STA5A_MOUSE
ID STA5A_MOUSE Reviewed; 793 AA.
AC P42230;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Signal transducer and activator of transcription 5A;
DE AltName: Full=Mammary gland factor;
GN Name=Stat5a; Synonyms=Mgf, Mpf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND PHOSPHORYLATION.
RC STRAIN=C57BL/6 X A/J; TISSUE=Liver;
RX PubMed=7720707; DOI=10.1002/j.1460-2075.1995.tb07100.x;
RA Mui A.L.-F., Wakao H., O'Farrell A.-M., Harada N., Miyajima A.;
RT "Interleukin-3, granulocyte-macrophage colony stimulating factor and
RT interleukin-5 transduce signals through two STAT5 homologs.";
RL EMBO J. 14:1166-1175(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=7568026; DOI=10.1073/pnas.92.19.8831;
RA Liu X., Robinson G.W., Gouilleux F., Groner B., Hennighausen L.;
RT "Cloning and expression of Stat5 and an additional homologue (Stat5b)
RT involved in prolactin signal transduction in mouse mammary tissue.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8831-8835(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/HeN; TISSUE=Mammary gland;
RA Zhou L.X., Moore R.C., Oka T.;
RL Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH NR3C1.
RX PubMed=9528750; DOI=10.1128/mcb.18.4.1783;
RA Cella N., Groner B., Hynes N.E.;
RT "Characterization of Stat5a and Stat5b homodimers and heterodimers and
RT their association with the glucocortiocoid receptor in mammary cells.";
RL Mol. Cell. Biol. 18:1783-1792(1998).
RN [5]
RP FUNCTION, AND INTERACTION WITH ERBB4.
RX PubMed=10508857; DOI=10.1083/jcb.147.1.77;
RA Jones F.E., Welte T., Fu X.Y., Stern D.F.;
RT "ErbB4 signaling in the mammary gland is required for lobuloalveolar
RT development and Stat5 activation during lactation.";
RL J. Cell Biol. 147:77-88(1999).
RN [6]
RP PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
RX PubMed=11090077;
RA Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C.,
RA Gruning W., Kratz-Albers K., Serve S., Steur C., Buchner T., Kienast J.,
RA Kanakura Y., Berdel W.E., Serve H.;
RT "Flt3 mutations from patients with acute myeloid leukemia induce
RT transformation of 32D cells mediated by the Ras and STAT5 pathways.";
RL Blood 96:3907-3914(2000).
RN [7]
RP FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP ERBB4.
RX PubMed=16837552; DOI=10.1091/mbc.e06-02-0101;
RA Muraoka-Cook R.S., Sandahl M., Husted C., Hunter D., Miraglia L.,
RA Feng S.M., Elenius K., Earp H.S. III;
RT "The intracellular domain of ErbB4 induces differentiation of mammary
RT epithelial cells.";
RL Mol. Biol. Cell 17:4118-4129(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-694, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, and
RC Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP PHOSPHORYLATION IN RESPONSE TO KIT SIGNALING.
RX PubMed=21135090; DOI=10.1074/jbc.m110.182642;
RA Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.;
RT "Mechanisms of STAT protein activation by oncogenic KIT mutants in
RT neoplastic mast cells.";
RL J. Biol. Chem. 286:5956-5966(2011).
RN [10]
RP PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
RX PubMed=21262971; DOI=10.1074/jbc.m110.205021;
RA Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K.,
RA Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D.,
RA Muller J.P.;
RT "Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3
RT signaling.";
RL J. Biol. Chem. 286:10918-10929(2011).
RN [11]
RP ISGYLATION.
RX PubMed=22022510; DOI=10.1371/journal.pone.0026068;
RA Maragno A.L., Pironin M., Alcalde H., Cong X., Knobeloch K.P., Tangy F.,
RA Zhang D.E., Ghysdael J., Quang C.T.;
RT "ISG15 modulates development of the erythroid lineage.";
RL PLoS ONE 6:E26068-E26068(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 128-712.
RX PubMed=16192273; DOI=10.1074/jbc.m507682200;
RA Neculai D., Neculai A.M., Verrier S., Straub K., Klumpp K., Pfitzner E.,
RA Becker S.;
RT "Structure of the unphosphorylated STAT5a dimer.";
RL J. Biol. Chem. 280:40782-40787(2005).
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 {ECO:0000269|PubMed:10508857, ECO:0000269|PubMed:16837552,
CC ECO:0000269|PubMed:7720707}.
CC -!- SUBUNIT: Forms a homodimer or a heterodimer with a related family
CC member. Interacts with NCOA1 and SOCS7 (By similarity). Binds NR3C1.
CC Interacts with ERBB4. {ECO:0000250, ECO:0000269|PubMed:10508857,
CC ECO:0000269|PubMed:16837552, ECO:0000269|PubMed:9528750}.
CC -!- INTERACTION:
CC P42230; Q99490-2: AGAP2; Xeno; NbExp=2; IntAct=EBI-617434, EBI-7737644;
CC P42230; P19941: GHR; Xeno; NbExp=3; IntAct=EBI-617434, EBI-7526279;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16837552}. Nucleus
CC {ECO:0000269|PubMed:16837552}. Note=Translocated into the nucleus in
CC response to phosphorylation.
CC -!- TISSUE SPECIFICITY: In the virgin, found in most tissues except brain
CC and muscle. During lactation, abundantly found in mammary tissue, as
CC well as in other secretory organs such as salivary gland and seminal
CC vesicle.
CC -!- PTM: ISGylated. {ECO:0000269|PubMed:22022510}.
CC -!- PTM: Tyrosine phosphorylated in response to KITLG/SCF, IL2, IL3, IL7,
CC IL15, CSF2/GMCSF, GH1, PRL, EPO and THPO (PubMed:16837552). Activated
CC KIT promotes phosphorylation on tyrosine residues and subsequent
CC translocation to the nucleus (PubMed:21135090). 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 (PubMed:7720707). Serine phosphorylation is
CC also required for maximal transcriptional activity (By similarity).
CC Tyrosine phosphorylated in response to signaling via activated FLT3;
CC wild-type FLT3 results in much weaker phosphorylation than
CC constitutively activated mutant FLT3 (PubMed:11090077,
CC PubMed:21262971). Alternatively, can be phosphorylated by JAK2 at Tyr-
CC 694 (By similarity). {ECO:0000250|UniProtKB:P40763,
CC ECO:0000250|UniProtKB:P42229, ECO:0000250|UniProtKB:Q62771,
CC ECO:0000269|PubMed:11090077, ECO:0000269|PubMed:16837552,
CC ECO:0000269|PubMed:21135090, ECO:0000269|PubMed:21262971,
CC ECO:0000269|PubMed:7720707}.
CC -!- SIMILARITY: Belongs to the transcription factor STAT family.
CC {ECO:0000305}.
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DR EMBL; Z48538; CAA88419.1; -; mRNA.
DR EMBL; U21103; AAA80590.1; -; mRNA.
DR EMBL; U36502; AAA78945.1; -; mRNA.
DR CCDS; CCDS25439.1; -.
DR PIR; S54772; S54772.
DR RefSeq; NP_035618.1; NM_011488.3.
DR RefSeq; XP_006532784.1; XM_006532721.1.
DR RefSeq; XP_006532785.1; XM_006532722.1.
DR RefSeq; XP_017169891.1; XM_017314402.1.
DR PDB; 1Y1U; X-ray; 3.21 A; A/B/C=128-712.
DR PDBsum; 1Y1U; -.
DR AlphaFoldDB; P42230; -.
DR SMR; P42230; -.
DR BioGRID; 203525; 12.
DR CORUM; P42230; -.
DR DIP; DIP-897N; -.
DR IntAct; P42230; 7.
DR MINT; P42230; -.
DR STRING; 10090.ENSMUSP00000004145; -.
DR ChEMBL; CHEMBL5513; -.
DR iPTMnet; P42230; -.
DR PhosphoSitePlus; P42230; -.
DR SwissPalm; P42230; -.
DR EPD; P42230; -.
DR jPOST; P42230; -.
DR PaxDb; P42230; -.
DR PeptideAtlas; P42230; -.
DR PRIDE; P42230; -.
DR ProteomicsDB; 257443; -.
DR Antibodypedia; 3553; 1839 antibodies from 54 providers.
DR DNASU; 20850; -.
DR Ensembl; ENSMUST00000004145; ENSMUSP00000004145; ENSMUSG00000004043.
DR Ensembl; ENSMUST00000107356; ENSMUSP00000102979; ENSMUSG00000004043.
DR GeneID; 20850; -.
DR KEGG; mmu:20850; -.
DR UCSC; uc007lml.2; mouse.
DR CTD; 6776; -.
DR MGI; MGI:103036; Stat5a.
DR VEuPathDB; HostDB:ENSMUSG00000004043; -.
DR eggNOG; KOG3667; Eukaryota.
DR GeneTree; ENSGT01050000244952; -.
DR HOGENOM; CLU_014189_2_2_1; -.
DR InParanoid; P42230; -.
DR OMA; GCPMELV; -.
DR TreeFam; TF318648; -.
DR Reactome; R-MMU-1251985; Nuclear signaling by ERBB4.
DR Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR Reactome; R-MMU-1433557; Signaling by SCF-KIT.
DR Reactome; R-MMU-186763; Downstream signal transduction.
DR Reactome; R-MMU-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling.
DR Reactome; R-MMU-8854691; Interleukin-20 family signaling.
DR Reactome; R-MMU-8983432; Interleukin-15 signaling.
DR Reactome; R-MMU-8985947; Interleukin-9 signaling.
DR Reactome; R-MMU-9020558; Interleukin-2 signaling.
DR Reactome; R-MMU-9020958; Interleukin-21 signaling.
DR Reactome; R-MMU-982772; Growth hormone receptor signaling.
DR BioGRID-ORCS; 20850; 6 hits in 79 CRISPR screens.
DR ChiTaRS; Stat5a; mouse.
DR EvolutionaryTrace; P42230; -.
DR PRO; PR:P42230; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P42230; protein.
DR Bgee; ENSMUSG00000004043; Expressed in thoracic mammary gland and 168 other tissues.
DR ExpressionAtlas; P42230; baseline and differential.
DR Genevisible; P42230; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0042301; F:phosphate ion binding; IDA:ARUK-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0050798; P:activated T cell proliferation; IDA:MGI.
DR GO; GO:0030183; P:B cell differentiation; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISO:MGI.
DR GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:MGI.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0046543; P:development of secondary female sexual characteristics; IMP:MGI.
DR GO; GO:0046544; P:development of secondary male sexual characteristics; IMP:MGI.
DR GO; GO:0060742; P:epithelial cell differentiation involved in prostate gland development; IMP:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IGI:MGI.
DR GO; GO:0007565; P:female pregnancy; IGI:MGI.
DR GO; GO:0042492; P:gamma-delta T cell differentiation; IGI:MGI.
DR GO; GO:0060397; P:growth hormone receptor signaling pathway via JAK-STAT; IDA:BHF-UCL.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0019915; P:lipid storage; IGI:MGI.
DR GO; GO:0001553; P:luteinization; IGI:MGI.
DR GO; GO:0030098; P:lymphocyte differentiation; IGI:MGI.
DR GO; GO:0030879; P:mammary gland development; IMP:MGI.
DR GO; GO:0061180; P:mammary gland epithelium development; IMP:MGI.
DR GO; GO:0060056; P:mammary gland involution; ISO:MGI.
DR GO; GO:0033024; P:mast cell apoptotic process; IMP:MGI.
DR GO; GO:0060374; P:mast cell differentiation; IMP:MGI.
DR GO; GO:0070662; P:mast cell proliferation; IMP:MGI.
DR GO; GO:0000278; P:mitotic cell cycle; IGI:MGI.
DR GO; GO:0033028; P:myeloid cell apoptotic process; IGI:MGI.
DR GO; GO:0001779; P:natural killer cell differentiation; IMP:MGI.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IGI:MGI.
DR GO; GO:0033026; P:negative regulation of mast cell apoptotic process; IMP:MGI.
DR GO; GO:0033033; P:negative regulation of myeloid cell apoptotic process; IGI:MGI.
DR GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
DR GO; GO:0048541; P:Peyer's patch development; IGI:MGI.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:MGI.
DR GO; GO:0045579; P:positive regulation of B cell differentiation; IGI:MGI.
DR GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IGI:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IGI:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IGI:MGI.
DR GO; GO:0045621; P:positive regulation of lymphocyte differentiation; IGI:MGI.
DR GO; GO:0060376; P:positive regulation of mast cell differentiation; IMP:MGI.
DR GO; GO:0070668; P:positive regulation of mast cell proliferation; IMP:MGI.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IGI:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IGI:MGI.
DR GO; GO:0032825; P:positive regulation of natural killer cell differentiation; IMP:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:MGI.
DR GO; GO:0038026; P:reelin-mediated signaling pathway; ISO:MGI.
DR GO; GO:0030155; P:regulation of cell adhesion; IMP:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IGI:BHF-UCL.
DR GO; GO:0019218; P:regulation of steroid metabolic process; IGI:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0043434; P:response to peptide hormone; IDA:MGI.
DR GO; GO:0033077; P:T cell differentiation in thymus; IGI:MGI.
DR GO; GO:0043029; P:T cell homeostasis; IGI:MGI.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR GO; GO:0019530; P:taurine metabolic process; IGI:BHF-UCL.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR Gene3D; 1.10.532.10; -; 1.
DR Gene3D; 2.60.40.630; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR IDEAL; IID50279; -.
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 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; DNA-binding; Lactation; Nucleus;
KW Phosphoprotein; Reference proteome; SH2 domain; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..793
FT /note="Signal transducer and activator of transcription 5A"
FT /id="PRO_0000182424"
FT DOMAIN 589..686
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
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"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 779
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P42229"
FT HELIX 144..181
FT /evidence="ECO:0007829|PDB:1Y1U"
FT TURN 182..190
FT /evidence="ECO:0007829|PDB:1Y1U"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 199..249
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:1Y1U"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 273..300
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 309..330
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 348..355
FT /evidence="ECO:0007829|PDB:1Y1U"
FT TURN 356..361
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 376..383
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:1Y1U"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 435..437
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 439..449
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 456..462
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 475..488
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 500..503
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 504..519
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 527..538
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 545..550
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 555..559
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 566..569
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 570..584
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 586..591
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 600..608
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 615..620
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 626..631
FT /evidence="ECO:0007829|PDB:1Y1U"
FT STRAND 641..646
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 648..653
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 656..662
FT /evidence="ECO:0007829|PDB:1Y1U"
FT HELIX 675..679
FT /evidence="ECO:0007829|PDB:1Y1U"
FT TURN 680..682
FT /evidence="ECO:0007829|PDB:1Y1U"
SQ SEQUENCE 793 AA; 90831 MW; 7C66E435C37624DD CRC64;
MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDLDN PQDRGQATQL
LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR CPMELVRCIR HILYNEQRLV
REANNCSSPA GVLVDAMSQK HLQINQRFEE LRLITQDTEN ELKKLQQTQE YFIIQYQESL
RIQAQFAQLG QLNPQERMSR ETALQQKQVS LETWLQREAQ 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 VFLAQKLFNI
SSNHLEDYNS MSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPDRNL WNLKPFTTRD FSIRSLADRL
GDLNYLIYVF PDRPKDEVFA KYYTPVLAKA VDGYVKPQIK QVVPEFVNAS TDAGASATYM
DQAPSPVVCP QPHYNMYPPN PDPVLDQDGE FDLDESMDVA RHVEELLRRP MDSLDARLSP
PAGLFTSARS SLS
