CADH8_HUMAN
ID CADH8_HUMAN Reviewed; 799 AA.
AC P55286; B3KWC1; Q14DC6; Q9ULB2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cadherin-8;
DE Flags: Precursor;
GN Name=CDH8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10861224; DOI=10.1042/0264-6021:3490159;
RA Shimoyama Y., Tsujimoto G., Kitajima M., Natori M.;
RT "Identification of three human type-II classic cadherins and frequent
RT heterophilic interactions between different subclasses of type-II classic
RT cadherins.";
RL Biochem. J. 349:159-167(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-799.
RC TISSUE=Brain;
RX PubMed=7982033; DOI=10.3109/15419069409014199;
RA Tanihara H., Sano K., Heimark R.L., St John T., Suzuki S.;
RT "Cloning of five human cadherins clarifies characteristic features of
RT cadherin extracellular domain and provides further evidence for two
RT structurally different types of cadherin.";
RL Cell Adhes. Commun. 2:15-26(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 294-799.
RC TISSUE=Fetal brain;
RX PubMed=2059658; DOI=10.1091/mbc.2.4.261;
RA Suzuki S., Sano K., Tanihara H.;
RT "Diversity of the cadherin family: evidence for eight new cadherins in
RT nervous tissue.";
RL Cell Regul. 2:261-270(1991).
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 -!- TISSUE SPECIFICITY: Mainly expressed in brain. Found in certain nerve
CC cell lines, such as retinoblasts, glioma cells and neuroblasts.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA35628.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB035305; BAA87419.1; -; mRNA.
DR EMBL; AK124734; BAG54083.1; -; mRNA.
DR EMBL; BC113416; AAI13417.1; -; mRNA.
DR EMBL; L34060; AAA35628.1; ALT_INIT; mRNA.
DR CCDS; CCDS10802.1; -.
DR RefSeq; NP_001787.2; NM_001796.4.
DR AlphaFoldDB; P55286; -.
DR SMR; P55286; -.
DR BioGRID; 107441; 21.
DR IntAct; P55286; 17.
DR STRING; 9606.ENSP00000462701; -.
DR GlyGen; P55286; 6 sites.
DR iPTMnet; P55286; -.
DR PhosphoSitePlus; P55286; -.
DR BioMuta; CDH8; -.
DR DMDM; 13432121; -.
DR jPOST; P55286; -.
DR MassIVE; P55286; -.
DR PaxDb; P55286; -.
DR PeptideAtlas; P55286; -.
DR PRIDE; P55286; -.
DR ProteomicsDB; 56836; -.
DR TopDownProteomics; P55286; -.
DR Antibodypedia; 2754; 222 antibodies from 27 providers.
DR DNASU; 1006; -.
DR Ensembl; ENST00000577390.6; ENSP00000462701.1; ENSG00000150394.14.
DR GeneID; 1006; -.
DR KEGG; hsa:1006; -.
DR MANE-Select; ENST00000577390.6; ENSP00000462701.1; NM_001796.5; NP_001787.2.
DR UCSC; uc002eog.3; human.
DR CTD; 1006; -.
DR DisGeNET; 1006; -.
DR GeneCards; CDH8; -.
DR HGNC; HGNC:1767; CDH8.
DR HPA; ENSG00000150394; Tissue enriched (brain).
DR MIM; 603008; gene.
DR neXtProt; NX_P55286; -.
DR OpenTargets; ENSG00000150394; -.
DR PharmGKB; PA26304; -.
DR VEuPathDB; HostDB:ENSG00000150394; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000153691; -.
DR HOGENOM; CLU_005284_3_1_1; -.
DR InParanoid; P55286; -.
DR OMA; IYTAPMN; -.
DR OrthoDB; 188978at2759; -.
DR PhylomeDB; P55286; -.
DR TreeFam; TF329887; -.
DR PathwayCommons; P55286; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR SignaLink; P55286; -.
DR SIGNOR; P55286; -.
DR BioGRID-ORCS; 1006; 10 hits in 1068 CRISPR screens.
DR ChiTaRS; CDH8; human.
DR GeneWiki; CDH8; -.
DR GenomeRNAi; 1006; -.
DR Pharos; P55286; Tbio.
DR PRO; PR:P55286; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P55286; protein.
DR Bgee; ENSG00000150394; Expressed in endothelial cell and 133 other tissues.
DR ExpressionAtlas; P55286; baseline and differential.
DR Genevisible; P55286; HS.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0043679; C:axon terminus; IBA:GO_Central.
DR GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0043083; C:synaptic cleft; IBA:GO_Central.
DR GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
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; IEA:Ensembl.
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:0007155; P:cell adhesion; TAS:ProtInc.
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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Cleavage on pair of basic residues;
KW Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT PROPEP 30..61
FT /evidence="ECO:0000255"
FT /id="PRO_0000003773"
FT CHAIN 62..799
FT /note="Cadherin-8"
FT /id="PRO_0000003774"
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 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 355
FT /note="V -> D (in Ref. 4; AAA35628)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="K -> QK (in Ref. 4; AAA35628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 88253 MW; 9B119B86039C6A0A CRC64;
MPERLAEMLL DLWTPLIILW ITLPPCIYMA PMNQSQVLMS GSPLELNSLG EEQRILNRSK
RGWVWNQMFV LEEFSGPEPI LVGRLHTDLD PGSKKIKYIL SGDGAGTIFQ INDVTGDIHA
IKRLDREEKA EYTLTAQAVD WETSKPLEPP SEFIIKVQDI NDNAPEFLNG PYHATVPEMS
ILGTSVTNVT ATDADDPVYG NSAKLVYSIL EGQPYFSIEP ETAIIKTALP NMDREAKEEY
LVVIQAKDMG GHSGGLSGTT TLTVTLTDVN DNPPKFAQSL YHFSVPEDVV LGTAIGRVKA
NDQDIGENAQ SSYDIIDGDG TALFEITSDA QAQDGIIRLR KPLDFETKKS YTLKVEAANV
HIDPRFSGRG PFKDTATVKI VVEDADEPPV FSSPTYLLEV HENAALNSVI GQVTARDPDI
TSSPIRFSID RHTDLERQFN INADDGKITL ATPLDRELSV WHNITIIATE IRNHSQISRV
PVAIKVLDVN DNAPEFASEY EAFLCENGKP GQVIQTVSAM DKDDPKNGHY FLYSLLPEMV
NNPNFTIKKN EDNSLSILAK HNGFNRQKQE VYLLPIIISD SGNPPLSSTS TLTIRVCGCS
NDGVVQSCNV EAYVLPIGLS MGALIAILAC IILLLVIVVL FVTLRRHKNE PLIIKDDEDV
RENIIRYDDE GGGEEDTEAF DIATLQNPDG INGFLPRKDI KPDLQFMPRQ GLAPVPNGVD
VDEFINVRLH EADNDPTAPP YDSIQIYGYE GRGSVAGSLS SLESTTSDSD QNFDYLSDWG
PRFKRLGELY SVGESDKET
