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