CADH6_RAT
ID CADH6_RAT Reviewed; 789 AA.
AC P55280;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Cadherin-6;
DE AltName: Full=Kidney cadherin;
DE Short=K-cadherin;
DE Flags: Precursor;
GN Name=Cdh6; Synonyms=Kcad;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ACI; TISSUE=Kidney;
RX PubMed=8187093;
RA Xiang Y.Y., Tanaka M., Suzuki M., Igarashi H., Kiyokawa E., Naito Y.,
RA Ohtawara Y., Shen Q., Sugimura H., Kino I.;
RT "Isolation of complementary DNA encoding K-cadherin, a novel rat cadherin
RT preferentially expressed in fetal kidney and kidney carcinoma.";
RL Cancer Res. 54:3034-3041(1994).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-785, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 -!- TISSUE SPECIFICITY: Highly expressed in kidney and brain.
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; D25290; BAA04975.1; -; mRNA.
DR PIR; I52701; I52701.
DR RefSeq; NP_037059.1; NM_012927.1.
DR AlphaFoldDB; P55280; -.
DR SMR; P55280; -.
DR STRING; 10116.ENSRNOP00000018246; -.
DR GlyGen; P55280; 5 sites.
DR iPTMnet; P55280; -.
DR PhosphoSitePlus; P55280; -.
DR PaxDb; P55280; -.
DR PRIDE; P55280; -.
DR GeneID; 25409; -.
DR KEGG; rno:25409; -.
DR CTD; 1004; -.
DR RGD; 2322; Cdh6.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; P55280; -.
DR OrthoDB; 201053at2759; -.
DR PhylomeDB; P55280; -.
DR Reactome; R-RNO-418990; Adherens junctions interactions.
DR PRO; PR:P55280; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:0008585; P:female gonad development; IEP:RGD.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
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 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_0000003765"
FT CHAIN 54..789
FT /note="Cadherin-6"
FT /id="PRO_0000003766"
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..789
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 259..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 789
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 789 AA; 88341 MW; EE7474F0B07FE403 CRC64;
MRTYRYFLLL FWVGQPYPTF SNPLSKRTSG FPAKRRALEL SANSRNELSR SKRSWMWNQF
FLLEEYTGSD YQYVGKLHSD QDRGDGSLKY ILSGDGAGDL FIINENTGDI QATKRLDREE
KPVYILRAQA INRRTGRPVE PESEFIIKIH DINDNEPIFT KDVYTATVPE MADVGTFVVQ
VTATDADDPT YGNSAKVVYS ILQGQPYFSV ESETGIIKTA LLNMDRENRE QYQVVIQAKD
MGGQMGGLSG TTTVNITLTD VNDNPPRFPQ STYQFKTPES SPPGTPIGRI KASDADVGEN
AEIEYSITDG EGHDMFDVIT DQETQEGIIT VKKLLDFEKK RVYTLKVEAS NPHIEPRFLY
LGPFKDSATV RIVVDDVDEP PVFSKPAYIL QIREDAQINT TIGSVAAQDP DAARNPVKYS
VDRHTDMDRI FNIDSGNGSI FTSKLLDRET LLWHNITVIA TEINNPKQSS RVPLYIKVLD
VNDNAPEFAE FYETFVCEKA KADQLIQTLH AVDKDDPYSG HQFSFSLAPE AASGSNFTIQ
DNKDNTAGIL TRKNGYNRHE MSTYLLPVVI SDNDYPVQSS TGTVTVRVCA CDHHGNMQSC
HAEALIHPTG LSTGALVAIL LCIVILLVTV VLFAALRRQR KKEPLIISKE DIRDNIVSYN
DEGGGEEDTQ AFDIGTLRNP KPWRQQSRRD MVPEALFLPR RTPTARDNTD VRDFISQRLR
KMNTDPTAPP YDSLATYAYE GTGSVADSLS SLESVTTDGD QDYGYLSDWG PRFKKLADMY
GGMDSDKDS
