STA5A_PIG
ID STA5A_PIG Reviewed; 799 AA.
AC Q9TUZ1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Signal transducer and activator of transcription 5A;
GN Name=STAT5A;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Large white; TISSUE=Mammary gland;
RA Palin M.-F., Beaudry D., Roberge C., Farmer C.;
RL Submitted (MAR-1999) 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-699 (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; AF135122; AAD46163.1; -; mRNA.
DR RefSeq; NP_999455.1; NM_214290.1.
DR AlphaFoldDB; Q9TUZ1; -.
DR SMR; Q9TUZ1; -.
DR STRING; 9823.ENSSSCP00000018442; -.
DR PeptideAtlas; Q9TUZ1; -.
DR PRIDE; Q9TUZ1; -.
DR GeneID; 397550; -.
DR KEGG; ssc:397550; -.
DR CTD; 6776; -.
DR InParanoid; Q9TUZ1; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IEA:InterPro.
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 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..799
FT /note="Signal transducer and activator of transcription 5A"
FT /id="PRO_0000182425"
FT DOMAIN 589..686
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 778..799
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 699
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000250|UniProtKB:P51692"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42229"
FT VARIANT 197
FT /note="C -> R"
FT VARIANT 457
FT /note="F -> S"
FT VARIANT 711
FT /note="F -> L"
FT VARIANT 794
FT /note="T -> I"
SQ SEQUENCE 799 AA; 90954 MW; 310C123A8B624FF4 CRC64;
MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDVDN PQDRAQATQL
LENLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR CPMELVRCIR HILYNEQRLV
REANNGSSSA GILVDAMSQK HLQINQTFEE LRLVTQDTEN ELKKLQQTQE YFIIQYQESL
RIQAQFAQLA QLNPQECLSR ETALQQKQVT LEAWLQREAQ TLQQYRVELA EKHQKTLQLL
RKQQTIILDD ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA TVRLLVGGKL
NVHMNPPQVK ATIISEQQAK SLLKNESTRN ECSGEILNNC CVMEYHQATG TLSAHFRNMS
LKRIKRADRR GAESVTEEKF TVLFESQFSV GSNELVFQVK TLSLPVVVIV HGSQDHNATA
TVLWDNAFAE PGRVPFAVPD KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNS
SSSHLEDYSG MSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPDRNL WNLKPFTTRD FSIRSLADRL
GDLSYLIYVF PDRPKDEVFS KYYTPVLAPA SAAKAVDGYV KPQIKQVVPE FVSASSDSAG
GNATYMDQAP SPAVCPQAHY SIYPQNPDPV LDQDGEFDLD ETMDVARHVE ELLRRPMDSL
DPRLSPPAGL FASTRGSLS
