CADH4_CHICK
ID CADH4_CHICK Reviewed; 913 AA.
AC P24503;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cadherin-4;
DE AltName: Full=Retinal cadherin;
DE Short=R-CAD;
DE Short=R-cadherin;
DE Flags: Precursor;
GN Name=CDH4;
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 TISSUE=Retina;
RX PubMed=1712604; DOI=10.1016/0896-6273(91)90075-b;
RA Inuzuka H., Miyatani S., Takeichi M.;
RT "R-cadherin: a novel Ca(2+)-dependent cell-cell adhesion molecule expressed
RT in the retina.";
RL Neuron 7:69-79(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. May play an important role in retinal
CC development.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Embryonic brain and neuronal retina.
CC -!- DEVELOPMENTAL STAGE: Detected only after some degree of neuronal
CC differentiation has taken place and persists at least up to the newly
CC hatched stage.
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; D14459; BAA03356.1; -; mRNA.
DR PIR; JH0424; IJCHCR.
DR RefSeq; NP_001004391.1; NM_001004391.1.
DR AlphaFoldDB; P24503; -.
DR SMR; P24503; -.
DR STRING; 9031.ENSGALP00000008166; -.
DR PaxDb; P24503; -.
DR GeneID; 419222; -.
DR KEGG; gga:419222; -.
DR CTD; 1002; -.
DR VEuPathDB; HostDB:geneid_419222; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; P24503; -.
DR OrthoDB; 191117at2759; -.
DR PhylomeDB; P24503; -.
DR PRO; PR:P24503; -.
DR Proteomes; UP000000539; Unplaced.
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; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
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..19
FT /evidence="ECO:0000255"
FT PROPEP 20..166
FT /evidence="ECO:0000255"
FT /id="PRO_0000003753"
FT CHAIN 167..913
FT /note="Cadherin-4"
FT /id="PRO_0000003754"
FT TOPO_DOM 167..731
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 732..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..913
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 167..274
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 275..389
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 390..504
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 505..610
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 611..721
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 652
FT /note="P -> T (in one form)"
SQ SEQUENCE 913 AA; 100886 MW; BD2BB9ECC815DDD6 CRC64;
MRTGSRLLLV LLVWGSAAAL NGDLTVRPTC KPGFSEEDYT AFVSQNIMEG QKLLKVKFNN
CAGNKGVRYE TNSLDFKVRA DGTMYAVHQV QMASKQLILM VTAWDPQTLG RWEAIVRFLV
GEKLQHNGHK PKGRKSGPVD LAQQQSDTLL PWRQHQSAKG LRRQKRDWVI PPINVPENSR
GPFPQQLVRI RSDKDKEIHI RYSITGVGAD QPPMEVFSID PVSGRMYVTR PMDREERASY
HLRAHAVDMN GNKVENPIDL YIYVIDMNDN RPEFINQVYN GSVDEGSKPG TYVMTVTAND
ADDSTTANGM VRYRIVTQTP QSPSQNMFTI NSETGDIVTV AAGLDREKVQ QYMVIVQATD
MEGNLNYGLS NTATAIITVT DVNDNPPEFT TSTYSGEVPE NRVEVVVANL TVMDRDQPHS
PNWNAIYRII SGDPSGHFTI RTDPVTNEGM VTVVKAVDYE MNRAFMLTVM VSNQAPLASG
IQMSFQSTAG VTISVTDVNE APYFPTNHKL IRLEEGVPTG TVLTTFSAVD PDRFMQQAVR
YSKLSDPANW LNINATNGQI TTAAVLDRES DYIKNNVYEA TFLAADNGIP PASGTGTLQI
YLIDINDNAP ELLPKEAQIC EKPNLNVINI TAADADIDPN VGPFVFELPS VPSAVRKNWT
ITRLNGDYAQ LSLRIMYLEA GVYDVPIIVT DSGNPPLYNT SIIKVKVCPC DENGDCTTIG
AVAAAGLGTG AIIAILICII ILLTMVLLFV VWMKRREKER HTKQLLIDPE DDVRDNILKY
DEEGGGEEDQ DYDLSQLQQP ETMDHVLNKA PGVRRVDERP IGAEPQYPIR PVIPHPGDIG
DFINEGLRAA DNDPTAPPYD SLLVFDYEGS GSTAGSVSSL NSSSSGDQDY DYLNDWGPRF
KKLADMYGGG EED
