CAD24_HUMAN
ID CAD24_HUMAN Reviewed; 819 AA.
AC Q86UP0; D3DS44; Q86UP1; Q9NT84;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cadherin-24;
DE Flags: Precursor;
GN Name=CDH24; Synonyms=CDH11L; ORFNames=UNQ2834/PRO34009;
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] (ISOFORMS 1 AND 2), FUNCTION, AND INTERACTION
RP WITH CATENINS.
RX PubMed=12734196; DOI=10.1074/jbc.m304119200;
RA Katafiasz B.J., Nieman M.T., Wheelock M.J., Johnson K.R.;
RT "Characterization of cadherin-24, a novel alternatively spliced type II
RT cadherin.";
RL J. Biol. Chem. 278:27513-27519(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
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.
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
CC adhesion. {ECO:0000269|PubMed:12734196}.
CC -!- SUBUNIT: Associates with alpha-, beta- and delta-catenins.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long form;
CC IsoId=Q86UP0-1; Sequence=Displayed;
CC Name=2; Synonyms=Short form;
CC IsoId=Q86UP0-2; Sequence=VSP_008717;
CC Name=3;
CC IsoId=Q86UP0-3; Sequence=VSP_008718, VSP_008719;
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; AY260900; AAP20590.1; -; mRNA.
DR EMBL; AY260901; AAP20591.1; -; mRNA.
DR EMBL; AY358199; AAQ88566.1; -; mRNA.
DR EMBL; AL137477; CAB70758.1; -; mRNA.
DR EMBL; CH471078; EAW66190.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66192.1; -; Genomic_DNA.
DR CCDS; CCDS9585.1; -. [Q86UP0-1]
DR CCDS; CCDS9586.1; -. [Q86UP0-2]
DR PIR; T46418; T46418.
DR RefSeq; NP_071923.2; NM_022478.3. [Q86UP0-1]
DR RefSeq; NP_659422.2; NM_144985.3. [Q86UP0-2]
DR AlphaFoldDB; Q86UP0; -.
DR SMR; Q86UP0; -.
DR BioGRID; 122158; 5.
DR IntAct; Q86UP0; 2.
DR STRING; 9606.ENSP00000380517; -.
DR GlyGen; Q86UP0; 3 sites.
DR iPTMnet; Q86UP0; -.
DR PhosphoSitePlus; Q86UP0; -.
DR BioMuta; CDH24; -.
DR DMDM; 38257450; -.
DR UCD-2DPAGE; Q86UP0; -.
DR MassIVE; Q86UP0; -.
DR PaxDb; Q86UP0; -.
DR PeptideAtlas; Q86UP0; -.
DR PRIDE; Q86UP0; -.
DR ProteomicsDB; 69838; -. [Q86UP0-1]
DR ProteomicsDB; 69839; -. [Q86UP0-2]
DR Antibodypedia; 22384; 116 antibodies from 21 providers.
DR DNASU; 64403; -.
DR Ensembl; ENST00000267383.5; ENSP00000267383.5; ENSG00000139880.21. [Q86UP0-1]
DR Ensembl; ENST00000397359.7; ENSP00000380517.3; ENSG00000139880.21. [Q86UP0-1]
DR Ensembl; ENST00000487137.7; ENSP00000434821.2; ENSG00000139880.21. [Q86UP0-2]
DR Ensembl; ENST00000554034.5; ENSP00000452493.1; ENSG00000139880.21. [Q86UP0-2]
DR GeneID; 64403; -.
DR KEGG; hsa:64403; -.
DR MANE-Select; ENST00000487137.7; ENSP00000434821.2; NM_144985.4; NP_659422.2. [Q86UP0-2]
DR UCSC; uc001wil.4; human. [Q86UP0-1]
DR CTD; 64403; -.
DR DisGeNET; 64403; -.
DR GeneCards; CDH24; -.
DR HGNC; HGNC:14265; CDH24.
DR HPA; ENSG00000139880; Low tissue specificity.
DR MIM; 618599; gene.
DR neXtProt; NX_Q86UP0; -.
DR OpenTargets; ENSG00000139880; -.
DR PharmGKB; PA26297; -.
DR VEuPathDB; HostDB:ENSG00000139880; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000159567; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; Q86UP0; -.
DR OMA; ICRCKPD; -.
DR OrthoDB; 268531at2759; -.
DR PhylomeDB; Q86UP0; -.
DR TreeFam; TF329887; -.
DR PathwayCommons; Q86UP0; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; Q86UP0; -.
DR SIGNOR; Q86UP0; -.
DR BioGRID-ORCS; 64403; 24 hits in 1078 CRISPR screens.
DR GenomeRNAi; 64403; -.
DR Pharos; Q86UP0; Tbio.
DR PRO; PR:Q86UP0; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q86UP0; protein.
DR Bgee; ENSG00000139880; Expressed in ganglionic eminence and 115 other tissues.
DR ExpressionAtlas; Q86UP0; baseline and differential.
DR Genevisible; Q86UP0; HS.
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; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0045294; F:alpha-catenin binding; IPI:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:MGI.
DR GO; GO:0070097; F:delta-catenin binding; IPI:UniProtKB.
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; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT PROPEP 21..44
FT /evidence="ECO:0000255"
FT /id="PRO_0000003827"
FT CHAIN 45..819
FT /note="Cadherin-24"
FT /id="PRO_0000003828"
FT TOPO_DOM 45..641
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..819
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..517
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 517..630
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 768..800
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 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..427
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008718"
FT VAR_SEQ 428..492
FT /note="EGTIHTAAPLDREARAWHNLTVLATELGWSWGPERGWVPLLVAEWSAPAAPP
FT QRSPVGSAVGIPQ -> MNIVCTWYCSIHSATLFSTCTLHAYFMCFLCMLYASCGIHAH
FT APHMLRVNCVVCVWRVCFGVLPS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_008719"
FT VAR_SEQ 455..492
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12734196,
FT ECO:0000303|PubMed:12975309"
FT /id="VSP_008717"
SQ SEQUENCE 819 AA; 87752 MW; 9083034F18BA7E4A CRC64;
MWGLVRLLLA WLGGWGCMGR LAAPARAWAG SREHPGPALL RTRRSWVWNQ FFVIEEYAGP
EPVLIGKLHS DVDRGEGRTK YLLTGEGAGT VFVIDEATGN IHVTKSLDRE EKAQYVLLAQ
AVDRASNRPL EPPSEFIIKV QDINDNPPIF PLGPYHATVP EMSNVGTSVI QVTAHDADDP
SYGNSAKLVY TVLDGLPFFS VDPQTGVVRT AIPNMDRETQ EEFLVVIQAK DMGGHMGGLS
GSTTVTVTLS DVNDNPPKFP QSLYQFSVVE TAGPGTLVGR LRAQDPDLGD NALMAYSILD
GEGSEAFSIS TDLQGRDGLL TVRKPLDFES QRSYSFRVEA TNTLIDPAYL RRGPFKDVAS
VRVAVQDAPE PPAFTQAAYH LTVPENKAPG TLVGQISAAD LDSPASPIRY SILPHSDPER
CFSIQPEEGT IHTAAPLDRE ARAWHNLTVL ATELGWSWGP ERGWVPLLVA EWSAPAAPPQ
RSPVGSAVGI PQDSSAQASR VQVAIQTLDE NDNAPQLAEP YDTFVCDSAA PGQLIQVIRA
LDRDEVGNSS HVSFQGPLGP DANFTVQDNR DGSASLLLPS RPAPPRHAPY LVPIELWDWG
QPALSSTATV TVSVCRCQPD GSVASCWPEA HLSAAGLSTG ALLAIITCVG ALLALVVLFV
ALRRQKQEAL MVLEEEDVRE NIITYDDEGG GEEDTEAFDI TALQNPDGAA PPAPGPPARR
DVLPRARVSR QPRPPGPADV AQLLALRLRE ADEDPGVPPY DSVQVYGYEG RGSSCGSLSS
LGSGSEAGGA PGPAEPLDDW GPLFRTLAEL YGAKEPPAP
