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Serine protease HTRA1 (EC 3.4.21.-) (High-temperature requirement A serine peptidase 1) (L56) (Serine protease 11)

 HTRA1_HUMAN             Reviewed;         480 AA.
Q92743; D3DRE4; Q9UNS5;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
27-SEP-2017, entry version 165.
RecName: Full=Serine protease HTRA1;
EC=3.4.21.-;
AltName: Full=High-temperature requirement A serine peptidase 1;
AltName: Full=L56;
AltName: Full=Serine protease 11;
Flags: Precursor;
Name=HTRA1; Synonyms=HTRA, PRSS11;
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=Placenta;
PubMed=8977104; DOI=10.1016/S0014-5793(96)01229-X;
Zumbrunn J., Trueb B.;
"Primary structure of a putative serine protease specific for IGF-
binding proteins.";
FEBS Lett. 398:187-192(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Crowl R.M., Luk D., Milnamow M.;
"Genomic organization and promoter characterization of the human HTRA
(PRSS11) gene.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 144-480, PROTEIN SEQUENCE OF 33-44,
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
SER-328.
TISSUE=Cartilage;
PubMed=9852107; DOI=10.1074/jbc.273.51.34406;
Hu S.I., Carozza M., Klein M., Nantermet P., Luk D., Crowl R.M.;
"Human HtrA, an evolutionarily conserved serine protease identified as
a differentially expressed gene product in osteoarthritic cartilage.";
J. Biol. Chem. 273:34406-34412(1998).
[5]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=15208355; DOI=10.1369/jhc.3A6186.2004;
De Luca A., De Falco M., Fedele V., Cobellis L., Mastrogiacomo A.,
Laforgia V., Tuduce I.L., Campioni M., Giraldi D., Paggi M.G.,
Baldi A.;
"The serine protease HtrA1 is upregulated in the human placenta during
pregnancy.";
J. Histochem. Cytochem. 52:885-892(2004).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=16377621; DOI=10.1074/jbc.M500361200;
Grau S., Richards P.J., Kerr B., Hughes C., Caterson B.,
Williams A.S., Junker U., Jones S.A., Clausen T., Ehrmann M.;
"The role of human HtrA1 in arthritic disease.";
J. Biol. Chem. 281:6124-6129(2006).
[7]
INVOLVEMENT IN SUSCEPTIBILITY TO ARMD7.
PubMed=17053108; DOI=10.1126/science.1133807;
Dewan A., Liu M., Hartman S., Zhang S.S.-M., Liu D.T.L., Zhao C.,
Tam P.O.S., Chan W.M., Lam D.S.C., Snyder M., Barnstable C.,
Pang C.P., Hoh J.;
"HTRA1 promoter polymorphism in wet age-related macular
degeneration.";
Science 314:989-992(2006).
[8]
INVOLVEMENT IN SUSCEPTIBILITY TO ARMD7.
PubMed=17053109; DOI=10.1126/science.1133811;
Yang Z., Camp N.J., Sun H., Tong Z., Gibbs D., Cameron D.J., Chen H.,
Zhao Y., Pearson E., Li X., Chien J., DeWan A., Harmon J.,
Bernstein P.S., Shridhar V., Zabriskie N.A., Hoh J., Howes K.,
Zhang K.;
"A variant of the HTRA1 gene increases susceptibility to age-related
macular degeneration.";
Science 314:992-993(2006).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20671064; DOI=10.1158/1541-7786.MCR-09-0473;
Campioni M., Severino A., Manente L., Tuduce I.L., Toldo S.,
Caraglia M., Crispi S., Ehrmann M., He X., Maguire J., De Falco M.,
De Luca A., Shridhar V., Baldi A.;
"The serine protease HtrA1 specifically interacts and degrades the
tuberous sclerosis complex 2 protein.";
Mol. Cancer Res. 8:1248-1260(2010).
[10]
INVOLVEMENT IN CADASIL2, VARIANTS CADASIL2 ARG-121; SER-123; GLY-133;
LEU-166; PRO-173; ARG-284; GLY-284; GLN-285; VAL-286 AND HIS-450,
VARIANTS VAL-20 AND GLY-51, AND CHARACTERIZATION OF VARIANTS CADASIL2
ARG-121; LEU-166; PRO-173; ARG-284; GLY-284; GLN-285; VAL-286 AND
HIS-450.
PubMed=26063658; DOI=10.1093/brain/awv155;
Verdura E., Herve D., Scharrer E., del Mar Amador M.,
Guyant-Marechal L., Philippi A., Corlobe A., Bergametti F., Gazal S.,
Prieto-Morin C., Beaufort N., Le Bail B., Viakhireva I., Dichgans M.,
Chabriat H., Haffner C., Tournier-Lasserve E.;
"Heterozygous HTRA1 mutations are associated with autosomal dominant
cerebral small vessel disease.";
Brain 138:2347-2358(2015).
[11]
STRUCTURE BY NMR OF 367-480.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the PDZ-domain of human protease HTRA 1
precursor.";
Submitted (APR-2008) to the PDB data bank.
[12]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 158-480, HOMOTRIMERIZATION,
SUBCELLULAR LOCATION, MUTAGENESIS OF SER-328, SITE, AND ACTIVE SITE.
PubMed=21297635; DOI=10.1038/nsmb.2013;
Truebestein L., Tennstaedt A., Monig T., Krojer T., Canellas F.,
Kaiser M., Clausen T., Ehrmann M.;
"Substrate-induced remodeling of the active site regulates human HTRA1
activity.";
Nat. Struct. Mol. Biol. 18:386-388(2011).
[13]
VARIANTS CARASIL THR-252 AND MET-297, AND CHARACTERIZATION OF VARIANTS
CARASIL THR-252 AND MET-297.
PubMed=19387015; DOI=10.1056/NEJMoa0801560;
Hara K., Shiga A., Fukutake T., Nozaki H., Miyashita A., Yokoseki A.,
Kawata H., Koyama A., Arima K., Takahashi T., Ikeda M., Shiota H.,
Tamura M., Shimoe Y., Hirayama M., Arisato T., Yanagawa S., Tanaka A.,
Nakano I., Ikeda S., Yoshida Y., Yamamoto T., Ikeuchi T., Kuwano R.,
Nishizawa M., Tsuji S., Onodera O.;
"Association of HTRA1 mutations and familial ischemic cerebral small-
vessel disease.";
N. Engl. J. Med. 360:1729-1739(2009).
-!- FUNCTION: Serine protease with a variety of targets, including
extracellular matrix proteins such as fibronectin. HTRA1-generated
fibronectin fragments further induce synovial cells to up-regulate
MMP1 and MMP3 production. May also degrade proteoglycans, such as
aggrecan, decorin and fibromodulin. Through cleavage of
proteoglycans, may release soluble FGF-glycosaminoglycan complexes
that promote the range and intensity of FGF signals in the
extracellular space. Regulates the availability of insulin-like
growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits
signaling mediated by TGF-beta family members. This activity
requires the integrity of the catalytic site, although it is
unclear whether TGF-beta proteins are themselves degraded. By
acting on TGF-beta signaling, may regulate many physiological
processes, including retinal angiogenesis and neuronal survival
and maturation during development. Intracellularly, degrades TSC2,
leading to the activation of TSC2 downstream targets.
{ECO:0000269|PubMed:16377621, ECO:0000269|PubMed:20671064,
ECO:0000269|PubMed:9852107}.
-!- SUBUNIT: Forms homotrimers. In the presence of substrate, may form
higher-order multimers in a PDZ-independent manner. Interacts with
TGF-beta family members, including BMP4, TGFB1, TGFB2, activin A
and GDF5 (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21297635}.
Secreted {ECO:0000269|PubMed:15208355,
ECO:0000269|PubMed:9852107}. Cytoplasm, cytosol
{ECO:0000269|PubMed:15208355, ECO:0000269|PubMed:20671064}.
Note=Predominantly secreted (PubMed:15208355). Also found
associated with the plasma membrane (PubMed:21297635).
{ECO:0000269|PubMed:15208355, ECO:0000269|PubMed:21297635}.
-!- TISSUE SPECIFICITY: Widely expressed, with strongest expression in
placenta (at protein level). Secreted by synovial fibroblasts. Up-
regulated in osteoarthritis and rheumatoid arthritis synovial
fluids and cartilage as compared with non-arthritic (at protein
level). {ECO:0000269|PubMed:15208355, ECO:0000269|PubMed:16377621,
ECO:0000269|PubMed:9852107}.
-!- DEVELOPMENTAL STAGE: In the placenta, in the first trimester of
gestation, low expression in the cells surrounding villi both in
the inner layer of the cytotrophoblast and in the outer layer of
the syncytiotrophoblast (at protein level). In the third trimester
of gestation, very strong expression in the outer layer forming
the syncytiotrophoblast and lower in the cytotrophoblast (at
protein level). {ECO:0000269|PubMed:15208355}.
-!- DOMAIN: The IGFBP N-terminal domain mediates interaction with TSC2
substrate.
-!- DISEASE: Macular degeneration, age-related, 7 (ARMD7)
[MIM:610149]: A form of age-related macular degeneration, a
multifactorial eye disease and the most common cause of
irreversible vision loss in the developed world. In most patients,
the disease is manifest as ophthalmoscopically visible yellowish
accumulations of protein and lipid that lie beneath the retinal
pigment epithelium and within an elastin-containing structure
known as Bruch membrane. {ECO:0000269|PubMed:17053108,
ECO:0000269|PubMed:17053109}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Cerebral arteriopathy, autosomal recessive, with
subcortical infarcts and leukoencephalopathy (CARASIL)
[MIM:600142]: A cerebrovascular disease characterized by non-
hypertensive arteriopathy of cerebral small vessels with
subcortical infarcts, alopecia, and spondylosis. Small cerebral
arteries show arteriosclerotic changes, fibrous intimal
proliferation, and hyaline degeneration with splitting of the
intima and/or the internal elastic membrane. Neurologic features
include progressive dementia, gait disturbances, extrapyramidal
and pyramidal signs, and demyelination of the cerebral white
matter with sparing of U fibers. {ECO:0000269|PubMed:19387015}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Cerebral arteriopathy, autosomal dominant, with
subcortical infarcts and leukoencephalopathy, 2 (CADASIL2)
[MIM:616779]: A cerebrovascular disease characterized by multiple
subcortical infarcts, pseudobulbar palsy, dementia, and the
presence of granular deposits in small cerebral arteries producing
ischemic stroke. {ECO:0000269|PubMed:26063658}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the peptidase S1C family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HTRA1ID41877ch10q26.html";
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EMBL; Y07921; CAA69226.1; -; mRNA.
EMBL; AF157623; AAD41525.1; -; Genomic_DNA.
EMBL; CH471066; EAW49312.1; -; Genomic_DNA.
EMBL; CH471066; EAW49313.1; -; Genomic_DNA.
EMBL; AF097709; AAC97211.1; -; mRNA.
CCDS; CCDS7630.1; -.
RefSeq; NP_002766.1; NM_002775.4.
UniGene; Hs.501280; -.
PDB; 2JOA; NMR; -; A=380-480.
PDB; 2YTW; NMR; -; A=370-480.
PDB; 3NUM; X-ray; 2.75 A; A=158-480.
PDB; 3NWU; X-ray; 3.20 A; A/B/C=158-375.
PDB; 3NZI; X-ray; 2.75 A; A=158-480.
PDB; 3TJN; X-ray; 3.00 A; A/B/D=161-367.
PDB; 3TJO; X-ray; 2.30 A; A/B/D=161-370.
PDB; 3TJQ; X-ray; 2.00 A; A=35-156.
PDBsum; 2JOA; -.
PDBsum; 2YTW; -.
PDBsum; 3NUM; -.
PDBsum; 3NWU; -.
PDBsum; 3NZI; -.
PDBsum; 3TJN; -.
PDBsum; 3TJO; -.
PDBsum; 3TJQ; -.
ProteinModelPortal; Q92743; -.
SMR; Q92743; -.
BioGrid; 111635; 19.
DIP; DIP-33195N; -.
IntAct; Q92743; 8.
MINT; MINT-1198897; -.
STRING; 9606.ENSP00000357980; -.
MEROPS; S01.277; -.
iPTMnet; Q92743; -.
PhosphoSitePlus; Q92743; -.
BioMuta; HTRA1; -.
DMDM; 18202620; -.
EPD; Q92743; -.
PaxDb; Q92743; -.
PeptideAtlas; Q92743; -.
PRIDE; Q92743; -.
DNASU; 5654; -.
Ensembl; ENST00000368984; ENSP00000357980; ENSG00000166033.
GeneID; 5654; -.
KEGG; hsa:5654; -.
UCSC; uc001lgj.2; human.
CTD; 5654; -.
DisGeNET; 5654; -.
EuPathDB; HostDB:ENSG00000166033.11; -.
GeneCards; HTRA1; -.
GeneReviews; HTRA1; -.
HGNC; HGNC:9476; HTRA1.
HPA; HPA036655; -.
MalaCards; HTRA1; -.
MIM; 600142; phenotype.
MIM; 602194; gene.
MIM; 610149; phenotype.
MIM; 616779; phenotype.
neXtProt; NX_Q92743; -.
OpenTargets; ENSG00000166033; -.
Orphanet; 279; Age-related macular degeneration.
Orphanet; 199354; CARASIL.
PharmGKB; PA33829; -.
eggNOG; KOG1320; Eukaryota.
eggNOG; COG0265; LUCA.
GeneTree; ENSGT00510000046315; -.
HOGENOM; HOG000223641; -.
HOVERGEN; HBG052044; -.
InParanoid; Q92743; -.
KO; K08784; -.
OMA; TYANLCQ; -.
OrthoDB; EOG091G0LXR; -.
PhylomeDB; Q92743; -.
TreeFam; TF323480; -.
BRENDA; 3.4.21.108; 2681.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
ChiTaRS; HTRA1; human.
EvolutionaryTrace; Q92743; -.
GeneWiki; HTRA1; -.
GenomeRNAi; 5654; -.
PRO; PR:Q92743; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000166033; -.
CleanEx; HS_HTRA1; -.
ExpressionAtlas; Q92743; baseline and differential.
Genevisible; Q92743; HS.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005520; F:insulin-like growth factor binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; EXP:Reactome.
GO; GO:0008236; F:serine-type peptidase activity; ISS:UniProtKB.
GO; GO:0060718; P:chorionic trophoblast cell differentiation; IEA:Ensembl.
GO; GO:0097187; P:dentinogenesis; IEA:Ensembl.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0030514; P:negative regulation of BMP signaling pathway; IEA:Ensembl.
GO; GO:0050687; P:negative regulation of defense response to virus; IEA:Ensembl.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
GO; GO:0001890; P:placenta development; IEA:Ensembl.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IEA:InterPro.
InterPro; IPR009030; Growth_fac_rcpt_.
InterPro; IPR000867; IGFBP-like.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR001478; PDZ.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001940; Peptidase_S1C.
Pfam; PF00219; IGFBP; 1.
Pfam; PF07648; Kazal_2; 1.
Pfam; PF00595; PDZ; 1.
PRINTS; PR00834; PROTEASES2C.
SMART; SM00121; IB; 1.
SMART; SM00280; KAZAL; 1.
SMART; SM00228; PDZ; 1.
SUPFAM; SSF100895; SSF100895; 1.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS51323; IGFBP_N_2; 1.
PROSITE; PS51465; KAZAL_2; 1.
PROSITE; PS50106; PDZ; 1.
1: Evidence at protein level;
3D-structure; Age-related macular degeneration; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Growth factor binding; Hydrolase; Membrane;
Polymorphism; Protease; Reference proteome; Secreted; Serine protease;
Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 480 Serine protease HTRA1.
/FTId=PRO_0000026943.
DOMAIN 33 100 IGFBP N-terminal. {ECO:0000255|PROSITE-
ProRule:PRU00653}.
DOMAIN 98 157 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 365 467 PDZ. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
REGION 204 364 Serine protease.
ACT_SITE 220 220 Charge relay system.
{ECO:0000269|PubMed:21297635}.
ACT_SITE 250 250 Charge relay system.
{ECO:0000269|PubMed:21297635}.
ACT_SITE 328 328 Charge relay system.
{ECO:0000269|PubMed:21297635}.
SITE 169 169 Involved in trimer stabilization.
{ECO:0000269|PubMed:21297635}.
SITE 171 171 Involved in trimer stabilization.
{ECO:0000269|PubMed:21297635}.
SITE 278 278 Involved in trimer stabilization.
{ECO:0000269|PubMed:21297635}.
VARIANT 20 20 A -> V (in dbSNP:rs369149111).
{ECO:0000269|PubMed:26063658}.
/FTId=VAR_076371.
VARIANT 51 51 E -> G. {ECO:0000269|PubMed:26063658}.
/FTId=VAR_076372.
VARIANT 121 121 S -> R (in CADASIL2).
{ECO:0000269|PubMed:26063658}.
/FTId=VAR_076373.
VARIANT 123 123 A -> S (in CADASIL2).
{ECO:0000269|PubMed:26063658}.
/FTId=VAR_076374.
VARIANT 133 133 R -> G (in CADASIL2).
{ECO:0000269|PubMed:26063658}.
/FTId=VAR_076375.
VARIANT 166 166 R -> L (in CADASIL2; loss of proteolytic
activity; dbSNP:rs864622781).
{ECO:0000269|PubMed:26063658}.
/FTId=VAR_076376.
VARIANT 173 173 A -> P (in CADASIL2; loss of proteolytic
activity). {ECO:0000269|PubMed:26063658}.
/FTId=VAR_076377.
VARIANT 252 252 A -> T (in CARASIL; has 21 to 50% normal
protease activity; is unable to suppress
TGF-beta activity; dbSNP:rs113993968).
{ECO:0000269|PubMed:19387015}.
/FTId=VAR_063148.
VARIANT 284 284 S -> G (in CADASIL2; partial loss of
proteolytic activity).
{ECO:0000269|PubMed:26063658}.
/FTId=VAR_076378.
VARIANT 284 284 S -> R (in CADASIL2; loss of proteolytic
activity; dbSNP:rs864622782).
{ECO:0000269|PubMed:26063658}.
/FTId=VAR_076379.
VARIANT 285 285 P -> Q (in CADASIL2; loss of proteolytic
activity). {ECO:0000269|PubMed:26063658}.
/FTId=VAR_076380.
VARIANT 286 286 F -> V (in CADASIL2; loss of proteolytic
activity). {ECO:0000269|PubMed:26063658}.
/FTId=VAR_076381.
VARIANT 297 297 V -> M (in CARASIL; has 21 to 50% normal
protease activity; is unable to suppress
TGF-beta activity; dbSNP:rs113993969).
{ECO:0000269|PubMed:19387015}.
/FTId=VAR_063149.
VARIANT 450 450 D -> H (in CADASIL2; unknown pathological
significance; small decrease, if any, in
proteolytic activity).
{ECO:0000269|PubMed:26063658}.
/FTId=VAR_076382.
MUTAGEN 328 328 S->A: Loss of activity.
{ECO:0000269|PubMed:21297635,
ECO:0000269|PubMed:9852107}.
CONFLICT 323 323 I -> T (in Ref. 4; AAC97211).
{ECO:0000305}.
HELIX 43 45 {ECO:0000244|PDB:3TJQ}.
STRAND 57 59 {ECO:0000244|PDB:3TJQ}.
STRAND 65 68 {ECO:0000244|PDB:3TJQ}.
STRAND 74 77 {ECO:0000244|PDB:3TJQ}.
STRAND 87 90 {ECO:0000244|PDB:3TJQ}.
STRAND 108 113 {ECO:0000244|PDB:3TJQ}.
STRAND 118 123 {ECO:0000244|PDB:3TJQ}.
STRAND 125 128 {ECO:0000244|PDB:3TJQ}.
HELIX 129 141 {ECO:0000244|PDB:3TJQ}.
HELIX 165 168 {ECO:0000244|PDB:3TJO}.
HELIX 171 179 {ECO:0000244|PDB:3TJO}.
HELIX 180 182 {ECO:0000244|PDB:3TJO}.
STRAND 183 191 {ECO:0000244|PDB:3TJO}.
STRAND 193 196 {ECO:0000244|PDB:3NZI}.
STRAND 198 208 {ECO:0000244|PDB:3TJO}.
TURN 211 213 {ECO:0000244|PDB:3NUM}.
STRAND 214 218 {ECO:0000244|PDB:3TJO}.
TURN 219 221 {ECO:0000244|PDB:3TJO}.
STRAND 224 231 {ECO:0000244|PDB:3TJO}.
STRAND 233 235 {ECO:0000244|PDB:3NZI}.
STRAND 237 246 {ECO:0000244|PDB:3TJO}.
TURN 247 250 {ECO:0000244|PDB:3TJO}.
STRAND 251 255 {ECO:0000244|PDB:3TJO}.
HELIX 270 272 {ECO:0000244|PDB:3TJO}.
STRAND 278 286 {ECO:0000244|PDB:3TJO}.
STRAND 289 299 {ECO:0000244|PDB:3TJO}.
STRAND 301 303 {ECO:0000244|PDB:3TJN}.
HELIX 304 306 {ECO:0000244|PDB:3NZI}.
STRAND 317 321 {ECO:0000244|PDB:3TJO}.
TURN 325 329 {ECO:0000244|PDB:3TJO}.
STRAND 330 333 {ECO:0000244|PDB:3TJO}.
STRAND 339 348 {ECO:0000244|PDB:3TJO}.
STRAND 351 356 {ECO:0000244|PDB:3TJO}.
HELIX 357 368 {ECO:0000244|PDB:3TJO}.
STRAND 380 382 {ECO:0000244|PDB:2YTW}.
STRAND 384 389 {ECO:0000244|PDB:2JOA}.
HELIX 392 401 {ECO:0000244|PDB:2JOA}.
STRAND 411 417 {ECO:0000244|PDB:2JOA}.
STRAND 419 421 {ECO:0000244|PDB:2JOA}.
HELIX 422 426 {ECO:0000244|PDB:2JOA}.
STRAND 433 437 {ECO:0000244|PDB:2YTW}.
HELIX 445 454 {ECO:0000244|PDB:2JOA}.
STRAND 456 464 {ECO:0000244|PDB:2JOA}.
STRAND 467 473 {ECO:0000244|PDB:2JOA}.
STRAND 476 478 {ECO:0000244|PDB:2YTW}.
SEQUENCE 480 AA; 51287 MW; CA20A99480FB2330 CRC64;
MQIPRAALLP LLLLLLAAPA SAQLSRAGRS APLAAGCPDR CEPARCPPQP EHCEGGRARD
ACGCCEVCGA PEGAACGLQE GPCGEGLQCV VPFGVPASAT VRRRAQAGLC VCASSEPVCG
SDANTYANLC QLRAASRRSE RLHRPPVIVL QRGACGQGQE DPNSLRHKYN FIADVVEKIA
PAVVHIELFR KLPFSKREVP VASGSGFIVS EDGLIVTNAH VVTNKHRVKV ELKNGATYEA
KIKDVDEKAD IALIKIDHQG KLPVLLLGRS SELRPGEFVV AIGSPFSLQN TVTTGIVSTT
QRGGKELGLR NSDMDYIQTD AIINYGNSGG PLVNLDGEVI GINTLKVTAG ISFAIPSDKI
KKFLTESHDR QAKGKAITKK KYIGIRMMSL TSSKAKELKD RHRDFPDVIS GAYIIEVIPD
TPAEAGGLKE NDVIISINGQ SVVSANDVSD VIKRESTLNM VVRRGNEDIM ITVIPEEIDP


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