CADH6_MOUSE
ID CADH6_MOUSE Reviewed; 790 AA.
AC P97326; P70393; Q3KNY8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Cadherin-6;
DE AltName: Full=Kidney cadherin;
DE Short=K-cadherin;
DE Flags: Precursor;
GN Name=Cdh6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9126293; DOI=10.1006/dbio.1996.8501;
RA Inoue T., Chisaka O., Matsunami H., Takeichi M.;
RT "Cadherin-6 expression transiently delineates specific rhombomeres, other
RT neural tube subdivisions, and neural crest subpopulations in mouse
RT embryos.";
RL Dev. Biol. 183:183-194(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 479-666.
RC STRAIN=C57BL/6 X CBA; TISSUE=Kidney;
RA Faulkner-Jones B.E., Dziadek M.A.;
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=8879495; DOI=10.1095/biolreprod55.4.822;
RA Munro S.B., Blaschuk O.W.;
RT "A comprehensive survey of the cadherins expressed in the testes of fetal,
RT immature, and adult mice utilizing the polymerase chain reaction.";
RL Biol. Reprod. 55:822-827(1996).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-786 AND SER-790, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- DEVELOPMENTAL STAGE: Expressed in fetal, newborn and 7-day-old testis
CC but not in 21-day-old or adult testis. {ECO:0000269|PubMed:8879495}.
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; D82029; BAA11516.1; -; mRNA.
DR EMBL; BC107013; AAI07014.1; -; mRNA.
DR EMBL; U67399; AAB07550.1; -; mRNA.
DR CCDS; CCDS27393.1; -.
DR RefSeq; NP_031692.2; NM_007666.4.
DR RefSeq; XP_006520080.1; XM_006520017.1.
DR PDB; 3LND; X-ray; 2.82 A; A/B/C/D=58-260.
DR PDB; 6CGB; X-ray; 2.99 A; A=156-260.
DR PDB; 6CGU; X-ray; 1.90 A; A/B/C/D=54-260.
DR PDBsum; 3LND; -.
DR PDBsum; 6CGB; -.
DR PDBsum; 6CGU; -.
DR AlphaFoldDB; P97326; -.
DR SMR; P97326; -.
DR IntAct; P97326; 1.
DR MINT; P97326; -.
DR STRING; 10090.ENSMUSP00000037113; -.
DR GlyConnect; 2171; 4 N-Linked glycans (2 sites).
DR GlyGen; P97326; 5 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; P97326; -.
DR PhosphoSitePlus; P97326; -.
DR MaxQB; P97326; -.
DR PaxDb; P97326; -.
DR PeptideAtlas; P97326; -.
DR PRIDE; P97326; -.
DR ProteomicsDB; 265417; -.
DR Antibodypedia; 2354; 434 antibodies from 36 providers.
DR DNASU; 12563; -.
DR Ensembl; ENSMUST00000036439; ENSMUSP00000037113; ENSMUSG00000039385.
DR GeneID; 12563; -.
DR KEGG; mmu:12563; -.
DR UCSC; uc007vif.1; mouse.
DR CTD; 1004; -.
DR MGI; MGI:107435; Cdh6.
DR VEuPathDB; HostDB:ENSMUSG00000039385; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000154673; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; P97326; -.
DR OMA; TRKTRYN; -.
DR OrthoDB; 201053at2759; -.
DR PhylomeDB; P97326; -.
DR TreeFam; TF329887; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 12563; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Cdh6; mouse.
DR EvolutionaryTrace; P97326; -.
DR PRO; PR:P97326; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P97326; protein.
DR Bgee; ENSMUSG00000039385; Expressed in metanephric proximal tubule and 223 other tissues.
DR Genevisible; P97326; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
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; IDA:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..53
FT /evidence="ECO:0000255"
FT /id="PRO_0000003763"
FT CHAIN 54..790
FT /note="Cadherin-6"
FT /id="PRO_0000003764"
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 260..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 790
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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"
FT CONFLICT 43
FT /note="N -> D (in Ref. 1; BAA11516)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="S -> G (in Ref. 1; BAA11516)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="E -> G (in Ref. 1; BAA11516)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="N -> H (in Ref. 1; BAA11516)"
FT /evidence="ECO:0000305"
FT CONFLICT 346..348
FT /note="KVE -> RWK (in Ref. 1; BAA11516)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="G -> V (in Ref. 1; BAA11516)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="N -> K (in Ref. 1; BAA11516)"
FT /evidence="ECO:0000305"
FT CONFLICT 534
FT /note="S -> G (in Ref. 3; AAB07550)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="N -> T (in Ref. 3; AAB07550)"
FT /evidence="ECO:0000305"
FT CONFLICT 597..598
FT /note="MQ -> IE (in Ref. 1; BAA11516)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="T -> S (in Ref. 1; BAA11516)"
FT /evidence="ECO:0000305"
FT CONFLICT 640
FT /note="R -> E (in Ref. 1; BAA11516)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="L -> V (in Ref. 1; BAA11516)"
FT /evidence="ECO:0000305"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:3LND"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:6CGU"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:6CGU"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6CGU"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:6CGU"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 138..150
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 177..180
FT /evidence="ECO:0007829|PDB:6CGU"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 198..203
FT /evidence="ECO:0007829|PDB:6CGU"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:6CGU"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:6CGU"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 231..240
FT /evidence="ECO:0007829|PDB:6CGU"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:6CGU"
FT STRAND 249..259
FT /evidence="ECO:0007829|PDB:6CGU"
SQ SEQUENCE 790 AA; 88355 MW; 14389434D23B2A8F CRC64;
MRTYRYFLLL FWVGQPYPTF SNPLSKRTSG FPAKRKALEL SANSRNELSR SKRSWMWNQF
FLLEEYTGSD YQYVGKLHSD QDRGDGSLKY ILSGDGAGDL FIINENTGDI QATKRLDREE
KPVYILRAQA VNRRTGRPVE PESEFIIKIH DINDNEPIFT KDVYTATVPE MADVGTFVVQ
VTATDADDPT YGNSAKVVYS ILQGQPYFSV ESETGIIKTA LLNMDRENRE QYQVVIQAKD
MGGQMGGLSG TTTVNITLTD VNDNPPRFPQ STYQFKTPES SPPGTPIGRI KASDADVGEN
AEIEYSITDG EGHEMFDVIT DQETQEGIIT VKKLLDFEKK KVYTLKVEAS NPHVEPRFLY
LGPFKDSATV RIVVDDVDEP PVFSKLAYIL QIREDARINT TIGSVAAQDP DAARNPVKYS
VDRHTDMDRI FNIDSGNGSI FTSKLLDRET LLWHNITVIA TEINNPKQSS RVPLYIKVLD
VNDNAPEFAE FYETFVCEKA KADQLIQTLR AVDKDDPYSG HQFSFSLAPE AASSSNFTIQ
DNKDNTAGIL TRKNGYNRHE MSTYLLPVVI SDNDYPVQSS TGTVTVRVCA CDHHGNMQSC
HAEALIHPTG LSTGALVAIL LCIVILLVTV VLFAALRRQR KKEPLIISKE DIRDNIVSYN
DEGGGEEDTQ AFDIGTLRNP EAMEDSKSRR DIVPEALFLP RRTPTARDNT DVRDFINQRL
KENDTDPTAP PYDSLATYAY EGTGSVADSL SSLESVTTDG DQDYDYLSDW GPRFKKLADM
YGGMDSDKDS
