P85A_BOVIN
ID P85A_BOVIN Reviewed; 724 AA.
AC P23727;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Phosphatidylinositol 3-kinase regulatory subunit alpha;
DE Short=PI3-kinase regulatory subunit alpha;
DE Short=PI3K regulatory subunit alpha;
DE Short=PtdIns-3-kinase regulatory subunit alpha;
DE AltName: Full=Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha;
DE Short=PI3-kinase subunit p85-alpha;
DE Short=PtdIns-3-kinase regulatory subunit p85-alpha;
GN Name=PIK3R1;
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].
RX PubMed=1707345; DOI=10.1016/0092-8674(91)90411-q;
RA Otsu M., Hiles I.D., Goot I., Fry M.J., Ruiz-Larrea F., Panayotou G.,
RA Thompson A., Dhand R., Hsuan J., Totty N., Smith A.D., Morgan S.J.,
RA Courtneidge S.A., Parker P.J., Waterfield M.D.;
RT "Characterization of two 85 kd proteins that associate with receptor
RT tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase.";
RL Cell 65:91-104(1991).
RN [2]
RP CIRCULAR DICHROISM ANALYSIS, AND FLUORESCENCE SPECTROSCOPY.
RX PubMed=1330535; DOI=10.1002/j.1460-2075.1992.tb05524.x;
RA Panayotou G., Bax B., Gout I., Federwisch M., Wroblowski B., Dhand R.,
RA Fry M.J., Blundell T.L., Wollmer A., Waterfield M.D.;
RT "Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2
RT domain with a PDGF receptor phosphorylation site: structural features and
RT analysis of conformational changes.";
RL EMBO J. 11:4261-4272(1992).
RN [3]
RP INTERACTION WITH PDGFRB.
RX PubMed=1375321; DOI=10.1128/mcb.12.6.2534-2544.1992;
RA Kazlauskas A., Kashishian A., Cooper J.A., Valius M.;
RT "GTPase-activating protein and phosphatidylinositol 3-kinase bind to
RT distinct regions of the platelet-derived growth factor receptor beta
RT subunit.";
RL Mol. Cell. Biol. 12:2534-2544(1992).
RN [4]
RP STRUCTURE BY NMR OF 1-84.
RX PubMed=7684655; DOI=10.1016/0092-8674(93)90259-s;
RA Booker G.W., Gout I., Downing A.K., Driscoll P.C., Boyd J.,
RA Waterfield M.D., Campbell I.D.;
RT "Solution structure and ligand-binding site of the SH3 domain of the p85
RT alpha subunit of phosphatidylinositol 3-kinase.";
RL Cell 73:813-822(1993).
RN [5]
RP STRUCTURE BY NMR OF 314-431.
RX PubMed=1323062; DOI=10.1038/358684a0;
RA Booker G.W., Breeze A.L., Downing A.K., Panayotou G., Gout I.,
RA Waterfield M.D., Campbell I.D.;
RT "Structure of an SH2 domain of the p85 alpha subunit of
RT phosphatidylinositol-3-OH kinase.";
RL Nature 358:684-687(1992).
RN [6]
RP STRUCTURE BY NMR OF 321-434.
RX PubMed=8952511; DOI=10.1021/bi961783x;
RA Guenther U.L., Liu Y., Sanford D., Bachovchin W.W., Schaffhausen B.;
RT "NMR analysis of interactions of a phosphatidylinositol 3'-kinase SH2
RT domain with phosphotyrosine peptides reveals interdependence of major
RT binding sites.";
RL Biochemistry 35:15570-15581(1996).
RN [7]
RP STRUCTURE BY NMR OF 614-724.
RX PubMed=9512716; DOI=10.1006/jmbi.1997.1562;
RA Siegal G., Davis B., Kristensen S.M., Sankar A., Linacre J., Stein R.C.,
RA Panayotou G., Waterfield M.D., Driscoll P.C.;
RT "Solution structure of the C-terminal SH2 domain of the p85 alpha
RT regulatory subunit of phosphoinositide 3-kinase.";
RL J. Mol. Biol. 276:461-478(1998).
RN [8]
RP PHOSPHORYLATION AT SER-608.
RX PubMed=14729945; DOI=10.1128/mcb.24.3.966-975.2004;
RA Foukas L.C., Beeton C.A., Jensen J., Phillips W.A., Shepherd P.R.;
RT "Regulation of phosphoinositide 3-kinase by its intrinsic serine kinase
RT activity in vivo.";
RL Mol. Cell. Biol. 24:966-975(2004).
CC -!- FUNCTION: Binds to activated (phosphorylated) protein-Tyr kinases,
CC through its SH2 domain, and acts as an adapter, mediating the
CC association of the p110 catalytic unit to the plasma membrane.
CC Necessary for the insulin-stimulated increase in glucose uptake and
CC glycogen synthesis in insulin-sensitive tissues. Plays an important
CC role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF,
CC KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling.
CC Modulates the cellular response to ER stress by promoting nuclear
CC translocation of XBP1 in a ER stress- and/or insulin-dependent manner
CC during metabolic overloading in the liver and hence plays a role in
CC glucose tolerance improvement (By similarity).
CC {ECO:0000250|UniProtKB:P26450, ECO:0000250|UniProtKB:P27986}.
CC -!- SUBUNIT: Heterodimer of a regulatory subunit PIK3R1 and a p110
CC catalytic subunit (PIK3CA, PIK3CB or PIK3CD). Interacts (via SH2
CC domains) with CCDC88A/GIV (tyrosine-phosphorylated form); the
CC interaction enables recruitment of PIK3R1 to the EGFR receptor,
CC enhancing PI3K activity and cell migration (By similarity). Interacts
CC with PIK3R2; the interaction is dissociated in an insulin-dependent
CC manner (By similarity). Interacts with XBP1; the interaction is direct
CC and induces translocation of XBP1 into the nucleus in a ER
CC stress- and/or insulin-dependent but PI3K-independent manner (By
CC similarity). Interacts with phosphorylated LAT, LAX1, TRAT1 and LIME1
CC upon TCR and/or BCR activation. Interacts with CBLB. The SH2 domains
CC interact with the YTHM motif of phosphorylated INSR in vitro. Also
CC interacts with tyrosine-phosphorylated IGF1R in vitro. Interacts with
CC CD28 and CD3Z upon T-cell activation. Interacts with SOCS7. Interacts
CC with IRS1 and phosphorylated IRS4. Interacts with NISCH, RUFY3 and
CC HCST. Interacts with LYN (via SH3 domain); this enhances enzyme
CC activity. Interacts with AXL, FASLG, FER, FGR, HCK, KIT and BCR.
CC Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) (By
CC similarity). Interacts with PDGFRA (tyrosine phosphorylated). Interacts
CC with ERBB4 (phosphorylated) (By similarity). Interacts with NTRK1
CC (phosphorylated upon ligand-binding). Interacts with PTK2/FAK1 (By
CC similarity). Interacts with PDGFRB (tyrosine phosphorylated)
CC (PubMed:1375321). Interacts (via SH2 domain) with CSF1R (tyrosine
CC phosphorylated) (By similarity). Interacts with FAM83B; activates the
CC PI3K/AKT signaling cascade (By similarity). Interacts with APPL1 and
CC APPL2 (By similarity). Interacts with SRC (By similarity). Interacts
CC with ALOX5; this interaction bridges ALOX5 with CD40 after CD40
CC ligation in B cells and leads to the production of reactive oxygen
CC species (ROS) (By similarity). Interacts with TYK2 (By similarity).
CC {ECO:0000250|UniProtKB:P26450, ECO:0000250|UniProtKB:P27986,
CC ECO:0000250|UniProtKB:Q63787, ECO:0000269|PubMed:1375321}.
CC -!- INTERACTION:
CC P23727; P32871: PIK3CA; NbExp=4; IntAct=EBI-520244, EBI-1373130;
CC P23727; P23727: PIK3R1; NbExp=4; IntAct=EBI-520244, EBI-520244;
CC P23727; Q9ES52-1: Inpp5d; Xeno; NbExp=2; IntAct=EBI-520244, EBI-1452545;
CC P23727; Q07666: KHDRBS1; Xeno; NbExp=2; IntAct=EBI-520244, EBI-1364;
CC P23727; P09619: PDGFRB; Xeno; NbExp=6; IntAct=EBI-520244, EBI-641237;
CC P23727; P20339: RAB5A; Xeno; NbExp=5; IntAct=EBI-520244, EBI-399437;
CC -!- DOMAIN: The SH3 domain mediates the binding to CBLB. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated in T-cells by CBLB; which does not promote
CC proteasomal degradation but impairs association with CD28 and CD3Z upon
CC T-cell activation. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Tyrosine phosphorylated in response to signaling
CC by FGFR1, FGFR2, FGFR3 and FGFR4. Phosphorylated in response to KIT and
CC KITLG/SCF. Phosphorylated on tyrosine residues by TEK/TIE2.
CC Phosphorylated by FGR. Phosphorylated by CSF1R. Phosphorylated by
CC ERBB4. Dephosphorylated by PTPRJ (By similarity). Phosphorylated by
CC PIK3CA at Ser-608; phosphorylation is stimulated by insulin and PDGF.
CC The relevance of phosphorylation by PIK3CA is however unclear.
CC {ECO:0000250, ECO:0000269|PubMed:14729945}.
CC -!- SIMILARITY: Belongs to the PI3K p85 subunit family. {ECO:0000305}.
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DR EMBL; M61745; AAA79511.1; -; mRNA.
DR PIR; A38749; A38749.
DR RefSeq; NP_777000.1; NM_174575.1.
DR RefSeq; XP_005221493.1; XM_005221436.3.
DR PDB; 1BFI; NMR; -; A=614-724.
DR PDB; 1BFJ; NMR; -; A=614-724.
DR PDB; 1OO3; NMR; -; A=321-431.
DR PDB; 1OO4; NMR; -; A=321-431.
DR PDB; 1PNJ; NMR; -; A=1-84.
DR PDB; 1QAD; X-ray; 1.80 A; A=614-724.
DR PDB; 2PNA; NMR; -; A=328-431.
DR PDB; 2PNB; NMR; -; A=328-431.
DR PDB; 2PNI; NMR; -; A=1-84.
DR PDB; 5DXH; X-ray; 3.00 A; B/E=431-599.
DR PDB; 5DXU; X-ray; 2.64 A; B=431-599.
DR PDB; 5T8F; X-ray; 2.91 A; B=431-599.
DR PDB; 6D81; X-ray; 2.25 A; A/B=110-302.
DR PDB; 6D82; X-ray; 2.41 A; A/B=110-302.
DR PDB; 6D85; X-ray; 2.20 A; A/B=110-302.
DR PDB; 6D86; X-ray; 2.30 A; A/B=110-302.
DR PDB; 6D87; X-ray; 2.70 A; A/B=110-302.
DR PDB; 6G6W; X-ray; 2.72 A; B=431-599.
DR PDB; 6MRP; X-ray; 2.40 A; A/B=110-319.
DR PDB; 6OCO; X-ray; 2.58 A; B=431-600.
DR PDB; 6OCU; X-ray; 2.77 A; B=431-600.
DR PDB; 6R4R; EM; 3.40 A; A/B/C/D/E/F/G=1-84.
DR PDB; 7JIS; X-ray; 2.42 A; B=431-599.
DR PDBsum; 1BFI; -.
DR PDBsum; 1BFJ; -.
DR PDBsum; 1OO3; -.
DR PDBsum; 1OO4; -.
DR PDBsum; 1PNJ; -.
DR PDBsum; 1QAD; -.
DR PDBsum; 2PNA; -.
DR PDBsum; 2PNB; -.
DR PDBsum; 2PNI; -.
DR PDBsum; 5DXH; -.
DR PDBsum; 5DXU; -.
DR PDBsum; 5T8F; -.
DR PDBsum; 6D81; -.
DR PDBsum; 6D82; -.
DR PDBsum; 6D85; -.
DR PDBsum; 6D86; -.
DR PDBsum; 6D87; -.
DR PDBsum; 6G6W; -.
DR PDBsum; 6MRP; -.
DR PDBsum; 6OCO; -.
DR PDBsum; 6OCU; -.
DR PDBsum; 6R4R; -.
DR PDBsum; 7JIS; -.
DR AlphaFoldDB; P23727; -.
DR BMRB; P23727; -.
DR SMR; P23727; -.
DR BioGRID; 159569; 1.
DR CORUM; P23727; -.
DR DIP; DIP-34247N; -.
DR IntAct; P23727; 15.
DR MINT; P23727; -.
DR STRING; 9913.ENSBTAP00000014594; -.
DR iPTMnet; P23727; -.
DR PaxDb; P23727; -.
DR PRIDE; P23727; -.
DR Ensembl; ENSBTAT00000014594; ENSBTAP00000014594; ENSBTAG00000010989.
DR GeneID; 282307; -.
DR KEGG; bta:282307; -.
DR CTD; 5295; -.
DR VEuPathDB; HostDB:ENSBTAG00000010989; -.
DR VGNC; VGNC:32894; PIK3R1.
DR eggNOG; KOG4637; Eukaryota.
DR GeneTree; ENSGT00940000155553; -.
DR HOGENOM; CLU_007031_1_0_1; -.
DR InParanoid; P23727; -.
DR OMA; VIPVQWY; -.
DR OrthoDB; 737926at2759; -.
DR TreeFam; TF102033; -.
DR EvolutionaryTrace; P23727; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000010989; Expressed in granulosa cell and 108 other tissues.
DR ExpressionAtlas; P23727; baseline and differential.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005801; C:cis-Golgi network; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990578; C:perinuclear endoplasmic reticulum membrane; IEA:Ensembl.
DR GO; GO:0005942; C:phosphatidylinositol 3-kinase complex; IDA:BHF-UCL.
DR GO; GO:0005943; C:phosphatidylinositol 3-kinase complex, class IA; ISS:UniProtKB.
DR GO; GO:0046935; F:1-phosphatidylinositol-3-kinase regulator activity; IBA:GO_Central.
DR GO; GO:0043125; F:ErbB-3 class receptor binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043559; F:insulin binding; IEA:Ensembl.
DR GO; GO:0005158; F:insulin receptor binding; ISS:UniProtKB.
DR GO; GO:0043560; F:insulin receptor substrate binding; IDA:BHF-UCL.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISS:UniProtKB.
DR GO; GO:0005168; F:neurotrophin TRKA receptor binding; IEA:Ensembl.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:BHF-UCL.
DR GO; GO:0035014; F:phosphatidylinositol 3-kinase regulator activity; IDA:BHF-UCL.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IEA:Ensembl.
DR GO; GO:0001784; F:phosphotyrosine residue binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IDA:BHF-UCL.
DR GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
DR GO; GO:0001678; P:cellular glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IEA:Ensembl.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0060396; P:growth hormone receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0048009; P:insulin-like growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0097529; P:myeloid leukocyte migration; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0045671; P:negative regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IMP:BHF-UCL.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IDA:BHF-UCL.
DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; IEA:Ensembl.
DR GO; GO:0046326; P:positive regulation of glucose import; IMP:BHF-UCL.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0002687; P:positive regulation of leukocyte migration; IEA:Ensembl.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:BHF-UCL.
DR GO; GO:0033120; P:positive regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0043551; P:regulation of phosphatidylinositol 3-kinase activity; IDA:BHF-UCL.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IMP:BHF-UCL.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd12924; iSH2_PIK3R1; 1.
DR CDD; cd09930; SH2_cSH2_p85_like; 1.
DR CDD; cd09942; SH2_nSH2_p85_like; 1.
DR CDD; cd11910; SH3_PI3K_p85alpha; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 3.30.505.10; -; 2.
DR InterPro; IPR044124; ISH2_PIK3R1.
DR InterPro; IPR032498; PI3K_P85_iSH2.
DR InterPro; IPR035591; PI3K_p85alpha_SH3.
DR InterPro; IPR035020; PI3kinase_P85_cSH2.
DR InterPro; IPR035022; PI3kinase_P85_nSH2.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF16454; PI3K_P85_iSH2; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00017; SH2; 2.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00252; SH2; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
DR PROSITE; PS50238; RHOGAP; 1.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; SH2 domain; SH3 domain; Stress response;
KW Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P27986"
FT CHAIN 2..724
FT /note="Phosphatidylinositol 3-kinase regulatory subunit
FT alpha"
FT /id="PRO_0000080757"
FT DOMAIN 3..79
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 113..301
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT DOMAIN 333..428
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 624..718
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 79..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..99
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P27986"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27986"
FT MOD_RES 279
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P27986"
FT MOD_RES 467
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P26450"
FT MOD_RES 580
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P27986"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14729945"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:1PNJ"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:6R4R"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:6R4R"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:6R4R"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:6R4R"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:6R4R"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:6R4R"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6R4R"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:6D85"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:6D85"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:6D85"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:6D85"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:6D85"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:6D85"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:6D85"
FT HELIX 200..208
FT /evidence="ECO:0007829|PDB:6D85"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:6D85"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:6D85"
FT HELIX 235..251
FT /evidence="ECO:0007829|PDB:6D85"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:6D85"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:6D85"
FT HELIX 283..295
FT /evidence="ECO:0007829|PDB:6D85"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:1OO4"
FT TURN 341..344
FT /evidence="ECO:0007829|PDB:1OO3"
FT HELIX 345..349
FT /evidence="ECO:0007829|PDB:1OO3"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:1OO3"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:1OO3"
FT STRAND 370..378
FT /evidence="ECO:0007829|PDB:1OO3"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2PNA"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:1OO3"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:1OO3"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:1OO3"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:1OO3"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:1OO3"
FT HELIX 442..514
FT /evidence="ECO:0007829|PDB:7JIS"
FT HELIX 518..586
FT /evidence="ECO:0007829|PDB:7JIS"
FT HELIX 591..598
FT /evidence="ECO:0007829|PDB:7JIS"
FT HELIX 617..619
FT /evidence="ECO:0007829|PDB:1QAD"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:1QAD"
FT STRAND 625..628
FT /evidence="ECO:0007829|PDB:1QAD"
FT HELIX 631..638
FT /evidence="ECO:0007829|PDB:1QAD"
FT STRAND 645..650
FT /evidence="ECO:0007829|PDB:1QAD"
FT STRAND 652..655
FT /evidence="ECO:0007829|PDB:1BFI"
FT STRAND 657..663
FT /evidence="ECO:0007829|PDB:1QAD"
FT STRAND 666..675
FT /evidence="ECO:0007829|PDB:1QAD"
FT STRAND 678..682
FT /evidence="ECO:0007829|PDB:1QAD"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:1QAD"
FT HELIX 691..700
FT /evidence="ECO:0007829|PDB:1QAD"
FT HELIX 703..705
FT /evidence="ECO:0007829|PDB:1QAD"
SQ SEQUENCE 724 AA; 83497 MW; EBDF6E754BBF7321 CRC64;
MSAEGYQYRA LYDYKKEREE DIDLHLGDIL TVNKGSLVAL GFSDGQEAKP EEIGWLNGYN
ETTGERGDFP GTYVEYIGRK KISPPTPKPR PPRPLPVAPG PSKTEADSEQ QASTLPDLAE
QFAPPDVAPP LLIKLVEAIE KKGLECSTLY RTQSSSNPAE LRQLLDCDTA SLDLEMFDVH
VLADAFKRYL LDLPNPVIPV AVSSELISLA PEVQSSEEYI QLLKKLIRSP SIPHQYWLTL
QYLLKHFFKL SQTSSKNLLN ARVLSELFSP LLFRFPAASS ENTEHLIKII EILISTEWNE
RQPAPALPPK PPKPTTVANN GMNNNMSLQD AEWYWGDISR EEVNEKLRDT ADGTFLVRDA
STKMHGDYTL TLRKGGNNKL IKIFHRDGKY GFSDPLTFNS VVELINHYRN ESLAQYNPKL
DVKLLYPVSK YQQDQVVKED NIEAVGKKLH EYNTQFQEKS REYDRLYEDY TRTSQEIQMK
RTAIEAFNET IKIFEEQCQT QERYSKEYIE KFKREGNETE IQRIMHNYEK LKSRISEIVD
SRRRLEEDLK KQAAEYREID KRMNSIKPDL IQLRKTRDQY LMWLTQKGVR QKKLNEWLGN
ENTEDQYSLV EDDEDLPHHD EKTWNVGSSN RNKAENLLRG KRDGTFLVRE SSKQGCYACS
VVVDGEVKHC VINKTATGYG FAEPYNLYSS LKELVLHYQH TSLVQHNDSL NVTLAYPVYA
QQRR
