ID   STA5A_SHEEP             Reviewed;         794 AA.
AC   P42231;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   24-JAN-2024, entry version 143.
DE   RecName: Full=Signal transducer and activator of transcription 5A;
DE   AltName: Full=Mammary gland factor;
GN   Name=STAT5A; Synonyms=MGF, STAT5;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Mammary gland;
RX   PubMed=7514531; DOI=10.1002/j.1460-2075.1994.tb06495.x;
RA   Wakao H., Gouilleux F., Groner B.;
RT   "Mammary gland factor (MGF) is a novel member of the cytokine regulated
RT   transcription factor gene family and confers the prolactin response.";
RL   EMBO J. 13:2182-2191(1994).
RN   [2]
RP   ERRATUM OF PUBMED:7514531, AND SEQUENCE REVISION.
RX   PubMed=7882987; DOI=10.1002/j.1460-2075.1995.tb07064.x;
RA   Wakao H., Gouilleux F., Groner B.;
RL   EMBO J. 14:854-855(1995).
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Mammary gland;
RX   PubMed=7537213; DOI=10.1002/j.1460-2075.1995.tb07126.x;
RA   Azam M., Erdjument-Bromage H., Kreider B.L., Xia M., Quelle F., Basu R.,
RA   Saris C., Tempst P., Ihle J.N., Schindler C.;
RT   "Interleukin-3 signals through multiple isoforms of Stat5.";
RL   EMBO J. 14:1402-1411(1995).
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.
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). Interacts with EBF4. {ECO:0000250,
CC       ECO:0000250|UniProtKB:P42229}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated into the
CC       nucleus in response to phosphorylation.
CC   -!- TISSUE SPECIFICITY: Found in mammary gland and, in lesser extent, in
CC       ovary, thymus, spleen, kidney, lung, muscle and adrenal gland.
CC   -!- INDUCTION: By prolactin.
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; X78428; CAA55191.1; -; mRNA.
DR   PIR; S55527; S55527.
DR   RefSeq; NP_001009402.1; NM_001009402.1.
DR   AlphaFoldDB; P42231; -.
DR   SMR; P42231; -.
DR   STRING; 9940.ENSOARP00000000859; -.
DR   iPTMnet; P42231; -.
DR   PaxDb; 9940-ENSOARP00000000859; -.
DR   GeneID; 443419; -.
DR   KEGG; oas:443419; -.
DR   CTD; 6776; -.
DR   eggNOG; KOG3667; Eukaryota.
DR   OrthoDB; 7823at2759; -.
DR   Proteomes; UP000002356; Unplaced.
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:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:AgBase.
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: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:0030856; P:regulation of epithelial cell differentiation; ISS:AgBase.
DR   GO; GO:0019218; P:regulation of steroid metabolic process; ISS:AgBase.
DR   GO; GO:0043029; P:T cell homeostasis; ISS:AgBase.
DR   CDD; cd16855; STAT5_CCD; 1.
DR   CDD; cd16849; STAT5_DBD; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   Gene3D; 1.20.1050.20; STAT transcription factor, all-alpha domain; 1.
DR   Gene3D; 2.60.40.630; STAT transcription factor, DNA-binding domain; 1.
DR   Gene3D; 1.10.532.10; STAT transcription factor, N-terminal domain; 1.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR001217; STAT.
DR   InterPro; IPR046994; STAT5_CCD.
DR   InterPro; IPR035858; STAT5a/5b_DBD.
DR   InterPro; IPR048988; STAT_linker.
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; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION; 1.
DR   PANTHER; PTHR11801:SF47; SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 5A; 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   Pfam; PF21354; STAT_linker; 1.
DR   SMART; SM00252; SH2; 1.
DR   SMART; SM00964; STAT_int; 1.
DR   SUPFAM; SSF49417; p53-like transcription factors; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   SUPFAM; SSF47655; STAT; 1.
DR   SUPFAM; SSF48092; Transcription factor STAT-4 N-domain; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; Direct protein sequencing; DNA-binding; Lactation;
KW   Nucleus; Phosphoprotein; Reference proteome; SH2 domain; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..794
FT                   /note="Signal transducer and activator of transcription 5A"
FT                   /id="PRO_0000182427"
FT   DOMAIN          589..686
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   REGION          765..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         129
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"
SQ   SEQUENCE   794 AA;  90917 MW;  E69A4EC826AF60BE CRC64;
     MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDLDN PQDRAQVTQL
     LEGLVQELQK KAEHQVGEDG FLLKIKLGHY VHVSSRTRTT AAPWSWLRCI RHILYNEQRL
     VREATNGNSS AGILVDAMSQ KHLQINQTFE ELRLVTQDTE NELKKLQQTQ EYFIIQYQES
     LRIQAQFAQL AQLNPQERLS RETALQQKQV SLEAWLQREA QTLQQYRVEL AEKHQKTLQL
     LRKQQTIILD DELIQWKRRH DWRGMEAPPR SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC
     QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA TVRLLVGGKL
     NVHMNPPQVK ATIISEQQAK SLLKNENTRN ECSGEILNNC CVMEYHQRTG TLSAHFRNMS
     LKRIKRADRR GAESVTEEKF TVLFESQFSV GSNELVFQVK TLSLPVVVIV HGSQDHNATA
     TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL LFLAQKLFNN
     SSSHLEDYNG MSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK
     QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPDRNL WNLKPFTTRE GSIRSLADRL
     GDLNYLIYVF PDRPKDEVFS KYYTPVLAKA VDGYVKPQIK QVVPEFVSAS ADSAGSSATY
     MDQAPSPAVC PQPHYNMYPQ NPDPVLDQDG EFDLDETMDV ARHVEELLRR PNGQSGPLSP
     PPAGLFTPAR GSLS
//