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Thyroxine-binding globulin (Serpin A7) (T4-binding globulin)

 THBG_HUMAN              Reviewed;         415 AA.
P05543; D3DUX1;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
18-JUL-2018, entry version 192.
RecName: Full=Thyroxine-binding globulin;
AltName: Full=Serpin A7;
AltName: Full=T4-binding globulin;
Flags: Precursor;
Name=SERPINA7; Synonyms=TBG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=3094014; DOI=10.1073/pnas.83.20.7708;
Flink I.L., Bayley T.J., Gustafson T.A., Markham B.E., Morkin E.;
"Complete amino acid sequence of human thyroxine-binding globulin
deduced from cloned DNA: close homology to the serine antiproteases.";
Proc. Natl. Acad. Sci. U.S.A. 83:7708-7712(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8268226; DOI=10.1016/0167-4781(93)90013-4;
Akbari M.T., Kapadi A., Farmer M.J., Fitch N.J.S., McCann K.P.,
Kordestani S., Flink I.L., Sheppard M.C., Ramsden D.B.;
"The structure of the human thyroxine binding globulin (TBG) gene.";
Biochim. Biophys. Acta 1216:446-454(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8232304; DOI=10.1210/mend.7.8.8232304;
Hayashi Y., Mori Y., Janssen O.E., Sunthornthepvarakul T., Weiss R.E.,
Takeda K., Weinberg M., Seo H., Bell G.I., Refetoff S.;
"Human thyroxine-binding globulin gene: complete sequence and
transcriptional regulation.";
Mol. Endocrinol. 7:1049-1060(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[7]
PROTEIN SEQUENCE OF 21-40.
PubMed=414747; DOI=10.1016/0006-291X(77)91135-4;
Cheng S.-Y.;
"Partial amino acid sequence of human thyroxine-binding globulin.
Further evidence for a single polypeptide chain.";
Biochem. Biophys. Res. Commun. 79:1212-1218(1977).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-36 AND ASN-165.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
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).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-36, AND STRUCTURE OF
CARBOHYDRATES.
TISSUE=Cerebrospinal fluid;
PubMed=19838169; DOI=10.1038/nmeth.1392;
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,
Brinkmalm G., Larson G.;
"Enrichment of glycopeptides for glycan structure and attachment site
identification.";
Nat. Methods 6:809-811(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 39-415 IN COMPLEX WITH
THYROXINE.
PubMed=16938877; DOI=10.1073/pnas.0604080103;
Zhou A., Wei Z., Read R.J., Carrell R.W.;
"Structural mechanism for the carriage and release of thyroxine in the
blood.";
Proc. Natl. Acad. Sci. U.S.A. 103:13321-13326(2006).
[12]
REVIEW ON VARIANTS.
PubMed=18407078; DOI=10.1016/1043-2760(92)90043-Z;
Janssen O.E., Bertenshaw R., Takeda K., Weiss R., Refetoff S.;
"Molecular basis of inherited thyroxine-binding globulin defects.";
Trends Endocrinol. Metab. 3:49-53(1992).
[13]
POLYMORPHISM, AND VARIANT PRO-247.
PubMed=2155256; DOI=10.1210/jcem-70-3-804;
Mori Y., Takeda K., Charbonneau M., Refetoff S.;
"Replacement of Leu227 by Pro in thyroxine-binding globulin (TBG) is
associated with complete TBG deficiency in three of eight families
with this inherited defect.";
J. Clin. Endocrinol. Metab. 70:804-809(1990).
[14]
POLYMORPHISM, AND VARIANT ASN-116.
PubMed=2501669; DOI=10.1210/mend-3-3-575;
Mori Y., Seino S., Takeda K., Flink I.L., Murata Y., Bell G.I.,
Refetoff S.;
"A mutation causing reduced biological activity and stability of
thyroxine-binding globulin probably as a result of abnormal
glycosylation of the molecule.";
Mol. Endocrinol. 3:575-579(1989).
[15]
POLYMORPHISM, AND VARIANT LEU-383.
PubMed=1294376; DOI=10.1507/endocrj1954.39.577;
Shirotani T., Kishikawa H., Wake N., Miyamura N., Hashimoto Y.,
Motoyoshi S., Yamaguchi K., Shichiri M.;
"Thyroxine-binding globulin variant (TBG-Kumamoto): identification of
a point mutation and genotype analysis of its family.";
Endocrinol. Jpn. 39:577-584(1992).
[16]
POLYMORPHISM, AND VARIANT PRO-133.
PubMed=1906047; DOI=10.1007/BF00204164;
Janssen O.E., Takeda K., Refetoff S.;
"Sequence of the variant thyroxine-binding globulin (TBG) in a
Montreal family with partial TBG deficiency.";
Hum. Genet. 87:119-122(1991).
[17]
POLYMORPHISM, AND VARIANT TYR-351.
PubMed=1901689;
Bertenshaw R., Takeda K., Refetoff S.;
"Sequencing of the variant thyroxine-binding globulin (TBG)-Quebec
reveals two nucleotide substitutions.";
Am. J. Hum. Genet. 48:741-744(1991).
[18]
POLYMORPHISM, AND VARIANTS THR-43 AND PHE-303.
PubMed=1515456; DOI=10.1016/0925-4439(92)90105-V;
Bertenshaw R., Sarne D., Tornari J., Weinberg M., Refetoff S.;
"Sequencing of the variant thyroxine-binding globulin (TBG)-San Diego
reveals two nucleotide substitutions.";
Biochim. Biophys. Acta 1139:307-310(1992).
[19]
VARIANT TBG-A THR-211.
PubMed=2495303; DOI=10.1172/JCI114021;
Takeda K., Mori Y., Sobieszczyk S., Seo H., Dick M., Watson F.,
Flink I.L., Seino S., Bell G.I., Refetoff S.;
"Sequence of the variant thyroxine-binding globulin of Australian
aborigines. Only one of two amino acid replacements is responsible for
its altered properties.";
J. Clin. Invest. 83:1344-1348(1989).
[20]
VARIANT TBG-S ASN-191.
PubMed=2115061; DOI=10.1007/BF03349576;
Waltz M.R., Pullman T.N., Takeda K., Sobieszczyk P., Refetoff S.;
"Molecular basis for the properties of the thyroxine-binding globulin-
slow variant in American blacks.";
J. Endocrinol. Invest. 13:343-349(1990).
-!- FUNCTION: Major thyroid hormone transport protein in serum.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma.
-!- POLYMORPHISM: Genetic variants in SERPINA7 influence the serum
levels of thyroxine-binding globulin and define the thyroxine-
binding globulin quantitaive trait locus (TBGQTL) [MIM:300932].
Individuals with low or high serum levels of thyroxine-binding
globulin show, respectively, reduced or elevated protein-bound
iodine but are euthyroid and do not manifest major metabolic
alterations (PubMed:1294376, PubMed:1515456, PubMed:1901689,
PubMed:1906047, PubMed:2155256, PubMed:2501669). Two qualitative
TBG variants occur in particular populations. TBG-A is found in
40% of Australian aborigines, it has reduced affinity for
thyroxine and triiodothyroxine and increased susceptibility to
inactivation by heat or acid (PubMed:2495303). TBG-S ('s' for slow
shift on isoelectic focusing) is found in blacks, Eskimos,
Melanesians, Polynesians and Indonesians, but not in Caucasians;
TBG-S is slightly more thermolabile (PubMed:2115061).
{ECO:0000269|PubMed:1294376, ECO:0000269|PubMed:1515456,
ECO:0000269|PubMed:1901689, ECO:0000269|PubMed:1906047,
ECO:0000269|PubMed:2115061, ECO:0000269|PubMed:2155256,
ECO:0000269|PubMed:2495303, ECO:0000269|PubMed:2501669}.
-!- SIMILARITY: Belongs to the serpin family. {ECO:0000305}.
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EMBL; M14091; AAA60616.1; -; mRNA.
EMBL; X64171; CAA45509.1; -; Genomic_DNA.
EMBL; L13470; AAA16067.1; -; Genomic_DNA.
EMBL; Z83850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471120; EAX02747.1; -; Genomic_DNA.
EMBL; CH471120; EAX02748.1; -; Genomic_DNA.
EMBL; BC020747; AAH20747.1; -; mRNA.
CCDS; CCDS14518.1; -.
PIR; A47224; A47224.
RefSeq; NP_000345.2; NM_000354.5.
UniGene; Hs.76838; -.
PDB; 2CEO; X-ray; 2.80 A; A/B=39-415.
PDB; 2RIV; X-ray; 1.50 A; A=33-386, B=376-415.
PDB; 2RIW; X-ray; 2.04 A; A=39-386, B=376-415.
PDB; 2XN3; X-ray; 2.09 A; A=33-386, B=377-415.
PDB; 2XN5; X-ray; 1.70 A; A=32-380, B=381-415.
PDB; 2XN6; X-ray; 1.29 A; A=32-380, B=381-415.
PDB; 2XN7; X-ray; 1.43 A; A=32-380, B=381-415.
PDB; 4X30; X-ray; 1.55 A; A=21-415.
PDB; 4YIA; X-ray; 1.58 A; A=1-386, B=382-415.
PDBsum; 2CEO; -.
PDBsum; 2RIV; -.
PDBsum; 2RIW; -.
PDBsum; 2XN3; -.
PDBsum; 2XN5; -.
PDBsum; 2XN6; -.
PDBsum; 2XN7; -.
PDBsum; 4X30; -.
PDBsum; 4YIA; -.
ProteinModelPortal; P05543; -.
SMR; P05543; -.
BioGrid; 112769; 5.
IntAct; P05543; 1.
STRING; 9606.ENSP00000329374; -.
ChEMBL; CHEMBL3843; -.
DrugBank; DB00451; Levothyroxine.
DrugBank; DB00279; Liothyronine.
DrugBank; DB01583; Liotrix.
DrugBank; DB05235; NRP409.
MEROPS; I04.955; -.
GlyConnect; 750; -.
iPTMnet; P05543; -.
PhosphoSitePlus; P05543; -.
BioMuta; SERPINA7; -.
DMDM; 1351236; -.
EPD; P05543; -.
MaxQB; P05543; -.
PaxDb; P05543; -.
PeptideAtlas; P05543; -.
PRIDE; P05543; -.
ProteomicsDB; 51845; -.
DNASU; 6906; -.
Ensembl; ENST00000327674; ENSP00000329374; ENSG00000123561.
Ensembl; ENST00000372563; ENSP00000361644; ENSG00000123561.
GeneID; 6906; -.
KEGG; hsa:6906; -.
UCSC; uc004eme.3; human.
CTD; 6906; -.
DisGeNET; 6906; -.
EuPathDB; HostDB:ENSG00000123561.14; -.
GeneCards; SERPINA7; -.
HGNC; HGNC:11583; SERPINA7.
HPA; HPA002803; -.
MalaCards; SERPINA7; -.
MIM; 300932; phenotype.
MIM; 314200; gene.
neXtProt; NX_P05543; -.
OpenTargets; ENSG00000123561; -.
Orphanet; 209893; Congenital isolated thyroxine-binding globulin deficiency.
PharmGKB; PA36347; -.
eggNOG; KOG2392; Eukaryota.
eggNOG; COG4826; LUCA.
GeneTree; ENSGT00760000118839; -.
HOGENOM; HOG000238521; -.
HOVERGEN; HBG005957; -.
InParanoid; P05543; -.
KO; K20734; -.
OMA; CSLNFPK; -.
OrthoDB; EOG091G0ION; -.
PhylomeDB; P05543; -.
TreeFam; TF343201; -.
EvolutionaryTrace; P05543; -.
GenomeRNAi; 6906; -.
PRO; PR:P05543; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000123561; -.
CleanEx; HS_SERPINA7; -.
Genevisible; P05543; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0070327; P:thyroid hormone transport; IMP:UniProtKB.
InterPro; IPR023795; Serpin_CS.
InterPro; IPR023796; Serpin_dom.
InterPro; IPR000215; Serpin_fam.
InterPro; IPR036186; Serpin_sf.
PANTHER; PTHR11461; PTHR11461; 1.
Pfam; PF00079; Serpin; 1.
SMART; SM00093; SERPIN; 1.
SUPFAM; SSF56574; SSF56574; 1.
PROSITE; PS00284; SERPIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Glycoprotein; Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000269|PubMed:414747}.
CHAIN 21 415 Thyroxine-binding globulin.
/FTId=PRO_0000032436.
BINDING 293 293 Thyroxine. {ECO:0000269|PubMed:16938877}.
BINDING 398 398 Thyroxine. {ECO:0000269|PubMed:16938877}.
CARBOHYD 36 36 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19838169}.
CARBOHYD 99 99 N-linked (GlcNAc...) asparagine.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine; in
variant Gary. {ECO:0000305}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 253 253 N-linked (GlcNAc...) asparagine.
VARIANT 43 43 S -> T (polymorphism; associated with F-
303 in San Diego; partial thyroxine-
binding globulin deficiency;
dbSNP:rs72554662).
{ECO:0000269|PubMed:1515456}.
/FTId=VAR_007102.
VARIANT 116 116 I -> N (polymorphism; Gary; severe
thyroxine-binding globulin deficiency;
dbSNP:rs28933689).
{ECO:0000269|PubMed:2501669}.
/FTId=VAR_007103.
VARIANT 133 133 A -> P (polymorphism; Montreal/TBG-M;
partial thyroxine-binding globulin
deficiency; dbSNP:rs28933688).
{ECO:0000269|PubMed:1906047}.
/FTId=VAR_007104.
VARIANT 191 191 D -> N (polymorphism; TBG-S/Slow;
dbSNP:rs1050086).
{ECO:0000269|PubMed:2115061}.
/FTId=VAR_007105.
VARIANT 211 211 A -> T (polymorphism; TBG-A/Aborigine;
dbSNP:rs2234036).
{ECO:0000269|PubMed:2495303}.
/FTId=VAR_007106.
VARIANT 247 247 L -> P (polymorphism; CD5; complete
thyroxine-binding globulin deficiency;
dbSNP:rs28937312).
{ECO:0000269|PubMed:2155256}.
/FTId=VAR_007107.
VARIANT 303 303 L -> F (common polymorphism; associated
with T-43 in San Diego; dbSNP:rs1804495).
{ECO:0000269|PubMed:1515456}.
/FTId=VAR_007108.
VARIANT 351 351 H -> Y (polymorphism; Quebec; partial
thyroxine-binding globulin deficiency;
dbSNP:rs72554659).
{ECO:0000269|PubMed:1901689}.
/FTId=VAR_007109.
VARIANT 383 383 P -> L (polymorphism; Kumamoto; partial
thyroxine-binding globulin deficiency;
dbSNP:rs72554658).
{ECO:0000269|PubMed:1294376}.
/FTId=VAR_007110.
CONFLICT 30 31 CH -> DS (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 38 38 T -> S (in Ref. 7; AA sequence).
{ECO:0000305}.
CONFLICT 197 197 I -> T (in Ref. 1; AAA60616).
{ECO:0000305}.
HELIX 40 60 {ECO:0000244|PDB:2XN6}.
STRAND 66 68 {ECO:0000244|PDB:2XN6}.
HELIX 70 82 {ECO:0000244|PDB:2XN6}.
HELIX 86 95 {ECO:0000244|PDB:2XN6}.
TURN 100 102 {ECO:0000244|PDB:2XN6}.
HELIX 105 120 {ECO:0000244|PDB:2XN6}.
STRAND 126 137 {ECO:0000244|PDB:2XN6}.
HELIX 144 153 {ECO:0000244|PDB:2XN6}.
STRAND 156 161 {ECO:0000244|PDB:2XN6}.
HELIX 166 180 {ECO:0000244|PDB:2XN6}.
TURN 181 183 {ECO:0000244|PDB:2XN6}.
STRAND 198 212 {ECO:0000244|PDB:2XN6}.
HELIX 216 218 {ECO:0000244|PDB:2XN6}.
STRAND 220 228 {ECO:0000244|PDB:2XN6}.
STRAND 231 249 {ECO:0000244|PDB:2XN6}.
TURN 250 253 {ECO:0000244|PDB:2XN6}.
STRAND 254 272 {ECO:0000244|PDB:2XN6}.
HELIX 277 283 {ECO:0000244|PDB:2XN6}.
HELIX 286 295 {ECO:0000244|PDB:2XN6}.
STRAND 297 306 {ECO:0000244|PDB:2XN6}.
STRAND 308 315 {ECO:0000244|PDB:2XN6}.
HELIX 317 323 {ECO:0000244|PDB:2XN6}.
HELIX 327 329 {ECO:0000244|PDB:2XN6}.
TURN 336 338 {ECO:0000244|PDB:2XN6}.
STRAND 339 342 {ECO:0000244|PDB:4X30}.
STRAND 344 357 {ECO:0000244|PDB:2XN6}.
STRAND 359 374 {ECO:0000244|PDB:2XN6}.
STRAND 384 386 {ECO:0000244|PDB:2XN6}.
STRAND 391 397 {ECO:0000244|PDB:2XN6}.
TURN 398 401 {ECO:0000244|PDB:2XN6}.
STRAND 402 410 {ECO:0000244|PDB:2XN6}.
SEQUENCE 415 AA; 46325 MW; 8B24EF8C7CEF8F0A CRC64;
MSPFLYLVLL VLGLHATIHC ASPEGKVTAC HSSQPNATLY KMSSINADFA FNLYRRFTVE
TPDKNIFFSP VSISAALVML SFGACCSTQT EIVETLGFNL TDTPMVEIQH GFQHLICSLN
FPKKELELQI GNALFIGKHL KPLAKFLNDV KTLYETEVFS TDFSNISAAK QEINSHVEMQ
TKGKVVGLIQ DLKPNTIMVL VNYIHFKAQW ANPFDPSKTE DSSSFLIDKT TTVQVPMMHQ
MEQYYHLVDM ELNCTVLQMD YSKNALALFV LPKEGQMESV EAAMSSKTLK KWNRLLQKGW
VDLFVPKFSI SATYDLGATL LKMGIQHAYS ENADFSGLTE DNGLKLSNAA HKAVLHIGEK
GTEAAAVPEV ELSDQPENTF LHPIIQIDRS FMLLILERST RSILFLGKVV NPTEA


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