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Acidic mammalian chitinase (AMCase) (EC 3.2.1.14) (Lung-specific protein TSA1902)

 CHIA_HUMAN              Reviewed;         476 AA.
Q9BZP6; Q32W79; Q32W80; Q3B866; Q5U5Z5; Q5VUV4; Q86UD8; Q9ULY3;
Q9ULY4;
24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 155.
RecName: Full=Acidic mammalian chitinase;
Short=AMCase;
EC=3.2.1.14;
AltName: Full=Lung-specific protein TSA1902;
Flags: Precursor;
Name=CHIA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), AND VARIANTS VAL-339
AND GLY-432.
TISSUE=Lung;
PubMed=10548734; DOI=10.1016/S0378-1119(99)00394-7;
Saito A., Ozaki K., Fujiwara T., Nakamura Y., Tanigami A.;
"Isolation and mapping of a human lung-specific gene, TSA1902,
encoding a novel chitinase family member.";
Gene 239:325-331(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=11085997; DOI=10.1074/jbc.M009886200;
Boot R.G., Blommaart E.F.C., Swart E., Ghauharali-van der Vlugt K.,
Bijl N., Moe C., Place A., Aerts J.M.F.G.;
"Identification of a novel acidic mammalian chitinase distinct from
chitotriosidase.";
J. Biol. Chem. 276:6770-6778(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
TISSUE=Kidney;
Chen X.H., Cai G.P.;
"A novel chitinase family member.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[6]
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=15192232; DOI=10.1126/science.1095336;
Zhu Z., Zheng T., Homer R.J., Kim Y.K., Chen N.Y., Cohn L., Hamid Q.,
Elias J.A.;
"Acidic mammalian chitinase in asthmatic Th2 inflammation and IL-13
pathway activation.";
Science 304:1678-1682(2004).
[7]
FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH EGFR, AND SUBCELLULAR
LOCATION.
PubMed=18824549; DOI=10.1074/jbc.M805574200;
Hartl D., He C.H., Koller B., Da Silva C.A., Homer R., Lee C.G.,
Elias J.A.;
"Acidic mammalian chitinase is secreted via an ADAM17/epidermal growth
factor receptor-dependent pathway and stimulates chemokine production
by pulmonary epithelial cells.";
J. Biol. Chem. 283:33472-33482(2008).
[8]
FUNCTION, AND MUTAGENESIS OF ASP-138.
PubMed=19342690; DOI=10.4049/jimmunol.0803446;
Hartl D., He C.H., Koller B., Da Silva C.A., Kobayashi Y., Lee C.G.,
Flavell R.A., Elias J.A.;
"Acidic mammalian chitinase regulates epithelial cell apoptosis via a
chitinolytic-independent mechanism.";
J. Immunol. 182:5098-5106(2009).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 22-408 IN COMPLEX WITH
METHYLALLOSAMIDIN, CATALYTIC ACTIVITY, AND DISULFIDE BONDS.
PubMed=19241384; DOI=10.1002/pro.63;
Olland A.M., Strand J., Presman E., Czerwinski R., Joseph-McCarthy D.,
Krykbaev R., Schlingmann G., Chopra R., Lin L., Fleming M., Kriz R.,
Stahl M., Somers W., Fitz L., Mosyak L.;
"Triad of polar residues implicated in pH specificity of acidic
mammalian chitinase.";
Protein Sci. 18:569-578(2009).
[10]
VARIANTS ASP-45; ASN-47; MET-61; ARG-102; ARG-125; VAL-339; SER-354
AND GLY-432, CATALYTIC ACTIVITY, FUNCTION, AND CHARACTERIZATION OF
VARIANTS ASP-45; ASN-47 AND MET-61.
PubMed=19435888; DOI=10.1074/jbc.M109.012443;
Seibold M.A., Reese T.A., Choudhry S., Salam M.T., Beckman K., Eng C.,
Atakilit A., Meade K., Lenoir M., Watson H.G., Thyne S., Kumar R.,
Weiss K.B., Grammer L.C., Avila P., Schleimer R.P., Fahy J.V.,
Rodriguez-Santana J., Rodriguez-Cintron W., Boot R.G., Sheppard D.,
Gilliland F.D., Locksley R.M., Burchard E.G.;
"Differential enzymatic activity of common haplotypic versions of the
human acidic mammalian chitinase protein.";
J. Biol. Chem. 284:19650-19658(2009).
-!- FUNCTION: Degrades chitin and chitotriose. May participate in the
defense against nematodes, fungi and other pathogens. Plays a role
in T-helper cell type 2 (Th2) immune response. Contributes to the
response to IL-13 and inflammation in response to IL-13.
Stimulates chemokine production by pulmonary epithelial cells.
Protects lung epithelial cells against apoptosis and promotes
phosphorylation of AKT1. Its function in the inflammatory response
and in protecting cells against apoptosis is inhibited by
allosamidin, suggesting that the function of this protein depends
on carbohydrate binding. {ECO:0000269|PubMed:11085997,
ECO:0000269|PubMed:18824549, ECO:0000269|PubMed:19342690,
ECO:0000269|PubMed:19435888}.
-!- CATALYTIC ACTIVITY: Random endo-hydrolysis of N-acetyl-beta-D-
glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
{ECO:0000269|PubMed:18824549, ECO:0000269|PubMed:19241384,
ECO:0000269|PubMed:19435888}.
-!- SUBUNIT: Interacts with EGFR. {ECO:0000269|PubMed:18824549,
ECO:0000269|PubMed:19241384}.
-!- INTERACTION:
Q92609:TBC1D5; NbExp=4; IntAct=EBI-14357960, EBI-742381;
-!- SUBCELLULAR LOCATION: Isoform 1: Secreted. Note=Secretion depends
on EGFR activity.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9BZP6-1; Sequence=Displayed;
Name=2; Synonyms=TSA1902-L;
IsoId=Q9BZP6-2; Sequence=VSP_008635;
Name=3; Synonyms=TSA1902-S;
IsoId=Q9BZP6-3; Sequence=VSP_008634;
-!- TISSUE SPECIFICITY: Detected in lung epithelial cells from asthma
patients (at protein level). Highly expressed in stomach. Detected
at lower levels in lung. {ECO:0000269|PubMed:11085997,
ECO:0000269|PubMed:15192232}.
-!- INDUCTION: Up-regulated in lung epithelial cells from asthma
patients. {ECO:0000269|PubMed:15192232}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
class II subfamily. {ECO:0000305}.
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EMBL; AB025008; BAA86980.1; -; mRNA.
EMBL; AB025009; BAA86981.1; -; mRNA.
EMBL; AF290004; AAG60019.1; -; mRNA.
EMBL; AY789444; AAX81431.1; -; mRNA.
EMBL; AY789445; AAX81432.1; -; mRNA.
EMBL; AL513202; CAH70803.1; -; Genomic_DNA.
EMBL; AL356387; CAH70803.1; JOINED; Genomic_DNA.
EMBL; AL356387; CAI19265.1; -; Genomic_DNA.
EMBL; AL513202; CAI19265.1; JOINED; Genomic_DNA.
EMBL; BC047336; AAH47336.2; -; mRNA.
EMBL; BC036339; AAH36339.2; -; mRNA.
EMBL; BC106910; AAI06911.1; -; mRNA.
CCDS; CCDS41368.1; -. [Q9BZP6-1]
CCDS; CCDS58017.1; -. [Q9BZP6-3]
CCDS; CCDS832.1; -. [Q9BZP6-2]
RefSeq; NP_001035713.1; NM_001040623.2. [Q9BZP6-3]
RefSeq; NP_001244930.1; NM_001258001.1. [Q9BZP6-2]
RefSeq; NP_001244931.1; NM_001258002.1. [Q9BZP6-3]
RefSeq; NP_001244932.1; NM_001258003.1. [Q9BZP6-2]
RefSeq; NP_001244933.1; NM_001258004.1. [Q9BZP6-3]
RefSeq; NP_001244934.1; NM_001258005.1. [Q9BZP6-3]
RefSeq; NP_068569.2; NM_021797.3. [Q9BZP6-2]
RefSeq; NP_970615.2; NM_201653.3. [Q9BZP6-1]
RefSeq; XP_006710640.1; XM_006710577.3. [Q9BZP6-3]
RefSeq; XP_016856536.1; XM_017001047.1. [Q9BZP6-3]
RefSeq; XP_016856537.1; XM_017001048.1. [Q9BZP6-2]
UniGene; Hs.128814; -.
PDB; 2YBT; X-ray; 2.22 A; A/B/C/D/E/F=21-398.
PDB; 2YBU; X-ray; 2.25 A; A/B/C/D/E/F=21-398.
PDB; 3FXY; X-ray; 2.00 A; A/B/C/D=22-408.
PDB; 3FY1; X-ray; 1.70 A; A/B=22-408.
PDB; 3RM4; X-ray; 1.90 A; A/B=22-408.
PDB; 3RM8; X-ray; 1.80 A; A/B=22-408.
PDB; 3RM9; X-ray; 2.10 A; A/B=22-408.
PDB; 3RME; X-ray; 1.80 A; A/B=22-408.
PDBsum; 2YBT; -.
PDBsum; 2YBU; -.
PDBsum; 3FXY; -.
PDBsum; 3FY1; -.
PDBsum; 3RM4; -.
PDBsum; 3RM8; -.
PDBsum; 3RM9; -.
PDBsum; 3RME; -.
ProteinModelPortal; Q9BZP6; -.
SMR; Q9BZP6; -.
BioGrid; 118039; 18.
IntAct; Q9BZP6; 2.
STRING; 9606.ENSP00000341828; -.
BindingDB; Q9BZP6; -.
ChEMBL; CHEMBL1293197; -.
CAZy; CBM14; Carbohydrate-Binding Module Family 14.
CAZy; GH18; Glycoside Hydrolase Family 18.
iPTMnet; Q9BZP6; -.
PhosphoSitePlus; Q9BZP6; -.
BioMuta; CHIA; -.
DMDM; 37999771; -.
PaxDb; Q9BZP6; -.
PeptideAtlas; Q9BZP6; -.
PRIDE; Q9BZP6; -.
Ensembl; ENST00000343320; ENSP00000341828; ENSG00000134216. [Q9BZP6-1]
Ensembl; ENST00000353665; ENSP00000338970; ENSG00000134216. [Q9BZP6-3]
Ensembl; ENST00000369740; ENSP00000358755; ENSG00000134216. [Q9BZP6-1]
Ensembl; ENST00000430615; ENSP00000391132; ENSG00000134216. [Q9BZP6-2]
Ensembl; ENST00000451398; ENSP00000390476; ENSG00000134216. [Q9BZP6-3]
Ensembl; ENST00000483391; ENSP00000436946; ENSG00000134216. [Q9BZP6-3]
GeneID; 27159; -.
KEGG; hsa:27159; -.
UCSC; uc001eas.5; human. [Q9BZP6-1]
CTD; 27159; -.
DisGeNET; 27159; -.
EuPathDB; HostDB:ENSG00000134216.18; -.
GeneCards; CHIA; -.
HGNC; HGNC:17432; CHIA.
HPA; HPA059193; -.
MIM; 606080; gene.
neXtProt; NX_Q9BZP6; -.
OpenTargets; ENSG00000134216; -.
PharmGKB; PA142672117; -.
eggNOG; KOG2806; Eukaryota.
eggNOG; COG3325; LUCA.
GeneTree; ENSGT00550000074323; -.
HOVERGEN; HBG011684; -.
InParanoid; Q9BZP6; -.
KO; K01183; -.
OMA; TYSPNFA; -.
OrthoDB; EOG091G014W; -.
PhylomeDB; Q9BZP6; -.
TreeFam; TF315610; -.
BRENDA; 3.2.1.14; 2681.
Reactome; R-HSA-189085; Digestion of dietary carbohydrate.
EvolutionaryTrace; Q9BZP6; -.
GenomeRNAi; 27159; -.
PRO; PR:Q9BZP6; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000134216; -.
ExpressionAtlas; Q9BZP6; baseline and differential.
Genevisible; Q9BZP6; HS.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; NAS:UniProtKB.
GO; GO:0008061; F:chitin binding; TAS:UniProtKB.
GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0003796; F:lysozyme activity; NAS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006037; P:cell wall chitin metabolic process; TAS:UniProtKB.
GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
GO; GO:0006030; P:chitin metabolic process; NAS:UniProtKB.
GO; GO:0007586; P:digestion; NAS:UniProtKB.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
GO; GO:0044245; P:polysaccharide digestion; TAS:Reactome.
GO; GO:0090197; P:positive regulation of chemokine secretion; IDA:UniProtKB.
GO; GO:0002532; P:production of molecular mediator involved in inflammatory response; IDA:UniProtKB.
GO; GO:0009620; P:response to fungus; TAS:UniProtKB.
Gene3D; 2.170.140.10; -; 1.
Gene3D; 3.10.50.10; -; 1.
InterPro; IPR002557; Chitin-bd_dom.
InterPro; IPR036508; Chitin-bd_dom_sf.
InterPro; IPR011583; Chitinase_II.
InterPro; IPR029070; Chitinase_insertion.
InterPro; IPR001223; Glyco_hydro18_cat.
InterPro; IPR001579; Glyco_hydro_18_chit_AS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF01607; CBM_14; 1.
Pfam; PF00704; Glyco_hydro_18; 1.
SMART; SM00494; ChtBD2; 1.
SMART; SM00636; Glyco_18; 1.
SUPFAM; SSF51445; SSF51445; 2.
SUPFAM; SSF54556; SSF54556; 1.
SUPFAM; SSF57625; SSF57625; 1.
PROSITE; PS50940; CHIT_BIND_II; 1.
PROSITE; PS01095; CHITINASE_18; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis;
Carbohydrate metabolism; Chitin degradation; Chitin-binding;
Complete proteome; Cytoplasm; Disulfide bond; Glycosidase; Hydrolase;
Immunity; Inflammatory response; Polymorphism;
Polysaccharide degradation; Reference proteome; Secreted; Signal.
SIGNAL 1 21 {ECO:0000250}.
CHAIN 22 476 Acidic mammalian chitinase.
/FTId=PRO_0000011944.
DOMAIN 427 476 Chitin-binding type-2.
{ECO:0000255|PROSITE-ProRule:PRU00144}.
REGION 70 71 Chitooligosaccharide binding.
{ECO:0000305}.
REGION 97 100 Chitooligosaccharide binding.
{ECO:0000305}.
REGION 210 213 Chitooligosaccharide binding.
{ECO:0000305}.
COMPBIAS 415 420 Poly-Ser.
ACT_SITE 140 140 Proton donor. {ECO:0000305}.
BINDING 141 141 Chitooligosaccharide. {ECO:0000250}.
BINDING 360 360 Chitooligosaccharide. {ECO:0000250}.
DISULFID 26 51 {ECO:0000255|PROSITE-ProRule:PRU00144,
ECO:0000269|PubMed:19241384}.
DISULFID 49 394 {ECO:0000255|PROSITE-ProRule:PRU00144,
ECO:0000269|PubMed:19241384}.
DISULFID 307 372 {ECO:0000255|PROSITE-ProRule:PRU00144,
ECO:0000269|PubMed:19241384}.
VAR_SEQ 1 161 Missing (in isoform 3).
{ECO:0000303|PubMed:10548734,
ECO:0000303|Ref.3}.
/FTId=VSP_008634.
VAR_SEQ 1 108 Missing (in isoform 2).
{ECO:0000303|PubMed:10548734,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3}.
/FTId=VSP_008635.
VARIANT 45 45 N -> D (increased chitinase activity;
when associated with N-47 and M-61;
dbSNP:rs41282492).
{ECO:0000269|PubMed:19435888}.
/FTId=VAR_063030.
VARIANT 47 47 D -> N (increased chitinase activity;
when associated with N-47 and M-61;
dbSNP:rs41282494).
{ECO:0000269|PubMed:19435888}.
/FTId=VAR_063031.
VARIANT 61 61 R -> M (increased chitinase activity;
when associated with N-47 and M-61;
dbSNP:rs41282496).
{ECO:0000269|PubMed:19435888}.
/FTId=VAR_063032.
VARIANT 102 102 G -> R (in dbSNP:rs3818822).
{ECO:0000269|PubMed:19435888}.
/FTId=VAR_049192.
VARIANT 125 125 K -> R (in dbSNP:rs61756687).
{ECO:0000269|PubMed:19435888}.
/FTId=VAR_063033.
VARIANT 324 324 V -> G (in dbSNP:rs2256721).
/FTId=VAR_033730.
VARIANT 339 339 I -> V (in dbSNP:rs2275253).
{ECO:0000269|PubMed:10548734,
ECO:0000269|PubMed:19435888}.
/FTId=VAR_049193.
VARIANT 354 354 F -> S (in dbSNP:rs2275254).
{ECO:0000269|PubMed:19435888}.
/FTId=VAR_049194.
VARIANT 377 377 F -> L (in dbSNP:rs36011905).
/FTId=VAR_049195.
VARIANT 432 432 V -> G (in dbSNP:rs2256721).
{ECO:0000269|PubMed:10548734,
ECO:0000269|PubMed:19435888}.
/FTId=VAR_049196.
MUTAGEN 138 138 D->A: Loss of chitinase activity. No
effect on protection against apoptosis or
on AKT1 activation.
{ECO:0000269|PubMed:19342690}.
CONFLICT 203 203 Y -> C (in Ref. 3; AAX81431).
{ECO:0000305}.
STRAND 23 29 {ECO:0000244|PDB:3FY1}.
HELIX 32 34 {ECO:0000244|PDB:3FY1}.
HELIX 37 39 {ECO:0000244|PDB:3FY1}.
HELIX 43 45 {ECO:0000244|PDB:3FY1}.
TURN 48 50 {ECO:0000244|PDB:3RM8}.
STRAND 52 62 {ECO:0000244|PDB:3FY1}.
STRAND 65 67 {ECO:0000244|PDB:3FY1}.
HELIX 73 82 {ECO:0000244|PDB:3FY1}.
HELIX 83 85 {ECO:0000244|PDB:3FY1}.
STRAND 91 97 {ECO:0000244|PDB:3FY1}.
HELIX 99 101 {ECO:0000244|PDB:3FY1}.
HELIX 104 110 {ECO:0000244|PDB:3FY1}.
HELIX 113 130 {ECO:0000244|PDB:3FY1}.
STRAND 133 138 {ECO:0000244|PDB:3FY1}.
HELIX 151 173 {ECO:0000244|PDB:3FY1}.
STRAND 179 184 {ECO:0000244|PDB:3FY1}.
HELIX 188 194 {ECO:0000244|PDB:3FY1}.
HELIX 197 203 {ECO:0000244|PDB:3FY1}.
STRAND 205 209 {ECO:0000244|PDB:3FY1}.
HELIX 217 219 {ECO:0000244|PDB:3FY1}.
HELIX 236 240 {ECO:0000244|PDB:3FY1}.
HELIX 243 252 {ECO:0000244|PDB:3FY1}.
HELIX 257 259 {ECO:0000244|PDB:3FY1}.
STRAND 260 275 {ECO:0000244|PDB:3FY1}.
STRAND 284 288 {ECO:0000244|PDB:3FY1}.
TURN 293 295 {ECO:0000244|PDB:3FY1}.
STRAND 300 302 {ECO:0000244|PDB:3FY1}.
HELIX 303 311 {ECO:0000244|PDB:3FY1}.
STRAND 315 319 {ECO:0000244|PDB:3FY1}.
TURN 320 323 {ECO:0000244|PDB:3FY1}.
STRAND 324 329 {ECO:0000244|PDB:3FY1}.
STRAND 332 335 {ECO:0000244|PDB:3FY1}.
HELIX 339 351 {ECO:0000244|PDB:3FY1}.
STRAND 355 360 {ECO:0000244|PDB:3FY1}.
HELIX 362 364 {ECO:0000244|PDB:3FY1}.
STRAND 367 369 {ECO:0000244|PDB:3FY1}.
TURN 370 372 {ECO:0000244|PDB:3FY1}.
HELIX 378 386 {ECO:0000244|PDB:3FY1}.
HELIX 392 394 {ECO:0000244|PDB:3FXY}.
SEQUENCE 476 AA; 52271 MW; 92B27BAD2F7EB4CC CRC64;
MTKLILLTGL VLILNLQLGS AYQLTCYFTN WAQYRPGLGR FMPDNIDPCL CTHLIYAFAG
RQNNEITTIE WNDVTLYQAF NGLKNKNSQL KTLLAIGGWN FGTAPFTAMV STPENRQTFI
TSVIKFLRQY EFDGLDFDWE YPGSRGSPPQ DKHLFTVLVQ EMREAFEQEA KQINKPRLMV
TAAVAAGISN IQSGYEIPQL SQYLDYIHVM TYDLHGSWEG YTGENSPLYK YPTDTGSNAY
LNVDYVMNYW KDNGAPAEKL IVGFPTYGHN FILSNPSNTG IGAPTSGAGP AGPYAKESGI
WAYYEICTFL KNGATQGWDA PQEVPYAYQG NVWVGYDNIK SFDIKAQWLK HNKFGGAMVW
AIDLDDFTGT FCNQGKFPLI STLKKALGLQ SASCTAPAQP IEPITAAPSG SGNGSGSSSS
GGSSGGSGFC AVRANGLYPV ANNRNAFWHC VNGVTYQQNC QAGLVFDTSC DCCNWA


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