ID   D6RF86_HUMAN            Unreviewed;       608 AA.
AC   D6RF86;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   02-SEP-2026, entry version 95.
DE   SubName: Full=Cadherin 6 {ECO:0000313|Ensembl:ENSP00000424843.1};
GN   Name=CDH6 {ECO:0000313|Ensembl:ENSP00000424843.1};
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 {ECO:0000313|Ensembl:ENSP00000424843.1, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000424843.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11237011; DOI=10.1038/35057062;
RG   International Human Genome Sequencing Consortium;
RA   Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J.,
RA   Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K.,
RA   Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P.,
RA   McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J.,
RA   Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C.,
RA   Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J.,
RA   Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C.,
RA   Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I.,
RA   Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S.,
RA   Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S.,
RA   Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S.,
RA   Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A.,
RA   Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R.,
RA   Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A.,
RA   Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W.,
RA   Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T.,
RA   Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E.,
RA   Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B.,
RA   Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L.,
RA   Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y.,
RA   Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C.,
RA   Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W.,
RA   Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P.,
RA   Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M.,
RA   Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A.,
RA   Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A.,
RA   Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M.,
RA   Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R.,
RA   Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A.,
RA   Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J.,
RA   Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N.,
RA   Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L.,
RA   Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G.,
RA   Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R.,
RA   Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G.,
RA   Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W.,
RA   Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J.,
RA   Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M.,
RA   McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J.,
RA   Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E.,
RA   Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J.,
RA   Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F.,
RA   Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A.,
RA   Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K.,
RA   Shizuya H., Choi S., Chen Y.J.;
RT   "Initial sequencing and analysis of the human genome.";
RL   Nature 409:860-921(2001).
RN   [2] {ECO:0000313|Ensembl:ENSP00000424843.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [3] {ECO:0000313|Ensembl:ENSP00000424843.1, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496913; DOI=10.1038/nature03001;
RG   International Human Genome Sequencing Consortium;
RT   "Finishing the euchromatic sequence of the human genome.";
RL   Nature 431:931-945(2004).
RN   [4] {ECO:0000313|Ensembl:ENSP00000424843.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-2026) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00037319}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC       Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
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DR   EMBL; AC091898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC113386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; D6RF86; -.
DR   SMR; D6RF86; -.
DR   MassIVE; D6RF86; -.
DR   ProteomicsDB; 14492; -.
DR   Antibodypedia; 2354; 460 antibodies from 39 providers.
DR   Ensembl; ENST00000514738.5; ENSP00000424843.1; ENSG00000113361.14.
DR   UCSC; uc063cqv.1; human.
DR   HGNC; HGNC:1765; CDH6.
DR   VEuPathDB; HostDB:ENSG00000113361; -.
DR   GeneTree; ENSGT00940000154673; -.
DR   HOGENOM; CLU_005284_4_3_1; -.
DR   OrthoDB; 6252479at2759; -.
DR   ChiTaRS; CDH6; human.
DR   Proteomes; UP000005640; Chromosome 5.
DR   Bgee; ENSG00000113361; Expressed in type B pancreatic cell and 177 other cell types or tissues.
DR   ExpressionAtlas; D6RF86; baseline and differential.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0007156; P:homophilic cell-cell adhesion; IEA:InterPro.
DR   CDD; cd11304; Cadherin_repeat; 5.
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   Gene3D; 2.60.40.60; Cadherins; 5.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF322; CADHERIN-6; 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; 2.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   1: Evidence at protein level;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW   ProRule:PRU00043}; Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:D6RF86,
KW   ECO:0007829|ProteomicsDB:D6RF86};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        555..577
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..104
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          105..213
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          214..328
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          329..433
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          433..555
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   REGION          204..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   608 AA;  67403 MW;  BEF5A4C6C5644583 CRC64;
     MWNQFFLLEE YTGSDYQYVG KLHSDQDRGD GSLKYILSGD GAGDLFIINE NTGDIQATKR
     LDREEKPVYI LRAQAINRRT GRPVEPESEF IIKIHDINDN EPIFTKEVYT ATVPEMSDVG
     TFVVQVTATD ADDPTYGNSA KVVYSILQGQ PYFSVESETG IIKTALLNMD RENREQYQVV
     IQAKDMGGQM GGLSGTTTVN ITLTDVNDNP PRFPQSTYQF KTPESSPPGT PIGRIKASDA
     DVGENAEIEY SITDGEGLDM FDVITDQETQ EGIITVKKLL DFEKKKVYTL KVEASNPYVE
     PRFLYLGPFK DSATVRIVVE DVDEPPVFSK LAYILQIRED AQINTTIGSV TAQDPDAARN
     PVKYSVDRHT DMDRIFNIDS GNGSIFTSKL LDRETLLWHN ITVIATEINN PKQSSRVPLY
     IKVLDVNDNA PEFAEFYETF VCEKAKADQL IQTLHAVDKD DPYSGHQFSF SLAPEAASGS
     NFTIQDNKDN TAGILTRKNG YNRHEMSTYL LPVVISDNDY PVQSSTGTVT VRVCACDHHG
     NMQSCHAEAL IHPTGLSTGA LVAILLCIVI LLGKLVLPAS YLPMVRGSHC YCDTLDLSAS
     PIKAYSLI
//