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Cadherin-2 (Neural cadherin) (N-cadherin) (CD antigen CD325)

 CADH2_MOUSE             Reviewed;         906 AA.
P15116; Q64260; Q6GU11;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
27-SEP-2017, entry version 175.
RecName: Full=Cadherin-2;
AltName: Full=Neural cadherin;
Short=N-cadherin;
AltName: CD_antigen=CD325;
Flags: Precursor;
Name=Cdh2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2762814; DOI=10.1126/science.2762814;
Miyatani S., Shimamura K., Hatta M., Nagafuchi A., Nose A.,
Matsunaga M., Hatta K., Takeichi M.;
"Neural cadherin: role in selective cell-cell adhesion.";
Science 245:631-635(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Tamura K.;
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[3]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=1528849; DOI=10.1073/pnas.89.18.8443;
Miyatani S., Copeland N.G., Gilbert D.J., Jenkins N.A., Takeichi M.;
"Genomic structure and chromosomal mapping of the mouse N-cadherin
gene.";
Proc. Natl. Acad. Sci. U.S.A. 89:8443-8447(1992).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; 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).
[6]
DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=8879495; DOI=10.1095/biolreprod55.4.822;
Munro S.B., Blaschuk O.W.;
"A comprehensive survey of the cadherins expressed in the testes of
fetal, immature, and adult mice utilizing the polymerase chain
reaction.";
Biol. Reprod. 55:822-827(1996).
[7]
FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH FGFR4; PLCG1; FRS2;
SRC; GAP43 AND CTTN.
PubMed=11433297; DOI=10.1038/35083041;
Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.;
"N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-
receptor signalling.";
Nat. Cell Biol. 3:650-657(2001).
[8]
FUNCTION, AND PCDH8-MEDIATED ENDOCYTOSIS.
PubMed=17988630; DOI=10.1016/j.neuron.2007.08.020;
Yasuda S., Tanaka H., Sugiura H., Okamura K., Sakaguchi T., Tran U.,
Takemiya T., Mizoguchi A., Yagita Y., Sakurai T., De Robertis E.M.,
Yamagata K.;
"Activity-induced protocadherin arcadlin regulates dendritic spine
number by triggering N-cadherin endocytosis via TAO2beta and p38 MAP
kinases.";
Neuron 56:456-471(2007).
[9]
PROTEOLYTIC PROCESSING.
PubMed=19805319; DOI=10.1073/pnas.0908507106;
Folgueras A.R., Valdes-Sanchez T., Llano E., Menendez L., Baamonde A.,
Denlinger B.L., Belmonte C., Juarez L., Lastra A., Garcia-Suarez O.,
Astudillo A., Kirstein M., Pendas A.M., Farinas I., Lopez-Otin C.;
"Metalloproteinase MT5-MMP is an essential modulator of neuro-immune
interactions in thermal pain stimulation.";
Proc. Natl. Acad. Sci. U.S.A. 106:16451-16456(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Liver, Lung, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
CALCIUM-BINDING SITES, AND MUTAGENESIS OF ASP-262 AND ASP-293.
PubMed=21366346; DOI=10.1021/bi101872b;
Vunnam N., Pedigo S.;
"Sequential binding of calcium leads to dimerization in neural
cadherin.";
Biochemistry 50:2973-2982(2011).
[12]
INTERACTION WITH OBSCN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
PHOSPHORYLATION.
PubMed=23392350; DOI=10.1096/fj.12-221317;
Hu L.Y., Kontrogianni-Konstantopoulos A.;
"The kinase domains of obscurin interact with intercellular adhesion
proteins.";
FASEB J. 27:2001-2012(2013).
[13]
SUBCELLULAR LOCATION.
PubMed=25232112; DOI=10.1523/JNEUROSCI.1280-14.2014;
Wang S.H., Celic I., Choi S.Y., Riccomagno M., Wang Q., Sun L.O.,
Mitchell S.P., Vasioukhin V., Huganir R.L., Kolodkin A.L.;
"Dlg5 regulates dendritic spine formation and synaptogenesis by
controlling subcellular N-cadherin localization.";
J. Neurosci. 34:12745-12761(2014).
[14]
FUNCTION, DISRUPTION PHENOTYPE, AND PROTEOLYTIC PROCESSING.
PubMed=24952463; DOI=10.1038/ncb2993;
Porlan E., Marti-Prado B., Morante-Redolat J.M., Consiglio A.,
Delgado A.C., Kypta R., Lopez-Otin C., Kirstein M., Farinas I.;
"MT5-MMP regulates adult neural stem cell functional quiescence
through the cleavage of N-cadherin.";
Nat. Cell Biol. 16:629-638(2014).
[15]
SUBCELLULAR LOCATION.
PubMed=26403541; DOI=10.1038/ncomms9391;
Sharma P., Abbasi C., Lazic S., Teng A.C., Wang D., Dubois N.,
Ignatchenko V., Wong V., Liu J., Araki T., Tiburcy M., Ackerley C.,
Zimmermann W.H., Hamilton R., Sun Y., Liu P.P., Keller G.,
Stagljar I., Scott I.C., Kislinger T., Gramolini A.O.;
"Evolutionarily conserved intercalated disc protein Tmem65 regulates
cardiac conduction and connexin 43 function.";
Nat. Commun. 6:8391-8391(2015).
[16]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 160-267.
PubMed=7885471; DOI=10.1038/374327a0;
Shapiro L., Fannon A.M., Kwong P.D., Thompson A., Lehmann M.S.,
Gruebel G., Legrand J.-F., Als-Nielsen J., Colman D.R.,
Hendrickson W.A.;
"Structural basis of cell-cell adhesion by cadherins.";
Nature 374:327-337(1995).
[17]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 160-374.
PubMed=9655503; DOI=10.1016/S0896-6273(00)80496-1;
Tamura K., Shan W.S., Hendrickson W.A., Colman D.R., Shapiro L.;
"Structure-function analysis of cell adhesion by neural (N-)
cadherin.";
Neuron 20:1153-1163(1998).
-!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
They preferentially interact with themselves in a homophilic
manner in connecting cells; cadherins may thus contribute to the
sorting of heterogeneous cell types. Acts as a regulator of neural
stem cells quiescence by mediating anchorage of neural stem cells
to ependymocytes in the adult subependymal zone: upon cleavage by
MMP24, CDH2-mediated anchorage is affected, leading to modulate
neural stem cell quiescence (PubMed:24952463). CDH2 may be
involved in neuronal recognition mechanism. In hippocampal
neurons, may regulate dendritic spine density.
{ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:17988630,
ECO:0000269|PubMed:24952463}.
-!- SUBUNIT: Interacts with CDCP1 (By similarity). Interacts with
PCDH8; this complex may also include TAOK2 (By similarity). The
interaction with PCDH8 may lead to internalization through
TAOK2/p38 MAPK pathway (By similarity). Identified in a complex
containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and
CTTN (PubMed:11433297). May interact with OBSCN (via protein
kinase domain 2) (PubMed:23392350). {ECO:0000250|UniProtKB:P19022,
ECO:0000250|UniProtKB:Q9Z1Y3, ECO:0000269|PubMed:11433297,
ECO:0000269|PubMed:23392350}.
-!- INTERACTION:
P18031:PTPN1 (xeno); NbExp=3; IntAct=EBI-397974, EBI-968788;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26403541};
Single-pass type I membrane protein {ECO:0000255}. Cell membrane,
sarcolemma {ECO:0000269|PubMed:23392350}. Cell junction
{ECO:0000250|UniProtKB:P19022}. Cell surface
{ECO:0000269|PubMed:25232112}. Note=Colocalizes with TMEM65 at the
intercalated disk in cardiomyocytes (PubMed:26403541). Colocalizes
with OBSCN at the intercalated disk and sarcolemma in
cardiomyocytes (PubMed:23392350). {ECO:0000269|PubMed:23392350,
ECO:0000269|PubMed:26403541}.
-!- TISSUE SPECIFICITY: Expressed in cardiac muscle (at protein
level). {ECO:0000269|PubMed:23392350}.
-!- DEVELOPMENTAL STAGE: Expressed at all stages of testicular
development with highest levels found in testes of 21-day-old
mice. {ECO:0000269|PubMed:8879495}.
-!- DOMAIN: Three calcium ions are usually bound at the interface of
each cadherin domain and rigidify the connections, imparting a
strong curvature to the full-length ectodomain. Calcium-binding
sites are occupied sequentially in the order of site 3, then site
2 and site 1.
-!- PTM: Cleaved by MMP24. Ectodomain cleavage leads to the generation
of a soluble 90 kDa amino-terminal soluble fragment and a 45 kDa
membrane-bound carboxy-terminal fragment 1 (CTF1), which is
further cleaved by gamma-secretase into a 35 kDa. Cleavage in
neural stem cells by MMP24 affects CDH2-mediated anchorage of
neural stem cells to ependymocytes in the adult subependymal zone,
leading to modulate neural stem cell quiescence.
{ECO:0000269|PubMed:19805319, ECO:0000269|PubMed:24952463}.
-!- PTM: May be phosphorylated by OBSCN.
{ECO:0000269|PubMed:23392350}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality.
{ECO:0000269|PubMed:24952463}.
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EMBL; M31131; AAA37353.1; -; mRNA.
EMBL; AB008811; BAA23549.1; -; mRNA.
EMBL; S45011; AAB23356.1; -; Genomic_DNA.
EMBL; CH466557; EDK96930.1; -; Genomic_DNA.
EMBL; BC022107; AAH22107.1; -; mRNA.
CCDS; CCDS29076.1; -.
PIR; A32759; IJMSCN.
RefSeq; NP_031690.3; NM_007664.5.
UniGene; Mm.257437; -.
PDB; 1NCG; X-ray; 2.10 A; A=160-267.
PDB; 1NCH; X-ray; 2.10 A; A/B=160-267.
PDB; 1NCI; X-ray; 2.10 A; A/B=160-267.
PDB; 1NCJ; X-ray; 3.40 A; A=160-374.
PDB; 1OP4; NMR; -; A=24-159.
PDB; 2QVI; X-ray; 3.01 A; A=160-374.
PDB; 3Q2W; X-ray; 3.20 A; A=160-712.
PDB; 4NUM; X-ray; 3.30 A; A/B/C/D=160-374.
PDB; 4NUP; X-ray; 2.70 A; A/B/C=162-374.
PDB; 4NUQ; X-ray; 2.12 A; A=160-374.
PDBsum; 1NCG; -.
PDBsum; 1NCH; -.
PDBsum; 1NCI; -.
PDBsum; 1NCJ; -.
PDBsum; 1OP4; -.
PDBsum; 2QVI; -.
PDBsum; 3Q2W; -.
PDBsum; 4NUM; -.
PDBsum; 4NUP; -.
PDBsum; 4NUQ; -.
ProteinModelPortal; P15116; -.
SMR; P15116; -.
BioGrid; 198637; 21.
CORUM; P15116; -.
DIP; DIP-31564N; -.
IntAct; P15116; 10.
MINT; MINT-4089694; -.
STRING; 10090.ENSMUSP00000025166; -.
iPTMnet; P15116; -.
PhosphoSitePlus; P15116; -.
MaxQB; P15116; -.
PaxDb; P15116; -.
PeptideAtlas; P15116; -.
PRIDE; P15116; -.
Ensembl; ENSMUST00000025166; ENSMUSP00000025166; ENSMUSG00000024304.
GeneID; 12558; -.
KEGG; mmu:12558; -.
UCSC; uc008edx.2; mouse.
CTD; 1000; -.
MGI; MGI:88355; Cdh2.
eggNOG; KOG3594; Eukaryota.
eggNOG; ENOG410XQHI; LUCA.
GeneTree; ENSGT00760000118906; -.
HOGENOM; HOG000231254; -.
HOVERGEN; HBG106438; -.
InParanoid; P15116; -.
KO; K06736; -.
OMA; FLEAGIY; -.
OrthoDB; EOG091G01FV; -.
TreeFam; TF316817; -.
Reactome; R-MMU-375170; CDO in myogenesis.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-418990; Adherens junctions interactions.
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
EvolutionaryTrace; P15116; -.
PRO; PR:P15116; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024304; -.
CleanEx; MM_CDH2; -.
ExpressionAtlas; P15116; baseline and differential.
Genevisible; P15116; MM.
GO; GO:0005912; C:adherens junction; IDA:MGI.
GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
GO; GO:0016342; C:catenin complex; ISO:MGI.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005913; C:cell-cell adherens junction; ISO:MGI.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005916; C:fascia adherens; IDA:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density of dendrite; IDA:SynGO.
GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0045294; F:alpha-catenin binding; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0045295; F:gamma-catenin binding; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0048514; P:blood vessel morphogenesis; IMP:MGI.
GO; GO:0048854; P:brain morphogenesis; IGI:MGI.
GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MGI.
GO; GO:0007155; P:cell adhesion; IDA:MGI.
GO; GO:0016477; P:cell migration; IDA:MGI.
GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IDA:UniProtKB.
GO; GO:0021987; P:cerebral cortex development; IGI:MGI.
GO; GO:0090002; P:establishment of protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0010001; P:glial cell differentiation; IDA:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MGI.
GO; GO:0048872; P:homeostasis of number of cells; IGI:MGI.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
GO; GO:0060563; P:neuroepithelial cell differentiation; IGI:MGI.
GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; IMP:BHF-UCL.
GO; GO:0097150; P:neuronal stem cell population maintenance; IDA:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IGI:MGI.
GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IMP:BHF-UCL.
GO; GO:0060019; P:radial glial cell differentiation; IGI:MGI.
GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; IGI:MGI.
GO; GO:1902897; P:regulation of postsynaptic density protein 95 clustering; IMP:BHF-UCL.
GO; GO:0051146; P:striated muscle cell differentiation; IGI:MGI.
GO; GO:0021537; P:telencephalon development; IGI:MGI.
Gene3D; 4.10.900.10; -; 1.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR000233; Cadherin_cytoplasmic-dom.
InterPro; IPR014868; Cadherin_pro_dom.
InterPro; IPR027397; Catenin_binding_dom.
InterPro; IPR030051; CDH2.
PANTHER; PTHR24027:SF365; PTHR24027:SF365; 1.
Pfam; PF00028; Cadherin; 5.
Pfam; PF01049; Cadherin_C; 1.
Pfam; PF08758; Cadherin_pro; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 5.
SMART; SM01055; Cadherin_pro; 1.
SUPFAM; SSF49313; SSF49313; 6.
PROSITE; PS00232; CADHERIN_1; 3.
PROSITE; PS50268; CADHERIN_2; 5.
1: Evidence at protein level;
3D-structure; Calcium; Cell adhesion; Cell junction; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Glycoprotein;
Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
PROPEP 26 159 {ECO:0000255}.
/FTId=PRO_0000003733.
CHAIN 160 906 Cadherin-2.
/FTId=PRO_0000003734.
TOPO_DOM 160 724 Extracellular. {ECO:0000255}.
TRANSMEM 725 745 Helical. {ECO:0000255}.
TOPO_DOM 746 906 Cytoplasmic. {ECO:0000255}.
DOMAIN 160 267 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 268 382 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 383 497 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 498 603 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 604 717 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
COMPBIAS 863 878 Ser-rich.
METAL 262 262 Calcium 1. {ECO:0000269|PubMed:21366346}.
METAL 262 262 Calcium 2. {ECO:0000269|PubMed:21366346}.
METAL 293 293 Calcium 3. {ECO:0000269|PubMed:21366346}.
CARBOHYD 190 190 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 273 273 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 325 325 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 402 402 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 572 572 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 651 651 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 692 692 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 262 262 D->A: Abolishes dimerization.
{ECO:0000269|PubMed:21366346}.
MUTAGEN 293 293 D->A: Severely impaired the binding of
calcium to all three sites.
{ECO:0000269|PubMed:21366346}.
CONFLICT 7 9 APR -> GRG (in Ref. 1; AAA37353).
{ECO:0000305}.
CONFLICT 565 567 NVK -> YVQ (in Ref. 1; AAA37353).
{ECO:0000305}.
CONFLICT 624 624 T -> A (in Ref. 1; AAA37353).
{ECO:0000305}.
STRAND 40 43 {ECO:0000244|PDB:1OP4}.
STRAND 55 57 {ECO:0000244|PDB:1OP4}.
STRAND 69 72 {ECO:0000244|PDB:1OP4}.
STRAND 76 82 {ECO:0000244|PDB:1OP4}.
TURN 83 85 {ECO:0000244|PDB:1OP4}.
STRAND 86 91 {ECO:0000244|PDB:1OP4}.
STRAND 96 98 {ECO:0000244|PDB:1OP4}.
STRAND 100 108 {ECO:0000244|PDB:1OP4}.
TURN 109 112 {ECO:0000244|PDB:1OP4}.
STRAND 113 121 {ECO:0000244|PDB:1OP4}.
STRAND 166 171 {ECO:0000244|PDB:1NCG}.
STRAND 176 182 {ECO:0000244|PDB:1NCG}.
HELIX 186 190 {ECO:0000244|PDB:1NCG}.
STRAND 194 199 {ECO:0000244|PDB:1NCG}.
TURN 200 202 {ECO:0000244|PDB:1NCG}.
STRAND 203 206 {ECO:0000244|PDB:1NCG}.
STRAND 209 212 {ECO:0000244|PDB:1NCG}.
TURN 214 216 {ECO:0000244|PDB:1NCG}.
STRAND 218 221 {ECO:0000244|PDB:1NCG}.
TURN 227 229 {ECO:0000244|PDB:1NCG}.
STRAND 232 240 {ECO:0000244|PDB:1NCG}.
TURN 242 244 {ECO:0000244|PDB:2QVI}.
STRAND 246 248 {ECO:0000244|PDB:1NCI}.
STRAND 251 258 {ECO:0000244|PDB:1NCG}.
STRAND 266 268 {ECO:0000244|PDB:4NUQ}.
STRAND 270 277 {ECO:0000244|PDB:4NUQ}.
STRAND 285 288 {ECO:0000244|PDB:4NUQ}.
HELIX 300 302 {ECO:0000244|PDB:4NUQ}.
STRAND 305 313 {ECO:0000244|PDB:4NUQ}.
STRAND 321 323 {ECO:0000244|PDB:4NUQ}.
TURN 325 327 {ECO:0000244|PDB:4NUQ}.
STRAND 329 332 {ECO:0000244|PDB:4NUQ}.
TURN 339 341 {ECO:0000244|PDB:4NUQ}.
STRAND 344 353 {ECO:0000244|PDB:4NUQ}.
HELIX 354 356 {ECO:0000244|PDB:4NUQ}.
TURN 358 360 {ECO:0000244|PDB:4NUQ}.
STRAND 363 373 {ECO:0000244|PDB:4NUQ}.
STRAND 381 394 {ECO:0000244|PDB:3Q2W}.
STRAND 396 406 {ECO:0000244|PDB:3Q2W}.
TURN 414 416 {ECO:0000244|PDB:3Q2W}.
STRAND 421 425 {ECO:0000244|PDB:3Q2W}.
STRAND 431 435 {ECO:0000244|PDB:3Q2W}.
TURN 437 439 {ECO:0000244|PDB:3Q2W}.
STRAND 441 446 {ECO:0000244|PDB:3Q2W}.
TURN 452 454 {ECO:0000244|PDB:3Q2W}.
STRAND 456 463 {ECO:0000244|PDB:3Q2W}.
STRAND 466 468 {ECO:0000244|PDB:3Q2W}.
HELIX 478 480 {ECO:0000244|PDB:3Q2W}.
STRAND 481 489 {ECO:0000244|PDB:3Q2W}.
STRAND 496 508 {ECO:0000244|PDB:3Q2W}.
STRAND 515 518 {ECO:0000244|PDB:3Q2W}.
STRAND 526 528 {ECO:0000244|PDB:3Q2W}.
STRAND 532 538 {ECO:0000244|PDB:3Q2W}.
STRAND 544 546 {ECO:0000244|PDB:3Q2W}.
TURN 548 550 {ECO:0000244|PDB:3Q2W}.
STRAND 552 557 {ECO:0000244|PDB:3Q2W}.
STRAND 561 563 {ECO:0000244|PDB:3Q2W}.
STRAND 568 579 {ECO:0000244|PDB:3Q2W}.
STRAND 581 583 {ECO:0000244|PDB:3Q2W}.
STRAND 586 596 {ECO:0000244|PDB:3Q2W}.
STRAND 604 606 {ECO:0000244|PDB:3Q2W}.
STRAND 621 623 {ECO:0000244|PDB:3Q2W}.
STRAND 633 636 {ECO:0000244|PDB:3Q2W}.
STRAND 638 640 {ECO:0000244|PDB:3Q2W}.
STRAND 643 645 {ECO:0000244|PDB:3Q2W}.
HELIX 646 651 {ECO:0000244|PDB:3Q2W}.
STRAND 652 656 {ECO:0000244|PDB:3Q2W}.
STRAND 658 660 {ECO:0000244|PDB:3Q2W}.
STRAND 662 666 {ECO:0000244|PDB:3Q2W}.
STRAND 674 683 {ECO:0000244|PDB:3Q2W}.
STRAND 685 688 {ECO:0000244|PDB:3Q2W}.
STRAND 691 700 {ECO:0000244|PDB:3Q2W}.
SEQUENCE 906 AA; 99796 MW; BDAB8063A23E1F13 CRC64;
MCRIAGAPRT LLPLLAALLQ ASVEASGEIA LCKTGFPEDV YSAVLPKDVH EGQPLLNVKF
SNCNRKRKVQ YESSEPADFK VDEDGTVYAV RSFPLTAEQA KFLIYAQDKE TQEKWQVAVN
LSREPTLTEE PMKEPHEIEE IVFPRQLAKH SGALQRQKRD WVIPPINLPE NSRGPFPQEL
VRIRSDRDKN LSLRYSVTGP GADQPPTGIF IINPISGQLS VTKPLDRELI ARFHLRAHAV
DINGNQVENP IDIVINVIDM NDNRPEFLHQ VWNGSVPEGS KPGTYVMTVT AIDADDPNAL
NGMLRYRILS QAPSTPSPNM FTINNETGDI ITVAAGLDRE KVQQYTLIIQ ATDMEGNPTY
GLSNTATAVI TVTDVNDNPP EFTAMTFYGE VPENRVDVIV ANLTVTDKDQ PHTPAWNAAY
RISGGDPTGR FAILTDPNSN DGLVTVVKPI DFETNRMFVL TVAAENQVPL AKGIQHPPQS
TATVSVTVID VNENPYFAPN PKIIRQEEGL HAGTMLTTLT AQDPDRYMQQ NIRYTKLSDP
ANWLKIDPVN GQITTIAVLD RESPNVKNNI YNATFLASDN GIPPMSGTGT LQIYLLDIND
NAPQVLPQEA ETCETPEPNS INITALDYDI DPNAGPFAFD LPLSPVTIKR NWTINRLNGD
FAQLNLKIKF LEAGIYEVPI IITDSGNPPK SNISILRVKV CQCDSNGDCT DVDRIVGAGL
GTGAIIAILL CIIILLILVL MFVVWMKRRD KERQAKQLLI DPEDDVRDNI LKYDEEGGGE
EDQDYDLSQL QQPDTVEPDA IKPVGIRRLD ERPIHAEPQY PVRSAAPHPG DIGDFINEGL
KAADNDPTAP PYDSLLVFDY EGSGSTAGSL SSLNSSSSGG DQDYDYLNDW GPRFKKLADM
YGGGDD


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