ANGT_MOUSE
ID ANGT_MOUSE Reviewed; 477 AA.
AC P11859;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Angiotensinogen;
DE AltName: Full=Serpin A8;
DE Contains:
DE RecName: Full=Angiotensin-1;
DE AltName: Full=Angiotensin 1-10;
DE AltName: Full=Angiotensin I;
DE Short=Ang I;
DE Contains:
DE RecName: Full=Angiotensin-2;
DE AltName: Full=Angiotensin 1-8;
DE AltName: Full=Angiotensin II;
DE Short=Ang II;
DE Contains:
DE RecName: Full=Angiotensin-3;
DE AltName: Full=Angiotensin 2-8;
DE AltName: Full=Angiotensin III;
DE Short=Ang III;
DE AltName: Full=Des-Asp[1]-angiotensin II;
DE Contains:
DE RecName: Full=Angiotensin-4;
DE AltName: Full=Angiotensin 3-8;
DE AltName: Full=Angiotensin IV;
DE Short=Ang IV;
DE Contains:
DE RecName: Full=Angiotensin 1-9;
DE Contains:
DE RecName: Full=Angiotensin 1-7;
DE Contains:
DE RecName: Full=Angiotensin 1-5;
DE Contains:
DE RecName: Full=Angiotensin 1-4;
DE Flags: Precursor;
GN Name=Agt; Synonyms=Serpina8;
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 [GENOMIC DNA].
RX PubMed=3397061; DOI=10.1016/0888-7543(88)90008-0;
RA Clouston W.M., Evans B.A., Haralambidis J., Richards R.I.;
RT "Molecular cloning of the mouse angiotensinogen gene.";
RL Genomics 2:240-248(1988).
RN [2]
RP FUNCTION OF ANGIOTENSIN 1-7 AS LIGAND FOR MAS1.
RX PubMed=12829792; DOI=10.1073/pnas.1432869100;
RA Santos R.A.S., Simoes e Silva A.C., Maric C., Silva D.M.R., Machado R.P.,
RA de Buhr I., Heringer-Walther S., Pinheiro S.V.B., Lopes M.T., Bader M.,
RA Mendes E.P., Lemos V.S., Campagnole-Santos M.J., Schultheiss H.-P.,
RA Speth R., Walther T.;
RT "Angiotensin-(1-7) is an endogenous ligand for the G protein-coupled
RT receptor Mas.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:8258-8263(2003).
RN [3]
RP FUNCTION OF ANGIOTENSIN 1-7.
RX PubMed=18026570; DOI=10.2119/2007-00073.fraga-silva;
RA Fraga-Silva R.A., Pinheiro S.V.B., Goncalves A.C., Alenina N., Bader M.,
RA Santos R.A.S.;
RT "The antithrombotic effect of angiotensin-(1-7) involves mas-mediated NO
RT release from platelets.";
RL Mol. Med. 14:28-35(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, and Testis;
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 [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-477, AND DISULFIDE BOND.
RX PubMed=20927107; DOI=10.1038/nature09505;
RA Zhou A., Carrell R.W., Murphy M.P., Wei Z., Yan Y., Stanley P.L.,
RA Stein P.E., Broughton Pipkin F., Read R.J.;
RT "A redox switch in angiotensinogen modulates angiotensin release.";
RL Nature 468:108-111(2010).
CC -!- FUNCTION: Essential component of the renin-angiotensin system (RAS), a
CC potent regulator of blood pressure, body fluid and electrolyte
CC homeostasis. {ECO:0000250|UniProtKB:P01019}.
CC -!- FUNCTION: [Angiotensin-2]: Acts directly on vascular smooth muscle as a
CC potent vasoconstrictor, affects cardiac contractility and heart rate
CC through its action on the sympathetic nervous system, and alters renal
CC sodium and water absorption through its ability to stimulate the zona
CC glomerulosa cells of the adrenal cortex to synthesize and secrete
CC aldosterone. Acts by binding to angiotensin receptors AGTR1 and AGTR2.
CC Also binds the DEAR/FBXW7-AS1 receptor. {ECO:0000250|UniProtKB:P01015,
CC ECO:0000250|UniProtKB:P01019}.
CC -!- FUNCTION: [Angiotensin-3]: Stimulates aldosterone release.
CC {ECO:0000250|UniProtKB:P01019}.
CC -!- FUNCTION: [Angiotensin 1-7]: Is a ligand for the G-protein coupled
CC receptor MAS1 (PubMed:12829792). Has vasodilator and antidiuretic
CC effects. Has an antithrombotic effect that involves MAS1-mediated
CC release of nitric oxide from platelets (PubMed:12829792,
CC PubMed:18026570). {ECO:0000269|PubMed:12829792,
CC ECO:0000269|PubMed:18026570}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01019}.
CC -!- PTM: In response to low blood pressure, the enzyme renin/REN cleaves
CC angiotensinogen to produce angiotensin-1. Angiotensin-1 is a substrate
CC of ACE (angiotensin converting enzyme) that removes a dipeptide to
CC yield the physiologically active peptide angiotensin-2. Angiotensin-1
CC and angiotensin-2 can be further processed to generate angiotensin-3,
CC angiotensin-4. Angiotensin 1-9 is cleaved from angiotensin-1 by ACE2
CC and can be further processed by ACE to produce angiotensin 1-7,
CC angiotensin 1-5 and angiotensin 1-4. Angiotensin 1-7 has also been
CC proposed to be cleaved from angiotensin-2 by ACE2 or from angiotensin-1
CC by MME (neprilysin) (By similarity). {ECO:0000250|UniProtKB:P01019}.
CC -!- PTM: The disulfide bond is labile. Angiotensinogen is present in the
CC circulation in a near 40:60 ratio with the oxidized disulfide-bonded
CC form, which preferentially interacts with receptor-bound renin.
CC {ECO:0000269|PubMed:20927107}.
CC -!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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DR EMBL; AF045887; AAC01765.1; -; Genomic_DNA.
DR EMBL; AF045886; AAC01765.1; JOINED; Genomic_DNA.
DR EMBL; AF045885; AAC01765.1; JOINED; Genomic_DNA.
DR EMBL; AF045884; AAC01765.1; JOINED; Genomic_DNA.
DR CCDS; CCDS40513.2; -.
DR PIR; A29978; A29978.
DR PDB; 2WXX; X-ray; 2.95 A; A/B/C/D=25-477.
DR PDB; 2WXY; X-ray; 2.10 A; C=25-477.
DR PDB; 2WY0; X-ray; 2.38 A; C=25-477.
DR PDBsum; 2WXX; -.
DR PDBsum; 2WXY; -.
DR PDBsum; 2WY0; -.
DR AlphaFoldDB; P11859; -.
DR SMR; P11859; -.
DR STRING; 10090.ENSMUSP00000066488; -.
DR MEROPS; I04.953; -.
DR GlyGen; P11859; 3 sites.
DR iPTMnet; P11859; -.
DR PhosphoSitePlus; P11859; -.
DR SwissPalm; P11859; -.
DR CPTAC; non-CPTAC-3527; -.
DR MaxQB; P11859; -.
DR PaxDb; P11859; -.
DR PeptideAtlas; P11859; -.
DR PRIDE; P11859; -.
DR ProteomicsDB; 296206; -.
DR MGI; MGI:87963; Agt.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; P11859; -.
DR PhylomeDB; P11859; -.
DR Reactome; R-MMU-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR ChiTaRS; Mgmt; mouse.
DR EvolutionaryTrace; P11859; -.
DR PRO; PR:P11859; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P11859; protein.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005179; F:hormone activity; ISO:MGI.
DR GO; GO:0048018; F:receptor ligand activity; ISO:MGI.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0017080; F:sodium channel regulator activity; ISO:MGI.
DR GO; GO:0031702; F:type 1 angiotensin receptor binding; IDA:MGI.
DR GO; GO:0031703; F:type 2 angiotensin receptor binding; IPI:MGI.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; IDA:MGI.
DR GO; GO:0007202; P:activation of phospholipase C activity; ISO:MGI.
DR GO; GO:0035932; P:aldosterone secretion; IMP:MGI.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; ISO:MGI.
DR GO; GO:0003051; P:angiotensin-mediated drinking behavior; ISO:MGI.
DR GO; GO:0001998; P:angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; IDA:MGI.
DR GO; GO:0014824; P:artery smooth muscle contraction; ISO:MGI.
DR GO; GO:0008306; P:associative learning; ISO:MGI.
DR GO; GO:0048143; P:astrocyte activation; IMP:MGI.
DR GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR GO; GO:0002035; P:brain renin-angiotensin system; IDA:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IDA:MGI.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0007160; P:cell-matrix adhesion; IMP:MGI.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:MGI.
DR GO; GO:0042756; P:drinking behavior; IMP:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0008065; P:establishment of blood-nerve barrier; IMP:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0042445; P:hormone metabolic process; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0000165; P:MAPK cascade; IMP:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; ISO:MGI.
DR GO; GO:0048662; P:negative regulation of smooth muscle cell proliferation; IMP:MGI.
DR GO; GO:0034104; P:negative regulation of tissue remodeling; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0035106; P:operant conditioning; ISO:MGI.
DR GO; GO:0035265; P:organ growth; IDA:MGI.
DR GO; GO:0001543; P:ovarian follicle rupture; IMP:MGI.
DR GO; GO:0030432; P:peristalsis; IMP:MGI.
DR GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; ISO:MGI.
DR GO; GO:0045777; P:positive regulation of blood pressure; ISO:MGI.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISO:MGI.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; ISO:MGI.
DR GO; GO:0043085; P:positive regulation of catalytic activity; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; ISO:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; ISO:MGI.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IMP:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:MGI.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; ISO:MGI.
DR GO; GO:1905589; P:positive regulation of L-arginine import across plasma membrane; ISO:MGI.
DR GO; GO:1905010; P:positive regulation of L-lysine import across plasma membrane; ISO:MGI.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:MGI.
DR GO; GO:1902632; P:positive regulation of membrane hyperpolarization; ISO:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0046622; P:positive regulation of organ growth; IDA:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; IDA:MGI.
DR GO; GO:0051247; P:positive regulation of protein metabolic process; ISO:MGI.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:MGI.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; ISO:MGI.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; ISO:MGI.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR GO; GO:1903779; P:regulation of cardiac conduction; ISO:MGI.
DR GO; GO:1901201; P:regulation of extracellular matrix assembly; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IDA:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:0014061; P:regulation of norepinephrine secretion; ISO:MGI.
DR GO; GO:0002019; P:regulation of renal output by angiotensin; IMP:MGI.
DR GO; GO:0035813; P:regulation of renal sodium excretion; ISO:MGI.
DR GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; IMP:MGI.
DR GO; GO:0051969; P:regulation of transmission of nerve impulse; ISO:MGI.
DR GO; GO:0001999; P:renal response to blood flow involved in circulatory renin-angiotensin regulation of systemic arterial blood pressure; IMP:MGI.
DR GO; GO:0003014; P:renal system process; ISO:MGI.
DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; IMP:MGI.
DR GO; GO:0009409; P:response to cold; IMP:MGI.
DR GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; ISO:MGI.
DR GO; GO:0009651; P:response to salt stress; IMP:MGI.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IDA:MGI.
DR GO; GO:0048659; P:smooth muscle cell proliferation; IDA:MGI.
DR GO; GO:0051403; P:stress-activated MAPK cascade; ISO:MGI.
DR GO; GO:0070471; P:uterine smooth muscle contraction; ISO:MGI.
DR GO; GO:1990874; P:vascular associated smooth muscle cell proliferation; IMP:MGI.
DR GO; GO:0042310; P:vasoconstriction; ISO:MGI.
DR GO; GO:0042311; P:vasodilation; ISO:MGI.
DR GO; GO:0030103; P:vasopressin secretion; IMP:MGI.
DR CDD; cd02054; serpinA8_AGT; 1.
DR Gene3D; 2.30.39.10; -; 1.
DR Gene3D; 3.30.497.10; -; 1.
DR InterPro; IPR000227; Angiotensinogen.
DR InterPro; IPR033834; Angiotensinogen_serpin_dom.
DR InterPro; IPR023796; Serpin_dom.
DR InterPro; IPR000215; Serpin_fam.
DR InterPro; IPR036186; Serpin_sf.
DR InterPro; IPR042178; Serpin_sf_1.
DR InterPro; IPR042185; Serpin_sf_2.
DR PANTHER; PTHR11461; PTHR11461; 1.
DR PANTHER; PTHR11461:SF13; PTHR11461:SF13; 1.
DR Pfam; PF00079; Serpin; 1.
DR PRINTS; PR00654; ANGIOTENSNGN.
DR SMART; SM00093; SERPIN; 1.
DR SUPFAM; SSF56574; SSF56574; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Reference proteome; Secreted;
KW Signal; Vasoactive; Vasoconstrictor.
FT SIGNAL 1..24
FT /evidence="ECO:0000305|PubMed:20927107"
FT CHAIN 25..477
FT /note="Angiotensinogen"
FT /id="PRO_0000032460"
FT PEPTIDE 25..34
FT /note="Angiotensin-1"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032461"
FT PEPTIDE 25..33
FT /note="Angiotensin 1-9"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420664"
FT PEPTIDE 25..32
FT /note="Angiotensin-2"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032462"
FT PEPTIDE 25..31
FT /note="Angiotensin 1-7"
FT /evidence="ECO:0000305|PubMed:12829792,
FT ECO:0000305|PubMed:18026570"
FT /id="PRO_0000420665"
FT PEPTIDE 25..29
FT /note="Angiotensin 1-5"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420666"
FT PEPTIDE 25..28
FT /note="Angiotensin 1-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420667"
FT PEPTIDE 26..32
FT /note="Angiotensin-3"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032463"
FT PEPTIDE 27..32
FT /note="Angiotensin-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420668"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 401
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..161
FT /evidence="ECO:0000269|PubMed:20927107"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2WXY"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2WY0"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:2WXY"
FT HELIX 88..115
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:2WXY"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:2WXY"
FT HELIX 144..151
FT /evidence="ECO:0007829|PDB:2WXY"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:2WXY"
FT HELIX 167..182
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 193..203
FT /evidence="ECO:0007829|PDB:2WXY"
FT HELIX 211..218
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:2WXY"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 267..284
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 303..315
FT /evidence="ECO:0007829|PDB:2WXY"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 320..340
FT /evidence="ECO:0007829|PDB:2WXY"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:2WXY"
FT HELIX 344..351
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:2WXY"
FT HELIX 383..389
FT /evidence="ECO:0007829|PDB:2WXY"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 416..427
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 452..458
FT /evidence="ECO:0007829|PDB:2WXY"
FT TURN 459..461
FT /evidence="ECO:0007829|PDB:2WXY"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:2WXY"
SQ SEQUENCE 477 AA; 51990 MW; A877F4029F338607 CRC64;
MTPTGAGLKA TIFCILTWVS LTAGDRVYIH PFHLLYHNKS TCAQLENPSV ETLPESTFEP
VPIQAKTSPV NEKTLHDQLV LAAEKLEDED RKRAAQVAMI ANFVGFRMYK MLNEAGSGAS
GAILSPPALF GTLVSFYLGS LDPTASQLQT LLDVPVKEGD CTSRLDGHKV LAALRAVQGL
LVTQGGSSSQ TPLLQSIMVG LFTAPGFRLK HSFVQSLALF TPALFPRSLD LSTDPVLATE
KINRFIKAVT GWKMNLPLEG VSTDSTLLFN TYVHFQGTMR GFSQLPGVHE FWVDNSISVS
VPMISGTGNF QHWSDAQNNF SVTCVPLGER ATLLLIQPHC TSDLDRVEAL IFRNDLLTWI
ENPPPRAIRL TLPQLEIRGS YNLQDLLAED KLPTLLGAEA NLSNIGDTNP RVGEVLNSIL
LELKAGEEEQ PTTSVQQPGS PEALDVTLSS PFLFAIYEQD SGTLHFLGRV NNPQSVV
