CADHF_XENLA
ID CADHF_XENLA Reviewed; 880 AA.
AC P33148; Q91543;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=EP-cadherin;
DE AltName: Full=C-cadherin;
DE Flags: Precursor;
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=1893866; DOI=10.1242/dev.111.2.315;
RA Ginsberg D., Desimone D., Geiger B.;
RT "Expression of a novel cadherin (EP-cadherin) in unfertilized eggs and
RT early Xenopus embryos.";
RL Development 111:315-325(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee C.H.;
RL Thesis (1994), University of California San Francisco, United States.
RN [3]
RP SEQUENCE REVISION TO 260.
RA Flament S.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 156-176.
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).
RN [5]
RP INTERACTION WITH CTNNB1.
RX PubMed=17052462; DOI=10.1016/j.molcel.2006.09.001;
RA Sampietro J., Dahlberg C.L., Cho U.S., Hinds T.R., Kimelman D., Xu W.;
RT "Crystal structure of a beta-catenin/BCL9/Tcf4 complex.";
RL Mol. Cell 24:293-300(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 156-695, CALCIUM-BINDING SITES,
RP AND GLYCOSYLATION AT THR-343; THR-382; THR-400; ASN-425; THR-428; THR-469;
RP THR-471; THR-473; THR-475; ASN-558; THR-562; THR-576; THR-578; THR-580 AND
RP ASN-681.
RX PubMed=11964443; DOI=10.1126/science.1071559;
RA Boggon T.J., Murray J., Chappuis-Flament S., Wong E., Gumbiner B.M.,
RA Shapiro L.;
RT "C-cadherin ectodomain structure and implications for cell adhesion
RT mechanisms.";
RL Science 296:1308-1313(2002).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 156-695.
RX PubMed=14526082; DOI=10.1126/science.1086957;
RA He W., Cowin P., Stokes D.L.;
RT "Untangling desmosomal knots with electron tomography.";
RL Science 302:109-113(2003).
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.
CC -!- SUBUNIT: Interacts with CTNNB1. {ECO:0000269|PubMed:17052462}.
CC -!- INTERACTION:
CC P33148; Q02248: Ctnnb1; Xeno; NbExp=4; IntAct=EBI-15603953, EBI-397872;
CC P33148; Q23993: nmo; Xeno; NbExp=4; IntAct=EBI-15603953, EBI-876224;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- DEVELOPMENTAL STAGE: Unfertilized eggs and early Xenopus embryos.
CC -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC cadherin domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA45252.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X63720; CAA45252.1; ALT_INIT; mRNA.
DR EMBL; U04707; AAC16910.1; -; mRNA.
DR PIR; B43785; IJXLCP.
DR RefSeq; NP_001080946.1; NM_001087477.1.
DR PDB; 1L3W; X-ray; 3.08 A; A=156-695.
DR PDBsum; 1L3W; -.
DR AlphaFoldDB; P33148; -.
DR SMR; P33148; -.
DR DIP; DIP-59585N; -.
DR IntAct; P33148; 4.
DR iPTMnet; P33148; -.
DR GeneID; 394290; -.
DR KEGG; xla:394290; -.
DR CTD; 394290; -.
DR Xenbase; XB-GENE-6254663; cdh3.S.
DR OrthoDB; 182239at2759; -.
DR EvolutionaryTrace; P33148; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 394290; Expressed in blastula and 16 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 PANTHER; PTHR24027; PTHR24027; 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 3D-structure; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Membrane; Metal-binding; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT PROPEP 29..155
FT /evidence="ECO:0000255"
FT /id="PRO_0000003725"
FT CHAIN 156..880
FT /note="EP-cadherin"
FT /id="PRO_0000003726"
FT TOPO_DOM 156..703
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..728
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 729..880
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 156..263
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 264..376
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 377..487
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 488..593
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 594..704
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 790..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 382
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 400
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 428
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 469
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 471
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 473
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 475
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 562
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 576
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 578
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 580
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT CARBOHYD 681
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:11964443"
FT DISULFID 603..687
FT DISULFID 685..694
FT CONFLICT 3
FT /note="S -> G (in Ref. 2; AAC16910)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="I -> N (in Ref. 2; AAC16910)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="K -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="R -> K (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="L -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 573
FT /note="S -> P (in Ref. 2; AAC16910)"
FT /evidence="ECO:0000305"
FT CONFLICT 864
FT /note="S -> P (in Ref. 2; AAC16910)"
FT /evidence="ECO:0000305"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:1L3W"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:1L3W"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:1L3W"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 214..217
FT /evidence="ECO:0007829|PDB:1L3W"
FT TURN 223..225
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 228..240
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 247..254
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 268..273
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 278..284
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 303..310
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 317..320
FT /evidence="ECO:0007829|PDB:1L3W"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:1L3W"
FT TURN 336..338
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 341..349
FT /evidence="ECO:0007829|PDB:1L3W"
FT HELIX 350..353
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 357..359
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 379..389
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 393..397
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 424..428
FT /evidence="ECO:0007829|PDB:1L3W"
FT TURN 430..432
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 435..441
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 458..461
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 472..479
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 486..489
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 502..508
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 522..526
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 535..537
FT /evidence="ECO:0007829|PDB:1L3W"
FT TURN 538..541
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 562..569
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 571..573
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 579..582
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 604..606
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 610..614
FT /evidence="ECO:0007829|PDB:1L3W"
FT TURN 620..623
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 634..637
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 646..652
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 665..667
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 670..672
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:1L3W"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:1L3W"
SQ SEQUENCE 880 AA; 97651 MW; C6CCD91566427D86 CRC64;
MGSTRLRNAS VWLCGLLCLL QVVPSINADV SGCKPGFSSA EYIFSVNRRE LERGRKLGKV
NFSDCTTRKH GLYDVGDSRF RVLPDGTVLV KRHVKLHKDT KFTISTWDAR GIKHSTNIAV
ASKRHRSGEE AHSRSSKLPV LTFPETHTGL KRKKRDWVIP PIKVSENERG PFPKRLVQIK
SNKDRFNKVY YSITGQGADN PPQGVFRIEW ETGWMLVTRP LDREEYDKYV LSSHAVSENG
SPVEEPMEIT INVIDQNDNR PKFTQDVFRG SVREGVQPGT QVMAVSATDE DDNIDSLNGV
LSYSILKQDP EEPIPNLFTI NRETGVISLI GTGLDREKFP EYTLTVQATD LEGAGLSVEG
KAIIQITDAN DNAPIFDPKT YTALVPENEI GFEVQRLSVT DLDMPGTPAW QAVYKIRVNE
GGFFNITTDP ESNQGILTTA KGLDFELRKQ YVLQITVENA EPFSVPLPTS TATVTVTVED
VNEAPFFVPA VSRVDVSEDL SRGEKIISLV AQDPDKQQIQ KLSYFIGNDP ARWLTVNKDN
GIVTGNGNLD RESEYVKNNT YTVIMLVTDD GVSVGTGTGT LILHVLDVND NGPVPSPRVF
TMCDQNPEPQ VLTISDADIP PNTYPYKVSL SHGSDLTWKA ELDSKGTSML LSPTQQLKKG
DYSIYVLLSD AQNNPQLTVV NATVCSCEGK AIKCQEKLVG GFDLPIILVI LGSVLALLIL
FLLLLLFLKR KKVVKEPLLL PEDDTRDNIF YYGEEGGGEE DQDYDLSQLH RGLDSRPDIM
RNDVVPTLMP APHYRPRPSN PDEIGNFIDE NLDAADNDPT APPYDSLLVF DYEGSGSEAA
SLSSLNSSNS NDEHDYNYLS DWGSRFRKLA DMYGGDDDEE
