ID   CADH8_RAT               Reviewed;         799 AA.
AC   O54800; O54801;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   24-JAN-2024, entry version 130.
DE   RecName: Full=Cadherin-8;
DE   Flags: Precursor;
GN   Name=Cdh8;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Brain;
RX   PubMed=9521872; DOI=10.1006/geno.1997.5152;
RA   Kido M., Obata S., Tanihara H., Rochelle J.M., Seldin M.F., Taketani S.,
RA   Suzuki S.T.;
RT   "Molecular properties and chromosomal location of cadherin-8.";
RL   Genomics 48:186-194(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O54800-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O54800-2; Sequence=VSP_000638, VSP_000639;
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; AB010436; BAA24452.1; -; mRNA.
DR   EMBL; AB010437; BAA24453.1; -; mRNA.
DR   AlphaFoldDB; O54800; -.
DR   SMR; O54800; -.
DR   STRING; 10116.ENSRNOP00000072182; -.
DR   GlyCosmos; O54800; 4 sites, No reported glycans.
DR   GlyGen; O54800; 4 sites.
DR   PhosphoSitePlus; O54800; -.
DR   PaxDb; 10116-ENSRNOP00000062147; -.
DR   UCSC; RGD:69286; rat. [O54800-1]
DR   AGR; RGD:69286; -.
DR   RGD; 69286; Cdh8.
DR   eggNOG; KOG3594; Eukaryota.
DR   InParanoid; O54800; -.
DR   PhylomeDB; O54800; -.
DR   Reactome; R-RNO-418990; Adherens junctions interactions.
DR   PRO; PR:O54800; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0043679; C:axon terminus; ISO:RGD.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR   GO; GO:0043083; C:synaptic cleft; ISO:RGD.
DR   GO; GO:0097060; C:synaptic membrane; ISO:RGD.
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; ISO:RGD.
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; NAS:RGD.
DR   GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR   GO; GO:0007268; P:chemical synaptic transmission; ISO:RGD.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0050807; P:regulation of synapse organization; ISO:RGD.
DR   GO; GO:0009409; P:response to cold; ISO:RGD.
DR   GO; GO:0007283; P:spermatogenesis; NAS:RGD.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR   CDD; cd11304; Cadherin_repeat; 5.
DR   Gene3D; 2.60.40.60; Cadherins; 5.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 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_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF273; CADHERIN-8; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 5.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 5.
DR   SUPFAM; SSF49313; Cadherin-like; 5.
DR   PROSITE; PS00232; CADHERIN_1; 3.
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   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_0000003777"
FT   CHAIN           62..799
FT                   /note="Cadherin-8"
FT                   /id="PRO_0000003778"
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:0000250|UniProtKB:P97291"
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   VAR_SEQ         514..532
FT                   /note="IQTVSAMDKDDPKNGHFFL -> NISMLLILNMFVYNCFLVN (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000638"
FT   VAR_SEQ         533..799
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000639"
SQ   SEQUENCE   799 AA;  88333 MW;  F01D145A80966CB6 CRC64;
     MPERLAETLL DLWTPLIILW ITLPSFVYMA PMNQAHVLTT GSPLELSRQS EEMRILNRSK
     RGWVWNQMFV LEEFSGPEPI LVGRLHTDLD PGSKKIKYIL SGDGAGTIFQ INDITGDIHA
     IKRLDREEKA EYTLTAQAVD WETNKPLEPP SEFIIKVQDI NDNAPEFLNG PYHATVPEMS
     ILGTSVTNVT ATDADDPVYG NSAKLVYSIL EGQPYFSIEP ETAIIKTALP NMDREAKEEY
     LVVIQAKDMG GHSGGLSGTT TLTVTLTDVN DNPPKFAQSL YHFSVPEDVV LGTAIGRVKA
     NDQDIGENAQ SSYDIIDGDG TALFEITSDA QAQDGVIRLR KPLDFETKKS YTLKVEAANI
     HIDPRFSGRG PFKDTATVKI VVEDADEPPV FSSPTYLLEV HENAALNSVI GQVTARDPDI
     TSSPIRFSID RHTDLERQFN INADDGKITL ATPLDRELSV WHNISIIATE IRNHSQISRV
     PVAIKVLDVN DNAPEFASEY EAFLCENGKP GQVIQTVSAM DKDDPKNGHF FLYSLLPEMV
     NNPNFTIKKN EDNSLSILAK HNGFNRQKQE VYLLPIVISD SGNPPLSSTS TLTIRVCGCS
     NDGVVQSCNV EPYVLPIGLS MGALIAILAC IILLLVIVVL FVTLRRHKNE PLIIKDDEDV
     RENIIRYDDE GGGEEDTEAF DIATLQNPDG INGFLPRKDI KPDLQFMPRQ GLAPVPNGVD
     VDEFINVRLH EADNDPTAPP YDSIQIYGYE GRGSVAGSLS SLESTTSDSD QNFDYLSDWG
     PRFKRLGELY SVGESDKET
//