CAD2B_XENLA
ID CAD2B_XENLA Reviewed; 905 AA.
AC P20310;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cadherin-2B;
DE AltName: Full=Neural cadherin B;
DE Short=N-cadherin B;
DE AltName: Full=Neural cadherin-1;
DE Short=N-cadherin-1;
DE Flags: Precursor;
GN Name=cdh2-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=2322458; DOI=10.1016/0896-6273(90)90108-r;
RA Detrick R.J., Dickey D., Kintner C.R.;
RT "The effects of N-cadherin misexpression on morphogenesis in Xenopus
RT embryos.";
RL Neuron 4:493-506(1990).
CC -!- FUNCTION: Calcium-dependent cell adhesion protein; preferentially
CC mediates homotypic cell-cell adhesion. Cadherins may thus contribute to
CC the sorting of heterogeneous cell types, and thereby play an important
CC role during embryonic development. {ECO:0000305|PubMed:2322458}.
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}. Cell membrane,
CC sarcolemma {ECO:0000250|UniProtKB:P15116}. Cell junction
CC {ECO:0000250|UniProtKB:P15116}. Cell surface
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}.
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DR PIR; JQ0442; IJXLC1.
DR AlphaFoldDB; P20310; -.
DR SMR; P20310; -.
DR PRIDE; P20310; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
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: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 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 Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..160
FT /evidence="ECO:0000255"
FT /id="PRO_0000003741"
FT CHAIN 161..905
FT /note="Cadherin-2B"
FT /id="PRO_0000003742"
FT TOPO_DOM 161..723
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..745
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 746..905
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 161..268
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 269..383
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 384..498
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 499..604
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 605..713
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 774..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 171
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 229
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="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 263
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 263
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="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 294
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 302
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P15116"
FT CARBOHYD 191
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 274
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 573
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 623
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 905 AA; 100549 MW; AE27EE830215FAAD CRC64;
MCRKQPFLLP TLLGILAALM LQQGPVEAFG GSRLCKTGFL EDVYHASVYR SVHEGQPLLN
VMFTDCGTDR RIQYETSNPT DFRIDGDGIV FASRTFDISP EQAEFLVYAQ DEDTRELWHV
TVKITLRPPH EHHSHQGFHK VREIKFSTQR NSNGLQRQKR DWVIPPINVP ENARGTFPQE
LVRIRSDRDK NLSLRYSVTG PGADQPPIGV FIINPIGGQL SVTKPLDREQ IANFHLRAHA
VDVNGNQVEN PIDIVINVID MNDNRPEFLH QIWNGSIPEG SKPGTYVMTV TAIDGDDPKQ
PNGMLRYKIL SQTPAISSPN MFTINNETGD IITLAAGLDR EKVQRYTLII QATDMEGNPT
YGLSNTATAV IAVTDVNDNP PEFTAMTFYG EVPENRVDVV VANLTVTDKD QPHTPAWNAV
YRIVGGDGTG RFAIKTDANS NDGLVTVVKP IDYETKSTYI LTVVAENQVD LIRGIQFKPE
STATVSVTVI DVNENPYFTP NPKLIRQEEG LFASKMLTTF SAQDPDRYMQ QTIRYSKLSD
PANWLKIDPV NGLITTTAVL DRESMYVKNN MYNATFLATD SGIPPMSGTG TLQIYLLDIN
DNAPYVYPQE VEICERPDPN AINITALDAD INPNSGPFIF ELPYSPMDIK NWTVTRLSGD
HAQLSLKIGS LDYGIYNIPI HITDSGNPAM SNTSYLRVKV CSCEHEYCST TAPIIGTGLG
TGAIIAILLC IIILLTLVLM FVVWMKRRDK ERQAKQLLID PEDDVRDNIL KYDEEGGGEE
DQDYDLSQLQ QPDTMEPDTI KPVGIRRMDE RPIHAEPQYP IRSAAPHPGD IGDFINEGLK
AADNDPTAPP YDSLLVFDYE GSGSTAGSLS SLNSSSSGGE QDYDYLNDWG PRFKKLADMY
GGSDD
