CADH2_CHICK
ID CADH2_CHICK Reviewed; 912 AA.
AC P10288; Q90630;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cadherin-2;
DE AltName: Full=Neural cadherin;
DE Short=N-cadherin {ECO:0000303|PubMed:1638632};
DE Flags: Precursor;
GN Name=CDH2;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=2831236; DOI=10.1083/jcb.106.3.873;
RA Hatta K., Nose A., Nagafuchi A., Takeichi M.;
RT "Cloning and expression of cDNA encoding a neural calcium-dependent cell
RT adhesion molecule: its identity in the cadherin gene family.";
RL J. Cell Biol. 106:873-881(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RC STRAIN=Cornish white rock Cockerel;
RX PubMed=9210582; DOI=10.1016/s0378-1119(97)00006-1;
RA Li B., Paradies N.E., Brackenbury R.W.;
RT "Isolation and characterization of the promoter region of the chicken N-
RT cadherin gene.";
RL Gene 191:7-13(1997).
RN [3]
RP INTERACTION WITH CTNNA2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic brain;
RX PubMed=1638632; DOI=10.1016/0092-8674(92)90103-j;
RA Hirano S., Kimoto N., Shimoyama Y., Hirohashi S., Takeichi M.;
RT "Identification of a neural alpha-catenin as a key regulator of cadherin
RT function and multicellular organization.";
RL Cell 70:293-301(1992).
CC -!- FUNCTION: Calcium-dependent cell adhesion protein; preferentially
CC mediates homotypic cell-cell adhesion (PubMed:2831236). Cadherins may
CC thus contribute to the sorting of heterogeneous cell types, and thereby
CC play an important role during embryonic development (By similarity).
CC {ECO:0000250|UniProtKB:Q90275, ECO:0000269|PubMed:2831236}.
CC -!- SUBUNIT: Homodimer (via extracellular region). Can also form
CC heterodimers with other cadherins (via extracellular region).
CC Dimerization occurs in trans, i.e. with a cadherin chain from another
CC cell (By similarity). Interacts with CTNNA2 (PubMed:1638632).
CC {ECO:0000250|UniProtKB:P15116, ECO:0000269|PubMed:1638632}.
CC -!- INTERACTION:
CC P10288; O42486: Bcat; NbExp=5; IntAct=EBI-985728, EBI-972394;
CC P10288; O13016: PTPN1; NbExp=10; IntAct=EBI-985728, EBI-6938259;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1638632,
CC ECO:0000269|PubMed:2831236}; Single-pass type I membrane protein
CC {ECO:0000255}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P15116}. Cell junction
CC {ECO:0000250|UniProtKB:P15116}. Cell surface
CC {ECO:0000250|UniProtKB:P15116}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic brain and heart (at protein
CC level) (PubMed:1638632). Detected in embryonic brain and heart
CC (PubMed:2831236). {ECO:0000269|PubMed:1638632,
CC ECO:0000269|PubMed:2831236}.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain and rigidify the connections, imparting a strong
CC curvature to the full-length ectodomain. Calcium-binding sites are
CC occupied sequentially in the order of site 3, then site 2 and site 1.
CC {ECO:0000250|UniProtKB:P15116}.
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DR EMBL; X07277; CAA30258.1; -; mRNA.
DR EMBL; U15563; AAB62980.1; -; Genomic_DNA.
DR PIR; A29964; IJCHCN.
DR RefSeq; NP_001001615.1; NM_001001615.1.
DR AlphaFoldDB; P10288; -.
DR SMR; P10288; -.
DR DIP; DIP-29636N; -.
DR IntAct; P10288; 9.
DR MINT; P10288; -.
DR STRING; 9031.ENSGALP00000024371; -.
DR PaxDb; P10288; -.
DR PRIDE; P10288; -.
DR Ensembl; ENSGALT00000024417; ENSGALP00000024371; ENSGALG00000015132.
DR GeneID; 414745; -.
DR KEGG; gga:414745; -.
DR CTD; 1000; -.
DR VEuPathDB; HostDB:geneid_414745; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000155981; -.
DR HOGENOM; CLU_005284_2_0_1; -.
DR InParanoid; P10288; -.
DR OMA; NVRFQSC; -.
DR OrthoDB; 191117at2759; -.
DR PhylomeDB; P10288; -.
DR TreeFam; TF316817; -.
DR Reactome; R-GGA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-GGA-418990; Adherens junctions interactions.
DR Reactome; R-GGA-525793; Myogenesis.
DR Reactome; R-GGA-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P10288; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000015132; Expressed in heart and 13 other tissues.
DR ExpressionAtlas; P10288; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IDA:AgBase.
DR GO; GO:0045177; C:apical part of cell; IDA:AgBase.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0044297; C:cell body; IDA:AgBase.
DR GO; GO:0009986; C:cell surface; IDA:AgBase.
DR GO; GO:0005911; C:cell-cell junction; IDA:AgBase.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IBA:GO_Central.
DR GO; GO:0099059; C:integral component of presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0045294; F:alpha-catenin binding; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0045296; F:cadherin binding; IMP:AgBase.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0050840; F:extracellular matrix binding; TAS:AgBase.
DR GO; GO:0045295; F:gamma-catenin binding; IPI:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR GO; GO:0048514; P:blood vessel morphogenesis; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0001502; P:cartilage condensation; TAS:AgBase.
DR GO; GO:0007155; P:cell adhesion; TAS:AgBase.
DR GO; GO:0098743; P:cell aggregation; IMP:AgBase.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IMP:AgBase.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:AgBase.
DR GO; GO:0007043; P:cell-cell junction assembly; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:Ensembl.
DR GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0060173; P:limb development; TAS:AgBase.
DR GO; GO:0090497; P:mesenchymal cell migration; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:AgBase.
DR GO; GO:0036032; P:neural crest cell delamination; IMP:AgBase.
DR GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
DR GO; GO:0001841; P:neural tube formation; IMP:AgBase.
DR GO; GO:0060563; P:neuroepithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0097118; P:neuroligin clustering involved in postsynaptic membrane assembly; IEA:Ensembl.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; IEA:Ensembl.
DR GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0060019; P:radial glial cell differentiation; IEA:Ensembl.
DR GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0070445; P:regulation of oligodendrocyte progenitor proliferation; IEA:Ensembl.
DR GO; GO:1902897; P:regulation of postsynaptic density protein 95 clustering; IEA:Ensembl.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IBA:GO_Central.
DR GO; GO:0061561; P:trigeminal ganglion formation; IMP:AgBase.
DR GO; GO:0061563; P:trigeminal ganglion structural organization; IMP:AgBase.
DR GO; GO:0003323; P:type B pancreatic cell development; IEA:Ensembl.
DR Gene3D; 4.10.900.10; -; 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR InterPro; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR030051; CDH2.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR PANTHER; PTHR24027:SF79; PTHR24027:SF79; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..164
FT /evidence="ECO:0000255"
FT /id="PRO_0000003737"
FT CHAIN 165..912
FT /note="Cadherin-2"
FT /id="PRO_0000003738"
FT TOPO_DOM 165..729
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 730..752
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 753..912
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 165..272
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 273..387
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 388..502
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 503..609
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 610..720
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 869..890
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 265
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 268
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 298
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 300
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 306
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 358
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 330
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 407
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 657
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 21
FT /note="A -> G (in Ref. 2; AAB62980)"
FT /evidence="ECO:0000305"
SQ 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
