CADH2_DANRE
ID CADH2_DANRE Reviewed; 893 AA.
AC Q90275; Q8UVQ7;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Cadherin-2;
DE AltName: Full=Neural cadherin;
DE Short=N-cadherin {ECO:0000303|PubMed:12091300, ECO:0000303|PubMed:7873785};
DE AltName: Full=Parachute {ECO:0000303|PubMed:12091300};
DE AltName: Full=ZNCAD;
DE Flags: Precursor;
GN Name=cdh2; Synonyms=pac {ECO:0000303|PubMed:12091300};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12020083; DOI=10.1017/s0952523801186098;
RA Liu Q., Babb S.G., Novince Z.M., Doedens A.L., Marrs J., Raymond P.A.;
RT "Differential expression of cadherin-2 and cadherin-4 in the developing and
RT adult zebrafish visual system.";
RL Vis. Neurosci. 18:923-933(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND MUTAGENESIS OF 501-SER--ASP-893
RP AND 514-TYR--ASP-893.
RX PubMed=12091300; DOI=10.1242/dev.129.14.3281;
RA Lele Z., Folchert A., Concha M., Rauch G.-J., Geisler R., Rosa F.,
RA Wilson S.W., Hammerschmidt M., Bally-Cuif L.;
RT "Parachute/n-cadherin is required for morphogenesis and maintained
RT integrity of the zebrafish neural tube.";
RL Development 129:3281-3294(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-893, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Embryo;
RX PubMed=7873785; DOI=10.1002/aja.1002010204;
RA Bitzur S., Kam Z., Geiger B.;
RT "Structure and distribution of N-cadherin in developing zebrafish embryos:
RT morphogenetic effects of ectopic over-expression.";
RL Dev. Dyn. 201:121-136(1994).
CC -!- FUNCTION: Calcium-dependent cell adhesion protein; preferentially
CC mediates homotypic cell-cell adhesion (By similarity). Cadherins
CC contribute to the sorting of heterogeneous cell types, and thereby play
CC an important role during embryonic development (PubMed:12091300).
CC Required for normal neural tube morphogenesis. Required to allow
CC mid- and hindbrain neurons to reach and maintain their appropriate
CC positions within the neural tube by restricting neuronal motility
CC within the embryonic mid- and hindbrain (PubMed:12091300).
CC {ECO:0000250|UniProtKB:P15116, ECO:0000269|PubMed:12091300}.
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. {ECO:0000250|UniProtKB:P15116}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15116};
CC Single-pass type I membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expression in the embryo is initially found in all
CC deep cells but later becomes restricted to various epithelial and
CC neuronal tissues. Found in discrete areas of cell-cell adhesion when
CC epiboly is nearly completed. Expressed in adult brain, eyes and trunk.
CC {ECO:0000269|PubMed:7873785}.
CC -!- DEVELOPMENTAL STAGE: Expression is first detected in the embryo during
CC gastrulation. {ECO:0000269|PubMed:7873785}.
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; AF430842; AAN61915.1; -; mRNA.
DR EMBL; AF418565; AAL59160.1; -; mRNA.
DR EMBL; X67648; CAA47890.1; -; mRNA.
DR RefSeq; NP_571156.2; NM_131081.2.
DR AlphaFoldDB; Q90275; -.
DR SMR; Q90275; -.
DR STRING; 7955.ENSDARP00000003949; -.
DR PaxDb; Q90275; -.
DR GeneID; 30291; -.
DR KEGG; dre:30291; -.
DR CTD; 1000; -.
DR ZFIN; ZDB-GENE-990415-171; cdh2.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q90275; -.
DR OrthoDB; 191117at2759; -.
DR PhylomeDB; Q90275; -.
DR Reactome; R-DRE-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-DRE-418990; Adherens junctions interactions.
DR Reactome; R-DRE-525793; Myogenesis.
DR Reactome; R-DRE-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q90275; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0045177; C:apical part of cell; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IDA:ZFIN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
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:0014704; C:intercalated disc; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ZFIN.
DR GO; GO:0005886; C:plasma membrane; IDA:ZFIN.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IDA:ZFIN.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0034332; P:adherens junction organization; IMP:ZFIN.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:ZFIN.
DR GO; GO:0048331; P:axial mesoderm structural organization; IMP:ZFIN.
DR GO; GO:0007411; P:axon guidance; IMP:ZFIN.
DR GO; GO:0007413; P:axonal fasciculation; IMP:ZFIN.
DR GO; GO:0048514; P:blood vessel morphogenesis; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IMP:ZFIN.
DR GO; GO:0010002; P:cardioblast differentiation; IMP:ZFIN.
DR GO; GO:0001502; P:cartilage condensation; IMP:ZFIN.
DR GO; GO:0021535; P:cell migration in hindbrain; IMP:ZFIN.
DR GO; GO:0090248; P:cell migration involved in somitogenic axis elongation; IMP:ZFIN.
DR GO; GO:0000902; P:cell morphogenesis; IMP:ZFIN.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISS:UniProtKB.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:ZFIN.
DR GO; GO:0060271; P:cilium assembly; IMP:ZFIN.
DR GO; GO:0071679; P:commissural neuron axon guidance; IMP:ZFIN.
DR GO; GO:0060030; P:dorsal convergence; IMP:ZFIN.
DR GO; GO:0035142; P:dorsal fin morphogenesis; IMP:ZFIN.
DR GO; GO:0007398; P:ectoderm development; IMP:ZFIN.
DR GO; GO:0048048; P:embryonic eye morphogenesis; IMP:ZFIN.
DR GO; GO:0035118; P:embryonic pectoral fin morphogenesis; IMP:ZFIN.
DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IMP:ZFIN.
DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; IMP:ZFIN.
DR GO; GO:0048699; P:generation of neurons; IMP:ZFIN.
DR GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
DR GO; GO:0030902; P:hindbrain development; IMP:ZFIN.
DR GO; GO:0021577; P:hindbrain structural organization; IMP:ZFIN.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0048332; P:mesoderm morphogenesis; IMP:ZFIN.
DR GO; GO:0030901; P:midbrain development; IMP:ZFIN.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:ZFIN.
DR GO; GO:0097475; P:motor neuron migration; IMP:ZFIN.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IMP:ZFIN.
DR GO; GO:0001755; P:neural crest cell migration; IGI:ZFIN.
DR GO; GO:0021915; P:neural tube development; IMP:ZFIN.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IMP:ZFIN.
DR GO; GO:0001764; P:neuron migration; IMP:ZFIN.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IMP:ZFIN.
DR GO; GO:0007422; P:peripheral nervous system development; IMP:ZFIN.
DR GO; GO:0070285; P:pigment cell development; IGI:ZFIN.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:ZFIN.
DR GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0042478; P:regulation of eye photoreceptor cell development; IMP:ZFIN.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:ZFIN.
DR GO; GO:0048752; P:semicircular canal morphogenesis; IMP:ZFIN.
DR GO; GO:0070654; P:sensory epithelium regeneration; IMP:ZFIN.
DR GO; GO:0001756; P:somitogenesis; IMP:ZFIN.
DR GO; GO:0021511; P:spinal cord patterning; IMP:ZFIN.
DR GO; GO:0007416; P:synapse assembly; IEP:ZFIN.
DR GO; GO:0042246; P:tissue regeneration; IEP:ZFIN.
DR GO; GO:0021591; P:ventricular system development; IMP:ZFIN.
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 membrane; Cleavage on pair of basic residues;
KW Developmental protein; Differentiation; Glycoprotein; Membrane;
KW Metal-binding; Neurogenesis; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..146
FT /evidence="ECO:0000255"
FT /id="PRO_0000003739"
FT CHAIN 147..893
FT /note="Cadherin-2"
FT /id="PRO_0000003740"
FT TOPO_DOM 147..711
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 712..732
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 733..893
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 148..254
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 255..369
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 370..484
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 485..590
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 591..702
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 777..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..872
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 249
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 250
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 288
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 559
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 609
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 501..893
FT /note="Missing: In pac(fr7); causes abnormal embryonic
FT brain and tail morphogenesis."
FT /evidence="ECO:0000269|PubMed:12091300"
FT MUTAGEN 514..893
FT /note="Missing: In pac(tm101B); causes abnormal embryonic
FT brain and tail morphogenesis."
FT /evidence="ECO:0000269|PubMed:12091300"
FT CONFLICT 510
FT /note="D -> DD (in Ref. 3; CAA47890)"
FT /evidence="ECO:0000305"
FT CONFLICT 530
FT /note="W -> L (in Ref. 3; CAA47890)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 893 AA; 98990 MW; 5E3FF0CDD92B3A6F CRC64;
MYPSGGVMLG LLAALQVAVQ GTGAMPCQPG FTENEYNVMT ADVITEGQVL LKVDFVDCGR
GSGLRFESGD PADFRIDADG TVMAARTLQL TDRKGQSLEI KAKDENSQEQ WMVHINFTQP
KQVPVILFPR HSVLVKGDDS VNRVKRDWVI PPVNVLENSR KQFPEELVKI QSDKDKSNTL
RYSVTGPGAD QNPTGLFIID PISGLLSVTK PLDREHIPNF HLRAHAVDIN GNQMENPIDI
IINVIDMNDN RPEFTHQIWN GTVDEGAKPG TFVMTVTSQD KDDPNTANGM LRYKILSQTP
ESPSSNMFTI NNKTGKIITV AAGLDREKVP QYTLIIQATD MEGNPTYGLS NTATAVIRLL
DVNDNAPEFT RETFHGEVPE NRVNVIVTNL TVTDKDEPGT PAWNAVYRII SGDPTGRFSI
PTDPVTNEGL VTVVKPVDFE MNRSFMLTVV ADNEVPLASG IHRTRQSTAT VSIRVIDVNE
SPNFDPNPKQ IKLEEGLPQW SMLTTFTAHD PDRYMQQTIS YSKLYDPANW LEIDPNNGRI
STIAVLDRES PYVKNNLYNA TFMASDNGVP RASGTGTLQI YLLDINDNAP RVFPQEAEVC
ERPEPNAINI TAVDGDLNPN AGPYAFELPN RPSDIRRNWT LTRISGDHAQ LSLKISYLES
GIYELPISIT DSGNLPMSNT TYLRIKVCQC DHHGDCVDME RIMAAGLGTG AIIAILICII
ILLVLVLMFV MWMKRRDKER QAKQLLIDPE DDVRDNILKY DEEGGGEEDQ DYDLSQLQQP
DTLEPDMIKP VGIRRLDERP MHSEPNYPIR SAAPHPGDIG EFIHEGLKAA DTDPTAPPYD
SLLVFDYEGS GSTAGSLSSL HSSSSGGDQD YDYLNDWGPR FRKLADMYGG NDD
