ANGT_RAT
ID ANGT_RAT Reviewed; 477 AA.
AC P01015;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 175.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=6572971; DOI=10.1073/pnas.80.8.2196;
RA Ohkubo H., Kageyama R., Ujihara M., Hirose T., Inayama S., Nakanishi S.;
RT "Cloning and sequence analysis of cDNA for rat angiotensinogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:2196-2200(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6330095; DOI=10.1016/s0021-9258(17)39689-8;
RA Tanaka T., Ohkubo H., Nakanishi S.;
RT "Common structural organization of the angiotensinogen and the alpha 1-
RT antitrypsin genes.";
RL J. Biol. Chem. 259:8063-8065(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 25-34.
RX PubMed=4344907; DOI=10.1248/cpb.20.1579;
RA Nakayama T., Nakajima T., Sokabe H.;
RT "Comparative studies on angiotensins. II. Structure of rat angiotensin and
RT its identification by DNS-method.";
RL Chem. Pharm. Bull. 20:1579-1581(1972).
RN [5]
RP FUNCTION.
RC STRAIN=Sprague-Dawley;
RX PubMed=9508787; DOI=10.1007/bf03401733;
RA Ruiz-Opazo N., Hirayama K., Akimoto K., Herrera V.L.;
RT "Molecular characterization of a dual endothelin-1/Angiotensin II
RT receptor.";
RL Mol. Med. 4:96-108(1998).
RN [6]
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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 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 (By similarity). Also binds the DEAR/FBXW7-AS1 receptor
CC (PubMed:9508787). {ECO:0000250|UniProtKB:P01019,
CC ECO:0000269|PubMed:9508787}.
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 (By similarity). Has vasodilator and antidiuretic effects
CC (By similarity). Has an antithrombotic effect that involves MAS1-
CC mediated release of nitric oxide from platelets (PubMed:18026570).
CC {ECO:0000250|UniProtKB:P11859, ECO:0000269|PubMed:18026570}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:4344907}.
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; L00094; AAA98779.1; -; Genomic_DNA.
DR EMBL; L00091; AAA98779.1; JOINED; Genomic_DNA.
DR EMBL; L00092; AAA98779.1; JOINED; Genomic_DNA.
DR EMBL; L00093; AAA98779.1; JOINED; Genomic_DNA.
DR EMBL; BC078741; AAH78741.1; -; mRNA.
DR EMBL; BC087679; AAH87679.1; -; mRNA.
DR PIR; A93945; ANRT.
DR RefSeq; NP_602308.1; NM_134432.2.
DR RefSeq; XP_008770819.1; XM_008772597.2.
DR PDB; 1SMR; X-ray; 2.00 A; B/D/F/H=30-33.
DR PDB; 2WXZ; X-ray; 2.80 A; A/C=25-477.
DR PDB; 2WY1; X-ray; 3.15 A; A/B=25-477.
DR PDBsum; 1SMR; -.
DR PDBsum; 2WXZ; -.
DR PDBsum; 2WY1; -.
DR AlphaFoldDB; P01015; -.
DR SMR; P01015; -.
DR BioGRID; 246369; 1.
DR STRING; 10116.ENSRNOP00000024917; -.
DR BindingDB; P01015; -.
DR MEROPS; I04.953; -.
DR GlyGen; P01015; 2 sites.
DR iPTMnet; P01015; -.
DR PhosphoSitePlus; P01015; -.
DR SwissPalm; P01015; -.
DR PaxDb; P01015; -.
DR PRIDE; P01015; -.
DR GeneID; 24179; -.
DR KEGG; rno:24179; -.
DR UCSC; RGD:2069; rat.
DR CTD; 183; -.
DR RGD; 2069; Agt.
DR VEuPathDB; HostDB:ENSRNOG00000018445; -.
DR eggNOG; KOG2392; Eukaryota.
DR HOGENOM; CLU_045267_1_0_1; -.
DR InParanoid; P01015; -.
DR OMA; FMGFRMY; -.
DR OrthoDB; 450590at2759; -.
DR PhylomeDB; P01015; -.
DR TreeFam; TF343201; -.
DR Reactome; R-RNO-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR EvolutionaryTrace; P01015; -.
DR PRO; PR:P01015; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000018445; Expressed in liver and 19 other tissues.
DR Genevisible; P01015; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005179; F:hormone activity; IDA:BHF-UCL.
DR GO; GO:0048018; F:receptor ligand activity; ISS:BHF-UCL.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IBA:GO_Central.
DR GO; GO:0031702; F:type 1 angiotensin receptor binding; ISO:RGD.
DR GO; GO:0031703; F:type 2 angiotensin receptor binding; ISO:RGD.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; ISO:RGD.
DR GO; GO:0007202; P:activation of phospholipase C activity; IMP:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0035932; P:aldosterone secretion; ISO:RGD.
DR GO; GO:0038166; P:angiotensin-activated signaling pathway; ISS:BHF-UCL.
DR GO; GO:0003051; P:angiotensin-mediated drinking behavior; IDA:RGD.
DR GO; GO:0001998; P:angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0014824; P:artery smooth muscle contraction; IDA:RGD.
DR GO; GO:0008306; P:associative learning; IDA:RGD.
DR GO; GO:0048143; P:astrocyte activation; ISO:RGD.
DR GO; GO:0001568; P:blood vessel development; ISO:RGD.
DR GO; GO:0002035; P:brain renin-angiotensin system; ISO:RGD.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISO:RGD.
DR GO; GO:0061049; P:cell growth involved in cardiac muscle cell development; IDA:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:RGD.
DR GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR GO; GO:1904385; P:cellular response to angiotensin; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IMP:RGD.
DR GO; GO:0042756; P:drinking behavior; ISO:RGD.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:RGD.
DR GO; GO:0008065; P:establishment of blood-nerve barrier; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0048144; P:fibroblast proliferation; IDA:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0042445; P:hormone metabolic process; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IDA:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0010951; P:negative regulation of endopeptidase activity; IBA:GO_Central.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; ISO:RGD.
DR GO; GO:0034104; P:negative regulation of tissue remodeling; IDA:RGD.
DR GO; GO:0035106; P:operant conditioning; IDA:RGD.
DR GO; GO:0001543; P:ovarian follicle rupture; ISO:RGD.
DR GO; GO:0030432; P:peristalsis; ISO:RGD.
DR GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; ISO:RGD.
DR GO; GO:0045777; P:positive regulation of blood pressure; IDA:RGD.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISO:RGD.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IDA:RGD.
DR GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IDA:BHF-UCL.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0010873; P:positive regulation of cholesterol esterification; ISO:RGD.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IEA:Ensembl.
DR GO; GO:0001819; P:positive regulation of cytokine production; ISO:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0003331; P:positive regulation of extracellular matrix constituent secretion; IDA:RGD.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:BHF-UCL.
DR GO; GO:1903598; P:positive regulation of gap junction assembly; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:RGD.
DR GO; GO:1905589; P:positive regulation of L-arginine import across plasma membrane; IDA:RGD.
DR GO; GO:1905010; P:positive regulation of L-lysine import across plasma membrane; IDA:RGD.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:RGD.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IDA:RGD.
DR GO; GO:0046622; P:positive regulation of organ growth; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:RGD.
DR GO; GO:1900020; P:positive regulation of protein kinase C activity; ISO:RGD.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISO:RGD.
DR GO; GO:0035815; P:positive regulation of renal sodium excretion; IDA:RGD.
DR GO; GO:0032930; P:positive regulation of superoxide anion generation; IDA:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IDA:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IDA:RGD.
DR GO; GO:0006606; P:protein import into nucleus; IDA:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; IDA:RGD.
DR GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:RGD.
DR GO; GO:1903779; P:regulation of cardiac conduction; ISO:RGD.
DR GO; GO:1901201; P:regulation of extracellular matrix assembly; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0002027; P:regulation of heart rate; IDA:RGD.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:RGD.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:RGD.
DR GO; GO:0014061; P:regulation of norepinephrine secretion; IMP:RGD.
DR GO; GO:0002019; P:regulation of renal output by angiotensin; ISO:RGD.
DR GO; GO:0035813; P:regulation of renal sodium excretion; IDA:RGD.
DR GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; ISO:RGD.
DR GO; GO:0051969; P:regulation of transmission of nerve impulse; IDA:RGD.
DR GO; GO:0001999; P:renal response to blood flow involved in circulatory renin-angiotensin regulation of systemic arterial blood pressure; ISO:RGD.
DR GO; GO:0003014; P:renal system process; ISO:RGD.
DR GO; GO:0002018; P:renin-angiotensin regulation of aldosterone production; IDA:RGD.
DR GO; GO:0009409; P:response to cold; ISO:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0014873; P:response to muscle activity involved in regulation of muscle adaptation; IMP:BHF-UCL.
DR GO; GO:0009651; P:response to salt stress; ISO:RGD.
DR GO; GO:0051145; P:smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0048659; P:smooth muscle cell proliferation; IDA:RGD.
DR GO; GO:0051403; P:stress-activated MAPK cascade; IDA:RGD.
DR GO; GO:0070471; P:uterine smooth muscle contraction; IDA:RGD.
DR GO; GO:0042310; P:vasoconstriction; IDA:RGD.
DR GO; GO:0042311; P:vasodilation; IDA:RGD.
DR GO; GO:0030103; P:vasopressin secretion; ISO:RGD.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Reference proteome; Secreted; Signal; Vasoactive; Vasoconstrictor.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:4344907"
FT CHAIN 25..477
FT /note="Angiotensinogen"
FT /id="PRO_0000032468"
FT PEPTIDE 25..34
FT /note="Angiotensin-1"
FT /evidence="ECO:0000269|PubMed:4344907"
FT /id="PRO_0000032469"
FT PEPTIDE 25..33
FT /note="Angiotensin 1-9"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420674"
FT PEPTIDE 25..32
FT /note="Angiotensin-2"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032470"
FT PEPTIDE 25..31
FT /note="Angiotensin 1-7"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420675"
FT PEPTIDE 25..29
FT /note="Angiotensin 1-5"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420676"
FT PEPTIDE 25..28
FT /note="Angiotensin 1-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420677"
FT PEPTIDE 26..32
FT /note="Angiotensin-3"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000032471"
FT PEPTIDE 27..32
FT /note="Angiotensin-4"
FT /evidence="ECO:0000250|UniProtKB:P01019"
FT /id="PRO_0000420678"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..161
FT /evidence="ECO:0000269|PubMed:20927107"
FT TURN 33..35
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 39..43
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 72..84
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 88..115
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 167..181
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 193..203
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:2WXZ"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 224..228
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 235..250
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 267..279
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:2WY1"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 303..315
FT /evidence="ECO:0007829|PDB:2WXZ"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 320..340
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 344..351
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 366..373
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 383..389
FT /evidence="ECO:0007829|PDB:2WXZ"
FT TURN 393..396
FT /evidence="ECO:0007829|PDB:2WXZ"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 416..425
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 452..458
FT /evidence="ECO:0007829|PDB:2WXZ"
FT TURN 459..462
FT /evidence="ECO:0007829|PDB:2WXZ"
FT STRAND 463..471
FT /evidence="ECO:0007829|PDB:2WXZ"
SQ SEQUENCE 477 AA; 51982 MW; 689051A5788D693D CRC64;
MTPTGAGLKA TIFCILTWVS LTAGDRVYIH PFHLLYYSKS TCAQLENPSV ETLPEPTFEP
VPIQAKTSPV DEKTLRDKLV LATEKLEAED RQRAAQVAMI ANFMGFRMYK MLSEARGVAS
GAVLSPPALF GTLVSFYLGS LDPTASQLQV LLGVPVKEGD CTSRLDGHKV LTALQAVQGL
LVTQGGSSSQ TPLLQSTVVG LFTAPGLRLK QPFVESLGPF TPAIFPRSLD LSTDPVLAAQ
KINRFVQAVT GWKMNLPLEG VSTDSTLFFN TYVHFQGKMR GFSQLTGLHE FWVDNSTSVS
VPMLSGTGNF QHWSDAQNNF SVTRVPLGES VTLLLIQPQC ASDLDRVEVL VFQHDFLTWI
KNPPPRAIRL TLPQLEIRGS YNLQDLLAQA KLSTLLGAEA NLGKMGDTNP RVGEVLNSIL
LELQAGEEEQ PTESAQQPGS PEVLDVTLSS PFLFAIYERD SGALHFLGRV DNPQNVV
