O00910 (STATA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Dictyostelium discoideum (Slime mold) [Reference proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	707 AA.
Sequence status	Complete.
Protein existence	Evidence 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 aggreggates 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 process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil SH2 domain
Ligand	DNA-binding
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.5. Source: dictyBase positive regulation of gene expression Inferred from direct assay PubMed 15470642. Source: dictyBase sorocarp stalk cell differentiation Inferred from mutant phenotype Ref.5. Source: dictyBase transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay Ref.3. Source: dictyBase nucleus Inferred from direct assay PubMed 11032815PubMed 12506009Ref.3. Source: dictyBase
Molecular_function	DNA binding Inferred from direct assay Ref.7Ref.1. Source: dictyBase calcium ion binding Inferred from electronic annotation. Source: InterPro phosphoprotein binding Inferred from sequence or structural similarity PubMed 15073273. Source: dictyBase protein homodimerization activity Inferred from direct assay Ref.7. Source: dictyBase signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 707

707

Signal transducer and activator of transcription A

PRO_0000328082

Regions

Domain

583 – 686

104

SH2

DNA binding

443 – 487

45

Coiled coil

242 – 356

115

Ref.7

Compositional bias

90 – 111

22

Poly-Gln

Compositional bias

158 – 213

56

Poly-Asn

Compositional bias

214 – 236

23

Poly-Gln

Sites

Site

380

1

Interaction with DNA By similarity

Site

577

1

Interaction with DNA By similarity

Amino acid modifications

Modified residue

702

1

Phosphotyrosine Ref.3

Experimental info

Mutagenesis

443

1

K → D: Loss of DNA binding. Ref.7

Mutagenesis

449 – 450

2

RK → DD: About 3-fold reduced DNA binding.

Mutagenesis

484

1

N → A: Loss of DNA binding. Ref.7

Secondary structure

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707

Helix Strand Turn

Details...

Helix

245 – 274

30

Helix

282 – 315

34

Helix

320 – 351

32

Beta strand

363 – 368

6

Beta strand

374 – 376

3

Turn

383 – 385

3

Beta strand

386 – 391

6

Beta strand

398 – 409

12

Turn

433 – 436

4

Beta strand

437 – 439

3

Beta strand

453 – 463

11

Beta strand

468 – 472

5

Beta strand

479 – 484

6

Turn

485 – 487

3

Helix

488 – 501

14

Beta strand

505 – 508

4

Helix

509 – 523

15

Beta strand

528 – 530

3

Helix

537 – 546

10

Turn

547 – 550

4

Beta strand

552 – 555

4

Helix

556 – 575

20

Helix

579 – 584

6

Helix

594 – 599

6

Turn

601 – 603

3

Beta strand

609 – 613

5

Beta strand

615 – 617

3

Beta strand

621 – 626

6

Beta strand

628 – 631

4

Beta strand

634 – 638

5

Helix

641 – 643

3

Turn

646 – 648

3

Helix

651 – 655

5

Beta strand

663 – 669

7

Beta strand

675 – 679

5

Helix

682 – 685

4

Helix

687 – 689

3

Sequences

	Sequence		Length	Mass (Da)
	O00910 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 9803388BD324D7B6	FASTA	707	79,792
	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

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY, FUNCTION, SUBUNIT, DEVELOPMENTAL STAGE, TYROSINE PHOSPHORYLATION. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y13097 mRNA. Translation: CAA73551.1.
AAFI02000041 Genomic DNA. Translation: EAL66672.1.

RefSeq

XP_640661.1. XM_635569.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UUR	X-ray	2.70	A	235-707	[»]
1UUS	X-ray	2.80	A	235-707	[»]

ProteinModelPortal

O00910.

SMR

O00910. Positions 239-707.

ModBase

Search...

Protein-protein interaction databases

STRING

44689.DDB_0215388.

Proteomic databases

PRIDE

O00910.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblProtists

DDB0215388; DDB0215388; DDB_G0281381.

GeneID

8623045.

KEGG

ddi:DDB_G0281381.

Organism-specific databases

dictyBase

DDB_G0281381. dstA.

Phylogenomic databases

eggNOG

NOG245085.

OMA

MNTEMSA.

ProtClustDB

CLSZ2429261.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.
1.20.58.240. 1 hit.
2.60.40.340. 1 hit.
3.30.505.10. 1 hit.

InterPro

IPR011992. EF-hand-like_dom.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
IPR000980. SH2.
IPR015988. STAT_TF_coiled-coil.
IPR015347. STAT_TF_homologue_coiled-coil.
[Graphical view]

Pfam

PF09267. Dict-STAT-coil. 1 hit.
PF00017. SH2. 1 hit.
[Graphical view]

SMART

SM00252. SH2. 1 hit.
[Graphical view]

SUPFAM

SSF49417. P53_like_DNA_bnd. 1 hit.
SSF47655. STAT. 1 hit.

PROSITE

PS50001. SH2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O00910.

Entry information

Entry name

STATA_DICDI

Accession

Primary (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 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)