STATB_CAEEL
ID STATB_CAEEL Reviewed; 567 AA.
AC Q20977; B2D6L5; Q20978; Q95ZS4; Q9U9L4;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 4.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Signal transducer and activator of transcription b;
DE AltName: Full=Zinc finger protein STAT-B;
GN Name=sta-2 {ECO:0000312|WormBase:F58E6.1};
GN Synonyms=stat-b {ECO:0000312|WormBase:F58E6.1}; ORFNames=F58E6.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Liu X., Quinn A.M., Chin Y.E., Fu X.;
RT "STAT genes found in Caenorhabditis elegans.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP FUNCTION.
RX PubMed=22470487; DOI=10.1371/journal.pone.0033887;
RA Labed S.A., Omi S., Gut M., Ewbank J.J., Pujol N.;
RT "The pseudokinase NIPI-4 is a novel regulator of antimicrobial peptide gene
RT expression.";
RL PLoS ONE 7:E33887-E33887(2012).
CC -!- FUNCTION: Carries out a dual function: signal transduction and
CC activation of transcription (By similarity). By regulating the up-
CC regulation in the epidermis of antimicrobial peptides nlp-29, plays a
CC role in resistance to fungal infection and in the response to physical
CC wounding and phorbol ester PMA treatment (PubMed:22470487).
CC {ECO:0000250|UniProtKB:P51692, ECO:0000269|PubMed:22470487}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Translocated into the nucleus in response to phosphorylation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD45535.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AF164113; AAD45535.1; ALT_SEQ; mRNA.
DR EMBL; Z70754; CAQ35047.1; -; Genomic_DNA.
DR PIR; T22925; T22925.
DR RefSeq; NP_001122963.1; NM_001129491.1.
DR AlphaFoldDB; Q20977; -.
DR SMR; Q20977; -.
DR BioGRID; 532609; 4.
DR STRING; 6239.F58E6.1; -.
DR EPD; Q20977; -.
DR PaxDb; Q20977; -.
DR PeptideAtlas; Q20977; -.
DR PRIDE; Q20977; -.
DR EnsemblMetazoa; F58E6.1.1; F58E6.1.1; WBGene00010251.
DR GeneID; 3565291; -.
DR KEGG; cel:CELE_F58E6.1; -.
DR CTD; 3565291; -.
DR WormBase; F58E6.1; CE42515; WBGene00010251; sta-2.
DR eggNOG; KOG1609; Eukaryota.
DR GeneTree; ENSGT01050000244905; -.
DR HOGENOM; CLU_493742_0_0_1; -.
DR InParanoid; Q20977; -.
DR OMA; LIYPDID; -.
DR OrthoDB; 327469at2759; -.
DR PhylomeDB; Q20977; -.
DR Reactome; R-CEL-1059683; Interleukin-6 signaling.
DR Reactome; R-CEL-1169408; ISG15 antiviral mechanism.
DR Reactome; R-CEL-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-CEL-186763; Downstream signal transduction.
DR Reactome; R-CEL-201556; Signaling by ALK.
DR Reactome; R-CEL-3249367; STAT6-mediated induction of chemokines.
DR Reactome; R-CEL-6783783; Interleukin-10 signaling.
DR Reactome; R-CEL-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-CEL-877300; Interferon gamma signaling.
DR Reactome; R-CEL-8854691; Interleukin-20 family signaling.
DR Reactome; R-CEL-8983432; Interleukin-15 signaling.
DR Reactome; R-CEL-8984722; Interleukin-35 Signalling.
DR Reactome; R-CEL-8985947; Interleukin-9 signaling.
DR Reactome; R-CEL-9008059; Interleukin-37 signaling.
DR Reactome; R-CEL-9020591; Interleukin-12 signaling.
DR Reactome; R-CEL-9020933; Interleukin-23 signaling.
DR Reactome; R-CEL-9020956; Interleukin-27 signaling.
DR Reactome; R-CEL-909733; Interferon alpha/beta signaling.
DR Reactome; R-CEL-9701898; STAT3 nuclear events downstream of ALK signaling.
DR PRO; PR:Q20977; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00010251; Expressed in larva and 3 other tissues.
DR GO; GO:0045177; C:apical part of cell; IDA:WormBase.
DR GO; GO:0030139; C:endocytic vesicle; IDA:WormBase.
DR GO; GO:0030056; C:hemidesmosome; IDA:WormBase.
DR GO; GO:0098733; C:hemidesmosome associated protein complex; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
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:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0002804; P:positive regulation of antifungal peptide production; IMP:WormBase.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
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:0009611; P:response to wounding; IMP:UniProtKB.
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; IPR013801; STAT_TF_DNA-bd.
DR InterPro; IPR012345; STAT_TF_DNA-bd_N.
DR PANTHER; PTHR11801; PTHR11801; 1.
DR Pfam; PF02864; STAT_bind; 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..567
FT /note="Signal transducer and activator of transcription b"
FT /id="PRO_0000234104"
FT DOMAIN 449..548
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
SQ SEQUENCE 567 AA; 65018 MW; 69DBBDE560D10A82 CRC64;
MSSVVSDQMD IESSSAFSPA EPVVDGAFVS KHNLSAEAYQ GFKECADSLL SGKIAQNEQL
PFIQRTLQIC ENVILNFEDE KQHLMSDVLL VWAMKQQKLS IATLHTQQLH YKELDLINLQ
FEYFGELLQQ TLSGLDYLKQ YYPNVGFEEV HSKVRNLTHY FLYYSIIVSR QPPSVIVKCG
EAENHRRSRF WFNTEIRILG GSAFGIDTNN ENSNVNCYLI TDETAKQLLN NAYLDIFESE
EFCIEPNTST FQKKDARGIK AKFDDMKVAK KVALRRDSVA TKRYCLCYNI QLQTNCGIEL
VGKKVSLPFA VLVGPKADVE AKLFLERSFA DLVRHPLSDI PTHVSCAEMA DALEMKFQAI
IETPQKNTDG PSVVQPRKFN MQTKQHLVMR MKPNNQGFLP LDNFMKLPVA EEFQHKKSAS
AEGDWKLVPF YDWFFKLAEI TNKYLYSMWY DGLVYGFCSK EDAENILRCI PRSVLLVRFS
DIEYGKIKIS VKNRNGEIRH HWYEHADLNA RSLNSELLSN HKFSDVDLIY PDIDLEVALG
GRNKPRIRLP RNLAPDEIYF DNQGAAT
