CAD26_HUMAN
ID CAD26_HUMAN Reviewed; 832 AA.
AC Q8IXH8; A2A2M5; B3KNX3; Q6P5Y6; Q8TCH3; Q9BQN4; Q9NRU1;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 4.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Cadherin-like protein 26;
DE AltName: Full=Cadherin-like protein VR20;
DE Flags: Precursor;
GN Name=CDH26;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Lung, and Tonsillar carcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
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 410-832 (ISOFORM 1).
RA Kools P.F.J., van Roy F.;
RT "Identification and characterization of a novel human cadherin with
RT similarity to N-cadherin.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION, SUBUNIT,
RP AND IDENTIFICATION IN A CADHERIN/CATENIN ADHESION COMPLEX.
RX PubMed=28051089; DOI=10.1038/mi.2016.120;
RA Caldwell J.M., Collins M.H., Kemme K.A., Sherrill J.D., Wen T., Rochman M.,
RA Stucke E.M., Amin L., Tai H., Putnam P.E., Jimenez-Dalmaroni M.J.,
RA Wormald M.R., Porollo A., Abonia J.P., Rothenberg M.E.;
RT "Cadherin 26 is an alpha integrin-binding epithelial receptor regulated
RT during allergic inflammation.";
RL Mucosal Immunol. 10:1190-1201(2017).
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. Ligand for integrins alpha-E/beta-7,
CC ITGAE:ITGAB7, alpha-4/beta-7, ITGA4:ITGAB7 and alpha-4/beta-1,
CC ITGA4:ITGAB1 through which modulates CD4(+) T cells activation
CC (PubMed:28051089). {ECO:0000269|PubMed:28051089}.
CC -!- SUBUNIT: Homodimer (PubMed:28051089). Component of a cadherin:catenin
CC adhesion complex composed of at least of CDH26, beta-catenin/CTNNB1,
CC alpha-catenin/CTNNA1 and p120 catenin/CTNND1 (PubMed:28051089).
CC {ECO:0000269|PubMed:28051089}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28051089};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:28051089}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=3;
CC IsoId=Q8IXH8-4; Sequence=Displayed;
CC Name=1; Synonyms=a;
CC IsoId=Q8IXH8-1; Sequence=VSP_059693;
CC Name=2; Synonyms=b;
CC IsoId=Q8IXH8-2; Sequence=VSP_008333, VSP_008334;
CC Name=4;
CC IsoId=Q8IXH8-5; Sequence=VSP_008333, VSP_008334, VSP_059694;
CC -!- TISSUE SPECIFICITY: Expressed by epithelial cells of gastrointestinal
CC tissue. {ECO:0000269|PubMed:28051089}.
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 -!- PTM: N-glycosylated. {ECO:0000269|PubMed:28051089}.
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DR EMBL; AK055202; BAG51485.1; -; mRNA.
DR EMBL; AK074477; BAB85093.1; -; mRNA.
DR EMBL; AL109928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75420.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75421.1; -; Genomic_DNA.
DR EMBL; BC062570; AAH62570.1; -; mRNA.
DR EMBL; AF169690; AAF89687.1; -; mRNA.
DR CCDS; CCDS13485.1; -. [Q8IXH8-4]
DR CCDS; CCDS13486.1; -. [Q8IXH8-2]
DR CCDS; CCDS86964.1; -. [Q8IXH8-5]
DR RefSeq; NP_001335133.1; NM_001348204.1. [Q8IXH8-5]
DR RefSeq; NP_068582.2; NM_021810.5. [Q8IXH8-2]
DR RefSeq; NP_817089.1; NM_177980.3. [Q8IXH8-4]
DR AlphaFoldDB; Q8IXH8; -.
DR SMR; Q8IXH8; -.
DR BioGRID; 121909; 4.
DR STRING; 9606.ENSP00000339390; -.
DR CarbonylDB; Q8IXH8; -.
DR GlyGen; Q8IXH8; 5 sites.
DR iPTMnet; Q8IXH8; -.
DR PhosphoSitePlus; Q8IXH8; -.
DR BioMuta; CDH26; -.
DR DMDM; 152031568; -.
DR MassIVE; Q8IXH8; -.
DR PeptideAtlas; Q8IXH8; -.
DR PRIDE; Q8IXH8; -.
DR Antibodypedia; 2400; 155 antibodies from 24 providers.
DR DNASU; 60437; -.
DR Ensembl; ENST00000244049.7; ENSP00000244049.3; ENSG00000124215.17. [Q8IXH8-5]
DR Ensembl; ENST00000348616.9; ENSP00000339390.4; ENSG00000124215.17. [Q8IXH8-4]
DR Ensembl; ENST00000350849.10; ENSP00000310845.7; ENSG00000124215.17. [Q8IXH8-2]
DR GeneID; 60437; -.
DR KEGG; hsa:60437; -.
DR MANE-Select; ENST00000348616.9; ENSP00000339390.4; NM_177980.4; NP_817089.1.
DR UCSC; uc002ybe.4; human. [Q8IXH8-4]
DR CTD; 60437; -.
DR GeneCards; CDH26; -.
DR HGNC; HGNC:15902; CDH26.
DR HPA; ENSG00000124215; Tissue enhanced (prostate).
DR MIM; 617685; gene.
DR neXtProt; NX_Q8IXH8; -.
DR OpenTargets; ENSG00000124215; -.
DR PharmGKB; PA26298; -.
DR VEuPathDB; HostDB:ENSG00000124215; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000161589; -.
DR HOGENOM; CLU_005284_5_0_1; -.
DR InParanoid; Q8IXH8; -.
DR OMA; WRAKFNI; -.
DR OrthoDB; 158870at2759; -.
DR PhylomeDB; Q8IXH8; -.
DR TreeFam; TF316817; -.
DR PathwayCommons; Q8IXH8; -.
DR BioGRID-ORCS; 60437; 12 hits in 1068 CRISPR screens.
DR GenomeRNAi; 60437; -.
DR Pharos; Q8IXH8; Tbio.
DR PRO; PR:Q8IXH8; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q8IXH8; protein.
DR Bgee; ENSG00000124215; Expressed in bronchial epithelial cell and 117 other tissues.
DR ExpressionAtlas; Q8IXH8; baseline and differential.
DR Genevisible; Q8IXH8; HS.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045294; F:alpha-catenin binding; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0070097; F:delta-catenin binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0035710; P:CD4-positive, alpha-beta T cell activation; IDA:UniProtKB.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 3.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 4.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 2.
DR PROSITE; PS50268; CADHERIN_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..832
FT /note="Cadherin-like protein 26"
FT /evidence="ECO:0000255"
FT /id="PRO_0000003829"
FT TOPO_DOM 28..614
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..832
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..165
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 166..275
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 276..396
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 397..500
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 813..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 85
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 462
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..667
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008333"
FT VAR_SEQ 668..673
FT /note="KGTSAQ -> MKPLIW (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_008334"
FT VAR_SEQ 700..832
FT /note="DLEEVPPSAASQSAQARCALGSWGYGKPFEPRSVKNIHSTPAYPDATMHRQL
FT LAPVEGRMAETLNQKLHVANVLEDDPGYLPHVYSEEGECGGAPSLSSLASLEQELQPDL
FT LDSLGSKATPFEEIYSESGVPS -> AYPDATMHRQLLAPVEGRMAETLNQSKERNRFS
FT LSRGCIIPQGRATAGRGLPQDIYKEMMPRRLTQTGKRKHGALARTPSFKKVVYDHKEDE
FT ENKAGRKQRSHLFKVMQLRNEQGGVRVQSAHSPSPLNKKACFPGDYRGESAGGHNCRAV
FT SG (in isoform 1)"
FT /id="VSP_059693"
FT VAR_SEQ 700..740
FT /note="Missing (in isoform 4)"
FT /id="VSP_059694"
FT VARIANT 144
FT /note="I -> T (in dbSNP:rs6015609)"
FT /id="VAR_055568"
FT VARIANT 301
FT /note="R -> G (in dbSNP:rs11086690)"
FT /id="VAR_055569"
FT VARIANT 448
FT /note="V -> A (in dbSNP:rs34866303)"
FT /id="VAR_055570"
FT VARIANT 479
FT /note="P -> L (in dbSNP:rs6071067)"
FT /id="VAR_055571"
FT VARIANT 615
FT /note="V -> L (in dbSNP:rs194998)"
FT /id="VAR_055572"
SQ SEQUENCE 832 AA; 92416 MW; 0CEF6129FE255BBB CRC64;
MAMRSGRHPS LLLLLVLLLW LLQVSIIDSV QQETDDLTKQ TKEKIYQPLR RSKRRWVITT
LELEEEDPGP FPKLIGELFN NMSYNMSLMY LISGPGVDEY PEIGLFSLED HENGRIYVHR
PVDREMTPSF TVYFDVVERS TGKIVDTSLI FNIRISDVND HAPQFPEKEF NITVQENQSA
GQPIFQMLAV DLDEENTPNS QVLYFLISQT PLLKESGFRV DRLSGEIRLS GCLDYETAPQ
FTLLIRARDC GEPSLSSTTT VHVDVQEGNN HRPAFTQENY KVQIPEGRAS QGVLRLLVQD
RDSPFTSAWR AKFNILHGNE EGHFDISTDP ETNEGILNVI KPLDYETRPA QSLIIVVENE
ERLVFCERGK LQPPRKAAAS ATVSVQVTDA NDPPAFHPQS FIVNKEEGAR PGTLLGTFNA
MDPDSQIRYE LVHDPANWVS VDKNSGVVIT VEPIDRESPH VNNSFYVIII HAVDDGFPPQ
TATGTLMLFL SDINDNVPTL RPRSRYMEVC ESAVHEPLHI EAEDPDLEPF SDPFTFELDN
TWGNAEDTWK LGRNWGQSVE LLTLRSLPRG NYLVPLFIGD KQGLSQKQTV HVRICPCASG
LTCVELADAE VGLHVGALFP VCAAFVALAV ALLFLLRCYF VLEPKRHGCS VSNDEGHQTL
VMYNAESKGT SAQTWSDVEG QRPALLICTA AAGPTQGVKD LEEVPPSAAS QSAQARCALG
SWGYGKPFEP RSVKNIHSTP AYPDATMHRQ LLAPVEGRMA ETLNQKLHVA NVLEDDPGYL
PHVYSEEGEC GGAPSLSSLA SLEQELQPDL LDSLGSKATP FEEIYSESGV PS
