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UniProtKB/Swiss-Prot entry P01011

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

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Entry information
Entry name AACT_HUMAN
Primary accession number P01011
Secondary accession numbers Q13703 Q2TU87 Q2TU88 Q59GP9 Q6LBY8 Q6LDT7 Q6NSC9 Q8N177 Q96DW8 Q9UC47 Q9UNU9
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on August 1, 1991 (Sequence version 2)
Annotations were last modified on    September 23, 2008 (Entry version 122)
Name and origin of the protein
Protein name Alpha-1-antichymotrypsin [Precursor]
Synonyms ACT
Cell growth-inhibiting gene 24/25 protein
Contains Alpha-1-antichymotrypsin His-Pro-less
Gene name
Name: SERPINA3
Synonyms: AACT
ORFNames: GIG24, GIG25
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] (ISOFORM 1).
TISSUE=Liver;
DOI=10.1021/bi00291a001; PubMed=6606438 [NCBI, ExPASy, EBI, Israel, Japan]
Chandra T., Stackhouse R., Kidd V.J., Robson K.J.H., Woo S.L.C.;
"Sequence homology between human alpha 1-antichymotrypsin, alpha 1-antitrypsin, and antithrombin III.";
Biochemistry 22:5055-5061(1983).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN COPD, AND VARIANTS BOCHUM-1 PRO-78 AND BONN-1 ALA-252.
DOI=10.1006/geno.1993.1396; PubMed=8244391 [NCBI, ExPASy, EBI, Israel, Japan]
Poller W., Faber J.-P., Weidinger S., Tief K., Scholz S., Fischer M., Olek K., Kirchgesser M., Heidtmann H.-H.;
"A leucine-to-proline substitution causes a defective alpha 1-antichymotrypsin allele associated with familial obstructive lung disease.";
Genomics 17:740-743(1993).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-9.
Kim J.W.;
"Identification of a human cell growth inhibiting gene.";
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-9.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS THR-9 AND ARG-267.
TISSUE=Brain, Liver, and Skin;
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).
[6]
 NUCLEOTIDE SEQUENCE [MRNA] OF 1-46, AND TISSUE SPECIFICITY.
TISSUE=Liver;
DOI=10.1016/0092-8674(88)90462-X; PubMed=3257719 [NCBI, ExPASy, EBI, Israel, Japan]
Abraham C.R., Selkoe D.J., Potter H.;
"Immunochemical identification of the serine protease inhibitor alpha 1-antichymotrypsin in the brain amyloid deposits of Alzheimer's disease.";
Cell 52:487-501(1988).
[7]
 NUCLEOTIDE SEQUENCE [MRNA] OF 17-423 (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Hippocampus;
DOI=10.1074/jbc.274.3.1821; PubMed=9880565 [NCBI, ExPASy, EBI, Israel, Japan]
Hwang S.-R., Steineckert B., Kohn A., Palkovits M., Hook V.Y.H.;
"Molecular studies define the primary structure of alpha1-antichymotrypsin (ACT) protease inhibitor in Alzheimer's disease brains. Comparison of act in hippocampus and liver.";
J. Biol. Chem. 274:1821-1827(1999).
[8]
 NUCLEOTIDE SEQUENCE [MRNA] OF 22-86 AND 130-423 (ISOFORM 1).
Rubin H.;
Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases.
[9]
 PROTEIN SEQUENCE OF 24-34.
DOI=10.1016/0167-4838(89)90139-8; PubMed=2787670 [NCBI, ExPASy, EBI, Israel, Japan]
Lindmark B., Hilja H., Alan R., Eriksson S.;
"The microheterogeneity of desialylated alpha 1-antichymotrypsin: the occurrence of two amino-terminal isoforms, one lacking a His-Pro dipeptide.";
Biochim. Biophys. Acta 997:90-95(1989).
[10]
 NUCLEOTIDE SEQUENCE [MRNA] OF 36-45.
PubMed=7521171 [NCBI, ExPASy, EBI, Israel, Japan]
Korzus E., Luisetti M., Travis J.;
"Interactions of alpha-1-antichymotrypsin, alpha-1-proteinase inhibitor, and alpha-2-macroglobulin with the fungal enzyme, seaprose.";
Biol. Chem. Hoppe-Seyler 375:335-341(1994).
[11]
 PROTEIN SEQUENCE OF 41-60.
DOI=10.1016/0006-291X(83)90325-X; PubMed=6687683 [NCBI, ExPASy, EBI, Israel, Japan]
Morii M., Travis J.;
"Structural alterations in alpha 1-antichymotrypsin from normal and acute phase human plasma.";
Biochem. Biophys. Res. Commun. 111:438-443(1983).
[12]
 PROTEIN SEQUENCE OF 48-68 (ISOFORMS 1/2).
DOI=10.1002/(SICI)1097-0215(19960529)66:5<636::AID-IJC10>3.0.CO;2-2; PubMed=8647626 [NCBI, ExPASy, EBI, Israel, Japan]
Pinczower G.D., Williams R.P.W., Gianello R.D., Robinson H.C., Preston B.N., Linnane A.W.;
"Characterisation of the tumour-associated carbohydrate epitope recognised by monoclonal antibody 4D3.";
Int. J. Cancer 66:636-644(1996).
[13]
 NUCLEOTIDE SEQUENCE [MRNA] OF 87-129 (ISOFORMS 1/2), AND FUNCTION.
TISSUE=Liver;
PubMed=2404007 [NCBI, ExPASy, EBI, Israel, Japan]
Rubin H., Wang Z., Nickbarg E.B., McLarney S., Naidoo N., Schoenberger O.L., Johnson J.L., Cooperman B.S.;
"Cloning, expression, purification, and biological activity of recombinant native and variant human alpha 1-antichymotrypsins.";
J. Biol. Chem. 265:1199-1207(1990).
[14]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 205-423.
DOI=10.1038/311175a0; PubMed=6547997 [NCBI, ExPASy, EBI, Israel, Japan]
Hill R.E., Shaw P.H., Boyd P.A., Baumann H., Hastie N.D.;
"Plasma protease inhibitors in mouse and man: divergence within the reactive centre regions.";
Nature 311:175-177(1984).
[15]
 ACTIVE SITE.
PubMed=6556193 [NCBI, ExPASy, EBI, Israel, Japan]
Morii M., Travis J.;
"Amino acid sequence at the reactive site of human alpha 1-antichymotrypsin.";
J. Biol. Chem. 258:12749-12752(1983).
[16]
 GLYCOSYLATION AT ASN-93 AND ASN-106.
DOI=10.1038/nbt827; PubMed=12754519 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[17]
 INTERACTION WITH DNAJC1.
DOI=10.1074/jbc.M310903200; PubMed=14668352 [NCBI, ExPASy, EBI, Israel, Japan]
Kroczynska B., Evangelista C.M., Samant S.S., Elguindi E.C., Blond S.Y.;
"The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity.";
J. Biol. Chem. 279:11432-11443(2004).
[18]
 REGION RCL.
DOI=10.1007/s00239-004-2640-9; PubMed=15638460 [NCBI, ExPASy, EBI, Israel, Japan]
Horvath A.J., Forsyth S.L., Coughlin P.B.;
"Expression patterns of murine antichymotrypsin-like genes reflect evolutionary divergence at the Serpina3 locus.";
J. Mol. Evol. 59:488-497(2004).
[19]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-93, AND MASS SPECTROMETRY.
TISSUE=Plasma;
DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan]
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.";
Proteomics 4:454-465(2004).
[20]
 GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-33; ASN-93; ASN-106; ASN-127; ASN-186 AND ASN-271, 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).
[21]
 X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 24-423.
DOI=10.1016/0022-2836(91)90704-A; PubMed=2016749 [NCBI, ExPASy, EBI, Israel, Japan]
Baumann U., Huber R., Bode W., Grosse D., Lesjak M., Laurell C.-B.;
"Crystal structure of cleaved human alpha 1-antichymotrypsin at 2.7-A resolution and its comparison with other serpins.";
J. Mol. Biol. 218:595-606(1991).
[22]
 X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370 AND ARG-372.
DOI=10.1038/nsb1096-888; PubMed=8836107 [NCBI, ExPASy, EBI, Israel, Japan]
Lukacs C.M., Zhong J.Q., Plotnick M.I., Rubin H., Cooperman B.S., Christianson D.W.;
"Arginine substitutions in the hinge region of antichymotrypsin affect serpin beta-sheet rearrangement.";
Nat. Struct. Biol. 3:888-893(1996).
[23]
 X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 43-423 OF MUTANTS ARG-370; ARG-372 AND ARG-374.
DOI=10.1021/bi972359e; PubMed=9521649 [NCBI, ExPASy, EBI, Israel, Japan]
Lukacs C.M., Rubin H., Christianson D.W.;
"Engineering an anion-binding cavity in antichymotrypsin modulates the 'spring-loaded' serpin-protease interaction.";
Biochemistry 37:3297-3304(1998).
[24]
 X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 26-423.
DOI=10.1073/pnas.97.1.67; PubMed=10618372 [NCBI, ExPASy, EBI, Israel, Japan]
Gooptu B., Hazes B., Chang W.-S.W., Dafforn T.R., Carrell R.W., Read R.J., Lomas D.A.;
"Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease.";
Proc. Natl. Acad. Sci. U.S.A. 97:67-72(2000).
[25]
 VARIANT ISEHARA-1 VAL-401.
DOI=10.1016/0014-5793(92)80590-D; PubMed=1618300 [NCBI, ExPASy, EBI, Israel, Japan]
Tsuda M., Sei Y., Yamamura M., Yamamoto M., Shinohara Y.;
"Detection of a new mutant alpha-1-antichymotrypsin in patients with occlusive-cerebrovascular disease.";
FEBS Lett. 304:66-68(1992).
[26]
 VARIANT BONN-1 ALA-252.
DOI=10.1016/0140-6736(92)91301-N; PubMed=1351206 [NCBI, ExPASy, EBI, Israel, Japan]
Poller W., Faber J.-P., Scholz S., Weindinger S., Bartholome K., Olek K., Eriksson S.;
"Mis-sense mutation of alpha 1-antichymotrypsin gene associated with chronic lung disease.";
Lancet 339:1538-1538(1992).
[27]
 VARIANT VAL-401.
DOI=10.1007/s100380170125; PubMed=11289720 [NCBI, ExPASy, EBI, Israel, Japan]
Tachikawa H., Tsuda M., Onoe K., Ueno M., Takagi S., Shinohara Y.;
"Alpha-1-antichymotrypsin gene A1252G variant (ACT Isehara-1) is associated with a lacunar type of ischemic cerebrovascular disease.";
J. Hum. Genet. 46:45-47(2001).
Comments
  • FUNCTION: Although its physiological function is unclear, it can inhibit neutrophil cathepsin G and mast cell chymase, both of which can convert angiotensin-1 to the active angiotensin-2.
  • SUBUNIT: Interacts with DNAJC1.
  • SUBCELLULAR LOCATION: Secreted.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDP01011-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDP01011-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_014227, VSP_014228.
    Name3
    Isoform IDP01011-3
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_014225, VSP_014226.
  • TISSUE SPECIFICITY: Plasma. Synthesized in the liver. Like the related alpha-1-antitrypsin, its concentration increases in the acute phase of inflammation or infection. Found in the myloid plaques from the hippocampus of Alzheimer's disease brains.
  • DOMAIN: The reactive center loop (RCL) extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.
  • DISEASE: Defects in SERPINA3 may be a cause of chronic obstructive pulmonary disease (COPD) [MIM:107280].
  • MISCELLANEOUS: Alpha-1-antichymotrypsin can bind DNA.
  • SIMILARITY: Belongs to the serpin family.
  • CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
  • SEQUENCE CAUTION:
    • Sequence=AAA51543.1; Type=Frameshift; Positions=101, 106, 111, 117, 123, 129, 421;
    • Sequence=AAT08029.1; Type=Erroneous initiation; Note=Translation N-terminally shortened
    • Sequence=AAT08029.1; Type=Frameshift; Positions=4;
  • WEB RESOURCE: Name=Wikipedia; Note=Alpha-1 antichymotrypsin entry; URL="http://en.wikipedia.org/wiki/Alpha_1-antichymotrypsin";.
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
K01500; AAA51543.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68733; CAA48671.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68734; CAA48671.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68735; CAA48671.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68736; CAA48671.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X68737; CAA48671.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY513275; AAT08028.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY513276; AAT08029.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209060; BAD92297.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003559; AAH03559.3; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010530; AAH10530.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC013189; AAH13189.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC034554; AAH34554.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC070265; AAH70265.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M18906; AAA51559.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF089747; AAD08810.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J05176; AAA51560.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00947; CAA25459.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A90475; ITHUC.
S62374; S62374.
RefSeq NP_001076.2; -.
UniGene Hs.534293
3D structure databases
PDB
1AS4; X-ray; 2.10 A; A=43-383, B=387-423.[ExPASy / RCSB / EBI]
1QMN; X-ray; 2.27 A; A=26-423.[ExPASy / RCSB / EBI]
2ACH; X-ray; 2.70 A; A=24-383, B=384-423.[ExPASy / RCSB / EBI]
3CAA; X-ray; 2.40 A; A=43-383, B=387-423.[ExPASy / RCSB / EBI]
4CAA; X-ray; 2.90 A; A=43-383, B=387-423.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AS4; -.
1QMN; -.
2ACH; -.
3CAA; -.
4CAA; -.
ModBase P01011.
Protein family/group databases
MEROPS I04.002; -.
PTM databases
GlycoSuiteDB P01011; -.
PhosphoSite P01011; -.
2D gel databases
SWISS-2DPAGE P01011; -.
DOSAC-COBS-2DPAGE P01011; -.
Siena-2DPAGE P01011; -.
Organism-specific databases
H-InvDB HIX0011931; -.
HIX0079611; -.
HGNC HGNC:16; SERPINA3.
GenAtlas SERPINA3.
HPA CAB016647; -.
HPA002560; -.
MIM 107280; gene. [NCBI / EBI]
PharmGKB PA35020; -.
GeneCards P01011.
Gene expression databases
ArrayExpress P01011; -.
GermOnline ENSG00000196136; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0005634; Cellular component: nucleus (traceable author statement from UniProtKB).
GO:0030569; Molecular function: chymotrypsin inhibitor activity (non-traceable author statement from UniProtKB).
GO:0003677; Molecular function: DNA binding (traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0006954; Biological process: inflammatory response (non-traceable author statement from UniProtKB).
GO:0019216; Biological process: regulation of lipid metabolic process (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro 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.
SMART SM00093; SERPIN; 1.
SMART graphical view of domain structure.
PROSITE PS00284; SERPIN; 1.
BLOCKS P01011.
Genome annotation databases
Ensembl ENSG00000196136; Homo sapiens. [Contig view]
GeneID 12; -.
KEGG hsa:12; -.
Phylogenomic databases
HOVERGEN P01011; -.
Other
LinkHub P01011; -.
SOURCE SERPINA3; Homo sapiens.
ProtoNet P01011.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acute phase; Alternative splicing; Direct protein sequencing; Disease mutation; Glycoprotein; Polymorphism; Protease inhibitor; Secreted; Serine protease inhibitor; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    23  23      
CHAIN   24   423  400     Alpha-1-antichymotrypsin. PRO_0000032411
CHAIN   26   423  398     Alpha-1-antichymotrypsin His-Pro-less. PRO_0000032412
DNA_BIND   235   237  3      
REGION   369   394  26     RCL. 
SITE   383   384  2     Reactive bond. 
CARBOHYD   33    33        N-linked (GlcNAc...). 
CARBOHYD   93    93        N-linked (GlcNAc...). 
CARBOHYD   106   106        N-linked (GlcNAc...). 
CARBOHYD   127   127        N-linked (GlcNAc...). 
CARBOHYD   186   186        N-linked (GlcNAc...). 
CARBOHYD   271   271        N-linked (GlcNAc...). 
VAR_SEQ   64    95        LVLKAPDKNVIFSPLSISTALAFLSLGAHNTT -> SPRWSIRLCLMYLRRAQKHLLPQQSKSPSFLH (in isoform 3). VSP_014225
VAR_SEQ   96   423        Missing (in isoform 3). VSP_014226
VAR_SEQ   215   216        AK -> ER (in isoform 2). VSP_014227
VAR_SEQ   217   423        Missing (in isoform 2). VSP_014228
VARIANT   9     9  1     A -> T (in dbSNP:rs4934 [NCBI]). VAR_006973 
VARIANT   78    78  1     L -> P (in COPD; Bochum-1; dbSNP:rs1800463 [NCBI]). VAR_006974 
VARIANT   167   167  1     A -> G. VAR_006975 
VARIANT   252   252  1     P -> A (in COPD; Bonn-1; dbSNP:rs17473 [NCBI]). VAR_006976 
VARIANT   267   267  1     K -> R (in dbSNP:rs17853314 [NCBI]). VAR_037902 
VARIANT   401   401  1     M -> V (associated with occlusive-cerebrovascular disease; Isehara-1). VAR_006977 [3D]
VARIANT   407   407  1     D -> G (in dbSNP:rs10956 [NCBI]). VAR_011742 [3D]
CONFLICT   55    55        D -> S (in Ref. 11; AA sequence). 
CONFLICT   69    69        P -> L (in Ref. 1; AAA51543). 
CONFLICT   101   101        K -> R (in Ref. 4; BAD92297). 
CONFLICT   106   106        N -> Y (in Ref. 3; AAT08028). 
CONFLICT   198   198        D -> N (in Ref. 3; AAT08029). 
CONFLICT   199   199        L -> P (in Ref. 1; AAA51543). 
CONFLICT   234   234        S -> N (in Ref. 3; AAT08029). 
CONFLICT   339   339        S -> G (in Ref. 3; AAT08028). 
CONFLICT   346   346        I -> S (in Ref. 3; AAT08028). 
CONFLICT   361   363        AVL -> VVS (in Ref. 1; AAA51543). 
HELIX   49    67  19      
STRAND   73    75  3      
HELIX   77    88  12      
HELIX   93   102  10      
TURN   107   109  3      
HELIX   112   126  15      
STRAND   134   144  11      
HELIX   151   161  11      
STRAND   164   168  5      
HELIX   173   187  15      
TURN   188   190  3      
STRAND   203   219  17      
HELIX   223   225  3      
STRAND   227   234  8      
STRAND   237   256  20      
TURN   257   260  4      
STRAND   261   279  19      
HELIX   284   289  6      
HELIX   293   302  10      
STRAND   304   314  11      
STRAND   316   323  8      
HELIX   325   330  6      
HELIX   335   337  3      
HELIX   344   347  4      
STRAND   348   350  3      
STRAND   352   365  14      
STRAND   367   382  16      
STRAND   391   394  4      
STRAND   399   405  7      
STRAND   412   418  7      
Sequence information
Length: 423 AA [This is the length of the unprocessed precursor] Molecular weight: 47651 Da [This is the MW of the unprocessed precursor] CRC64: B002F946C86A8951 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MERMLPLLAL GLLAAGFCPA VLCHPNSPLD EENLTQENQD RGTHVDLGLA SANVDFAFSL 

        70         80         90        100        110        120 
YKQLVLKAPD KNVIFSPLSI STALAFLSLG AHNTTLTEIL KGLKFNLTET SEAEIHQSFQ 

       130        140        150        160        170        180 
HLLRTLNQSS DELQLSMGNA MFVKEQLSLL DRFTEDAKRL YGSEAFATDF QDSAAAKKLI 

       190        200        210        220        230        240 
NDYVKNGTRG KITDLIKDLD SQTMMVLVNY IFFKAKWEMP FDPQDTH