CADH6_BOVIN
ID CADH6_BOVIN Reviewed; 790 AA.
AC Q3SWX5;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Cadherin-6;
DE Flags: Precursor;
GN Name=CDH6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) 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 (By similarity). {ECO:0000250}.
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; BC104618; AAI04619.1; -; mRNA.
DR RefSeq; NP_001029812.1; NM_001034640.2.
DR RefSeq; XP_010815116.1; XM_010816814.2.
DR AlphaFoldDB; Q3SWX5; -.
DR SMR; Q3SWX5; -.
DR STRING; 9913.ENSBTAP00000017274; -.
DR PaxDb; Q3SWX5; -.
DR PRIDE; Q3SWX5; -.
DR Ensembl; ENSBTAT00000017274; ENSBTAP00000017274; ENSBTAG00000012992.
DR GeneID; 537946; -.
DR KEGG; bta:537946; -.
DR CTD; 1004; -.
DR VEuPathDB; HostDB:ENSBTAG00000012992; -.
DR VGNC; VGNC:27105; CDH6.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000154673; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q3SWX5; -.
DR OMA; TRKTRYN; -.
DR OrthoDB; 201053at2759; -.
DR TreeFam; TF329887; -.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000012992; Expressed in adult mammalian kidney and 85 other tissues.
DR ExpressionAtlas; Q3SWX5; baseline and differential.
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; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..53
FT /evidence="ECO:0000255"
FT /id="PRO_0000285118"
FT CHAIN 54..790
FT /note="Cadherin-6"
FT /id="PRO_0000285119"
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..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97326"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97326"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 399
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; 88309 MW; C59941C62DB57C4A CRC64;
MRTYRYFLLL FWVGQPYPTF STPLSKRTSG FPAKKRTLEL SGNSKNELSR SKRSWMWNQF
FLLEEYTGSD YQYVGKLHSD QDRGDGSLKY ILSGDGAGDL FIINENTGDI QATKRLDREE
KPVYILRAQA INRKTGRPVE PESEFIIKIH DINDNEPIFT KEVYTATVPE MSDVGTFVVQ
VTATDADDPT YGNSAKVVYS ILQGQPYFSV ESETGIIKTA LLNMDRENRE QYQVVIQAKD
MGGQMGGLSG TTTVNITLTD VNDNPPRFPQ STYQFKTPES SPPGTPIGRI KASDADVGEN
AEIEYSITEG EGLDMFDVIT DQETQEGIIT VKKLLDFEKK KVYTLKVEAS NPHVEPRFLY
LGPFKDSATV RIMVEDVDEP PVFSKLAYIL QIREDAQINT TIGSVTAQDP DAARNPVKYS
VDRHTDMDRI FNIDSGNGSI FTSKLLDRET LLWHNITVIA TEINNPKQSS RVPLYIKVLD
VNDNPPEFAE FYETFVCEKA KADQLIQTLR AIDKDDPYSG HQFSFSLAPE AASGSNFTIQ
DNKDNTAGIF TRKNGYNRHE MSTYLLPVVI SDNDYPVQSS TGTVTVRVCA CDHQGNMQSC
HAEALVHPTG LSTGALIAIL LCIVTLLVTV VLFAALRRQR KKEPLIISKE DIRDNIVSYN
DEGGGEEDTQ AFDIGTLRNP EAIEDSKLRR DIVPEALFLP RRTPAARDNT DVRDFINQRL
KENDTDPTAP PYDSLATYAY EGAGSVADSL SSLESVTTDG DQDYDYLSDW GPRFKKLADM
YGGVDSDKDS
