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 02-SEP-2026, entry version 205. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001349364.1; NM_001362435.2. [P55285-2] DR RefSeq; NP_004923.1; NM_004932.4. [P55285-1] DR RefSeq; XP_011512223.1; XM_011513921.4. [P55285-1] DR RefSeq; XP_054207350.1; XM_054351375.1. [P55285-1] DR RefSeq; XP_054207351.1; XM_054351376.1. [P55285-1] DR PDB; 5VEB; X-ray; 2.34 A; X/Y=490-608. DR AlphaFoldDB; P55285; -. DR SMR; P55285; -. DR BioGRID; 107439; 9. DR FunCoup; P55285; 200. DR IntAct; P55285; 2. DR MINT; P55285; -. DR NDEx; IQUERY-CP-CDH6; 9 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000265071; -. DR CarbonylDB; P55285; -. DR GlyCosmos; P55285; 6 sites, No reported glycans. DR GlyGen; P55285; 8 sites, 78 N-linked glycans (4 sites), 1 O-linked glycan (2 sites). DR iPTMnet; P55285; -. DR PhosphoSitePlus; P55285; -. DR BioMuta; CDH6; -. DR DMDM; 1705545; -. DR jPOST; P55285; -. DR MassIVE; P55285; -. DR PaxDb; 9606-ENSP00000265071; -. DR PeptideAtlas; P55285; -. DR ProteomicsDB; 56834; -. [P55285-1] DR ProteomicsDB; 56835; -. [P55285-2] DR ABCD; P55285; 1 sequenced antibody. DR Antibodypedia; 2354; 460 antibodies from 39 providers. DR DNASU; 1004; -. DR Ensembl; ENST00000265071.3; ENSP00000265071.2; ENSG00000113361.14. [P55285-1] DR Ensembl; ENST00000899823.1; ENSP00000569882.1; ENSG00000113361.14. [P55285-1] DR Ensembl; ENST00000899824.1; ENSP00000569883.1; ENSG00000113361.14. [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 AGR; HGNC:1765; -. DR ClinPGx; PA26302; -. DR CTD; 1004; -. DR DisGeNET; 1004; -. DR GeneCards; CDH6; -. DR HGNC; HGNC:1765; CDH6. DR HPA; ENSG00000113361; Tissue enhanced (blood vessel, kidney). DR MIM; 603007; gene. DR OpenTargets; ENSG00000113361; -. DR VEuPathDB; HostDB:ENSG00000113361; -. DR eggNOG; KOG3594; Eukaryota. DR GeneTree; ENSGT00940000154673; -. DR HOGENOM; CLU_005284_3_1_1; -. DR InParanoid; P55285; -. DR OMA; RQDLHRS; -. DR OrthoDB; 6252479at2759; -. DR PAN-GO; P55285; 11 GO annotations based on evolutionary models. DR PhylomeDB; P55285; -. DR PathwayCommons; P55285; -. DR Reactome; R-HSA-418990; Adherens junctions interactions. DR SignaLink; P55285; -. DR SIGNOR; P55285; -. DR Agora; ENSG00000113361; -. DR BioGRID-ORCS; 1004; 10 hits in 1147 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 177 other cell types or tissues. DR ExpressionAtlas; P55285; 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:0030054; C:cell junction; IDA:HPA. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central. DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0034332; P:adherens junction organization; IBA:GO_Central. DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion; IBA:GO_Central. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0016477; P:cell migration; IBA:GO_Central. DR GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central. DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central. DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central. DR GO; GO:0007156; P:homophilic cell-cell adhesion; IEA:InterPro. DR GO; GO:0099560; P:synaptic membrane adhesion; IBA:GO_Central. DR CDD; cd11304; Cadherin_repeat; 5. DR DisProt; DP03681; -. DR FunFam; 2.60.40.60:FF:000297; Cadherin 12; 1. DR FunFam; 2.60.40.60:FF:000009; Cadherin 24; 1. DR FunFam; 2.60.40.60:FF:000012; Cadherin 24; 1. DR FunFam; 2.60.40.60:FF:000017; Cadherin 24; 1. DR FunFam; 2.60.40.60:FF:000014; Cadherin 8; 1. DR FunFam; 4.10.900.10:FF:000006; Cadherin-9 preproprotein; 1. DR Gene3D; 2.60.40.60; Cadherins; 5. DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 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_Y-type_LIR. DR InterPro; IPR027397; Catenin-bd_sf. DR PANTHER; PTHR24027; CADHERIN-23; 1. DR PANTHER; PTHR24027:SF322; CADHERIN-6; 1. DR Pfam; PF01049; CADH_Y-type_LIR; 1. DR Pfam; PF00028; Cadherin; 5. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 5. DR SUPFAM; SSF49313; Cadherin-like; 5. DR PROSITE; PS00232; CADHERIN_1; 3. DR PROSITE; PS50268; CADHERIN_2; 5. DR PDBsum; 5VEB; -. 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; Proteomics identification; Reference proteome; Repeat; KW Signal; Transmembrane; 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 269..279 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 //