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UniProtKB/Swiss-Prot entry P01019


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ANGT_HUMAN
Primary accession number P01019
Secondary accession numbers Q16358 Q16359 Q96F91
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 121)
Name and origin of the protein
Protein name Angiotensinogen [Precursor]
Synonym Serpin A8
Contains Angiotensin-1
     (Angiotensin I)
     (Ang I)
Angiotensin-2
     (Angiotensin II)
     (Ang II)
Angiotensin-3
     (Angiotensin III)
     (Ang III)
     (Des-Asp[1]-angiotensin II)
Gene name
Name: AGT
Synonyms: SERPINA8
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00311a006; PubMed=6089875 [NCBI, ExPASy, EBI, Israel, Japan]
Kageyama R., Ohkubo H., Nakanishi S.;
"Primary structure of human preangiotensinogen deduced from the cloned cDNA sequence.";
Biochemistry 23:3603-3609(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2924688 [NCBI, ExPASy, EBI, Israel, Japan]
Gaillard I., Clauser E., Corvol P.;
"Structure of human angiotensinogen gene.";
DNA 8:87-99(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1692023 [NCBI, ExPASy, EBI, Israel, Japan]
Fukamizu A., Takahashi S., Seo M.S., Tada M., Tanimoto K., Uehara S., Murakami K.;
"Structure and expression of the human angiotensinogen gene. Identification of a unique and highly active promoter.";
J. Biol. Chem. 265:7576-7582(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-335.
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-338.
PubMed=2885106 [NCBI, ExPASy, EBI, Israel, Japan]
Kunapuli S.P., Kumar A.;
"Molecular cloning of human angiotensinogen cDNA and evidence for the presence of its mRNA in rat heart.";
Circ. Res. 60:786-790(1987).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 32-184.
DOI=10.1016/0003-9861(87)90148-2; PubMed=3579322 [NCBI, ExPASy, EBI, Israel, Japan]
Kunapuli S.P., Benedict C.R., Kumar A.;
"Tissue specific hormonal regulation of the rat angiotensinogen gene expression.";
Arch. Biochem. Biophys. 254:642-646(1987).
[7]
PROTEIN SEQUENCE OF 34-58.
DOI=10.1016/0006-291X(81)90762-2; PubMed=7259779 [NCBI, ExPASy, EBI, Israel, Japan]
Tewksbury D.A., Dart R.A., Travis J.;
"The amino terminal amino acid sequence of human angiotensinogen.";
Biochem. Biophys. Res. Commun. 99:1311-1315(1981).
[8]
PROTEIN SEQUENCE OF 34-45, AND SUBUNIT.
TISSUE=Serum;
DOI=10.1074/jbc.270.23.13645; PubMed=7539791 [NCBI, ExPASy, EBI, Israel, Japan]
Oxvig C., Haaning J., Kristensen L., Wagner J.M., Rubin I., Stigbrand T., Gleich G.J., Sottrup-Jensen L.;
"Identification of angiotensinogen and complement C3dg as novel proteins binding the proform of eosinophil major basic protein in human pregnancy serum and plasma.";
J. Biol. Chem. 270:13645-13651(1995).
[9]
PROTEIN SEQUENCE OF 34-43.
PubMed=4300938 [NCBI, ExPASy, EBI, Israel, Japan]
Arakawa K., Minohara A., Yamada J., Nakamura M.;
"Enzymatic degradation and electrophoresis of human angiotensin I.";
Biochim. Biophys. Acta 168:106-112(1968).
[10]
GLYCOSYLATION AT ASN-47; ASN-170; ASN-304 AND ASN-328.
DOI=10.1016/0303-7207(85)90039-5; PubMed=3934016 [NCBI, ExPASy, EBI, Israel, Japan]
Campbell D.J., Bouhnik J., Coezy E., Menard J., Corvol P.;
"Processing of rat and human angiotensinogen precursors by microsomal membranes.";
Mol. Cell. Endocrinol. 43:31-40(1985).
[11]
FUNCTION OF ANGIOTENSIN-3.
PubMed=1132082 [NCBI, ExPASy, EBI, Israel, Japan]
Goodfriend T.L., Peach M.J.;
"Angiotensin III: (DES-Aspartic Acid-1)-Angiotensin II. Evidence and speculation for its role as an important agonist in the renin - angiotensin system.";
Circ. Res. 36:38-48(1975).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan]
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[13]
DECARBOXYLATION AT ASP-34, FUNCTION, AND MASS SPECTROMETRY.
DOI=10.1161/01.ATV.0000253889.09765.5f; PubMed=17138938 [NCBI, ExPASy, EBI, Israel, Japan]
Jankowski V., Vanholder R., van der Giet M., Tolle M., Karadogan S., Gobom J., Furkert J., Oksche A., Krause E., Tran T.N., Tepel M., Schuchardt M., Schluter H., Wiedon A., Beyermann M., Bader M., Todiras M., Zidek W., Jankowski J.;
"Mass-spectrometric identification of a novel angiotensin peptide in human plasma.";
Arterioscler. Thromb. Vasc. Biol. 27:297-302(2007).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-47, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan]
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[15]
STRUCTURE BY NMR OF ANGIOTENSIN-2.
DOI=10.1046/j.1432-1327.1998.2510448.x; PubMed=9492317 [NCBI, ExPASy, EBI, Israel, Japan]
Carpenter K.A., Wilkes B.C., Schiller P.W.;
"The octapeptide angiotensin II adopts a well-defined structure in a phospholipid environment.";
Eur. J. Biochem. 251:448-453(1998).
[16]
VARIANTS MET-207; THR-268 AND CYS-281.
DOI=10.1016/0092-8674(92)90275-H; PubMed=1394429 [NCBI, ExPASy, EBI, Israel, Japan]
Jeunemaitre X., Soubrier F., Kotelevtsev Y.V., Lifton R.P., Williams C.S., Charru A., Hunt S.C., Hopkins P.N., Williams R.R., Lalouel J.-M., Corvol P.;
"Molecular basis of human hypertension: role of angiotensinogen.";
Cell 71:169-180(1992).
[17]
VARIANT THR-268.
DOI=10.1038/ng0593-59; PubMed=8513325 [NCBI, ExPASy, EBI, Israel, Japan]
Ward K., Hata A., Jeunemaitre X., Helin C., Nelson L., Namikawa C., Farrington P.F., Ogasawara M., Suzumori K., Tomoda S., Berrebi S., Sasaki M., Corvol P., Lifton R.P., Lalouel J.-M.;
"A molecular variant of angiotensinogen associated with preeclampsia.";
Nat. Genet. 4:59-61(1993).
[18]
VARIANTS ILE-242; ARG-244 AND CYS-281.
DOI=10.1007/BF00214197; PubMed=7607642 [NCBI, ExPASy, EBI, Israel, Japan]
Hixson J.E., Powers P.K.;
"Detection and characterization of new mutations in the human angiotensinogen gene (AGT).";
Hum. Genet. 96:110-112(1995).
[19]
VARIANT PRE-ECLAMPSIA PHE-43.
DOI=10.1074/jbc.270.19.11430; PubMed=7744780 [NCBI, ExPASy, EBI, Israel, Japan]
Inoue I., Rohrwasser A., Helin C., Jeunemaitre X., Crain P., Bohlender J., Lifton R.P., Corvol P., Ward K., Lalouel J.-M.;
"A mutation of angiotensinogen in a patient with preeclampsia leads to altered kinetics of the renin-angiotensin system.";
J. Biol. Chem. 270:11430-11436(1995).
[20]
CHARACTERIZATION OF VARIANT CYS-281.
DOI=10.1074/jbc.271.16.9838; PubMed=8621667 [NCBI, ExPASy, EBI, Israel, Japan]
Gimenez-Roqueplo A.P., Leconte I., Cohen P., Simon D., Guyene T.T., Celerier J., Pau B., Corvol P., Clauser E., Jeunemaitre X.;
"The natural mutation Y248C of human angiotensinogen leads to abnormal glycosylation and altered immunological recognition of the protein.";
J. Biol. Chem. 271:9838-9844(1996).
[21]
VARIANT RTD GLN-375.
DOI=10.1038/ng1623; PubMed=16116425 [NCBI, ExPASy, EBI, Israel, Japan]
Gribouval O., Gonzales M., Neuhaus T., Aziza J., Bieth E., Laurent N., Bouton J.M., Feuillet F., Makni S., Ben Amar H., Laube G., Delezoide A.-L., Bouvier R., Dijoud F., Ollagnon-Roman E., Roume J., Joubert M., Antignac C., Gubler M.-C.;
"Mutations in genes in the renin-angiotensin system are associated with autosomal recessive renal tubular dysgenesis.";
Nat. Genet. 37:964-968(2005).
Comments
  • FUNCTION: In response to lowered blood pressure, the enzyme renin cleaves angiotensin-1, from angiotensinogen. ACE (angiotensin converting enzyme) then removes a dipeptide to yield the physiologically active peptide angiotensin-2, the most potent pressor substance known, which helps regulate volume and mineral balance of body fluids.
  • FUNCTION: Angiotensin-3 stimulates aldosterone release.
  • SUBUNIT: During pregnancy, exists as a disulfide-linked 2:2 heterotetramer with the proform of PRG2 and as a complex (probably a 2:2:2 heterohexamer) with pro-PRG2 and C3dg.
  • SUBCELLULAR LOCATION: Secreted.
  • TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
  • PTM: Beta-decarboxylation of Asp-34 in angiotensin-2, by mononuclear leukocytes produces alanine. The resulting peptide form, angiotensin-A, has the same affinity for the AT1 receptor as angiotensin-2, but a higher affinity for the AT2 receptor.
  • DISEASE: Defects in AGT are associated with susceptibility to essential hypertension [MIM:145500]. Hypertension also occurs in 5-7% of all pregnancies where it is a leading cause of maternal, fetal and neonatal morbidity and mortality. Among pregnancy-induced hypertension cases, severe pre-eclampsia [MIM:189800] is characterized by the development of hypertension and proteinuria after the 20th week of pregnancy and is the most distinctive, life-threatening form.
  • DISEASE: Defects in AGT are a cause of renal tubular dysgenesis (RTD) [MIM:267430]. RTD is an autosomal recessive severe disorder of renal tubular development characterized by persistent fetal anuria and perinatal death, probably due to pulmonary hypoplasia from early-onset oligohydramnios (the Potter phenotype).
  • SIMILARITY: Belongs to the serpin family.
  • CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=AGT";.
  • WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and polymorphism database; URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=AGT";.
  • WEB RESOURCE: Name=Wikipedia; Note=Angiotensin entry; URL="http://en.wikipedia.org/wiki/Angiotensin";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
K02215; AAA51731.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24689; AAA51679.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24686; AAA51679.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24687; AAA51679.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M24688; AAA51679.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15324; CAA33385.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15325; CAA33385.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15326; CAA33385.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X15327; CAA33385.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011519; AAH11519.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M69110; AAA52282.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S78529; AAD14287.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
S78530; AAD14288.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00032220; -.
PIR A35203; ANHU.
RefSeq NP_000020.1; -.
UniGene Hs.19383
3D structure databases
PDB
1N9U; NMR; -; A=34-43.[ExPASy / RCSB / EBI]
1N9V; NMR; -; A=34-41.[ExPASy / RCSB / EBI]
2JP8; NMR; -; P=34-40.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1N9U; -.
1N9V; -.
2JP8; -.
ModBase P01019.
Protein-protein interaction databases
DIP DIP:309N; -.
IntAct P01019; 2.
Enzyme and pathway databases
Pathway_Interaction_DB prlsignalingeventspathway; Signaling events mediated by PRL.
Reactome REACT_14797; Signaling by GPCR.
2D gel databases
SWISS-2DPAGE P01019; -.
Organism-specific databases
GeneCards GC01M228904; -.
H-InvDB HIX0001686; -.
HGNC HGNC:333; AGT.
GenAtlas AGT.
HPA HPA001557; -.
MIM 106150; gene. [NCBI / EBI]
145500; phenotype. [NCBI / EBI]
267430; phenotype. [NCBI / EBI]
Orphanet 3033; Renal tubular dysgenesis.
PharmGKB PA42; -.
Gene expression databases
ArrayExpress P01019; -.
Bgee P01019; -.
CleanEx HS_AGT; -.
GermOnline ENSG00000135744; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005615; Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0010698; Molecular function: acetyltransferase activator activity (inferred from direct assay from UniProtKB).
GO:0008083; Molecular function: growth factor activity (traceable author statement from UniProtKB).
GO:0005179; Molecular function: hormone activity (inferred by curator from UniProtKB).
GO:0004867; Molecular function: serine-type endopeptidase inhibitor activity (traceable author statement from ProtInc).
GO:0031702; Molecular function: type 1 angiotensin receptor binding (inferred from physical interaction from UniProtKB).
GO:0031703; Molecular function: type 2 angiotensin receptor binding (inferred from physical interaction from UniProtKB).
GO:0007200; Biological process: activation of phospholipase C activity by G-protein coupled receptor protein signaling pathway coupled to IP3 second messenger (non-traceable author statement from UniProtKB).
GO:0001974; Biological process: blood vessel remodeling (traceable author statement from UniProtKB).
GO:0007267; Biological process: cell-cell signaling (traceable author statement from ProtInc).
GO:0007199; Biological process: G-protein signaling, coupled to cGMP nucleotide second messenger (traceable author statement from UniProtKB).
GO:0034374; Biological process: low-density lipoprotein particle remodeling (non-traceable author statement from UniProtKB).
GO:0051387; Biological process: negative regulation of nerve growth factor receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0007263; Biological process: nitric oxide mediated signal transduction (traceable author statement from UniProtKB).
GO:0006800; Biological process: oxygen and reactive oxygen species metabolic process (traceable author statement from UniProtKB).
GO:0043065; Biological process: positive regulation of apoptosis (inferred from direct assay from UniProtKB).
GO:0010613; Biological process: positive regulation of cardiac muscle hypertrophy (inferred from sequence or structural similarity from UniProtKB).
GO:0010873; Biological process: positive regulation of cholesterol esterification (inferred from direct assay from UniProtKB).
GO:0001819; Biological process: positive regulation of cytokine production (traceable author statement from UniProtKB).
GO:0010595; Biological process: positive regulation of endothelial cell migration (inferred from direct assay from UniProtKB).
GO:0045742; Biological process: positive regulation of epidermal growth factor receptor signaling pathway (inferred from direct assay from UniProtKB).
GO:0048146; Biological process: positive regulation of fibroblast proliferation (inferred from sequence or structural similarity from UniProtKB).
GO:0010744; Biological process: positive regulation of foam cell differentiation (inferred by curator from UniProtKB).
GO:0050729; Biological process: positive regulation of inflammatory response (traceable author statement from UniProtKB).
GO:0033864; Biological process: positive regulation of NAD(P)H oxidase activity (traceable author statement from UniProtKB).
GO:0051092; Biological process: positive regulation of NF-kappaB transcription factor activity (traceable author statement from UniProtKB).
GO:0050731; Biological process: positive regulation of peptidyl-tyrosine phosphorylation (inferred from direct assay from UniProtKB).
GO:0014068; Biological process: positive regulation of phosphoinositide 3-kinase cascade (inferred from direct assay from UniProtKB).
GO:0001558; Biological process: regulation of cell growth (non-traceable author statement from UniProtKB).
GO:0003078; Biological process: regulation of natriuresis (non-traceable author statement from UniProtKB).
GO:0002019; Biological process: regulation of renal output by angiotensin (non-traceable author statement from UniProtKB).
GO:0019229; Biological process: regulation of vasoconstriction (non-traceable author statement from UniProtKB).
GO:0002018; Biological process: renin-angiotensin regulation of aldosterone production (non-traceable author statement from UniProtKB).
GO:0014873; Biological process: response to muscle activity involved in regulation of muscle adaptation (inferred from sequence or structural similarity from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000227; Angiotensngn.
IPR000215; Protease_inhib_I4_serpin.
Graphical view of domain structure.
PANTHER PTHR11461; Prot_inh_serpin; 1.
Pfam PF00079; Serpin; 1.
Pfam graphical view of domain structure.
PRINTS PR00654; ANGIOTENSNGN.
SMART SM00093; SERPIN; 1.
SMART graphical view of domain structure.
PROSITE PS00284; SERPIN; 1.
Proteomic databases
PeptideAtlas P01019; -.
PRIDE P01019; -.
Genome annotation databases
Ensembl ENSG00000135744; Homo sapiens. [Contig view]
GeneID 183; -.
KEGG hsa:183; -.
Phylogenomic databases
HOVERGEN P01019; -.
OMA P01019; TYVHFQG.
Other
DrugBank DB01258; Aliskiren.
DB01076; Atorvastatin.
DB01340; Cilazapril.
DB01029; Irbesartan.
DB00722; Lisinopril.
DB01092; Ouabain.
DB00641; Simvastatin.
NextBio 748; -.
PMAP-CutDB P01019; -.
SOURCE AGT; Homo sapiens.
ProtoNet P01019.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Disease mutation; Disulfide bond; Glycoprotein; Polymorphism; Secreted; Signal; Vasoactive; Vasoconstrictor.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    33  33      
CHAIN   34   485  452     Angiotensinogen. PRO_0000032456
PEPTIDE   34    43  10     Angiotensin-1. PRO_0000032457
PEPTIDE   34    41  8     Angiotensin-2. PRO_0000032458
PEPTIDE   35    41  7     Angiotensin-3. PRO_0000032459
MOD_RES   34    34        Beta-decarboxylated aspartate; in form angiotensin-A. 
CARBOHYD   47    47        N-linked (GlcNAc...). 
CARBOHYD   170   170        N-linked (GlcNAc...). 
CARBOHYD   304   304        N-linked (GlcNAc...). 
CARBOHYD   328   328        N-linked (GlcNAc...). 
VARIANT   43    43  1     L -> F (in pre-eclampsia; alters the reactions with renin and angiotensin-converting enzyme; dbSNP:rs41271499 [NCBI]). VAR_022933 
VARIANT   98    98  1     E -> K (in dbSNP:rs11568032 [NCBI]). VAR_029166 
VARIANT   114   114  1     G -> C (in dbSNP:rs2229389 [NCBI]). VAR_051939 
VARIANT   137   137  1     T -> M (in dbSNP:rs34829218 [NCBI]). VAR_035431 
VARIANT   207   207  1     T -> M (associated with hypertension; dbSNP:rs4762 [NCBI]). VAR_007093 
VARIANT   242   242  1     T -> I (in hypertension). VAR_007094 
VARIANT   244   244  1     L -> R (in hypertension; dbSNP:rs5041 [NCBI]). VAR_007095 
VARIANT   268   268  1     M -> I (in dbSNP:rs11568053 [NCBI]). VAR_029167 
VARIANT   268   268  1     M -> T (associated with essential hypertension and pre-eclampsia; dbSNP:rs699 [NCBI]). VAR_007096 
VARIANT   281   281  1     Y -> C (in hypertension; alters the structure, glycosylation and secretion of angiotensinogen). VAR_007097 
VARIANT   335   335  1     P -> S (in dbSNP:rs17856352 [NCBI]). VAR_035432 
VARIANT   375   375  1     R -> Q (in RTD). VAR_035433 
VARIANT   392   392  1     L -> M (in dbSNP:rs1805090 [NCBI]). VAR_014573 
CONFLICT   51    51        C -> S (in Ref. 7; AA sequence). 
CONFLICT   58    58        N -> D (in Ref. 7; AA sequence). 
CONFLICT   333   333        Q -> E (in Ref. 2; AAA51679). 
Sequence information
Length: 485 AA [This is the length of the unprocessed precursor] Molecular weight: 53154 Da [This is the MW of the unprocessed precursor] CRC64: 5026C2DFB2DD236E [This is a checksum on the sequence]
        10         20         30         40         50         60 
MRKRAPQSEM APAGVSLRAT ILCLLAWAGL AAGDRVYIHP FHLVIHNEST CEQLAKANAG 

        70         80         90        100        110        120 
KPKDPTFIPA PIQAKTSPVD EKALQDQLVL VAAKLDTEDK LRAAMVGMLA NFLGFRIYGM 

       130        140        150        160        170        180 
HSELWGVVHG ATVLSPTAVF GTLASLYLGA LDHTADRLQA ILGVPWKDKN CTSRLDAHKV 

       190        200        210        220        230        240 
LSALQAVQGL LVAQGRADSQ AQLLLSTVVG VFTAPGLHLK QPFVQGLALY TPVVLPRSLD 

       250        260        270        280        290        300 
FTELDVAAEK IDRFMQAVTG WKTGCSLMGA SVDSTLAFNT YVHFQGKMKG FSLLAEPQEF 

       310        320        330        340        350        360 
WVDNSTSVSV PMLSGMGTFQ HWSDIQDNFS VTQVPFTESA CLLLIQPHYA SDLDKVEGLT 

       370        380        390        400        410        420 
FQQNSLNWMK KLSPRTIHLT MPQLVLQGSY DLQDLLAQAE LPAILHTELN LQKLSNDRIR 

       430        440        450        460        470        480 
VGEVLNSIFF ELEADEREPT ESTQQLNKPE VLEVTLNRPF LFAVYDQSAT ALHFLGRVAN 


PLSTA 

P01019 in FASTA format

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