CADH4_MOUSE
ID CADH4_MOUSE Reviewed; 913 AA.
AC P39038;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cadherin-4;
DE AltName: Full=Retinal cadherin;
DE Short=R-CAD;
DE Short=R-cadherin;
DE Flags: Precursor;
GN Name=Cdh4;
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 [MRNA].
RC TISSUE=Pancreatic islet;
RX PubMed=8247017; DOI=10.1210/mend.7.9.8247017;
RA Hutton J.C., Christofori G., Chi W.Y., Edman U., Guest P.C., Hanahan D.,
RA Kelly R.B.;
RT "Molecular cloning of mouse pancreatic islet R-cadherin: differential
RT expression in endocrine and exocrine tissue.";
RL Mol. Endocrinol. 7:1151-1160(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8270638; DOI=10.1242/jcs.106.1.401;
RA Matsunami H., Miyatani S., Inoue T., Copeland N.G., Gilbert D.,
RA Jenkins N.A., Takeichi M.;
RT "Cell binding specificity of mouse R-cadherin and chromosomal mapping of
RT the gene.";
RL J. Cell Sci. 106:401-409(1993).
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. May play an important role in retinal
CC development.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Distributed widely in mouse tissues with high
CC levels present in brain, skeletal muscle and thymus.
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; X69966; CAA49589.1; -; mRNA.
DR EMBL; D14888; BAA03605.1; -; mRNA.
DR CCDS; CCDS17164.1; -.
DR PIR; A47543; A47543.
DR RefSeq; NP_033997.1; NM_009867.3.
DR AlphaFoldDB; P39038; -.
DR SMR; P39038; -.
DR BioGRID; 198639; 1.
DR IntAct; P39038; 2.
DR MINT; P39038; -.
DR STRING; 10090.ENSMUSP00000000314; -.
DR GlyConnect; 2170; 7 N-Linked glycans (2 sites).
DR GlyGen; P39038; 7 sites, 7 N-linked glycans (2 sites).
DR iPTMnet; P39038; -.
DR PhosphoSitePlus; P39038; -.
DR jPOST; P39038; -.
DR MaxQB; P39038; -.
DR PaxDb; P39038; -.
DR PeptideAtlas; P39038; -.
DR PRIDE; P39038; -.
DR ProteomicsDB; 281744; -.
DR TopDownProteomics; P39038; -.
DR Antibodypedia; 2666; 334 antibodies from 32 providers.
DR DNASU; 12561; -.
DR Ensembl; ENSMUST00000000314; ENSMUSP00000000314; ENSMUSG00000000305.
DR GeneID; 12561; -.
DR KEGG; mmu:12561; -.
DR UCSC; uc008ohv.2; mouse.
DR CTD; 1002; -.
DR MGI; MGI:99218; Cdh4.
DR VEuPathDB; HostDB:ENSMUSG00000000305; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000158073; -.
DR HOGENOM; CLU_005284_2_0_1; -.
DR InParanoid; P39038; -.
DR OMA; QICERPG; -.
DR OrthoDB; 191117at2759; -.
DR PhylomeDB; P39038; -.
DR TreeFam; TF316817; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR Reactome; R-MMU-525793; Myogenesis.
DR BioGRID-ORCS; 12561; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cdh4; mouse.
DR PRO; PR:P39038; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P39038; protein.
DR Bgee; ENSMUSG00000000305; Expressed in glomerular capsule and 222 other tissues.
DR ExpressionAtlas; P39038; baseline and differential.
DR Genevisible; P39038; MM.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048675; P:axon extension; IDA:MGI.
DR GO; GO:0007411; P:axon guidance; IDA:MGI.
DR GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IDA:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; IDA:MGI.
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; IPR014868; Cadherin_pro_dom.
DR InterPro; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF01049; Cadherin_C; 1.
DR Pfam; PF08758; Cadherin_pro; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SMART; SM01055; Cadherin_pro; 1.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 3.
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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..166
FT /evidence="ECO:0000255"
FT /id="PRO_0000003751"
FT CHAIN 167..913
FT /note="Cadherin-4"
FT /id="PRO_0000003752"
FT TOPO_DOM 167..731
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 732..753
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 754..913
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 167..274
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 275..389
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 390..504
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 505..610
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 611..721
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 554
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 658
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 699
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 913 AA; 100030 MW; 1245A8CE8C338481 CRC64;
MTTGSVLPLL LLGLSGALRA HREDLTVREA CKAGFSEEGY TALISPNVLE GEKLLKVEFS
SCVGTKGMQY ETNSLDFKVG ADGTVFATRE LKIPSEQVAF TVTARERQSA EQWAAMVRLL
VAQTSSAHSE HKKGQTVALD PSQPPNDTLL PWPQHQSSGG LRRQKRDWVI PPINVPENSR
GPFPQQLVRI RSDKDNDIPI RYSITGVGAD QPPMEVFNID SMSGRMYVTR PMDREERASY
HLRAHAVDMN GNKVENPIDL YIYVIDMNDN RPEFINQVYN GSVDEGSKPG TYVMTVTAND
ADDSTTANGM VRYRIVTQTP QSPSQNMFTI NSETGDIVTV AAGLDREKVQ QYTVIVQATD
MEGNLNYGLS NTATAIITVT DVNDNPPEFT TSTFAGEVPE NRIETVVANL TVMDRDQPHS
PNWNAVYRII SGDPSGHFSV RTDPVTNEGM VTVVKAVDYE LNRAFMLTVM VSNQAPLASG
IQMSFQSTAG VTISVTDVNE APYFPSNHKL IRLEEGVPAG TALTTFSAVD PDRFMQQAVR
YSKLSDPANW LHINTSNGQI TTAAILDRES LYTKNNVYEA TFLAADNGIP PASGTGTLQI
YLIDINDNAP QLLPKEAQIC ERPGLNAINI TAADADMDPN IGPYVFELPF IPTTVRKNWT
ITRLNGDYAQ LSLRILYLEA GVYDVPIIVT DSGNPPLSNT SVIKVKVCPC DENGDCTTVG
AVAAAGLGTG AIVAILICIV ILLIMVLLFV VWMKRREKER HTKQLLIDPE DDVRDNILKY
DEEGGGEEDQ DYDLSQLQQP EAMEHVLSKT PGVRRVDERP VGAEPQYPVR PVVPHPGDIG
DFINEGLRAA DNDPTAPPYD SLLVFDYEGS GSTAGSVSSL NSSSSGDQDY DYLNDWGPRF
KKLADMYGGG EED
