CADH2_CRIGR
ID CADH2_CRIGR Reviewed; 238 AA.
AC O55075;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Cadherin-2;
DE AltName: Full=Neural cadherin;
DE Short=N-cadherin;
DE AltName: CD_antigen=CD325;
DE Flags: Fragment;
GN Name=CDH2;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RA Levenberg S., Sadot E., Goichberg P., Geiger B.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-dependent cell adhesion protein; preferentially
CC mediates homotypic cell-cell adhesion by dimerization with a CDH2 chain
CC from another cell. Cadherins may thus contribute to the sorting of
CC heterogeneous cell types. Acts as a regulator of neural stem cells
CC quiescence by mediating anchorage of neural stem cells to ependymocytes
CC in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated
CC anchorage is affected, leading to modulate neural stem cell quiescence.
CC CDH2 may be involved in neuronal recognition mechanism. In hippocampal
CC neurons, may regulate dendritic spine density.
CC {ECO:0000250|UniProtKB:P15116}.
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 CDCP1 (By similarity). Interacts
CC with PCDH8; this complex may also include TAOK2 (By similarity). The
CC interaction with PCDH8 may lead to internalization through TAOK2/p38
CC MAPK pathway (By similarity). Identified in a complex containing FGFR4,
CC NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. May interact with
CC OBSCN (via protein kinase domain 2) (By similarity).
CC {ECO:0000250|UniProtKB:P15116, ECO:0000250|UniProtKB:P19022,
CC ECO:0000250|UniProtKB:Q9Z1Y3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15116};
CC Single-pass type I membrane protein {ECO:0000255}. Cell membrane,
CC sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction
CC {ECO:0000250|UniProtKB:P19022}. Cell surface
CC {ECO:0000250|UniProtKB:P15116}. Note=Colocalizes with TMEM65 at the
CC intercalated disk in cardiomyocytes. Colocalizes with OBSCN at the
CC intercalated disk and sarcolemma in cardiomyocytes.
CC {ECO:0000250|UniProtKB:P15116}.
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}.
CC -!- PTM: Cleaved by MMP24. Ectodomain cleavage leads to the generation of a
CC soluble 90 kDa amino-terminal soluble fragment and a 45 kDa membrane-
CC bound carboxy-terminal fragment 1 (CTF1), which is further cleaved by
CC gamma-secretase into a 35 kDa. Cleavage in neural stem cells by MMP24
CC affects CDH2-mediated anchorage of neural stem cells to ependymocytes
CC in the adult subependymal zone, leading to modulate neural stem cell
CC quiescence (By similarity). {ECO:0000250}.
CC -!- PTM: May be phosphorylated by OBSCN. {ECO:0000250|UniProtKB:P15116}.
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DR EMBL; AJ003143; CAA05899.1; -; mRNA.
DR AlphaFoldDB; O55075; -.
DR SMR; O55075; -.
DR STRING; 10029.XP_007637632.1; -.
DR eggNOG; KOG3594; Eukaryota.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
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:0010001; P:glial cell differentiation; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR030051; CDH2.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR PANTHER; PTHR24027:SF79; PTHR24027:SF79; 1.
DR Pfam; PF00028; Cadherin; 2.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 1.
DR SUPFAM; SSF49313; SSF49313; 3.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 3.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane; Glycoprotein;
KW Membrane; Metal-binding; Phosphoprotein; Repeat; Transmembrane.
FT CHAIN <1..>238
FT /note="Cadherin-2"
FT /id="PRO_0000126641"
FT TOPO_DOM <1..>238
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN <1..46
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 47..161
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 162..>238
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT BINDING 5
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 7
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 7
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 39
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 41
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 80
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 181
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 238
SQ SEQUENCE 238 AA; 26234 MW; C523220F9BC6FBAB CRC64;
TKPLDRELIA RFHLRAHAVD INGNRVENPI DIVINVIDMN DNRPEFLHQV WNGSVPEGSK
PGTYVMTVTA IDADDPNALN GMLRYRILSQ APSTPSPNMF TINNETGDII TVAAGLDREK
VQQYTLIIQA TDMEGNPTYG LSNTATAVIT VTDVNDNPPE FTAMTFYGEV PENRVEVIVA
NLTVTDKDQP HTPAWNAVYR ISGGDPTGRF AIHTDPNSND GLVTVVKPID FETNRMFV
