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CADH4_RAT
ID   CADH4_RAT               Reviewed;         296 AA.
AC   Q63149;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Cadherin-4;
DE   AltName: Full=Retinal cadherin;
DE            Short=R-CAD;
DE            Short=R-cadherin;
DE   Flags: Fragment;
GN   Name=Cdh4;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Retina;
RA   Yanagita T.;
RT   "R-cadherin expression in the rat retina during postnatal development.";
RL   Submitted (JUL-1996) 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. May play an important role in retinal
CC       development.
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}.
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DR   EMBL; D86742; BAA13166.1; -; mRNA.
DR   AlphaFoldDB; Q63149; -.
DR   SMR; Q63149; -.
DR   GlyGen; Q63149; 2 sites.
DR   iPTMnet; Q63149; -.
DR   PhosphoSitePlus; Q63149; -.
DR   RGD; 621091; Cdh4.
DR   InParanoid; Q63149; -.
DR   PhylomeDB; Q63149; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR   GO; GO:0007411; P:axon guidance; ISO:RGD.
DR   GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR   GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISO:RGD.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISO:RGD.
DR   GO; GO:0045773; P:positive regulation of axon extension; ISO:RGD.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   PANTHER; PTHR24027; PTHR24027; 1.
DR   Pfam; PF00028; Cadherin; 3.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 2.
DR   SUPFAM; SSF49313; SSF49313; 3.
DR   PROSITE; PS00232; CADHERIN_1; 2.
DR   PROSITE; PS50268; CADHERIN_2; 3.
PE   2: Evidence at transcript level;
KW   Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW   Metal-binding; Reference proteome; Repeat; Transmembrane.
FT   CHAIN           <1..>296
FT                   /note="Cadherin-4"
FT                   /id="PRO_0000126644"
FT   TOPO_DOM        <1..>296
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          <1..101
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          102..216
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          217..>296
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   CARBOHYD        107
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        236
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
FT   NON_TER         296
SQ   SEQUENCE   296 AA;  32912 MW;  722FBC3C0A463FE8 CRC64;
     NVPENSRGPF PQQLVRIRSD KDNDIPIRYS ITGVGADQPP MEVFNIDSMS GRMYVTRPMD
     REERASYHLR AHAVDMNGNK VENPIDLYIY VIDMNDNRPE FINQVYNGSV DEGSKPGTYV
     MTVTANDADD STTANGMVRY RIVTQTPQSP SQNMFTINSE TGDIVTVAAG LDREKVQQYT
     VIVQATDMEG NLNYGLSNTA TAIITVTDVN DNPPEFTTST FAGEVPENRI ETVVANLTVM
     DRDQPHSPNW NAVYRIISGD PSGHFSVRTD PVTNEGMVTV VKAVDYELNR AFMLTI
 
 
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