STATA_DICDI
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 25-MAY-2022, entry version 133.
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 (Slime mold).
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 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.DDB0215388; -.
DR iPTMnet; O00910; -.
DR PaxDb; O00910; -.
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 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 transcription, DNA-templated; 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 Gene3D; 2.60.40.340; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR IDEAL; IID50264; -.
DR InterPro; IPR041604; EF-hand_12.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
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; PTHR11801; 3.
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; SSF47655; SSF47655; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF55550; SSF55550; 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
