CADH6_HUMAN
ID CADH6_HUMAN Reviewed; 790 AA.
AC P55285; A8K5H5; Q9BWS0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Cadherin-6;
DE AltName: Full=Kidney cadherin;
DE Short=K-cadherin;
DE Flags: Precursor;
GN Name=CDH6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7743525;
RA Shimoyama Y., Gotoh M., Terasaki T., Kitajima M., Hirohashi S.;
RT "Isolation and sequence analysis of human cadherin-6 complementary DNA for
RT the full coding sequence and its expression in human carcinoma cells.";
RL Cancer Res. 55:2206-2211(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 377-790 (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=2059658; DOI=10.1091/mbc.2.4.261;
RA Suzuki S., Sano K., Tanihara H.;
RT "Diversity of the cadherin family: evidence for eight new cadherins in
RT nervous tissue.";
RL Cell Regul. 2:261-270(1991).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-399.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55285-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55285-2; Sequence=VSP_000636, VSP_000637;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain, cerebellum, and kidney.
CC Lung, pancreas, and gastric mucosa show a weak expression. Also
CC expressed in certain liver and kidney carcinomas.
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; D31784; BAA06562.1; -; mRNA.
DR EMBL; AK291290; BAF83979.1; -; mRNA.
DR EMBL; CH471118; EAX10764.1; -; Genomic_DNA.
DR EMBL; BC000019; AAH00019.1; -; mRNA.
DR CCDS; CCDS3894.1; -. [P55285-1]
DR PIR; I37016; I37016.
DR RefSeq; NP_004923.1; NM_004932.3. [P55285-1]
DR RefSeq; XP_011512223.1; XM_011513921.2. [P55285-1]
DR RefSeq; XP_016864399.1; XM_017008910.1. [P55285-1]
DR RefSeq; XP_016864400.1; XM_017008911.1.
DR PDB; 5VEB; X-ray; 2.34 A; X/Y=490-608.
DR PDBsum; 5VEB; -.
DR AlphaFoldDB; P55285; -.
DR SMR; P55285; -.
DR BioGRID; 107439; 8.
DR IntAct; P55285; 2.
DR MINT; P55285; -.
DR STRING; 9606.ENSP00000265071; -.
DR CarbonylDB; P55285; -.
DR GlyGen; P55285; 6 sites.
DR iPTMnet; P55285; -.
DR PhosphoSitePlus; P55285; -.
DR BioMuta; CDH6; -.
DR DMDM; 1705545; -.
DR EPD; P55285; -.
DR jPOST; P55285; -.
DR MassIVE; P55285; -.
DR PaxDb; P55285; -.
DR PeptideAtlas; P55285; -.
DR PRIDE; P55285; -.
DR ProteomicsDB; 56834; -. [P55285-1]
DR ProteomicsDB; 56835; -. [P55285-2]
DR ABCD; P55285; 1 sequenced antibody.
DR Antibodypedia; 2354; 434 antibodies from 36 providers.
DR DNASU; 1004; -.
DR Ensembl; ENST00000265071.3; ENSP00000265071.2; ENSG00000113361.13. [P55285-1]
DR GeneID; 1004; -.
DR KEGG; hsa:1004; -.
DR MANE-Select; ENST00000265071.3; ENSP00000265071.2; NM_004932.4; NP_004923.1.
DR UCSC; uc003jhe.3; human. [P55285-1]
DR CTD; 1004; -.
DR DisGeNET; 1004; -.
DR GeneCards; CDH6; -.
DR HGNC; HGNC:1765; CDH6.
DR HPA; ENSG00000113361; Tissue enhanced (kidney).
DR MIM; 603007; gene.
DR neXtProt; NX_P55285; -.
DR OpenTargets; ENSG00000113361; -.
DR PharmGKB; PA26302; -.
DR VEuPathDB; HostDB:ENSG00000113361; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000154673; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; P55285; -.
DR OMA; TRKTRYN; -.
DR OrthoDB; 201053at2759; -.
DR PhylomeDB; P55285; -.
DR TreeFam; TF329887; -.
DR PathwayCommons; P55285; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; P55285; -.
DR SIGNOR; P55285; -.
DR BioGRID-ORCS; 1004; 8 hits in 1067 CRISPR screens.
DR ChiTaRS; CDH6; human.
DR GeneWiki; CDH6; -.
DR GenomeRNAi; 1004; -.
DR Pharos; P55285; Tbio.
DR PRO; PR:P55285; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P55285; protein.
DR Bgee; ENSG00000113361; Expressed in type B pancreatic cell and 176 other tissues.
DR ExpressionAtlas; P55285; baseline and differential.
DR Genevisible; P55285; HS.
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; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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:0007155; P:cell adhesion; TAS:ProtInc.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; 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_0000003761"
FT CHAIN 54..790
FT /note="Cadherin-6"
FT /id="PRO_0000003762"
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 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 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 49
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 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952"
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 VAR_SEQ 628..663
FT /note="VTVVLFAALRRQRKKEPLIISKEDIRDNIVSYNDEG -> GKLVLPASYLPM
FT VRGSHCYCDTLDLSASPIKAYSLI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_000636"
FT VAR_SEQ 664..790
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_000637"
FT CONFLICT 421
FT /note="V -> I (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="T -> I (in Ref. 5; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:5VEB"
FT STRAND 505..512
FT /evidence="ECO:0007829|PDB:5VEB"
FT STRAND 524..527
FT /evidence="ECO:0007829|PDB:5VEB"
FT TURN 529..531
FT /evidence="ECO:0007829|PDB:5VEB"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:5VEB"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:5VEB"
FT STRAND 543..551
FT /evidence="ECO:0007829|PDB:5VEB"
FT TURN 558..560
FT /evidence="ECO:0007829|PDB:5VEB"
FT STRAND 562..571
FT /evidence="ECO:0007829|PDB:5VEB"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:5VEB"
FT STRAND 579..589
FT /evidence="ECO:0007829|PDB:5VEB"
SQ SEQUENCE 790 AA; 88309 MW; C175004FC8A61100 CRC64;
MRTYRYFLLL FWVGQPYPTL STPLSKRTSG FPAKKRALEL SGNSKNELNR SKRSWMWNQF
FLLEEYTGSD YQYVGKLHSD QDRGDGSLKY ILSGDGAGDL FIINENTGDI QATKRLDREE
KPVYILRAQA INRRTGRPVE PESEFIIKIH DINDNEPIFT KEVYTATVPE MSDVGTFVVQ
VTATDADDPT YGNSAKVVYS ILQGQPYFSV ESETGIIKTA LLNMDRENRE QYQVVIQAKD
MGGQMGGLSG TTTVNITLTD VNDNPPRFPQ STYQFKTPES SPPGTPIGRI KASDADVGEN
AEIEYSITDG EGLDMFDVIT DQETQEGIIT VKKLLDFEKK KVYTLKVEAS NPYVEPRFLY
LGPFKDSATV RIVVEDVDEP PVFSKLAYIL QIREDAQINT TIGSVTAQDP 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 EAIEDNKLRR DIVPEALFLP RRTPTARDNT DVRDFINQRL
KENDTDPTAP PYDSLATYAY EGTGSVADSL SSLESVTTDA DQDYDYLSDW GPRFKKLADM
YGGVDSDKDS
