CADH7_CHICK
ID CADH7_CHICK Reviewed; 785 AA.
AC Q90763;
DT 24-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Cadherin-7;
DE Flags: Precursor;
GN Name=CDH7;
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; TISSUE=Brain;
RX PubMed=7540531; DOI=10.1242/dev.121.5.1321;
RA Nakagawa S., Takeichi M.;
RT "Neural crest cell-cell adhesion controlled by sequential and
RT subpopulation-specific expression of novel cadherins.";
RL Development 121:1321-1332(1995).
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; Single-pass type I membrane
CC protein.
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; D42150; BAA07721.1; -; mRNA.
DR PIR; I50180; I50180.
DR RefSeq; NP_989518.2; NM_204187.2.
DR AlphaFoldDB; Q90763; -.
DR SMR; Q90763; -.
DR STRING; 9031.ENSGALP00000022341; -.
DR PaxDb; Q90763; -.
DR GeneID; 374007; -.
DR KEGG; gga:374007; -.
DR CTD; 1005; -.
DR VEuPathDB; HostDB:geneid_374007; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q90763; -.
DR OrthoDB; 217088at2759; -.
DR PhylomeDB; Q90763; -.
DR PRO; PR:Q90763; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IBA:GO_Central.
DR GO; GO:0001502; P:cartilage condensation; IMP:AgBase.
DR GO; GO:0016477; P:cell migration; IMP:AgBase.
DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0060591; P:chondroblast differentiation; IEP:AgBase.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0060173; P:limb development; IEP:AgBase.
DR GO; GO:0036032; P:neural crest cell delamination; IMP:AgBase.
DR GO; GO:0001841; P:neural tube formation; IMP:AgBase.
DR GO; GO:0042060; P:wound healing; IMP:AgBase.
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..27
FT /evidence="ECO:0000255"
FT PROPEP 28..47
FT /evidence="ECO:0000255"
FT /id="PRO_0000003771"
FT CHAIN 48..785
FT /note="Cadherin-7"
FT /id="PRO_0000003772"
FT TOPO_DOM 48..607
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 629..785
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 49..153
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 154..262
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 263..377
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 378..482
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 482..599
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 449
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 785 AA; 87172 MW; 895B06D8141E34D4 CRC64;
MKLGKVEFCH LLQIIALFLC LSGMNQAEPS RSRSKPYFQS GRTRTKRSWV WNQFFVLEEY
MGSDPLYVGK LHSDVDKGDG SIKYILSGEG ASSIFIIDEN TGDIHATKRL DREEQAYYTL
RAQAHDRLTN KPVEPESEFV IKIQDINDNE PKFLDGPYTA GVPEMSPVGT SVVQVTATDA
DDPTYGNSAR VVYSILQGQP YFSVEPKTGI IKTALPNMDR EAKDQYLLVI QAKDMVGQNG
GLSGTTSVTV TLTDVNDNPP RFPRRSYQYN VPESLPLASV VARIKAADAD VGPNAEMEYK
IVDGDGLGVF KISVDKDTQE GIITIQKELD FEAKTSYTLR IEAANMHVDP RFLSLGPFSD
MTTVKIIVED VDEPPVFTSR LYSMVVSEAA KVGTIIGTVA AHDPDASNSP VRYSIDRNTD
LERYFNIDAN SGVITTAKSL DRETNAVHNI TVLAMESQNP AQIGRGYVAI TILDINDNAP
EFAMEYETTV CENAQPGQII QKISAIDKDD PPNGHQFYFS LTAEAANNHN FTLQDNKDNT
ATVLTRRNGF RRQEQSVFYL PIFIVDSGSP SLSSTNTLTI RVCDCDADGI AQTCNAEAYI
LPAGLSTGAL IAILACVLTL LVLVLLIVTM RRRKKEPLIF DEERDIRENI VRYDDEGGGE
EDTEAFDMAA LRNLNIIRDT KTRRDVTPEI QFLSRPTFKS IPDNVIFREF IWERLKEADV
DPCAPPYDSL QTYAFEGNGS VAESLSSLDS ISSNSDQNYD YLSDWGPRFK RLADMYGSGP
DCLYS
