CADH6_CHICK
ID CADH6_CHICK Reviewed; 790 AA.
AC Q90762;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cadherin-6;
DE AltName: Full=Cadherin-6B;
DE Short=c-cad6B;
DE Flags: Precursor;
GN Name=CDH6;
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], AND DEVELOPMENTAL STAGE.
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 {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: First expressed in splanchnic mesoderm of stage 4
CC embryos. At stage 6, strongly expressed along the neural fold in a
CC region corresponding to the future neural crest. Expression in the
CC neural fold continues during closure of the neural tube but diminishes
CC after neural crest cells have left the neural tube.
CC {ECO:0000269|PubMed:7540531}.
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; D42149; BAA07720.1; -; mRNA.
DR PIR; I50178; I50178.
DR RefSeq; NP_001001758.1; NM_001001758.2.
DR AlphaFoldDB; Q90762; -.
DR SMR; Q90762; -.
DR STRING; 9031.ENSGALP00000030382; -.
DR PaxDb; Q90762; -.
DR Ensembl; ENSGALT00000031019; ENSGALP00000030382; ENSGALG00000012917.
DR GeneID; 414842; -.
DR KEGG; gga:414842; -.
DR CTD; 1004; -.
DR VEuPathDB; HostDB:geneid_414842; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000154673; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q90762; -.
DR OMA; TRKTRYN; -.
DR OrthoDB; 201053at2759; -.
DR PhylomeDB; Q90762; -.
DR TreeFam; TF329887; -.
DR Reactome; R-GGA-418990; Adherens junctions interactions.
DR PRO; PR:Q90762; -.
DR Proteomes; UP000000539; Chromosome 2.
DR Bgee; ENSGALG00000012917; Expressed in brain and 4 other tissues.
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:0005654; C:nucleoplasm; IEA:Ensembl.
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: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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
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..30
FT /evidence="ECO:0000255"
FT PROPEP 31..53
FT /evidence="ECO:0000255"
FT /id="PRO_0000003767"
FT CHAIN 54..790
FT /note="Cadherin-6"
FT /id="PRO_0000003768"
FT TOPO_DOM 54..615
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 637..790
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 REGION 261..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 790 AA; 88660 MW; 0FD3756749DB5CC5 CRC64;
MRTYHCFWLL FWAGQPHQSF LTLLSKRTSG FPEKEKVLVL SGNSRRDLSR SKRSWMWNQF
FLLEEYTGTD YQYVGKLHSD QDKGDGSLKY ILSGDGAGDL FIINENTGDI QATKRLDREE
KPVYILRAQA INRRTGRPVE PESEFIIKIH DINDNEPMFT KDVYNASIPE MSDVGTFVVQ
VTATDADDPT YGNSAKVVYS ILQGQPYFSV ESETGIIKTA LLNMDRENRE QYQVVIQAKD
MGGQMGGLSG TTTVNITLTD VNDNPPRFPQ STYQFRAPES TPPDSPIGRI KANDADVDEN
AEIEYSITEG DGYDMFGITT DKDTQEGIIT VKKALDFENK NLYILKVEAT NTHVDPRFLY
LGPFKDSATI RIQVEDVDEP PVFSRPAYII EVKEDVPINS VIGTVTAQDP DAAKNPVKYS
VDRHTDMDRV FNINSGNGSI FTSKTLDRET LLWHNITVIA AEINNPKQSS RVPVFIKVLD
VNDNAPEFAM FYETFVCENA KAEQLIQTLS AVDKDDSYSG HQFSFSIAPE AASSSNFTLQ
DNRDNTAGIF TRKIRYNRHE MSTYLLPVVI SDNDYPIQSS TETVTIRVCA CDHRGKMLSC
NAEALIHPTG LSTGALIAIL LCIIILLVTV VLFAALRRQR KKEPLIISKE DIRDNIVSYN
DEGGGEEDTQ AFDIGTLRNP EAIDDNKLRR DIVPETLFMP RRTATARDNT DVRDFINQRL
KENDTDPAAP PYDSLATYAY EGNGSVAESL SSLESVTTDG DQDYDYLSDW GPRFKKLADM
YGSMDSDKDS
