CAD20_XENLA
ID CAD20_XENLA Reviewed; 790 AA.
AC Q91838;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cadherin-20;
DE AltName: Full=F-cadherin;
DE Flags: Precursor;
GN Name=cdh20;
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 TISSUE SPECIFICITY.
RC TISSUE=Neurula;
RX PubMed=7496627; DOI=10.1006/mcne.1995.1017;
RA Espeseth A., Johnson E., Kintner C.;
RT "Xenopus F-cadherin, a novel member of the cadherin family of cell adhesion
RT molecules, is expressed at boundaries in the neural tube.";
RL Mol. Cell. Neurosci. 6:199-212(1995).
RN [2]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9486803; DOI=10.1242/dev.125.2.301;
RA Espeseth A., Marnellos G., Kintner C.;
RT "The role of F-cadherin in localizing cells during neural tube formation in
RT Xenopus embryos.";
RL Development 125:301-312(1998).
CC -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC preferentially interact with themselves in a homophilic manner in
CC connecting cells; cadherins may thus contribute to the sorting of
CC heterogeneous cell types. {ECO:0000269|PubMed:9486803}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic posterior neural plate,
CC embryonic neural tube, sulcus limitans and embryonic kidney.
CC {ECO:0000269|PubMed:7496627, ECO:0000269|PubMed:9486803}.
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. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X85330; CAA59679.1; -; mRNA.
DR PIR; I51638; I51638.
DR RefSeq; NP_001131054.1; NM_001137582.1.
DR AlphaFoldDB; Q91838; -.
DR SMR; Q91838; -.
DR GeneID; 100192361; -.
DR KEGG; xla:100192361; -.
DR CTD; 100192361; -.
DR Xenbase; XB-GENE-1011623; cdh20.L.
DR OrthoDB; 217088at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 100192361; Expressed in brain and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; 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; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..52
FT /evidence="ECO:0000255"
FT /id="PRO_0000340245"
FT CHAIN 53..790
FT /note="Cadherin-20"
FT /id="PRO_0000340246"
FT TOPO_DOM 26..612
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..633
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 634..790
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..158
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 159..267
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 268..382
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 383..487
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 487..605
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 790 AA; 88506 MW; C944348A20208A75 CRC64;
MSCKRSYHRH CALVYYMVLL DLTNAVFEFS HPLIRDSGNS QSRQLLHHRL KRSWVWNQFF
VLEEYTGTEP LYVGKLHSDM DKGEGSITYI LSGDGAGTMF TIDETTGDIH AIQRLDREER
SQYTLKAQAL DRRTTRPMEP ESEFIVKIQD INDNEPKFLD GPYTASVPEM SPVGTSIIQV
SATDADDPTY GSSARVVYSI LQGQPYFSVD SKTGIIRTAL TNMDRESRDY YEVIIQAKDM
GGQLGGLAGT TTVNVTLSDV NDNPPRFPQK HYQMSVLESL LINSTVGRVL AMDLDEGVNA
EMKYNIIDGD EFEVFDIVTD PSNQVGVITV KKPLDFETKK SYTLKIEGSN AHLEIRFLNL
GPFRDTTSVH ITVEDVDEPP VFGSSFYFVE VSENVDIGTT IQIVSAKDPD ATNNSVRYSI
DRSSDPGRYF YVDVTTGALM TARPLDREEV SWHNITILAM EMNNPAQIGG VPVTIKVLDV
NDNAPTFTKF SETLMCENAK ADQLIQTVSA VDQDDPQEGQ HISYSLAPDA ANNPNFTLRD
NQDNTAWILT RRPGFKQSEQ STFYLPLLIS DNGNPRLSST GTLTIQVCSC DKDGDIMSCN
AEPYTLPISL SRGALIAILT CIFVLLVLVL LILSMRRHRK QPYTIDEEDN VHENIVRYDD
EGGGEEDTEA FDIAALWNPR EAHMGKTRQD MKPEIESLSR YVTQTCRMDN NVHSYMLAKL
YEADTDVCAP PFDSLQTYMF EGEGSVAHSL SSLQSLSTDS EQSYDYLSDW GPRFKKLAEM
YGTKDNNGSL
