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 27-MAR-2024, entry version 118.
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 (Social amoeba).
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.Q54BD4; -.
DR iPTMnet; Q54BD4; -.
DR PaxDb; 44689-DDB0215378; -.
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; NEIPWAS; -.
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 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:1990782; F:protein tyrosine kinase 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 DNA-templated transcription; 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:0080135; P:regulation of cellular response to stress; IMP:dictyBase.
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 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 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; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION; 1.
DR PANTHER; PTHR11801:SF50; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION C; 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 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
//
