ID   STATA_DICDI             Reviewed;         707 AA.
AC   O00910; Q54U00;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 138.
DE   RecName: Full=Signal transducer and activator of transcription A;
DE   AltName: Full=Dd-STATa;
DE   AltName: Full=STAT5 homolog A;
GN   Name=dstA; Synonyms=stat5, statA; ORFNames=DDB_G0281381;
OS   Dictyostelium discoideum (Social amoeba).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBUNIT,
RP   DEVELOPMENTAL STAGE, TYROSINE PHOSPHORYLATION, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=AX2;
RX   PubMed=9200609; DOI=10.1016/s0092-8674(00)80276-7;
RA   Kawata T., Shevchenko A., Fukuzawa M., Jermyn K.A., Totty N.F.,
RA   Zhukovskaya N.V., Sterling A.E., Mann M., Williams J.G.;
RT   "SH2 signaling in a lower eukaryote: a STAT protein that regulates stalk
RT   cell differentiation in dictyostelium.";
RL   Cell 89:909-916(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [3]
RP   PHOSPHORYLATION AT TYR-702, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=9670017; DOI=10.1093/emboj/17.14.4018;
RA   Araki T., Gamper M., Early A., Fukuzawa M., Abe T., Kawata T., Kim E.,
RA   Firtel R.A., Williams J.G.;
RT   "Developmentally and spatially regulated activation of a Dictyostelium STAT
RT   protein by a serpentine receptor.";
RL   EMBO J. 17:4018-4028(1998).
RN   [4]
RP   CYCLIC AMP-INDUCED PHOSPHORYLATION.
RX   PubMed=11319871; DOI=10.1006/dbio.2001.0217;
RA   Briscoe C., Moniakis J., Kim J.-Y., Brown J.M., Hereld D., Devreotes P.N.,
RA   Firtel R.A.;
RT   "The phosphorylated C-terminus of cAR1 plays a role in cell-type-specific
RT   gene expression and STATa tyrosine phosphorylation.";
RL   Dev. Biol. 233:225-236(2001).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=10393118; DOI=10.1242/dev.126.15.3391;
RA   Mohanty S., Jermyn K.A., Early A., Kawata T., Aubry L., Ceccarelli A.,
RA   Schaap P., Williams J.G., Firtel R.A.;
RT   "Evidence that the Dictyostelium Dd-STATa protein is a repressor that
RT   regulates commitment to stalk cell differentiation and is also required for
RT   efficient chemotaxis.";
RL   Development 126:3391-3405(1999).
RN   [6]
RP   SUBCELLULAR LOCATION, FUNCTION, AND MODULATION OF TYROSINE PHOSPHORYLATION.
RX   PubMed=11254360; DOI=10.1006/dbio.2001.0171;
RA   Early A., Gamper M., Moniakis J., Kim E., Hunter T., Williams J.G.,
RA   Firtel R.A.;
RT   "Protein tyrosine phosphatase PTP1 negatively regulates Dictyostelium STATa
RT   and is required for proper cell-type proportioning.";
RL   Dev. Biol. 232:233-245(2001).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 235-707 OF TYROSINE PHOSPHORYLATED
RP   HOMODIMER, COILED-COIL DOMAIN, FUNCTION, SUBUNIT, AND MUTAGENESIS OF
RP   LYS-443; 449-ARG-LYS-450 AND ASN-484.
RX   PubMed=15053873; DOI=10.1016/s1097-2765(04)00130-3;
RA   Soler-Lopez M., Petosa C., Fukuzawa M., Ravelli R., Williams J.G.,
RA   Mueller C.W.;
RT   "Structure of an activated Dictyostelium STAT in its DNA-unbound form.";
RL   Mol. Cell 13:791-804(2004).
CC   -!- FUNCTION: Transcription factor that binds to 5'-TTGAATTGA-3' elements
CC       in the promoter region of target genes. Functions as a repressor of the
CC       ecmB gene. Regulates the differentiation of prestalk cells during
CC       development. {ECO:0000269|PubMed:10393118, ECO:0000269|PubMed:11254360,
CC       ECO:0000269|PubMed:15053873, ECO:0000269|PubMed:9200609}.
CC   -!- SUBUNIT: Monomer, in the absence of tyrosine phosphorylation.
CC       Homodimer, or heterodimer with another family member, when tyrosine
CC       phosphorylated. {ECO:0000269|PubMed:15053873,
CC       ECO:0000269|PubMed:9200609}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in growing
CC       cells. Translocated into the nucleus in response to cAMP-induced
CC       tyrosine phosphorylation. Nuclear at the tight mound stage and in the
CC       upper, prestalk region of tipped aggregates and in cells at the tip of
CC       the slug. Subject to crm1-dependent nuclear export.
CC   -!- DEVELOPMENTAL STAGE: Constitutively expressed with a slight increase
CC       during the tight mound stage (at protein level). Detected at very low
CC       levels in growing cells and aggregates up to the loose mound stage.
CC       Highly expressed in tipped aggregates and in the Mexican hat stage.
CC       Expressed at lower levels in early and late culminants and in fruiting
CC       bodies. {ECO:0000269|PubMed:9200609, ECO:0000269|PubMed:9670017}.
CC   -!- PTM: Tyrosine phosphorylated in response to cAMP. Not tyrosine
CC       phosphorylated in growing cells. Tyrosine phosphorylation is first
CC       detected at the tight mound stage, continues throughout the slug stage
CC       and early culmination, and starts to decrease at mid-culmination.
CC       Barely detectable in fruiting bodies. {ECO:0000269|PubMed:9670017}.
CC   -!- DISRUPTION PHENOTYPE: Cells are hypersensitive to the chlorinated
CC       hexaphenone DIF. They form slugs, but there is little or no stalk cell
CC       differentiation. After several days of developmental arrest very small
CC       spore masses appear that are supported by columns of apparently
CC       undifferentiated cells. {ECO:0000269|PubMed:10393118}.
CC   -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC       {ECO:0000305}.
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DR   EMBL; Y13097; CAA73551.1; -; mRNA.
DR   EMBL; AAFI02000041; EAL66672.1; -; Genomic_DNA.
DR   RefSeq; XP_640661.1; XM_635569.1.
DR   PDB; 1UUR; X-ray; 2.70 A; A=235-707.
DR   PDB; 1UUS; X-ray; 2.80 A; A=235-707.
DR   PDBsum; 1UUR; -.
DR   PDBsum; 1UUS; -.
DR   AlphaFoldDB; O00910; -.
DR   SMR; O00910; -.
DR   STRING; 44689.O00910; -.
DR   iPTMnet; O00910; -.
DR   PaxDb; 44689-DDB0215388; -.
DR   EnsemblProtists; EAL66672; EAL66672; DDB_G0281381.
DR   GeneID; 8623045; -.
DR   KEGG; ddi:DDB_G0281381; -.
DR   dictyBase; DDB_G0281381; dstA.
DR   eggNOG; KOG3667; Eukaryota.
DR   HOGENOM; CLU_390520_0_0_1; -.
DR   InParanoid; O00910; -.
DR   OMA; QMNTEMS; -.
DR   PhylomeDB; O00910; -.
DR   Reactome; R-DDI-1059683; Interleukin-6 signaling.
DR   Reactome; R-DDI-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-DDI-201556; Signaling by ALK.
DR   Reactome; R-DDI-3249367; STAT6-mediated induction of chemokines.
DR   Reactome; R-DDI-6783783; Interleukin-10 signaling.
DR   Reactome; R-DDI-6785807; Interleukin-4 and Interleukin-13 signaling.
DR   Reactome; R-DDI-877300; Interferon gamma signaling.
DR   Reactome; R-DDI-877312; Regulation of IFNG signaling.
DR   Reactome; R-DDI-8854691; Interleukin-20 family signaling.
DR   Reactome; R-DDI-8983432; Interleukin-15 signaling.
DR   Reactome; R-DDI-8984722; Interleukin-35 Signalling.
DR   Reactome; R-DDI-8985947; Interleukin-9 signaling.
DR   Reactome; R-DDI-9008059; Interleukin-37 signaling.
DR   Reactome; R-DDI-9020591; Interleukin-12 signaling.
DR   Reactome; R-DDI-9020933; Interleukin-23 signaling.
DR   Reactome; R-DDI-9020956; Interleukin-27 signaling.
DR   Reactome; R-DDI-909733; Interferon alpha/beta signaling.
DR   Reactome; R-DDI-9701898; STAT3 nuclear events downstream of ALK signaling.
DR   Reactome; R-DDI-9833482; PKR-mediated signaling.
DR   EvolutionaryTrace; O00910; -.
DR   PRO; PR:O00910; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR   GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR   GO; GO:0003677; F:DNA binding; IDA:dictyBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:dictyBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0031154; P:culmination involved in sorocarp development; IMP:dictyBase.
DR   GO; GO:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:dictyBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:dictyBase.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0097696; P:receptor signaling pathway via STAT; IDA:dictyBase.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0010468; P:regulation of gene expression; IDA:dictyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0030587; P:sorocarp development; HMP:dictyBase.
DR   GO; GO:0031149; P:sorocarp stalk cell differentiation; IMP:dictyBase.
DR   CDD; cd09919; SH2_STAT_family; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 2.60.40.340; Rel homology domain (RHD), DNA-binding domain; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   IDEAL; IID50264; -.
DR   InterPro; IPR041604; EF-hand_12.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR   InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR001217; STAT.
DR   InterPro; IPR015988; STAT_TF_coiled-coil.
DR   InterPro; IPR015347; STAT_TF_homologue_coiled-coil.
DR   InterPro; IPR041410; STATa_Ig.
DR   PANTHER; PTHR11801:SF65; C2H2-TYPE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR11801; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION; 1.
DR   Pfam; PF09267; Dict-STAT-coil; 1.
DR   Pfam; PF17901; EF-hand_12; 1.
DR   Pfam; PF00017; SH2; 1.
DR   Pfam; PF18214; STATa_Ig; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF49417; p53-like transcription factors; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF47655; STAT; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW   SH2 domain; Transcription; Transcription regulation.
FT   CHAIN           1..707
FT                   /note="Signal transducer and activator of transcription A"
FT                   /id="PRO_0000328082"
FT   DOMAIN          583..686
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DNA_BIND        443..487
FT   REGION          70..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          242..356
FT                   /evidence="ECO:0000269|PubMed:15053873"
FT   COMPBIAS        70..128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            380
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   SITE            577
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         702
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:9670017"
FT   MUTAGEN         443
FT                   /note="K->D: Loss of DNA binding."
FT                   /evidence="ECO:0000269|PubMed:15053873"
FT   MUTAGEN         449..450
FT                   /note="RK->DD: About 3-fold reduced DNA binding."
FT                   /evidence="ECO:0000269|PubMed:15053873"
FT   MUTAGEN         484
FT                   /note="N->A: Loss of DNA binding."
FT                   /evidence="ECO:0000269|PubMed:15053873"
FT   HELIX           245..274
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           282..315
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           320..351
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          363..368
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          374..376
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   TURN            383..385
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          386..391
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          398..409
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   TURN            433..436
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          437..439
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          453..463
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          468..472
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          479..484
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   TURN            485..487
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           488..501
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          505..508
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           509..523
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          528..530
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           537..546
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   TURN            547..550
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          552..555
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           556..575
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           579..584
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           594..599
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   TURN            601..603
FT                   /evidence="ECO:0007829|PDB:1UUS"
FT   STRAND          609..613
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          615..617
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          621..626
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          628..631
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          634..638
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           641..643
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   TURN            646..648
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           651..655
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          663..669
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   STRAND          675..679
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           682..685
FT                   /evidence="ECO:0007829|PDB:1UUR"
FT   HELIX           687..689
FT                   /evidence="ECO:0007829|PDB:1UUR"
SQ   SEQUENCE   707 AA;  79792 MW;  9803388BD324D7B6 CRC64;
     MSSAEFSMDD FEDTFDSNAT ISTKDLFEGS DRLPLNQSIN TTIQNLYLPN GGFAIGDQSQ
     QQYYQAMPPL NQSDQFNLGR SNNLTPRTNQ LQQLQQQQQQ QQQPQQQQQQ QTYGTQSPIH
     MSQTPSSPLS SPLPSPTPFS RQQSYNNNNS NNTSSSQNYN NNNININNNN NNNNTNNNNN
     NNNGNNSNGN NGNNNNNNNN NNNNNTNNNN NNNQQQQQQQ QQQQQQQQQQ QQQQQQGNPN
     LSSPQPILDT IYKLLSEQEQ TLVQMIHEQS LLLNRLPPTL DENSLAPLKS LSQKQITLSG
     QMNTEMSALD ATKKGMILEP TDLAKLFALK QDLQIQFKQL SLLHNEIQSI LNPQHSAPKP
     NVALVLKSQP FPVVISKGKQ LGENQLVVLV LTGARSNFHI NGPVKATMIC DSHPTNKNNP
     TTPLEMDSQP IYPATLTAHF PLKFLAGTRK CSVNLKFGVN IRDLDNVTTT VESDASNPFV
     VITNECQWEG SAGVLLKKDA FDGQLEITWA QFINTLQRHF LIATKQDPVR PKRPLSSYDL
     KYIQTHFFGN RSIIHQQDFD KFWVWFGKSM QTLRYQRHIS TLWQEGIIYG YMGRQEVNDA
     LQNQDPGTFI IRFSERNPGQ FGIAYIGVEM PARIKHYLVQ PNDTAAAKKT FPDFLSEHSQ
     FVNLLQWTKD TNGAPRFLKL HKDTALGSFA PKRTAPVPVG GYEPLNS
//