STAT_ANOGA
ID STAT_ANOGA Reviewed; 722 AA.
AC Q7QDU4; O97164;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Signal transducer and transcription activator;
DE AltName: Full=Ag-STAT;
GN Name=Stat; ORFNames=AGAP010423;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAA09070.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=G3 {ECO:0000312|EMBL:CAA09070.1};
RX PubMed=10022838; DOI=10.1093/emboj/18.4.959;
RA Barillas-Mury C., Han Y.-S., Seeley D., Kafatos F.C.;
RT "Anopheles gambiae Ag-STAT, a new insect member of the STAT family is
RT activated in response to bacterial infection.";
RL EMBO J. 18:959-967(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:EAA07203.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST {ECO:0000312|EMBL:EAA07203.1};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: Signal transduction and activation of transcription. Plays an
CC important role in the segmental pattern formation in the early embryo
CC by activating specific stripes of pair rule gene expression (By
CC similarity). The STAT pathway directly participates in immune responses
CC in insects. {ECO:0000250|UniProtKB:Q24151,
CC ECO:0000269|PubMed:10022838}.
CC -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC member. {ECO:0000250|UniProtKB:P51692}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Translocated into the nucleus in response to phosphorylation.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in hemocytes, pericardial cells, midgut,
CC skeletal muscle and fat body cells. {ECO:0000269|PubMed:10022838}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all developmental stages.
CC {ECO:0000269|PubMed:10022838}.
CC -!- INDUCTION: Bacterial challenge results in nuclear translocation in fat
CC body cells and induction of DNA-binding activity that recognizes a STAT
CC target site. In vitro treatment with pervanadate (vanadate and
CC H(2)O(2)) translocates protein to the nucleus in midgut epithelial
CC cells. {ECO:0000269|PubMed:10022838}.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000255}.
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DR EMBL; AJ010299; CAA09070.1; -; Genomic_DNA.
DR EMBL; AAAB01008849; EAA07203.1; -; Genomic_DNA.
DR RefSeq; XP_311525.1; XM_311525.1.
DR AlphaFoldDB; Q7QDU4; -.
DR SMR; Q7QDU4; -.
DR STRING; 7165.AGAP010423-PA; -.
DR PaxDb; Q7QDU4; -.
DR GeneID; 1272625; -.
DR KEGG; aga:AgaP_AGAP010423; -.
DR CTD; 1272625; -.
DR VEuPathDB; VectorBase:AGAP010423; -.
DR eggNOG; KOG3667; Eukaryota.
DR HOGENOM; CLU_014189_2_0_1; -.
DR InParanoid; Q7QDU4; -.
DR OMA; PNCADQK; -.
DR OrthoDB; 327469at2759; -.
DR PhylomeDB; Q7QDU4; -.
DR Proteomes; UP000007062; Chromosome 3L.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
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: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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR Gene3D; 1.10.532.10; -; 1.
DR Gene3D; 2.60.40.630; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR001217; STAT.
DR InterPro; IPR036535; STAT_N_sf.
DR InterPro; IPR013800; STAT_TF_alpha.
DR InterPro; IPR015988; STAT_TF_coiled-coil.
DR InterPro; IPR013801; STAT_TF_DNA-bd.
DR InterPro; IPR012345; STAT_TF_DNA-bd_N.
DR InterPro; IPR013799; STAT_TF_prot_interaction.
DR PANTHER; PTHR11801; PTHR11801; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF01017; STAT_alpha; 1.
DR Pfam; PF02864; STAT_bind; 1.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00964; STAT_int; 1.
DR SUPFAM; SSF47655; SSF47655; 1.
DR SUPFAM; SSF48092; SSF48092; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 2: Evidence at transcript level;
KW Activator; Cytoplasm; Developmental protein; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; SH2 domain; Transcription;
KW Transcription regulation.
FT CHAIN 1..722
FT /note="Signal transducer and transcription activator"
FT /id="PRO_0000233907"
FT DOMAIN 545..644
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 667..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 155
FT /note="Q -> H (in Ref. 1; CAA09070)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="N -> Y (in Ref. 1; CAA09070)"
FT /evidence="ECO:0000305"
FT CONFLICT 311
FT /note="T -> S (in Ref. 1; CAA09070)"
FT /evidence="ECO:0000305"
FT CONFLICT 547
FT /note="D -> N (in Ref. 1; CAA09070)"
FT /evidence="ECO:0000305"
FT CONFLICT 684
FT /note="T -> A (in Ref. 1; CAA09070)"
FT /evidence="ECO:0000305"
FT CONFLICT 687..689
FT /note="NDM -> KDT (in Ref. 1; CAA09070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 722 AA; 83879 MW; BB106241A28F36CC CRC64;
METRLHQLPP CILEQFHFLN DLKYPVLIRQ HLGNWIKDSL HNAPTYTNNM QSMYELDAAK
FFTALVNEVD QVSANLPNKR KCLLCRSAIM LRDQNFQNLT QLYLTLLHQI QPNCEKGCKT
EYTIAQTSSD GQQTDVLYGL QQLHVMERNN WKETQQLIQE CEQDHVQRLS NQRSHNKRIQ
CYSLKQRSLV DAFQKTIRKA EEVLNLVYNK YIFEWQKTQM FPEVRSTNAY SLDEIQTWYE
SLAAIMWNTK DQIHLTMKSQ LREHVSQEIN SDLWKVMKDV KDFIKLLLHK AFIVENQPPQ
VMKMNTRFCA TVRLLIDNAL IMKIGNPKVT VSIISETQAQ QIQSTNAAAD FSAGEIENNI
GNLQYQLSNK FLANFSNMRL KKINRGNRKL NKLVVDEKFA LLFQSSFTLE QEELTVTVWT
LSLPAVVIVH VNQEQLAWTT IIWDNLCAKA DRKLFEVPNL IPWNRLVEAI SMTFSARVGR
GLTDENMQYM YRKAYRDKLS FSVSNDQMIS FAQFCKDTTP ECNYTFWEWL YAALKIIRDH
LQVLWVDNTI IGFIHKSTAE KYLAKCVPGT FLLRFTDSVL GGISIAWVHE SNDGQRQVLH
IQPFTAKDLV VRSLANRICD LGELTYLYPT IPKQEAFGRY TAPAIQKPRS KHYISAEMRT
VLIFAPSSNQ SSSSTPNAEQ SPSTSSNDMF SNEYVLTNLD EIYKFEIEND DMLSIQDYWE
QQ
