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   16-SEP-2015, entry version 120.
DE   RecName: Full=Cadherin-8;
DE   Flags: Precursor;
GN   Name=Cdh8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RP   BY 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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC       They preferentially interact with themselves in a homophilic
CC       manner in connecting cells; cadherins may thus contribute to the
CC       sorting of heterogeneous cell types.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- DOMAIN: Three calcium ions are usually bound at the interface of
CC       each cadherin domain and rigidify the connections, imparting a
CC       strong curvature to the full-length ectodomain. {ECO:0000250}.
CC   -!- SIMILARITY: Contains 5 cadherin domains. {ECO:0000255|PROSITE-
CC       ProRule:PRU00043}.
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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_006530631.1.
DR   UniGene; Mm.441131; -.
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   ProteinModelPortal; P97291; -.
DR   SMR; P97291; 63-597, 729-790.
DR   DIP; DIP-46028N; -.
DR   STRING; 10090.ENSMUSP00000117326; -.
DR   PhosphoSite; P97291; -.
DR   MaxQB; P97291; -.
DR   PaxDb; P97291; -.
DR   PRIDE; P97291; -.
DR   Ensembl; ENSMUST00000128860; ENSMUSP00000117326; ENSMUSG00000036510.
DR   GeneID; 12564; -.
DR   UCSC; uc009mzo.2; mouse.
DR   CTD; 1006; -.
DR   MGI; MGI:107434; Cdh8.
DR   eggNOG; NOG330572; -.
DR   GeneTree; ENSGT00760000118954; -.
DR   HOGENOM; HOG000231252; -.
DR   HOVERGEN; HBG005217; -.
DR   InParanoid; P97291; -.
DR   OMA; EEYFVVI; -.
DR   TreeFam; TF329887; -.
DR   Reactome; R-MMU-418990; Adherens junctions interactions.
DR   EvolutionaryTrace; P97291; -.
DR   NextBio; 281644; -.
DR   PRO; PR:P97291; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   CleanEx; MM_CDH8; -.
DR   ExpressionAtlas; P97291; baseline.
DR   GO; GO:0043679; C:axon terminus; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043083; C:synaptic cleft; IDA:MGI.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0009409; P:response to cold; IMP:MGI.
DR   GO; GO:0007268; P:synaptic transmission; IMP:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IMP:MGI.
DR   Gene3D; 2.60.40.60; -; 5.
DR   Gene3D; 4.10.900.10; -; 1.
DR   InterPro; IPR002126; Cadherin.
DR   InterPro; IPR015919; Cadherin-like.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR000233; Cadherin_cytoplasmic-dom.
DR   InterPro; IPR027397; Catenin_binding_dom.
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; Complete proteome; Glycoprotein;
KW   Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     29       {ECO:0000255}.
FT   PROPEP       30     61       {ECO:0000255}.
FT                                /FTId=PRO_0000003775.
FT   CHAIN        62    799       Cadherin-8.
FT                                /FTId=PRO_0000003776.
FT   TOPO_DOM     62    621       Extracellular. {ECO:0000255}.
FT   TRANSMEM    622    642       Helical. {ECO:0000255}.
FT   TOPO_DOM    643    799       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       62    167       Cadherin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      168    276       Cadherin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      277    391       Cadherin 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      392    494       Cadherin 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      495    616       Cadherin 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   MOD_RES     795    795       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   CARBOHYD    188    188       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    463    463       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    473    473       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    544    544       N-linked (GlcNAc...). {ECO:0000255}.
FT   CONFLICT    247    247       K -> I (in Ref. 1; CAA64857).
FT                                {ECO:0000305}.
FT   STRAND       67     70       {ECO:0000244|PDB:1ZXK}.
FT   HELIX        72     74       {ECO:0000244|PDB:1ZXK}.
FT   STRAND       76     78       {ECO:0000244|PDB:1ZXK}.
FT   STRAND       80     84       {ECO:0000244|PDB:1ZXK}.
FT   STRAND       96    102       {ECO:0000244|PDB:1ZXK}.
FT   TURN        106    108       {ECO:0000244|PDB:1ZXK}.
FT   STRAND      109    111       {ECO:0000244|PDB:1ZXK}.
FT   TURN        113    115       {ECO:0000244|PDB:1ZXK}.
FT   STRAND      117    120       {ECO:0000244|PDB:1ZXK}.
FT   TURN        126    128       {ECO:0000244|PDB:1ZXK}.
FT   STRAND      130    140       {ECO:0000244|PDB:1ZXK}.
FT   TURN        141    143       {ECO:0000244|PDB:1ZXK}.
FT   STRAND      146    148       {ECO:0000244|PDB:1ZXK}.
FT   STRAND      151    157       {ECO:0000244|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
//