CADH1_XENLA
ID CADH1_XENLA Reviewed; 872 AA.
AC P30944; Q91709;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cadherin-1;
DE AltName: Full=Epithelial cadherin;
DE Short=E-cadherin;
DE AltName: Full=Uvomorulin;
DE AltName: Full=xTCAD-1;
DE Flags: Precursor;
GN Name=cdh1;
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].
RX PubMed=7600966; DOI=10.1242/dev.120.4.901;
RA Levine E., Lee C.H., Kintner C., Gumbiner B.M.;
RT "Selective disruption of E-cadherin function in early Xenopus embryos by a
RT dominant negative mutant.";
RL Development 120:901-909(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tail bud;
RX PubMed=8086449; DOI=10.1016/0167-4781(94)90254-2;
RA Tooi O., Fujii G., Tashiro K., Shiokawa K.;
RT "Molecular cloning of cDNA for XTCAD-1, a novel Xenopus cadherin, and its
RT expression in adult tissues and embryos of Xenopus laevis.";
RL Biochim. Biophys. Acta 1219:121-128(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 149-872.
RX PubMed=8081882; DOI=10.3109/15419069309097259;
RA Broders F., Girault J.M., Simonneau L., Thiery J.P.;
RT "Sequence and distribution of Xenopus laevis E-cadherin transcripts.";
RL Cell Adhes. Commun. 1:265-277(1993).
RN [4]
RP PROTEIN SEQUENCE OF 149-169.
RX PubMed=1879345; DOI=10.1242/dev.111.3.829;
RA Angres B., Mueller A.H.J., Kellermann J., Hausen P.;
RT "Differential expression of two cadherins in Xenopus laevis.";
RL Development 111:829-844(1991).
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. E-cadherin is a ligand for integrin alpha-
CC E/beta-7.
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Non-neural epithelial tissues.
CC -!- DEVELOPMENTAL STAGE: Appears in the embryonic ectoderm during
CC gastrulation when epidermal differentiation commences and it disappears
CC from the neural plate aera upon neural induction.
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}.
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DR EMBL; U04708; AAA93116.1; -; mRNA.
DR EMBL; L29057; AAA61489.1; -; mRNA.
DR EMBL; X75454; CAA53206.1; -; mRNA.
DR PIR; S47518; S47518.
DR RefSeq; NP_001165703.1; NM_001172232.1.
DR AlphaFoldDB; P30944; -.
DR SMR; P30944; -.
DR BioGRID; 1078961; 1.
DR IntAct; P30944; 1.
DR GeneID; 100337618; -.
DR KEGG; xla:100337618; -.
DR CTD; 100337618; -.
DR Xenbase; XB-GENE-6464305; cdh1.S.
DR OrthoDB; 182239at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 100337618; Expressed in intestine and 13 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; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR030049; CDH1.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR PANTHER; PTHR24027:SF319; PTHR24027:SF319; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Direct protein sequencing; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..148
FT /evidence="ECO:0000269|PubMed:1879345"
FT /id="PRO_0000003723"
FT CHAIN 149..872
FT /note="Cadherin-1"
FT /id="PRO_0000003724"
FT TOPO_DOM 149..701
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..722
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 723..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 148..256
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 257..370
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 371..481
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 482..589
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 605..688
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 739..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 552
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 631
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 242
FT /note="I -> V (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="N -> T (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 487
FT /note="E -> R (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 501..502
FT /note="AT -> CS (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 539..541
FT /note="GNG -> EMA (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="K -> R (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="V -> G (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="P -> L (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 602..604
FT /note="GFR -> EPQ (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 638..640
FT /note="GQS -> DK (in Ref. 2; AAA61489)"
FT /evidence="ECO:0000305"
FT CONFLICT 640..647
FT /note="SILELRPK -> VYLSSDL (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 660
FT /note="T -> A (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="A -> S (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="P -> S (in Ref. 2; AAA61489 and 3; CAA53206)"
FT /evidence="ECO:0000305"
FT CONFLICT 870..871
FT /note="DE -> GED (in Ref. 3; CAA53206)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 872 AA; 96065 MW; 08637967EEFB4664 CRC64;
MGLKRPWLLG AVVLLTLIQV QGGLAEWTQC RMGFSKEKYS FLVPKNLETD KALGRVIFNS
CEGPVRIQFA SKDPNFEIHK DGTVYIKNPA KMKDNRKTFR VLAWETKGHV YSTNITLKRE
GHRHRQDLFS GKHSHHPKSE TGLKRQKRDW VIPPIIVSEN EKGPFPKRIV QIKSSYAKEV
KVYYSITGQG ADTPPEGVFA IGREDGWLNV TRPLDREAID NYVLFSHAVS SNGANVEDPM
EIIIKVQDQN DNDPVFTQSV FEGSVPEGSK PGTAVMTVSA TDADDSVDMY NGVITYSILN
QEPKEPTNKM FTIHSESGLI SVLTTGLDRE KNPVYTLTIQ AADGEFGKDR TTTATALIVV
MDTNDNPPVF DPTQYTAKVP ENEVGYEVAR LTVTDEDIEG TDAWNAVYKI IKGNEANYFS
IQTDTGNIGL LKTVKGLDYE LKKQYILSVI VTNKANFSVP LQTSTATVTV SVEDVNEAPI
FLPPVKEVSV SEDLPSGQVV ATYTAQDPDK EQNQKITYVI GNDPAGWVSV NKDNGIVTGN
GNLDRESKFV LNNTYKVIIL AADSGSPSAT GTGTLVLNLL DVNDNGPFLE PQQESFCQKD
PGFRVFTIID RDLSPNTYPY KAELTGESNE NWTAIVTGQS ILELRPKKEL EIGQYDVMIT
LLDSFGLSNV TKLHITICQC DGDKMQCEEK AAIAGGLGIS AIVGILGGIL ALLLLLLLLL
LFVRRKKVVK EPLLPPEDET RDNVFSYDEE GGGEEDQDFD LSQLHRGLDA RPDVIRNDVA
PVLAAPQYRP RPANPDEIGN FIDENLNAAD NDPTAPPYDS LLVFDYEGSG SEAASLSSLN
SPNSDLDQDY SALNDWGPRF TKLADMYGGD ED
