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Protein

Cadherin-8

Gene

CDH8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. adherens junction organization Source: Reactome
  2. cell adhesion Source: ProtInc
  3. cell-cell junction organization Source: Reactome
  4. cell junction assembly Source: Reactome
  5. homophilic cell adhesion via plasma membrane adhesion molecules Source: InterPro
  6. response to cold Source: Ensembl
  7. synaptic transmission, glutamatergic Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-8
Gene namesi
Name:CDH8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:1767. CDH8.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini62 – 621560ExtracellularSequence AnalysisAdd
BLAST
Transmembranei622 – 64221HelicalSequence AnalysisAdd
BLAST
Topological domaini643 – 799157CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. axon terminus Source: Ensembl
  2. integral component of membrane Source: UniProtKB-KW
  3. plasma membrane Source: Reactome
  4. synaptic cleft Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26304.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Propeptidei30 – 6132Sequence AnalysisPRO_0000003773Add
BLAST
Chaini62 – 799738Cadherin-8PRO_0000003774Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
Glycosylationi57 – 571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi188 – 1881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi473 – 4731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi544 – 5441N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Cleavage on pair of basic residues, Glycoprotein

Proteomic databases

PaxDbiP55286.
PeptideAtlasiP55286.
PRIDEiP55286.

PTM databases

PhosphoSiteiP55286.

Expressioni

Tissue specificityi

Mainly expressed in brain. Found in certain nerve cell lines, such as retinoblasts, glioma cells and neuroblasts.

Gene expression databases

BgeeiP55286.
CleanExiHS_CDH8.
ExpressionAtlasiP55286. baseline and differential.
GenevestigatoriP55286.

Organism-specific databases

HPAiHPA014908.

Interactioni

Protein-protein interaction databases

BioGridi107441. 1 interaction.
STRINGi9606.ENSP00000299345.

Structurei

3D structure databases

ProteinModelPortaliP55286.
SMRiP55286. Positions 63-597, 729-790.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini62 – 167106Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini168 – 276109Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini277 – 391115Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini392 – 494103Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini495 – 616122Cadherin 5PROSITE-ProRule annotationAdd
BLAST

Domaini

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain.By similarity

Sequence similaritiesi

Contains 5 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG330572.
GeneTreeiENSGT00760000118954.
HOGENOMiHOG000231252.
HOVERGENiHBG005217.
InParanoidiP55286.
KOiK06800.
OMAiGIVQSCN.
PhylomeDBiP55286.
TreeFamiTF329887.

Family and domain databases

Gene3Di2.60.40.60. 5 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR027397. Catenin_binding_dom.
[Graphical view]
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 5 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 5 hits.
PROSITEiPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P55286-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPERLAEMLL DLWTPLIILW ITLPPCIYMA PMNQSQVLMS GSPLELNSLG
60 70 80 90 100
EEQRILNRSK RGWVWNQMFV LEEFSGPEPI LVGRLHTDLD PGSKKIKYIL
110 120 130 140 150
SGDGAGTIFQ INDVTGDIHA IKRLDREEKA EYTLTAQAVD WETSKPLEPP
160 170 180 190 200
SEFIIKVQDI NDNAPEFLNG PYHATVPEMS ILGTSVTNVT ATDADDPVYG
210 220 230 240 250
NSAKLVYSIL EGQPYFSIEP ETAIIKTALP NMDREAKEEY LVVIQAKDMG
260 270 280 290 300
GHSGGLSGTT TLTVTLTDVN DNPPKFAQSL YHFSVPEDVV LGTAIGRVKA
310 320 330 340 350
NDQDIGENAQ SSYDIIDGDG TALFEITSDA QAQDGIIRLR KPLDFETKKS
360 370 380 390 400
YTLKVEAANV HIDPRFSGRG PFKDTATVKI VVEDADEPPV FSSPTYLLEV
410 420 430 440 450
HENAALNSVI GQVTARDPDI TSSPIRFSID RHTDLERQFN INADDGKITL
460 470 480 490 500
ATPLDRELSV WHNITIIATE IRNHSQISRV PVAIKVLDVN DNAPEFASEY
510 520 530 540 550
EAFLCENGKP GQVIQTVSAM DKDDPKNGHY FLYSLLPEMV NNPNFTIKKN
560 570 580 590 600
EDNSLSILAK HNGFNRQKQE VYLLPIIISD SGNPPLSSTS TLTIRVCGCS
610 620 630 640 650
NDGVVQSCNV EAYVLPIGLS MGALIAILAC IILLLVIVVL FVTLRRHKNE
660 670 680 690 700
PLIIKDDEDV RENIIRYDDE GGGEEDTEAF DIATLQNPDG INGFLPRKDI
710 720 730 740 750
KPDLQFMPRQ GLAPVPNGVD VDEFINVRLH EADNDPTAPP YDSIQIYGYE
760 770 780 790
GRGSVAGSLS SLESTTSDSD QNFDYLSDWG PRFKRLGELY SVGESDKET
Length:799
Mass (Da):88,253
Last modified:April 27, 2001 - v2
Checksum:i9B119B86039C6A0A
GO

Sequence cautioni

The sequence AAA35628.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti355 – 3551V → D in AAA35628 (PubMed:7982033).Curated
Sequence conflicti648 – 6481K → QK in AAA35628 (PubMed:7982033).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035305 mRNA. Translation: BAA87419.1.
AK124734 mRNA. Translation: BAG54083.1.
BC113416 mRNA. Translation: AAI13417.1.
L34060 mRNA. Translation: AAA35628.1. Different initiation.
CCDSiCCDS10802.1.
RefSeqiNP_001787.2. NM_001796.4.
XP_005255816.1. XM_005255759.2.
UniGeneiHs.368322.

Genome annotation databases

EnsembliENST00000577390; ENSP00000462701; ENSG00000150394.
GeneIDi1006.
KEGGihsa:1006.
UCSCiuc002eog.2. human.

Polymorphism databases

DMDMi13432121.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB035305 mRNA. Translation: BAA87419.1.
AK124734 mRNA. Translation: BAG54083.1.
BC113416 mRNA. Translation: AAI13417.1.
L34060 mRNA. Translation: AAA35628.1. Different initiation.
CCDSiCCDS10802.1.
RefSeqiNP_001787.2. NM_001796.4.
XP_005255816.1. XM_005255759.2.
UniGeneiHs.368322.

3D structure databases

ProteinModelPortaliP55286.
SMRiP55286. Positions 63-597, 729-790.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107441. 1 interaction.
STRINGi9606.ENSP00000299345.

PTM databases

PhosphoSiteiP55286.

Polymorphism databases

DMDMi13432121.

Proteomic databases

PaxDbiP55286.
PeptideAtlasiP55286.
PRIDEiP55286.

Protocols and materials databases

DNASUi1006.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000577390; ENSP00000462701; ENSG00000150394.
GeneIDi1006.
KEGGihsa:1006.
UCSCiuc002eog.2. human.

Organism-specific databases

CTDi1006.
GeneCardsiGC16M061681.
HGNCiHGNC:1767. CDH8.
HPAiHPA014908.
MIMi603008. gene.
neXtProtiNX_P55286.
PharmGKBiPA26304.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG330572.
GeneTreeiENSGT00760000118954.
HOGENOMiHOG000231252.
HOVERGENiHBG005217.
InParanoidiP55286.
KOiK06800.
OMAiGIVQSCN.
PhylomeDBiP55286.
TreeFamiTF329887.

Enzyme and pathway databases

ReactomeiREACT_19195. Adherens junctions interactions.

Miscellaneous databases

ChiTaRSiCDH8. human.
GeneWikiiCDH8.
GenomeRNAii1006.
NextBioi4230.
PROiP55286.
SOURCEiSearch...

Gene expression databases

BgeeiP55286.
CleanExiHS_CDH8.
ExpressionAtlasiP55286. baseline and differential.
GenevestigatoriP55286.

Family and domain databases

Gene3Di2.60.40.60. 5 hits.
4.10.900.10. 1 hit.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR027397. Catenin_binding_dom.
[Graphical view]
PfamiPF00028. Cadherin. 5 hits.
PF01049. Cadherin_C. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 5 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 5 hits.
PROSITEiPS00232. CADHERIN_1. 3 hits.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of three human type-II classic cadherins and frequent heterophilic interactions between different subclasses of type-II classic cadherins."
    Shimoyama Y., Tsujimoto G., Kitajima M., Natori M.
    Biochem. J. 349:159-167(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Cloning of five human cadherins clarifies characteristic features of cadherin extracellular domain and provides further evidence for two structurally different types of cadherin."
    Tanihara H., Sano K., Heimark R.L., St John T., Suzuki S.
    Cell Adhes. Commun. 2:15-26(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 7-799.
    Tissue: Brain.
  5. "Diversity of the cadherin family: evidence for eight new cadherins in nervous tissue."
    Suzuki S., Sano K., Tanihara H.
    Cell Regul. 2:261-270(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 294-799.
    Tissue: Fetal brain.

Entry informationi

Entry nameiCADH8_HUMAN
AccessioniPrimary (citable) accession number: P55286
Secondary accession number(s): B3KWC1, Q14DC6, Q9ULB2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 27, 2001
Last modified: January 7, 2015
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.