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Protein

Signal transducer and activator of transcription A

Gene

dstA

Organism
Dictyostelium discoideum (Slime mold)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei380 – 3801Interaction with DNABy similarity
Sitei577 – 5771Interaction with DNABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi443 – 48745Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: dictyBase
  2. protein homodimerization activity Source: dictyBase
  3. sequence-specific DNA binding transcription factor activity Source: InterPro
  4. signal transducer activity Source: InterPro

GO - Biological processi

  1. culmination involved in sorocarp development Source: dictyBase
  2. negative regulation of transcription, DNA-templated Source: dictyBase
  3. positive regulation of gene expression Source: dictyBase
  4. regulation of gene expression Source: dictyBase
  5. sorocarp development Source: dictyBase
  6. sorocarp stalk cell differentiation Source: dictyBase
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transducer and activator of transcription A
Alternative name(s):
Dd-STATa
STAT5 homolog A
Gene namesi
Name:dstA
Synonyms:stat5, statA
ORF Names:DDB_G0281381
OrganismiDictyostelium discoideum (Slime mold)
Taxonomic identifieri44689 [NCBI]
Taxonomic lineageiEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium
ProteomesiUP000002195: Chromosome 3, UP000002195: Unassembled WGS sequence

Organism-specific databases

dictyBaseiDDB_G0281381. dstA.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytosol Source: dictyBase
  2. nucleus Source: dictyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

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.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi443 – 4431K → D: Loss of DNA binding. 1 Publication
Mutagenesisi449 – 4502RK → DD: About 3-fold reduced DNA binding. 1 Publication
Mutagenesisi484 – 4841N → A: Loss of DNA binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 707707Signal transducer and activator of transcription APRO_0000328082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei702 – 7021Phosphotyrosine1 Publication

Post-translational modificationi

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.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiO00910.

Expressioni

Developmental stagei

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.2 Publications

Interactioni

Subunit structurei

Monomer, in the absence of tyrosine phosphorylation. Homodimer, or heterodimer with another family member, when tyrosine phosphorylated.2 Publications

Protein-protein interaction databases

STRINGi44689.DDB_0215388.

Structurei

Secondary structure

1
707
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi245 – 27430Combined sources
Helixi282 – 31534Combined sources
Helixi320 – 35132Combined sources
Beta strandi363 – 3686Combined sources
Beta strandi374 – 3763Combined sources
Turni383 – 3853Combined sources
Beta strandi386 – 3916Combined sources
Beta strandi398 – 40912Combined sources
Turni433 – 4364Combined sources
Beta strandi437 – 4393Combined sources
Beta strandi453 – 46311Combined sources
Beta strandi468 – 4725Combined sources
Beta strandi479 – 4846Combined sources
Turni485 – 4873Combined sources
Helixi488 – 50114Combined sources
Beta strandi505 – 5084Combined sources
Helixi509 – 52315Combined sources
Beta strandi528 – 5303Combined sources
Helixi537 – 54610Combined sources
Turni547 – 5504Combined sources
Beta strandi552 – 5554Combined sources
Helixi556 – 57520Combined sources
Helixi579 – 5846Combined sources
Helixi594 – 5996Combined sources
Turni601 – 6033Combined sources
Beta strandi609 – 6135Combined sources
Beta strandi615 – 6173Combined sources
Beta strandi621 – 6266Combined sources
Beta strandi628 – 6314Combined sources
Beta strandi634 – 6385Combined sources
Helixi641 – 6433Combined sources
Turni646 – 6483Combined sources
Helixi651 – 6555Combined sources
Beta strandi663 – 6697Combined sources
Beta strandi675 – 6795Combined sources
Helixi682 – 6854Combined sources
Helixi687 – 6893Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UURX-ray2.70A235-707[»]
1UUSX-ray2.80A235-707[»]
ProteinModelPortaliO00910.
SMRiO00910. Positions 239-707.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00910.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini583 – 686104SH2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili242 – 3561151 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi90 – 11122Poly-GlnAdd
BLAST
Compositional biasi158 – 21356Poly-AsnAdd
BLAST
Compositional biasi214 – 23623Poly-GlnAdd
BLAST

Sequence similaritiesi

Belongs to the transcription factor STAT family.Curated
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, SH2 domain

Phylogenomic databases

eggNOGiNOG245085.
InParanoidiO00910.
OMAiMNTEMSA.
PhylomeDBiO00910.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.20.58.240. 1 hit.
2.60.40.340. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011992. 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]
PANTHERiPTHR11801. PTHR11801. 1 hit.
PfamiPF09267. Dict-STAT-coil. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF47655. SSF47655. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00910-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSAEFSMDD FEDTFDSNAT ISTKDLFEGS DRLPLNQSIN TTIQNLYLPN
60 70 80 90 100
GGFAIGDQSQ QQYYQAMPPL NQSDQFNLGR SNNLTPRTNQ LQQLQQQQQQ
110 120 130 140 150
QQQPQQQQQQ QTYGTQSPIH MSQTPSSPLS SPLPSPTPFS RQQSYNNNNS
160 170 180 190 200
NNTSSSQNYN NNNININNNN NNNNTNNNNN NNNGNNSNGN NGNNNNNNNN
210 220 230 240 250
NNNNNTNNNN NNNQQQQQQQ QQQQQQQQQQ QQQQQQGNPN LSSPQPILDT
260 270 280 290 300
IYKLLSEQEQ TLVQMIHEQS LLLNRLPPTL DENSLAPLKS LSQKQITLSG
310 320 330 340 350
QMNTEMSALD ATKKGMILEP TDLAKLFALK QDLQIQFKQL SLLHNEIQSI
360 370 380 390 400
LNPQHSAPKP NVALVLKSQP FPVVISKGKQ LGENQLVVLV LTGARSNFHI
410 420 430 440 450
NGPVKATMIC DSHPTNKNNP TTPLEMDSQP IYPATLTAHF PLKFLAGTRK
460 470 480 490 500
CSVNLKFGVN IRDLDNVTTT VESDASNPFV VITNECQWEG SAGVLLKKDA
510 520 530 540 550
FDGQLEITWA QFINTLQRHF LIATKQDPVR PKRPLSSYDL KYIQTHFFGN
560 570 580 590 600
RSIIHQQDFD KFWVWFGKSM QTLRYQRHIS TLWQEGIIYG YMGRQEVNDA
610 620 630 640 650
LQNQDPGTFI IRFSERNPGQ FGIAYIGVEM PARIKHYLVQ PNDTAAAKKT
660 670 680 690 700
FPDFLSEHSQ FVNLLQWTKD TNGAPRFLKL HKDTALGSFA PKRTAPVPVG

GYEPLNS
Length:707
Mass (Da):79,792
Last modified:July 1, 1997 - v1
Checksum:i9803388BD324D7B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13097 mRNA. Translation: CAA73551.1.
AAFI02000041 Genomic DNA. Translation: EAL66672.1.
RefSeqiXP_640661.1. XM_635569.1.

Genome annotation databases

EnsemblProtistsiDDB0215388; DDB0215388; DDB_G0281381.
GeneIDi8623045.
KEGGiddi:DDB_G0281381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13097 mRNA. Translation: CAA73551.1.
AAFI02000041 Genomic DNA. Translation: EAL66672.1.
RefSeqiXP_640661.1. XM_635569.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UURX-ray2.70A235-707[»]
1UUSX-ray2.80A235-707[»]
ProteinModelPortaliO00910.
SMRiO00910. Positions 239-707.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB_0215388.

Proteomic databases

PRIDEiO00910.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiDDB0215388; DDB0215388; DDB_G0281381.
GeneIDi8623045.
KEGGiddi:DDB_G0281381.

Organism-specific databases

dictyBaseiDDB_G0281381. dstA.

Phylogenomic databases

eggNOGiNOG245085.
InParanoidiO00910.
OMAiMNTEMSA.
PhylomeDBiO00910.

Miscellaneous databases

EvolutionaryTraceiO00910.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.20.58.240. 1 hit.
2.60.40.340. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011992. 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]
PANTHERiPTHR11801. PTHR11801. 1 hit.
PfamiPF09267. Dict-STAT-coil. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF47655. SSF47655. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiSTATA_DICDI
AccessioniPrimary (citable) accession number: O00910
Secondary accession number(s): Q54U00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: July 1, 1997
Last modified: March 4, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Dictyostelium discoideum
    Dictyostelium discoideum: entries, gene names and cross-references to dictyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.