CADH2_PONAB
ID CADH2_PONAB Reviewed; 906 AA.
AC Q5R9X1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Cadherin-2;
DE AltName: Full=Neural cadherin;
DE Short=N-cadherin;
DE AltName: CD_antigen=CD325;
DE Flags: Precursor;
GN Name=CDH2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 Plays a role in cell-to-cell junction formation between pancreatic beta
CC cells and neural crest stem (NCS) cells, promoting the formation of
CC processes by NCS cells (By similarity). CDH2 may be involved in
CC neuronal recognition mechanism. In hippocampal neurons, may regulate
CC dendritic spine density. {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 (By similarity). Colocalizes with
CC OBSCN at the intercalated disk and sarcolemma in cardiomyocytes (By
CC similarity). {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 N-terminal soluble fragment and a 45 kDa membrane-bound
CC C-terminal fragment 1 (CTF1), which is further cleaved by gamma-
CC secretase into a 35 kDa (By similarity). Cleavage in neural stem cells
CC by MMP24 affects CDH2-mediated anchorage of neural stem cells to
CC ependymocytes in the adult subependymal zone, leading to modulate
CC neural stem cell quiescence (By similarity).
CC {ECO:0000250|UniProtKB:P15116}.
CC -!- PTM: May be phosphorylated by OBSCN. {ECO:0000250|UniProtKB:P15116}.
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DR EMBL; CR859259; CAH91439.1; -; mRNA.
DR RefSeq; NP_001125845.1; NM_001132373.1.
DR AlphaFoldDB; Q5R9X1; -.
DR SMR; Q5R9X1; -.
DR STRING; 9601.ENSPPYP00000010197; -.
DR GeneID; 100172774; -.
DR KEGG; pon:100172774; -.
DR CTD; 1000; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q5R9X1; -.
DR OrthoDB; 191117at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; ISS:UniProtKB.
DR GO; GO:0005911; C:cell-cell junction; 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:0007043; P:cell-cell junction assembly; 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:0014032; P:neural crest cell development; ISS:UniProtKB.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR GO; GO:0003323; P:type B pancreatic cell development; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell junction; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..159
FT /evidence="ECO:0000250"
FT /id="PRO_0000042785"
FT CHAIN 160..906
FT /note="Cadherin-2"
FT /id="PRO_0000042786"
FT TOPO_DOM 160..724
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 725..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 746..906
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 160..267
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 268..382
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 383..497
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 498..603
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 604..710
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 863..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 864..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 228
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 260
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 293
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 295
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 301
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19022"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P19022"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 273
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 325
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 402
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 572
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 651
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 906 AA; 99838 MW; 63C8E35F0EFF47E8 CRC64;
MCRIAGALRT LLPLLAALLQ ASVEASGEIA LCKTGFPEDV YSAVLSKDVH EGQPLLNVKF
SNCNGKRKVQ YESSEPADFK VDEDGMVYAV RSFPLSSEHA KFLIYAQEEE TQEKWQVAVK
LSLKPTLTEE SVKESAEVEE IVFPRQFSKH SGHLQRQKRD WVIPPINLPE NSRGPFPQEL
VRIRSDRDKN LSLRYSVTGP GADQPPTGIF IINPISGQLS VTKPLDREQI ARFHLRAHAV
DINGNQVENP IDIVINVIDM NDNRPEFLHQ VWNGTVPEGS KPGTYVMTVT AIDADDPNAL
NGMLRYRILS QAPSTPSPNM FTINNETGDI ITVAAGLDRE KVQQYTLIIQ ATDMEGNPTY
GLSNTATAII TVTDVNDNPP EFTAMTFYGE VPENRVDVIV ANLTVTDKDQ PHTPAWNAVY
RISGGDPTGR FAIQTDPNSN DGLVTVVKPI DFETNRMFVL TVAAENQVPL AKGIQHPPQS
TATVSVTVID VNENPYFAPN PKIIRQEEGL HAGTMLTTFT AQDPDRYMQQ NIRYTKLSDP
ANWLKIDPVN GQITTIAVLD RESPNVKNNI YNATFLASDN GIPPMSGTGT LQIYLLDIND
NAPQVLPQEA ETCETPDPNS INITALDYDI DPNAGPFAFD LPLSPVTIKR NWTITRLNGD
FAQLNLKIKF LEAGIYEVPI IITDSGNPPK SNISILRVKV CQCDSNGDCT DVDRIVGAGL
GTGAIIAILL CIIILLILVL MFVVWMKRRD KERQAKQLLI DPEDDVRDNI LKYDEEGGGE
EDQDYDLSQL QQPDTVEPDA IKPVGIRRMD ERPIHAEPQY PVRSAAPHPG DIGDFINEGL
KAADNDPTAP PYDSLLVFDY EGSGSTAGSL SSLNSSSSGG EQDYDYLNDW GPRFKKLADM
YGGGDD
