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Cadherin-2 (Neural cadherin) (N-cadherin)

 CADH2_CHICK             Reviewed;         912 AA.
P10288; Q90630;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
23-MAY-2018, entry version 147.
RecName: Full=Cadherin-2;
AltName: Full=Neural cadherin;
Short=N-cadherin;
Flags: Precursor;
Name=CDH2;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2831236; DOI=10.1083/jcb.106.3.873;
Hatta K., Nose A., Nagafuchi A., Takeichi M.;
"Cloning and expression of cDNA encoding a neural calcium-dependent
cell adhesion molecule: its identity in the cadherin gene family.";
J. Cell Biol. 106:873-881(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
STRAIN=Cornish white rock Cockerel;
PubMed=9210582; DOI=10.1016/S0378-1119(97)00006-1;
Li B., Paradies N.E., Brackenbury R.W.;
"Isolation and characterization of the promoter region of the chicken
N-cadherin gene.";
Gene 191:7-13(1997).
[3]
INTERACTION WITH CTNNA2.
TISSUE=Embryonic brain;
PubMed=1638632; DOI=10.1016/0092-8674(92)90103-J;
Hirano S., Kimoto N., Shimoyama Y., Hirohashi S., Takeichi M.;
"Identification of a neural alpha-catenin as a key regulator of
cadherin function and multicellular organization.";
Cell 70:293-301(1992).
-!- 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. CDH2 may be
involved in neuronal recognition mechanism (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Interacts with CTNNA2. {ECO:0000269|PubMed:1638632}.
-!- INTERACTION:
O42486:Bcat; NbExp=5; IntAct=EBI-985728, EBI-972394;
O13016:PTPN1; NbExp=10; IntAct=EBI-985728, EBI-6938259;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P15116}; Single-pass type I membrane
protein {ECO:0000255}.
-!- 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. {ECO:0000250}.
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EMBL; X07277; CAA30258.1; -; mRNA.
EMBL; U15563; AAB62980.1; -; Genomic_DNA.
PIR; A29964; IJCHCN.
RefSeq; NP_001001615.1; NM_001001615.1.
UniGene; Gga.1917; -.
ProteinModelPortal; P10288; -.
SMR; P10288; -.
DIP; DIP-29636N; -.
IntAct; P10288; 9.
MINT; P10288; -.
STRING; 9031.ENSGALP00000024371; -.
PaxDb; P10288; -.
Ensembl; ENSGALT00000024417; ENSGALP00000024371; ENSGALG00000015132.
GeneID; 414745; -.
KEGG; gga:414745; -.
CTD; 1000; -.
eggNOG; KOG3594; Eukaryota.
eggNOG; ENOG410XQHI; LUCA.
GeneTree; ENSGT00760000118906; -.
HOGENOM; HOG000231254; -.
HOVERGEN; HBG106438; -.
InParanoid; P10288; -.
KO; K06736; -.
OMA; FLEAGIY; -.
OrthoDB; EOG091G01FV; -.
PhylomeDB; P10288; -.
TreeFam; TF316817; -.
Reactome; R-GGA-375170; CDO in myogenesis.
Reactome; R-GGA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-GGA-418990; Adherens junctions interactions.
Reactome; R-GGA-8957275; Post-translational protein phosphorylation.
PRO; PR:P10288; -.
Proteomes; UP000000539; Chromosome 2.
Bgee; ENSGALG00000015132; -.
GO; GO:0005912; C:adherens junction; IDA:AgBase.
GO; GO:0045177; C:apical part of cell; IDA:AgBase.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0016342; C:catenin complex; IEA:Ensembl.
GO; GO:0005623; C:cell; IDA:AgBase.
GO; GO:0044297; C:cell body; IDA:AgBase.
GO; GO:0009986; C:cell surface; IDA:AgBase.
GO; GO:0005913; C:cell-cell adherens junction; IDA:AgBase.
GO; GO:0005911; C:cell-cell junction; IDA:AgBase.
GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:AgBase.
GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0043005; C:neuron projection; IDA:AgBase.
GO; GO:0005886; C:plasma membrane; IDA:AgBase.
GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0045294; F:alpha-catenin binding; IEA:Ensembl.
GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; IMP:AgBase.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0050840; F:extracellular matrix binding; TAS:AgBase.
GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl.
GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
GO; GO:0001502; P:cartilage condensation; TAS:AgBase.
GO; GO:0007155; P:cell adhesion; TAS:AgBase.
GO; GO:0098743; P:cell aggregation; IMP:AgBase.
GO; GO:0016477; P:cell migration; IEA:Ensembl.
GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IMP:AgBase.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:AgBase.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:Ensembl.
GO; GO:0060173; P:limb development; TAS:AgBase.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0030336; P:negative regulation of cell migration; IMP:AgBase.
GO; GO:0036032; P:neural crest cell delamination; IMP:AgBase.
GO; GO:0001841; P:neural tube formation; IMP:AgBase.
GO; GO:0060563; P:neuroepithelial cell differentiation; IEA:Ensembl.
GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; IEA:Ensembl.
GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IEA:Ensembl.
GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0060019; P:radial glial cell differentiation; IEA:Ensembl.
GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; IEA:Ensembl.
GO; GO:1902897; P:regulation of postsynaptic density protein 95 clustering; IEA:Ensembl.
GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
GO; GO:0061561; P:trigeminal ganglion formation; IMP:AgBase.
GO; GO:0061563; P:trigeminal ganglion structural organization; IMP:AgBase.
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_sf.
InterPro; IPR030051; CDH2.
PANTHER; PTHR24027:SF79; PTHR24027:SF79; 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;
Calcium; Cell adhesion; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Glycoprotein;
Membrane; Metal-binding; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
PROPEP 29 164 {ECO:0000255}.
/FTId=PRO_0000003737.
CHAIN 165 912 Cadherin-2.
/FTId=PRO_0000003738.
TOPO_DOM 165 729 Extracellular. {ECO:0000255}.
TRANSMEM 730 752 Helical. {ECO:0000255}.
TOPO_DOM 753 912 Cytoplasmic. {ECO:0000255}.
DOMAIN 165 272 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 273 387 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 388 502 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 503 609 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 610 720 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
COMPBIAS 869 884 Ser-rich.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 407 407 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 578 578 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 628 628 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 657 657 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 21 21 A -> G (in Ref. 2; AAB62980).
{ECO:0000305}.
SEQUENCE 912 AA; 100465 MW; 9BA5AC9DC1FFC489 CRC64;
MCRIAGTPPR ILPPLALMLL AALQQAPIKA TCEDMLCKMG FPEDVHSAVV SRSVHGGQPL
LNVRFQSCDE NRKIYFGSSE PEDFRVGEDG VVYAERSFQL SAEPTEFVVS ARDKETQEEW
QMKVKLTPEP AFTGASEKDQ KKIEDIIFPW QQYKDSSHLK RQKRDWVIPP INLPENSRGP
FPQELVRIRS DRDKSLSLRY SVTGPGADQP PTGIFIINPI SGQLSVTKPL DREQIASFHL
RAHAVDVNGN QVENPIDIVI NVIDMNDNRP EFLHQVWNGT VPEGSKPGTY VMTVTAIDAD
DPNAQNGMLR YRILSQAPSS PSPNMFTINN ETGDIITVAA GLDREKVQQY TLIIQATDME
GNPTYGLSNT ATAVITVTDV NDNPPEFTAM TFYGEVPENR VDVIVANLTV TDKDQPHTPA
WNARYQMTGG DPTGQFTILT DPNSNDGLVT VVKPIDFETN RMFVLTVAAE NQVPLAKGIQ
HPPQSTATVS ITVIDVNESP YFVPNPKLVR QEEGLLAGSM LTTFTARDPD RYMQQTSLRY
SKLSDPANWL KIDPVNGQIT TTAVLDRESI YVQNNMYNAT FLASDNGIPP MSGTGTLQIY
LLDINDNAPQ VNPKEATTCE TLQPNAINIT AVDPDIDPNA GPFAFELPDS PPSIKRNWTI
VRISGDHAQL SLRIRFLEAG IYDVPIVITD SGNPHASSTS VLKVKVCQCD INGDCTDVDR
IVGAGLGTGA IIAILLCIII LLILVLMFVV WMKRRDKERQ AKQLLIDPED DVRDNILKYD
EEGGGEEDQD YDLSQLQQPD TVEPDAIKPV GIRRLDERPI HAEPQYPVRS AAPHPGDIGD
FINEGLKAAD NDPTAPPYDS LLVFDYEGSG STAGSLSSLN SSSSGGEQDY DYLNDWGPRF
KKLADMYGGG DD


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