STA5A_BOVIN
ID STA5A_BOVIN Reviewed; 794 AA.
AC Q95115; O46628; O97606; Q9N0U8; Q9TUM1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Signal transducer and activator of transcription 5A;
DE AltName: Full=Mammary gland factor;
GN Name=STAT5A; Synonyms=MGF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RA Schroeder P., Thiesen H.-J., Seyfert H.-M.;
RT "Alternative STAT5A/MGF-factors in the mammary gland of ruminants.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10835485; DOI=10.1007/s002390010058;
RA Seyfert H.-M., Pitra C., Meyer L., Brunner R.M., Wheeler T.T., Molenaar A.,
RA McCracken J.Y., Herrmann J., Thiesen H.-J., Schwerin M.;
RT "Molecular characterization of STAT5A- and STAT5B-encoding genes reveals
RT extended intragenic sequence homogeneity in cattle and mouse and different
RT degrees of divergent evolution of various domains.";
RL J. Mol. Evol. 50:550-561(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
RC TISSUE=Blood;
RA Schroeder P., Meyer L., Wheeler T.T., Thiesen H.-J., Seyfert H.-M.;
RT "Cloning and sequencing of the bovine STAT5A cDNA reveals significant
RT sequence divergence with ovine.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 461-546.
RX PubMed=9589597; DOI=10.1111/j.1365-2052.1997.tb03298.x;
RA McCracken J.Y., Molenaar A.J., Snell R.J., Dayey H.W., Wilkins R.J.;
RT "A polymorphic TG repeat present within the bovine STAT5A gene.";
RL Anim. Genet. 28:459-459(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 582-677.
RX PubMed=10442998; DOI=10.1046/j.1365-2052.1999.00404-10.x;
RA Antoniou E., Hirst B.J., Grosz M., Skidmore C.J.;
RT "A single strand conformational polymorphism in the bovine gene STAT5A.";
RL Anim. Genet. 30:232-232(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 748-794.
RA LeBaron M.J., Yamashita H., Rui H.;
RT "Bos taurus partial sequence of STAT5a gene.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Carries out a dual function: signal transduction and
CC activation of transcription. Mediates cellular responses to the
CC cytokine KITLG/SCF and other growth factors. May mediate cellular
CC responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS
CC element and activates PRL-induced transcription. Regulates the
CC expression of milk proteins during lactation (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC member. Binds NR3C1. Interacts with NCOA1 and SOCS7. Interacts with
CC ERBB4 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Translocated into the nucleus in response to phosphorylation.
CC {ECO:0000250}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P42230}.
CC -!- PTM: Tyrosine phosphorylated in response to KITLG/SCF, IL2, IL3, IL7,
CC IL15, CSF2/GMCSF, GH1, PRL, EPO and THPO (By similarity). Activated KIT
CC promotes phosphorylation on tyrosine residues and subsequent
CC translocation to the nucleus (By similarity). Tyrosine phosphorylated
CC in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4
CC (By similarity). Tyrosine phosphorylation is required for DNA-binding
CC activity and dimerization. Serine phosphorylation is also required for
CC maximal transcriptional activity (By similarity). Tyrosine
CC phosphorylated in response to signaling via activated FLT3; wild-type
CC FLT3 results in much weaker phosphorylation than constitutively
CC activated mutant FLT3. Alternatively, can be phosphorylated by JAK2 at
CC Tyr-694 (By similarity). {ECO:0000250|UniProtKB:P40763,
CC ECO:0000250|UniProtKB:P42229, ECO:0000250|UniProtKB:P42230,
CC ECO:0000250|UniProtKB:Q62771}.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000305}.
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DR EMBL; Z72482; CAA96563.1; -; mRNA.
DR EMBL; AJ242522; CAB52173.1; -; Genomic_DNA.
DR EMBL; AJ237937; CAB52173.1; JOINED; Genomic_DNA.
DR EMBL; AJ223573; CAA11440.1; -; Genomic_DNA.
DR EMBL; U96644; AAB57696.1; -; Genomic_DNA.
DR EMBL; AF079568; AAC71005.1; -; Genomic_DNA.
DR EMBL; AF250911; AAF72972.1; -; Genomic_DNA.
DR RefSeq; NP_001012691.1; NM_001012673.1.
DR AlphaFoldDB; Q95115; -.
DR SMR; Q95115; -.
DR STRING; 9913.ENSBTAP00000034715; -.
DR PaxDb; Q95115; -.
DR PRIDE; Q95115; -.
DR Ensembl; ENSBTAT00000073514; ENSBTAP00000067878; ENSBTAG00000009496.
DR GeneID; 282375; -.
DR KEGG; bta:282375; -.
DR CTD; 6776; -.
DR VEuPathDB; HostDB:ENSBTAG00000009496; -.
DR VGNC; VGNC:35372; STAT5A.
DR eggNOG; KOG3667; Eukaryota.
DR GeneTree; ENSGT01050000244952; -.
DR InParanoid; Q95115; -.
DR OrthoDB; 327469at2759; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000009496; Expressed in parenchyma of mammary gland and 105 other tissues.
DR ExpressionAtlas; Q95115; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0003677; F:DNA binding; ISS:AgBase.
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:0019221; P:cytokine-mediated signaling pathway; ISS:AgBase.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0046543; P:development of secondary female sexual characteristics; ISS:AgBase.
DR GO; GO:0007565; P:female pregnancy; ISS:AgBase.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IBA:GO_Central.
DR GO; GO:0007595; P:lactation; ISS:AgBase.
DR GO; GO:0019915; P:lipid storage; ISS:AgBase.
DR GO; GO:0001553; P:luteinization; ISS:AgBase.
DR GO; GO:0030879; P:mammary gland development; ISS:AgBase.
DR GO; GO:0001779; P:natural killer cell differentiation; ISS:AgBase.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:AgBase.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:AgBase.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; ISS:AgBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:AgBase.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:AgBase.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISS:AgBase.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISS:AgBase.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISS:AgBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:AgBase.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISS:AgBase.
DR GO; GO:0030155; P:regulation of cell adhesion; ISS:AgBase.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; ISS:AgBase.
DR GO; GO:0019218; P:regulation of steroid metabolic process; ISS:AgBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043434; P:response to peptide hormone; IBA:GO_Central.
DR GO; GO:0043029; P:T cell homeostasis; ISS:AgBase.
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; IPR035858; STAT5a/5b.
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 PANTHER; PTHR11801:SF47; PTHR11801:SF47; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF01017; STAT_alpha; 1.
DR Pfam; PF02864; STAT_bind; 1.
DR Pfam; PF02865; STAT_int; 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; DNA-binding; Lactation; Nucleus; Phosphoprotein;
KW Reference proteome; SH2 domain; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..794
FT /note="Signal transducer and activator of transcription 5A"
FT /id="PRO_0000182422"
FT DOMAIN 589..686
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 771..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P42229"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42229"
FT MOD_RES 682
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P42229"
FT MOD_RES 694
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000250|UniProtKB:P51692"
FT CONFLICT 25
FT /note="H -> D (in Ref. 1; CAA96563)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="R -> C (in Ref. 2; CAB52173)"
FT /evidence="ECO:0000305"
FT CONFLICT 331..419
FT /note="TFIIEKQPPQVLKTQTKFAATVRLLVGGKLNVHMNPPQVKATIISEQQAKSL
FT LKNENTRNECSGEILNNCCVMEYHQATGTLSAHFRNM -> ECSGEILNNCCVMEYHQA
FT TGTLSAHFRNMHLHHREAAPSGPEDPDQVRGHRAPAGGWEAERAHEPPPGEGHHHQRAA
FT GQVTAQEREHPQ (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="Q -> L (in Ref. 1; CAA96563)"
FT /evidence="ECO:0000305"
FT CONFLICT 617
FT /note="L -> M (in Ref. 1; CAA96563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 794 AA; 90700 MW; C22EFBB9F46896A9 CRC64;
MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDLDN PQDRAQATQL
LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR CPMELVRCIR HILYNEQRLV
REANNGSSSA GILVDAMSQK HLQINQTFEE LRLVTQDTEN ELKKLQQTQE YFIIQYQESL
RIQAQFAQLA QLNPQERLSR ETALQQKQVS LEAWLQREAQ TLQQYRVELA EKHQKTLQLL
RKQQTIILDD ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA TVRLLVGGKL
NVHMNPPQVK ATIISEQQAK SLLKNENTRN ECSGEILNNC CVMEYHQATG TLSAHFRNMS
LKRIKRADRR GAESVTEEKF TVLFESQFSV GSNELVFQVK TLSLPVVVIV HGSQDHNATA
TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNS
SSSHLEDYNG MSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPDRNL WNLKPFTTRD FSIRSLADRL
GDLNYLIYVF PDRPKDEVFS KYYTPVLAKA VDGYVKPQIK QVVPEFVSAS ADSAGSNATY
MDQAPSPAVC PQPHYNMYPQ NPDPVLDQDG EFDLDETMDV ARHVEELLRR PMDSLEPSLP
PPTGLFTPGR GSLS
