGFAIGDQSQ 

        70         80         90        100        110        120 
QQYYQAMPPL NQSDQFNLGR SNNLTPRTNQ LQQLQQQQQQ QQQPQQQQQQ QTYGTQSPIH 

       130        140        150        160        170        180 
MSQTPSSPLS SPLPSPTPFS RQQSYNNNNS NNTSSSQNYN NNNININNNN NNNNTNNNNN 

       190        200        210        220        230        240 
NNNGNNSNGN NGNNNNNNNN NNNNNTNNNN NNNQQQQQQQ QQQQQQQQQQ QQQQQQGNPN 

       250        260        270        280        290        300 
LSSPQPILDT IYKLLSEQEQ TLVQMIHEQS LLLNRLPPTL DENSLAPLKS LSQKQITLSG 

       310        320        330        340        350        360 
QMNTEMSALD ATKKGMILEP TDLAKLFALK QDLQIQFKQL SLLHNEIQSI LNPQHSAPKP 

       370        380        390        400        410        420 
NVALVLKSQP FPVVISKGKQ LGENQLVVLV LTGARSNFHI NGPVKATMIC DSHPTNKNNP 

       430        440        450        460        470        480 
TTPLEMDSQP IYPATLTAHF PLKFLAGTRK CSVNLKFGVN IRDLDNVTTT VESDASNPFV 

       490        500        510        520        530        540 
VITNECQWEG SAGVLLKKDA FDGQLEITWA QFINTLQRHF LIATKQDPVR PKRPLSSYDL 

       550        560        570        580        590        600 
KYIQTHFFGN RSIIHQQDFD KFWVWFGKSM QTLRYQRHIS TLWQEGIIYG YMGRQEVNDA 

       610        620        630        640        650        660 
LQNQDPGTFI IRFSERNPGQ FGIAYIGVEM PARIKHYLVQ PNDTAAAKKT FPDFLSEHSQ 

       670        680        690        700 
FVNLLQWTKD TNGAPRFLKL HKDTALGSFA PKRTAPVPVG GYEPLNS 

« Hide

References

« Hide 'large scale' references
[1]"SH2 signaling in a lower eukaryote: a STAT protein that regulates stalk cell differentiation in dictyostelium."
Kawata T., Shevchenko A., Fukuzawa M., Jermyn K.A., Totty N.F., Zhukovskaya N.V., Sterling A.E., Mann M., Williams J.G.
Cell 89:909-916(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT, DEVELOPMENTAL STAGE, TYROSINE PHOSPHORYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: AX2.
[2]"The genome of the social amoeba Dictyostelium discoideum."
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. expand/collapse author list , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[3]"Developmentally and spatially regulated activation of a Dictyostelium STAT protein by a serpentine receptor."
Araki T., Gamper M., Early A., Fukuzawa M., Abe T., Kawata T., Kim E., Firtel R.A., Williams J.G.
EMBO J. 17:4018-4028(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-702, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[4]"The phosphorylated C-terminus of cAR1 plays a role in cell-type-specific gene expression and STATa tyrosine phosphorylation."
Briscoe C., Moniakis J., Kim J.-Y., Brown J.M., Hereld D., Devreotes P.N., Firtel R.A.
Dev. Biol. 233:225-236(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CYCLIC AMP-INDUCED PHOSPHORYLATION.
[5]"Evidence that the Dictyostelium Dd-STATa protein is a repressor that regulates commitment to stalk cell differentiation and is also required for efficient chemotaxis."
Mohanty S., Jermyn K.A., Early A., Kawata T., Aubry L., Ceccarelli A., Schaap P., Williams J.G., Firtel R.A.
Development 126:3391-3405(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[6]"Protein tyrosine phosphatase PTP1 negatively regulates Dictyostelium STATa and is required for proper cell-type proportioning."
Early A., Gamper M., Moniakis J., Kim E., Hunter T., Williams J.G., Firtel R.A.
Dev. Biol. 232:233-245(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION, MODULATION OF TYROSINE PHOSPHORYLATION.
[7]"Structure of an activated Dictyostelium STAT in its DNA-unbound form."
Soler-Lopez M., Petosa C., Fukuzawa M., Ravelli R., Williams J.G., Mueller C.W.
Mol. Cell 13:791-804(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 235-707 OF TYROSINE PHOSPHORYLATED HOMODIMER, COILED-COIL DOMAIN, FUNCTION, SUBUNIT, MUTAGENESIS OF LYS-443; 449-ARG-LYS-450 AND ASN-484.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y13097 mRNA. Translation: CAA73551.1.
AAFI02000041 Genomic DNA. Translation: EAL66672.1.
RefSeqXP_640661.1. XM_635569.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UURX-ray2.70A235-707[»]
1UUSX-ray2.80A235-707[»]
ProteinModelPortalO00910.
SMRO00910. Positions 239-707.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0215388.

Proteomic databases

PRIDEO00910.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0215388; DDB0215388; DDB_G0281381.
GeneID8623045.
KEGGddi:DDB_G0281381.

Organism-specific databases

dictyBaseDDB_G0281381. dstA.

Phylogenomic databases

eggNOGNOG245085.
OMAMNTEMSA.
PhylomeDBO00910.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
1.20.58.240. 1 hit.
2.60.40.340. 1 hit.
3.30.505.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
IPR000980. SH2.
IPR001217. STAT.
IPR015988. STAT_TF_coiled-coil.
IPR015347. STAT_TF_homologue_coiled-coil.
[Graphical view]
PANTHERPTHR11801. PTHR11801. 1 hit.
PfamPF09267. Dict-STAT-coil. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMSSF47655. SSF47655. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO00910.

Entry information

Entry nameSTATA_DICDI
AccessionPrimary (citable) accession number: O00910
Secondary accession number(s): Q54U00
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: July 1, 1997
Last modified: May 14, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase