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STATC_DICDI
ID   STATC_DICDI             Reviewed;         931 AA.
AC   Q54BD4; Q9BLX2;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Signal transducer and activator of transcription C;
DE   AltName: Full=Dd-STATc;
DE   AltName: Full=STAT5 homolog C;
GN   Name=dstC; Synonyms=statC; ORFNames=DDB_G0293532;
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], PHOSPHORYLATION AT TYR-924, DISRUPTION
RP   PHENOTYPE, FUNCTION, SUBUNIT, DEVELOPMENTAL STAGE, MUTAGENESIS OF TYR-924,
RP   AND SUBCELLULAR LOCATION.
RC   STRAIN=AX2;
RX   PubMed=11336701; DOI=10.1016/s1097-2765(01)00222-2;
RA   Fukuzawa M., Araki T., Adrian I., Williams J.G.;
RT   "Tyrosine phosphorylation-independent nuclear translocation of a
RT   dictyostelium STAT in response to DIF signaling.";
RL   Mol. Cell 7:779-788(2001).
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   SUBCELLULAR LOCATION, AND MUTAGENESIS OF 7-LYS--ARG-9.
RX   PubMed=12506009; DOI=10.1242/dev.00303;
RA   Fukuzawa M., Abe T., Williams J.G.;
RT   "The Dictyostelium prestalk cell inducer DIF regulates nuclear accumulation
RT   of a STAT protein by controlling its rate of export from the nucleus.";
RL   Development 130:797-804(2003).
RN   [4]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=17517120; DOI=10.1186/1471-2164-8-123;
RA   Na J., Tunggal B., Eichinger L.;
RT   "STATc is a key regulator of the transcriptional response to hyperosmotic
RT   shock.";
RL   BMC Genomics 8:123-123(2007).
CC   -!- FUNCTION: Transcription factor that regulates gene expression during
CC       development. May play a role in regulating gene expression in response
CC       to osmotic stress. {ECO:0000269|PubMed:11336701,
CC       ECO:0000269|PubMed:17517120}.
CC   -!- SUBUNIT: Monomer, in the absence of tyrosine phosphorylation.
CC       Homodimer, or heterodimer with another family member, when tyrosine
CC       phosphorylated. {ECO:0000269|PubMed:11336701}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Tyrosine phosphorylation
CC       is not required for translocation to the nucleus. DIF inhibits export
CC       from the nucleus. Predominantly nuclear in pstO cells at the rear of
CC       the prestalk region in the slug. Subject to crm1-dependent nuclear
CC       export.
CC   -!- DEVELOPMENTAL STAGE: Constitutively expressed during development (at
CC       protein level). {ECO:0000269|PubMed:11336701}.
CC   -!- INDUCTION: Up-regulated in response to hyperosmotic shock.
CC       {ECO:0000269|PubMed:17517120}.
CC   -!- PTM: Tyrosine phosphorylated in response to the chlorinated hexaphenone
CC       DIF. Minimally phosphorylated in the absence of DIF. Phosphorylation
CC       increases during development, is highest during the slug stage, with a
CC       strong decrease at culmination. {ECO:0000269|PubMed:11336701}.
CC   -!- DISRUPTION PHENOTYPE: Cells display abnormal regulation of gene
CC       expression and aberrant timing of development. Colonies growing on a
CC       bacterial lawn are smaller, have a rough edge and are surrounded by
CC       satellite fruiting bodies. {ECO:0000269|PubMed:11336701}.
CC   -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC       {ECO:0000305}.
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DR   EMBL; AJ301670; CAC33514.1; -; mRNA.
DR   EMBL; AAFI02000218; EAL60578.1; -; Genomic_DNA.
DR   RefSeq; XP_629095.1; XM_629093.1.
DR   AlphaFoldDB; Q54BD4; -.
DR   SMR; Q54BD4; -.
DR   STRING; 44689.DDB0215378; -.
DR   iPTMnet; Q54BD4; -.
DR   PaxDb; Q54BD4; -.
DR   EnsemblProtists; EAL60578; EAL60578; DDB_G0293532.
DR   GeneID; 8629388; -.
DR   KEGG; ddi:DDB_G0293532; -.
DR   dictyBase; DDB_G0293532; dstC.
DR   eggNOG; KOG3667; Eukaryota.
DR   HOGENOM; CLU_314362_0_0_1; -.
DR   InParanoid; Q54BD4; -.
DR   OMA; HPQKETF; -.
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   PRO; PR:Q54BD4; -.
DR   Proteomes; UP000002195; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; IDA:dictyBase.
DR   GO; GO:0005634; C:nucleus; 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:0006952; P:defense response; IBA:GO_Central.
DR   GO; GO:0006972; P:hyperosmotic response; IDA:dictyBase.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:dictyBase.
DR   GO; GO:0010628; P:positive regulation of gene expression; IMP:dictyBase.
DR   GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR   GO; GO:0047484; P:regulation of response to osmotic stress; IMP:dictyBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0043157; P:response to cation stress; IMP:dictyBase.
DR   GO; GO:1903013; P:response to differentiation-inducing factor 1; HDA:dictyBase.
DR   GO; GO:0009408; P:response to heat; IDA:dictyBase.
DR   GO; GO:0006970; P:response to osmotic stress; IMP:dictyBase.
DR   GO; GO:0006979; P:response to oxidative stress; IDA:dictyBase.
DR   GO; GO:0030587; P:sorocarp development; IEP:dictyBase.
DR   GO; GO:0031288; P:sorocarp morphogenesis; IMP:dictyBase.
DR   Gene3D; 2.60.40.340; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
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; 2.
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   Coiled coil; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; SH2 domain; Transcription; Transcription regulation.
FT   CHAIN           1..931
FT                   /note="Signal transducer and activator of transcription C"
FT                   /id="PRO_0000328083"
FT   DOMAIN          802..931
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DNA_BIND        662..706
FT                   /evidence="ECO:0000250"
FT   REGION          1..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          6..46
FT                   /note="Mediates DIF-inducible nuclear import"
FT   REGION          98..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          304..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..554
FT                   /note="Mediates nuclear export"
FT   COILED          471..577
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        27..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         924
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:11336701"
FT   MUTAGEN         7..9
FT                   /note="KKR->AAA: No effect on nuclear import."
FT                   /evidence="ECO:0000269|PubMed:12506009"
FT   MUTAGEN         924
FT                   /note="Y->F: Loss of activity. Has no effect on DIF-induced
FT                   translocation to the nucleus."
FT                   /evidence="ECO:0000269|PubMed:11336701"
FT   CONFLICT        116
FT                   /note="N -> Y (in Ref. 1; CAC33514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        119
FT                   /note="T -> TN (in Ref. 1; CAC33514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="I -> N (in Ref. 1; CAC33514)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        334..336
FT                   /note="Missing (in Ref. 1; CAC33514)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   931 AA;  107204 MW;  16C6D75D30812B32 CRC64;
     MSNNNPKKRP LDAISNTFEV KQEEPEFSSD GFNTTNDDLM SLMTFLDNGT GQQNQQNQQN
     QQPQPQPQPQ PQLPQPQSQQ PIYNSNTTTV TVKTEGIATS PLSNASSPIS TNNNINNNTN
     NNNNNNNNNN NNNNNNNNNN NNINTATPPA IGVQQNSNIP YSYPIYTDVT GQQTQHQQNI
     GQNSVNIDPY FQTIDGAQIQ QQQLLQQQLQ PIQQVNNPQI DQAQIQQQQA QQIQQQQAQI
     QAQQAQIQQQ QLEQQHLQQQ QFQFQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQHHQQ
     QQQQQQHQQQ QQHQQQQQHQ QHQQQQHQQH QQIHQNHQNQ LNHQNQLNNQ NQLNNQNQLN
     NQNQLNHQNQ LNQPTQPQMQ QIELPILHQL PVEPQHLHPI PTHINNNGNN NNNNNNNGSN
     SSNSSNGIGS PDDIIEPNIL SSIQHCNNNN LPLPDHLLIN TPYGNVLQPH QQIINECLKL
     HLAQKEQLDK MKIVQKQVLA HPQKETFQML DNEQNTLKKQ IDAEITSLQQ IDQTFVLSPP
     EIRNVIFLLH ELTIQSIQLE LYHEELQLLV RPQNPPPTIA ALVVIEQPFP MVITKCKPLE
     DDPVVVQLLC GTRTELQMIG KVRATMIVEN QQGSKTSSSP KTIETEVVSM DETNRLAKYH
     LKFLNGTRKN PVTLKFGMQV QVVGGTAVNI ESPPTSPFIV ITNECQYEES DGTLLKKDSF
     GNNNEIPWAS YANKLQRHFL RATRQDFMKP TRYLSRHELM YIHHQFFGSK PMIPQSSFDS
     FWIWFGKGLQ KLRYQRHVCS MWQSGLIYGF ISRQSVEEAL RNEEQGTFLI RFSERHAGHF
     AVGYKVDDPD PEKRIRHYLV KADDTAGAKK TLPDFLSECP QFTKILQLTI DVSTGEPRLR
     NFPKDVVLEP YYSKRETLPA TNGYDSLPTI L
 
 
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