CADH8_RAT
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 25-MAY-2022, entry version 123.
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.ENSRNOP00000062147; -.
DR GlyGen; O54800; 4 sites.
DR PaxDb; O54800; -.
DR PRIDE; O54800; -.
DR UCSC; RGD:69286; rat. [O54800-1]
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:0005887; C:integral component of plasma membrane; TAS: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: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; 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 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 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
