CADH8_MOUSE
ID CADH8_MOUSE Reviewed; 799 AA.
AC P97291; G3UVU4;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cadherin-8;
DE Flags: Precursor;
GN Name=Cdh8;
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 STRAIN=Swiss Webster / NIH;
RX PubMed=9022055;
RX DOI=10.1002/(sici)1097-0177(199702)208:2<178::aid-aja5>3.0.co;2-f;
RA Korematsu K., Redies C.;
RT "Restricted expression of cadherin-8 in segmental and functional
RT subdivisions of the embryonic mouse brain.";
RL Dev. Dyn. 208:178-189(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-795, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC -!- INTERACTION:
CC P97291; P97291: Cdh8; NbExp=2; IntAct=EBI-15719457, EBI-15719457;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X95600; CAA64857.1; -; mRNA.
DR EMBL; AC102643; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC162867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466525; EDL11191.1; -; Genomic_DNA.
DR CCDS; CCDS40448.1; -.
DR RefSeq; NP_031693.2; NM_007667.3.
DR RefSeq; XP_006530694.1; XM_006530631.2.
DR PDB; 1ZXK; X-ray; 2.00 A; A/B=62-159.
DR PDB; 2A62; X-ray; 4.50 A; A=63-383.
DR PDBsum; 1ZXK; -.
DR PDBsum; 2A62; -.
DR AlphaFoldDB; P97291; -.
DR SMR; P97291; -.
DR DIP; DIP-46028N; -.
DR STRING; 10090.ENSMUSP00000117326; -.
DR GlyConnect; 2172; 1 N-Linked glycan (1 site).
DR GlyGen; P97291; 4 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P97291; -.
DR PhosphoSitePlus; P97291; -.
DR MaxQB; P97291; -.
DR PaxDb; P97291; -.
DR PRIDE; P97291; -.
DR ProteomicsDB; 265418; -.
DR Antibodypedia; 2754; 222 antibodies from 27 providers.
DR DNASU; 12564; -.
DR Ensembl; ENSMUST00000128860; ENSMUSP00000117326; ENSMUSG00000036510.
DR GeneID; 12564; -.
DR KEGG; mmu:12564; -.
DR UCSC; uc009mzo.2; mouse.
DR CTD; 1006; -.
DR MGI; MGI:107434; Cdh8.
DR VEuPathDB; HostDB:ENSMUSG00000036510; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000153691; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; P97291; -.
DR OMA; IYTAPMN; -.
DR OrthoDB; 188978at2759; -.
DR PhylomeDB; P97291; -.
DR TreeFam; TF329887; -.
DR Reactome; R-MMU-418990; Adherens junctions interactions.
DR BioGRID-ORCS; 12564; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Cdh8; mouse.
DR EvolutionaryTrace; P97291; -.
DR PRO; PR:P97291; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P97291; protein.
DR Bgee; ENSMUSG00000036510; Expressed in habenula and 129 other tissues.
DR ExpressionAtlas; P97291; baseline and differential.
DR Genevisible; P97291; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0043679; C:axon terminus; IDA:MGI.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0043083; C:synaptic cleft; IDA:MGI.
DR GO; GO:0097060; C:synaptic membrane; IDA:SynGO.
DR GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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: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:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR GO; GO:0009409; P:response to cold; IMP:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP: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; IPR027397; Catenin-bd_sf.
DR PANTHER; PTHR24027; PTHR24027; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF01049; Cadherin_C; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 3.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane;
KW Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..61
FT /evidence="ECO:0000255"
FT /id="PRO_0000003775"
FT CHAIN 62..799
FT /note="Cadherin-8"
FT /id="PRO_0000003776"
FT TOPO_DOM 62..621
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 622..642
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 643..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 62..167
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 168..276
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 277..391
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 392..494
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 495..616
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 473
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 544
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 247
FT /note="K -> I (in Ref. 1; CAA64857)"
FT /evidence="ECO:0000305"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:1ZXK"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1ZXK"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1ZXK"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1ZXK"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:1ZXK"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:1ZXK"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1ZXK"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1ZXK"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:1ZXK"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1ZXK"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:1ZXK"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1ZXK"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1ZXK"
FT STRAND 151..157
FT /evidence="ECO:0007829|PDB:1ZXK"
SQ SEQUENCE 799 AA; 88215 MW; 0EF1285E5DD67F76 CRC64;
MPERLAETLM DLWTPLIILW ITLPSCVYTA PMNQAHVLTT GSPLELSRQS EDMRILSRSK
RGWVWNQMFV LEEFSGPEPI LVGRLHTDLD PGSKKIKYIL SGDGAGTIFQ INDITGDIHA
IKRLDREEKA EYTLTAQAVD FETNKPLEPP SEFIIKVQDI NDNAPEFLNG PYHATVPEMS
ILGTSVTNVT ATDADDPVYG NSAKLVYSIL EGQPYFSIEP ETAIIKTALP NMDREAKEEY
LVVIQAKDMG GHSGGLSGTT TLTVTLTDVN DNPPKFAQSL YHFSVPEDVV LGTAIGRVKA
NDQDIGENAQ SSYDIIDGDG TALFEITSDA QAQDGVIRLR KPLDFETKKS YTLKVEAANI
HIDPRFSSRG PFKDTATVKI VVEDADEPPV FSSPTYLLEV HENAALNSVI GQVTARDPDI
TSSPIRFSID RHTDLERQFN INADDGKITL ATPLDRELSV WHNITIIATE IRNHSQISRV
PVAIKVLDVN DNAPEFASEY EAFLCENGKP GQVIQTVSAM DKDDPKNGHF FLYSLLPEMV
NNPNFTIKKN EDNSLSILAK HNGFNRQKQE VYLLPIVISD SGNPPLSSTS TLTIRVCGCS
NDGVVQSCNV EAYVLPIGLS MGALIAILAC IILLLVIVVL FVTLRRHKNE PLIIKDDEDV
RENIIRYDDE GGGEEDTEAF DIATLQNPDG INGFLPRKDI KPDLQFMPRQ GLAPVPNGVD
VDEFINVRLH EADNDPTAPP YDSIQIYGYE GRGSVAGSLS SLESTTSDSD QNFDYLSDWG
PRFKRLGELY SVGESDKET
