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D3ZE55 (PCDH8_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protocadherin-8
Alternative name(s):
Activity-regulated cadherin-like protein
Short name=Arcadlin
Gene names
Name:Pcdh8
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1069 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-dependent cell-adhesion protein. May play a role in activity-induced synaptic reorganization underlying long term memory. Could be involved in CDH2 internalization through TAOK2/p38 MAPK pathway. In hippocampal neurons, may play a role in the down-regulation of dendritic spines, maybe through its action on CDH2 endocytosis. Ref.1 Ref.4

Subunit structure

The N-terminal extracellular domain forms homophilic interactions; these interactions activate p38 MAPK via TAOK2 and trigger endocytosis. Interacts with CDH2; this interaction may lead to CDH2 cointernalization. Interacts with CDH11. Interacts with TAOK2. Ref.1 Ref.4

Subcellular location

Cell membrane; Single-pass type I membrane protein By similarity. Cell projectiondendrite. Cell junctionsynapsepresynaptic cell membrane. Cell junctionsynapsepostsynaptic cell membrane. Note: Also expressed in the cell bodies of neurons of the hippocampus and cortex. Localized to excitatory, but not with inhibitory, synapses. Ref.1

Tissue specificity

Enriched in brain relative to peripheral tissues, with low expression in the testis. Expressed in hippocampal neurons (at protein level). Ref.1

Developmental stage

At E17, expressed in the auditory circuit, most prominently in the inferior colliculus, and later in the medial geniculate and the auditory cortex at P0. At P0, also expressed in targets of retinal projections, such as the superior colliculus, the suprachiasmatic nucleus, and the ventrolateral geniculate nucleus. At the same stage, detected in selected structures of the limbic circuit, including the anterior limbic thalamic nuclei, the hippocampus, amygdala and habenula. Ref.1

Induction

Rapidly and transiently induced by maximal electroconvulsive seizure in the hippocampal granule cells, and modestly induced in the pyramidal cells. Also induced by cAMP. Ref.1 Ref.4

Sequence similarities

Contains 6 cadherin domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: D3ZE55-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: No experimental confirmation available.
Isoform 2 (identifier: D3ZE55-2)

The sequence of this isoform differs from the canonical sequence as follows:
     779-875: Missing.
Note: May be the only physiologically relevant isoform (PubMed:10383464).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 10691040Protocadherin-8
PRO_0000404297

Regions

Topological domain30 – 747718Extracellular Potential
Transmembrane748 – 76821Helical; Potential
Topological domain769 – 1069301Cytoplasmic Potential
Domain30 – 135106Cadherin 1
Domain136 – 245110Cadherin 2
Domain247 – 354108Cadherin 3
Domain393 – 497105Cadherin 4
Domain498 – 609112Cadherin 5
Domain615 – 721107Cadherin 6

Amino acid modifications

Glycosylation6161N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence779 – 87597Missing in isoform 2.
VSP_040565

Experimental info

Sequence conflict3511A → P in BAA82442. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 8, 2011. Version 2.
Checksum: 307DB9763F69D7D3

FASTA1,069113,191
        10         20         30         40         50         60 
MSPVKRWGSP CLFPLQLFSL CWVLSVAQSK TVRYSTFEED APGTVIGTLA EDLHMKVSGD 

        70         80         90        100        110        120 
TSFRLMKQFN SSLLRVREGD GQLTVGDAGL DRERLCGQSP QCVLAFDVVS FSQEQFRLVH 

       130        140        150        160        170        180 
VEVEVRDVND HAPRFPRAQI PVEVSESAPV GTRIPLEVPV DEDVGANGLQ SVRLAEPHSP 

       190        200        210        220        230        240 
FRVELQTRAD GAQCADLVLL QELDRESQAS YSLELVAQDG GRPPRSATAA LSVRVLDAND 

       250        260        270        280        290        300 
HSPAFPQGAV AEVELAEDAP VGSLLLDLDA ADPDEGPNGD VVFTFGARTP PEARHLFRLD 

       310        320        330        340        350        360 
PRSGRLTLAG QVDYERQDTY ELDVRAQDRG PGPRTATCKV IVRIRDVNDN APDISITPLA 

       370        380        390        400        410        420 
APGAPATSPF AAAAAAAALG GADAASSAGS GTQETGVTSL VPEGAARESL VALVSTSDRD 

       430        440        450        460        470        480 
SGANGQVRCA LYGHEHFRLQ PAYAGSYLVV TAASLDRERI AEYNLTLVAE DRGAPPLRTV 

       490        500        510        520        530        540 
RPYTVRVGDE NDNAPLFTKP VYEVSVRENN PPGAYLATVA ARDPDLGRNG QVTYRLVEAE 

       550        560        570        580        590        600 
VGRSGEAVST YVSVDPATGA IYALRSFDYE TLRQLDVRVQ ASDGGSPQLS SNALVQVRVL 

       610        620        630        640        650        660 
DQNDHSPVLV HPAPANGSLE VAVPGRSTKD TAVARIQARD ADEGANGELA FDLLQQEPRE 

       670        680        690        700        710        720 
AFSIGRHTGE IVLTGDLSQE PPGRVFKALL VISDGGRPPL TTTATVSFVV TAGGGSAVPA 

       730        740        750        760        770        780 
SAGSPEHFRP PGSRLAPSGP SLQWDTPLIV IIVLAGSCTL LLAAIIAIAT TCNRRKKEVR 

       790        800        810        820        830        840 
KGGALREERP GAAGGGASAP GSPDETARGT GPRPNMFDVL TFPGSGKAPF GSPAADAPPP 

       850        860        870        880        890        900 
AVAAAEVPGS EGGSATGESA CHFEGQQRLR GAHAEPYSAS PGFGKEPAPP VAVWKGHSFN 

       910        920        930        940        950        960 
TISGREAEKF SGKDSGKGDS DFNDSDSDIS GDALKKDLIN HMQSGLWACT AECKILGHSD 

       970        980        990       1000       1010       1020 
RCWSPSCAGP NTHPPPHPPA QMSTFCKSTS LPRDPLRRDN YYQAQLPKTV GLQSVYEKVL 

      1030       1040       1050       1060 
HRDYDRTVTL LSPPRPGRLP DLQEIGVPLY ESPPGGRYVS PKKGTNENV 

« Hide

Isoform 2 [UniParc].

Checksum: 6968FA65FF82123F
Show »

FASTA972103,774

References

« Hide 'large scale' references
[1]"Arcadlin is a neural activity-regulated cadherin involved in long term potentiation."
Yamagata K., Andreasson K.I., Sugiura H., Maru E., Dominique M., Irie Y., Miki N., Hayashi Y., Yoshioka M., Kaneko K., Kato H., Worley P.F.
J. Biol. Chem. 274:19473-19479(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
Tissue: Hippocampus.
[2]"Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. expand/collapse author list , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Brown Norway.
[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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-694.
Strain: Brown Norway/NHsdMcwi.
Tissue: Embryonic brain.
[4]"Activity-induced protocadherin arcadlin regulates dendritic spine number by triggering N-cadherin endocytosis via TAO2beta and p38 MAP kinases."
Yasuda S., Tanaka H., Sugiura H., Okamura K., Sakaguchi T., Tran U., Takemiya T., Mizoguchi A., Yagita Y., Sakurai T., De Robertis E.M., Yamagata K.
Neuron 56:456-471(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDH2; CDH11 AND TAOK2, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB026154 mRNA. Translation: BAA82442.1.
CH473951 Genomic DNA. Translation: EDM02373.1.
BC128737 mRNA. Translation: AAI28738.1.
RefSeqNP_074059.1. NM_022868.1.
XP_006252437.1. XM_006252375.1. [D3ZE55-1]
UniGeneRn.23337.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000017599.

PTM databases

PhosphoSiteD3ZE55.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000017599; ENSRNOP00000017599; ENSRNOG00000013101. [D3ZE55-1]
GeneID64865.
KEGGrno:64865.

Organism-specific databases

CTD5100.
RGD69350. Pcdh8.

Phylogenomic databases

GeneTreeENSGT00750000117335.
HOVERGENHBG054878.
KOK16499.
OMAPAQMSTF.
OrthoDBEOG7J445X.
PhylomeDBD3ZE55.

Family and domain databases

Gene3D2.60.40.60. 6 hits.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013164. Cadherin_N.
[Graphical view]
PfamPF00028. Cadherin. 5 hits.
PF08266. Cadherin_2. 1 hit.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 6 hits.
[Graphical view]
SUPFAMSSF49313. SSF49313. 6 hits.
PROSITEPS00232. CADHERIN_1. 5 hits.
PS50268. CADHERIN_2. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio613776.
PROD3ZE55.

Entry information

Entry namePCDH8_RAT
AccessionPrimary (citable) accession number: D3ZE55
Secondary accession number(s): A1A5N4, Q9WVR2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 8, 2011
Last sequence update: February 8, 2011
Last modified: May 14, 2014
This is version 32 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families