CAD11_CHICK
ID CAD11_CHICK Reviewed; 792 AA.
AC O93319;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Cadherin-11;
DE Flags: Precursor;
GN Name=CDH11;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=White leghorn;
RA Wei J., Dong X.R., Topouzis S., Zimmer W.E., Broders F., Thiery J.P.,
RA Koteliansky V., Majesky M.W.;
RT "Molecular cloning of chick cadherin 11 and its expression during smooth
RT muscle differentiation and formation of the tunica media.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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; AF055342; AAC33675.1; -; mRNA.
DR RefSeq; NP_001004371.1; NM_001004371.1.
DR AlphaFoldDB; O93319; -.
DR SMR; O93319; -.
DR STRING; 9031.ENSGALP00000008451; -.
DR PaxDb; O93319; -.
DR GeneID; 415797; -.
DR KEGG; gga:415797; -.
DR CTD; 1009; -.
DR VEuPathDB; HostDB:geneid_415797; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; O93319; -.
DR OrthoDB; 188978at2759; -.
DR PhylomeDB; O93319; -.
DR PRO; PR:O93319; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; IDA:AgBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0008013; F:beta-catenin binding; NAS:AgBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; NAS:AgBase.
DR GO; GO:0098609; P:cell-cell adhesion; IMP:AgBase.
DR GO; GO:0030199; P:collagen fibril organization; IMP:AgBase.
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..22
FT /evidence="ECO:0000255"
FT PROPEP 23..53
FT /evidence="ECO:0000255"
FT /id="PRO_0000003789"
FT CHAIN 54..792
FT /note="Cadherin-11"
FT /id="PRO_0000003790"
FT TOPO_DOM 54..613
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 614..634
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..792
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 54..159
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 160..268
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 269..383
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 384..486
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 487..608
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 792 AA; 87573 MW; 3E3488C6686731AB CRC64;
MKEDNCLHAA LICLGMLYYS HAITTEKLNH VRPSLHGHHE KGKEGQVLHR SKRGWVWNQF
FVIEEYTGPD PVLVGRLHSD IDSGDGNIKY ILSGEGAGII FVIDDKSGNI HATKTLDREE
RAQYTLTAQA VDRNTNRPLE PPSEFIVKVQ DINDNPPEFL HENYHANVPE RSNVGTSVIQ
VTASDADDPT YGNSAKLVYS ILEGQPYFSV EAQTGIIRTA LPNMDREAKE EYHVVIQAKD
MGGHMGGLSG TTKVTITLTD VNDNPPKFPQ SVYQMSVSEA AVPGEEVGRV KAKDPDIGEN
GLVAYSIIDG DGMDMFEITT DYETQEGVVK LKKVLDFETK KSYSLKVEAA NVHIDPKFIS
NGPFKDTVTV KITVEDADEP PVFLKPSYIF EVQENAASGT VVGKVHAKDP DAANSAIRYS
IDRHTDLERY FTINADDGNI KTIKALDREE IAWHNISVFA VEVHKQHQEA KVPVAIKVVD
VNDNAPKFAA AYEAFVCENA RSNQQFITIS ADDKDDSANG PRFIFSLPPE IIHNPNFSLR
DNRDNTASVL VRREGFSRQK QDLYLLPIVI SDGGLPPMSS TNTLTIRVCG CDSNGSLLSC
NAEAYILNAG LSTGALIAIL ACIVILLVIV VLFVTLKRQK KEPLIVFEEE DVRENIITYD
DEGGGEEDTE AFDIATLQNP DGINGFIPRK DIKPEYQYMP RPGLRPAPNS VDVDDFINTR
IQEADNDPTA PPYDSIQIYG YEGRGSVAGS LSSLESATTD SDLDYDYLQN WGPRFKKLAD
LYGSKDTFDD DS
