CAD24_MOUSE
ID CAD24_MOUSE Reviewed; 781 AA.
AC Q6PFX6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Cadherin-24;
DE Flags: Precursor;
GN Name=Cdh24;
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 STRAIN=C57BL/6J; TISSUE=Brain;
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. Cadherin-24 mediate strong cell-cell adhesion
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Associates with alpha-, beta- and delta-catenins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
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; BC057373; AAH57373.1; -; mRNA.
DR CCDS; CCDS36923.1; -.
DR RefSeq; NP_955764.1; NM_199470.2.
DR AlphaFoldDB; Q6PFX6; -.
DR SMR; Q6PFX6; -.
DR STRING; 10090.ENSMUSP00000066005; -.
DR GlyGen; Q6PFX6; 3 sites.
DR PhosphoSitePlus; Q6PFX6; -.
DR PaxDb; Q6PFX6; -.
DR PRIDE; Q6PFX6; -.
DR ProteomicsDB; 265496; -.
DR Antibodypedia; 22384; 116 antibodies from 21 providers.
DR DNASU; 239096; -.
DR Ensembl; ENSMUST00000067784; ENSMUSP00000066005; ENSMUSG00000059674.
DR GeneID; 239096; -.
DR KEGG; mmu:239096; -.
DR UCSC; uc011zlc.1; mouse.
DR CTD; 64403; -.
DR MGI; MGI:1928330; Cdh24.
DR VEuPathDB; HostDB:ENSMUSG00000059674; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000159567; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q6PFX6; -.
DR OMA; ICRCKPD; -.
DR OrthoDB; 268531at2759; -.
DR PhylomeDB; Q6PFX6; -.
DR TreeFam; TF329887; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 239096; 1 hit in 74 CRISPR screens.
DR PRO; PR:Q6PFX6; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q6PFX6; protein.
DR Bgee; ENSMUSG00000059674; Expressed in thymus and 65 other tissues.
DR ExpressionAtlas; Q6PFX6; 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:0005911; C:cell-cell junction; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045294; F:alpha-catenin binding; ISO:MGI.
DR GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0070097; F:delta-catenin binding; ISO:MGI.
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:0000902; P:cell morphogenesis; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; ISO:MGI.
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 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; 4.
DR Pfam; PF01049; Cadherin_C; 1.
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; 5.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..44
FT /evidence="ECO:0000255"
FT /id="PRO_0000320100"
FT CHAIN 45..781
FT /note="Cadherin-24"
FT /id="PRO_0000320101"
FT TOPO_DOM 45..603
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 625..781
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..150
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 151..259
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 260..374
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 375..479
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 479..592
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 665..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 510
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 525
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 781 AA; 84104 MW; 15996D6E6C9835AA CRC64;
MWGLVRLLLA WLGGWGCMGR LAAPVPAWAG SRGHSGPTLL RTRRSWVWNQ FFVIEEYSGP
EPVLIGKLHS DVDRGEGRTK YLLTGEGAGT VFVIDEATGN IHVTKSLDRE EKAQYVLLAQ
AVDRASNRPL EPPSEFIIKV QDINDNPPVF PLGPYHATVP EMSNVGTSVI QVTAHDADDP
SYGNSAKLVY TVLDGLPFFS VDPQTGVVRT AIPNMDRETQ EEFLVVIQAK DMGGHMGGLS
GSTTVTVTLS DVNDNPPKFP QSLYQFSVVE TAGPGTLVGR LKAQDPDLGD NALVAYSILN
GEGSEVFSIS TDSQGQDGLL TVRKPLDFET RRSYTFRVEA TNTLIDPAYL RRGPFKDVAS
VRVTVQDAPE PPAFTQATYH LAVPENKAPG TLVGQISASD LDSPASPIRY SILPHSDPER
CFSIEPEDGT IRTAVRLDRE ARVWHNLTIL ATELDSSAQS SRVQVAIQTL DENDNAPQLA
EPYDIFVCDS AAPGQLIKVI RALDRDEVGN SSQVSLQGPV GPDANFTVRD NRDGSASLLL
PSRPAPPRQA PYLIPIELWD WGQPALSSTA TVTVSVCRCR PDGSMASCWP EAQLSPTGLS
TGALLAIVTC MGTLLALVVL FVALRRQKQE ALMVLEEEDV RENIITYDDE GGGEEDTEAF
DITALQNPDG AAPPAAGPPV RRDVLPRTRA PRQPRPPGPA DVVQLLALRL READEDPSVP
PYDSVQVYGY EGRGSSCGSL SSLGSGSEAG GVPGPAEPLD DWGPLFRTLA ELYGAKEPPA
P
