CAD26_MOUSE
ID CAD26_MOUSE Reviewed; 763 AA.
AC P59862;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cadherin-like protein 26;
DE Flags: Precursor;
GN Name=Cdh26; Synonyms=Gm1010;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium;
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).
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 {ECO:0000250|UniProtKB:Q8IXH8}.
CC -!- SUBUNIT: Homodimer. Component of a cadherin:catenin adhesion complex
CC composed of at least of CDH26, beta-catenin/CTNNB1, alpha-
CC catenin/CTNNA1 and p120 catenin/CTNND1. {ECO:0000250|UniProtKB:Q8IXH8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8IXH8};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q8IXH8}.
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:0000250|UniProtKB:Q8IXH8}.
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DR EMBL; BC053928; AAH53928.1; -; mRNA.
DR CCDS; CCDS17162.1; -.
DR RefSeq; NP_001278118.1; NM_001291189.1.
DR RefSeq; NP_941058.1; NM_198656.2.
DR AlphaFoldDB; P59862; -.
DR SMR; P59862; -.
DR BioGRID; 237927; 1.
DR STRING; 10090.ENSMUSP00000048829; -.
DR GlyGen; P59862; 5 sites.
DR PhosphoSitePlus; P59862; -.
DR PaxDb; P59862; -.
DR PRIDE; P59862; -.
DR ProteomicsDB; 273578; -.
DR Antibodypedia; 2400; 155 antibodies from 24 providers.
DR DNASU; 381409; -.
DR Ensembl; ENSMUST00000042092; ENSMUSP00000048829; ENSMUSG00000039155.
DR GeneID; 381409; -.
DR KEGG; mmu:381409; -.
DR UCSC; uc008ohr.2; mouse.
DR CTD; 60437; -.
DR MGI; MGI:2685856; Cdh26.
DR VEuPathDB; HostDB:ENSMUSG00000039155; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000161589; -.
DR InParanoid; P59862; -.
DR OMA; WRAKFNI; -.
DR OrthoDB; 158870at2759; -.
DR PhylomeDB; P59862; -.
DR TreeFam; TF316817; -.
DR BioGRID-ORCS; 381409; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cdh26; mouse.
DR PRO; PR:P59862; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P59862; protein.
DR Bgee; ENSMUSG00000039155; Expressed in olfactory epithelium and 33 other tissues.
DR ExpressionAtlas; P59862; baseline and differential.
DR Genevisible; P59862; MM.
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; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045294; F:alpha-catenin binding; ISS:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISS: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; ISS:UniProtKB.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0035710; P:CD4-positive, alpha-beta T cell activation; ISS: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 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..763
FT /note="Cadherin-like protein 26"
FT /id="PRO_0000003830"
FT TOPO_DOM 21..590
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..611
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 612..763
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 21..140
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 141..250
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 251..371
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 370..478
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 394
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 763 AA; 85084 MW; BBC59363837B2A35 CRC64;
MDTRGCAWLL LLLSLPQGQS HQPLHRSKRR WVLTTLELQE EDPGPFPKLV GELFNNMSNN
VSLIYLIRGP GVDEFPEIGL FSIEDHQSGK IYVHRPVDRE VTPSFMVHFD AVDRSTGKVV
DESLIFNIRI RDVNDHAPQF PEKEFNISVK ESQAAGQPIF QLLTVDLDQE NTPNSQVLYF
LVSQTPLLRE SGFRIDLISG EVRLSGCLHY ETAPLFTLIV RASDCGEPSL TSTATIHVSV
EDSNNHMPTF MEDRYEIRIS EGQVEQGVLY LPVQDGDSPF TPAWRTQFNI WDGNEEGHFD
IVTDPETNQG LLSIIKPLDY ESQVAHSLVV VVENQEQLFV CTEGQLQPLR KAMASTMVSV
QVLDTNDPPA FHPQSFIVSE EDGAWPAIQL GYFNATDPDR ADSQIRYKLV HDPENWVTVD
EKSGVVTTKK QIDRESPHVN DSFYTIIVHA VDNGLPPLTG TGTLMLFLSD VNDNAPTLRP
HSRHLEVCES AGSQPLLIEA EDADLDPYAD PFTFDLDNAQ GDVEETWMLR TKQGEGHSAE
LTMLRSVPPG DYLVPLFIAD RQGLAQKQTV HVRICSCRSG SECEEPSDTW LLWWALSPVG
AALMVLSAAL LCLLRCSCTF GPKRLRGFIP SDSGHQTLIV YNEESKVPSA QGCDTFFEPR
GVKTLLSSTP VYLDRMVPRQ QPLQLLEGRV VEAWSQKLQS IDVLEGDTGY LPHVYREEGE
CEGAETLSSL TFLEQDLSPK LLGCSGSKST PSEAMCFTSR VPS
