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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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi443 – 487Add BLAST45

GO - Molecular functioni

  • DNA binding Source: dictyBase
  • protein homodimerization activity Source: dictyBase
  • signal transducer activity Source: InterPro
  • transcription factor activity, sequence-specific DNA binding Source: InterPro

GO - Biological processi

  • culmination involved in sorocarp development Source: dictyBase
  • negative regulation of transcription, DNA-templated Source: dictyBase
  • positive regulation of gene expression Source: dictyBase
  • regulation of gene expression Source: dictyBase
  • sorocarp development Source: dictyBase
  • sorocarp stalk cell differentiation Source: dictyBase
  • 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
Proteomesi
  • UP000002195 Componentsi: Chromosome 3, 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

  • cytosol Source: dictyBase
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi443K → D: Loss of DNA binding. 1 Publication1
Mutagenesisi449 – 450RK → DD: About 3-fold reduced DNA binding. 1 Publication2
Mutagenesisi484N → A: Loss of DNA binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003280821 – 707Signal transducer and activator of transcription AAdd BLAST707

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei702Phosphotyrosine1 Publication1

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

PaxDbiO00910.

PTM databases

iPTMnetiO00910.

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei380Interaction with DNABy similarity1
Sitei577Interaction with DNABy similarity1

GO - Molecular functioni

  • protein homodimerization activity Source: dictyBase

Protein-protein interaction databases

STRINGi44689.DDB0215388.

Structurei

Secondary structure

1707
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi245 – 274Combined sources30
Helixi282 – 315Combined sources34
Helixi320 – 351Combined sources32
Beta strandi363 – 368Combined sources6
Beta strandi374 – 376Combined sources3
Turni383 – 385Combined sources3
Beta strandi386 – 391Combined sources6
Beta strandi398 – 409Combined sources12
Turni433 – 436Combined sources4
Beta strandi437 – 439Combined sources3
Beta strandi453 – 463Combined sources11
Beta strandi468 – 472Combined sources5
Beta strandi479 – 484Combined sources6
Turni485 – 487Combined sources3
Helixi488 – 501Combined sources14
Beta strandi505 – 508Combined sources4
Helixi509 – 523Combined sources15
Beta strandi528 – 530Combined sources3
Helixi537 – 546Combined sources10
Turni547 – 550Combined sources4
Beta strandi552 – 555Combined sources4
Helixi556 – 575Combined sources20
Helixi579 – 584Combined sources6
Helixi594 – 599Combined sources6
Turni601 – 603Combined sources3
Beta strandi609 – 613Combined sources5
Beta strandi615 – 617Combined sources3
Beta strandi621 – 626Combined sources6
Beta strandi628 – 631Combined sources4
Beta strandi634 – 638Combined sources5
Helixi641 – 643Combined sources3
Turni646 – 648Combined sources3
Helixi651 – 655Combined sources5
Beta strandi663 – 669Combined sources7
Beta strandi675 – 679Combined sources5
Helixi682 – 685Combined sources4
Helixi687 – 689Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO00910.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini583 – 686SH2PROSITE-ProRule annotationAdd BLAST104

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili242 – 3561 PublicationAdd BLAST115

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi90 – 111Poly-GlnAdd BLAST22
Compositional biasi158 – 213Poly-AsnAdd BLAST56
Compositional biasi214 – 236Poly-GlnAdd BLAST23

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

eggNOGiENOG410XPN8. LUCA.
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_DNA_bind_dom.
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

EnsemblProtistsiEAL66672; EAL66672; 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UURX-ray2.70A235-707[»]
1UUSX-ray2.80A235-707[»]
ProteinModelPortaliO00910.
SMRiO00910.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi44689.DDB0215388.

PTM databases

iPTMnetiO00910.

Proteomic databases

PaxDbiO00910.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiEAL66672; EAL66672; DDB_G0281381.
GeneIDi8623045.
KEGGiddi:DDB_G0281381.

Organism-specific databases

dictyBaseiDDB_G0281381. dstA.

Phylogenomic databases

eggNOGiENOG410XPN8. LUCA.
InParanoidiO00910.
OMAiMNTEMSA.
PhylomeDBiO00910.

Miscellaneous databases

EvolutionaryTraceiO00910.
PROiO00910.

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_DNA_bind_dom.
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...

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: November 2, 2016
This is version 106 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

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 one 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.