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Protocadherin-8 (Activity-regulated cadherin-like protein) (Arcadlin)

 PCDH8_RAT               Reviewed;        1069 AA.
D3ZE55; A1A5N4; Q9WVR2;
08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
08-FEB-2011, sequence version 2.
12-SEP-2018, entry version 58.
RecName: Full=Protocadherin-8;
AltName: Full=Activity-regulated cadherin-like protein;
Short=Arcadlin;
Flags: Precursor;
Name=Pcdh8;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBUNIT, SUBCELLULAR
LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
TISSUE=Hippocampus;
PubMed=10383464; DOI=10.1074/jbc.274.27.19473;
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.;
"Arcadlin is a neural activity-regulated cadherin involved in long
term potentiation.";
J. Biol. Chem. 274:19473-19479(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
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., 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.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-694.
STRAIN=Brown Norway/NHsdMcwi; TISSUE=Embryonic brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, INTERACTION WITH CDH2; CDH11 AND TAOK2, AND INDUCTION.
PubMed=17988630; DOI=10.1016/j.neuron.2007.08.020;
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.;
"Activity-induced protocadherin arcadlin regulates dendritic spine
number by triggering N-cadherin endocytosis via TAO2beta and p38 MAP
kinases.";
Neuron 56:456-471(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1052, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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. {ECO:0000269|PubMed:10383464,
ECO:0000269|PubMed:17988630}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10383464,
ECO:0000269|PubMed:17988630}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Cell projection, dendrite
{ECO:0000269|PubMed:10383464}. Cell junction, synapse, presynaptic
cell membrane {ECO:0000269|PubMed:10383464}. Cell junction,
synapse, postsynaptic cell membrane {ECO:0000269|PubMed:10383464}.
Note=Also expressed in the cell bodies of neurons of the
hippocampus and cortex. Localized to excitatory, but not with
inhibitory, synapses.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=D3ZE55-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=2;
IsoId=D3ZE55-2; Sequence=VSP_040565;
Note=May be the only physiologically relevant isoform.
{ECO:0000305|PubMed:10383464};
-!- TISSUE SPECIFICITY: Enriched in brain relative to peripheral
tissues, with low expression in the testis. Expressed in
hippocampal neurons (at protein level).
{ECO:0000269|PubMed:10383464}.
-!- 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.
{ECO:0000269|PubMed:10383464}.
-!- 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.
{ECO:0000269|PubMed:10383464, ECO:0000269|PubMed:17988630}.
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EMBL; AB026154; BAA82442.1; -; mRNA.
EMBL; CH473951; EDM02373.1; -; Genomic_DNA.
EMBL; BC128737; AAI28738.1; -; mRNA.
RefSeq; NP_074059.1; NM_022868.1.
RefSeq; XP_008769119.1; XM_008770897.2. [D3ZE55-1]
UniGene; Rn.23337; -.
SMR; D3ZE55; -.
STRING; 10116.ENSRNOP00000017599; -.
iPTMnet; D3ZE55; -.
PhosphoSitePlus; D3ZE55; -.
SwissPalm; D3ZE55; -.
UniCarbKB; D3ZE55; -.
PaxDb; D3ZE55; -.
PRIDE; D3ZE55; -.
Ensembl; ENSRNOT00000017599; ENSRNOP00000017599; ENSRNOG00000013101. [D3ZE55-1]
GeneID; 64865; -.
KEGG; rno:64865; -.
CTD; 5100; -.
RGD; 69350; Pcdh8.
eggNOG; KOG3594; Eukaryota.
eggNOG; ENOG410XQHI; LUCA.
GeneTree; ENSGT00900000140770; -.
HOVERGEN; HBG054878; -.
InParanoid; D3ZE55; -.
KO; K16499; -.
OMA; QWDTPLI; -.
OrthoDB; EOG091G00QD; -.
PhylomeDB; D3ZE55; -.
PRO; PR:D3ZE55; -.
Proteomes; UP000002494; Chromosome 15.
Bgee; ENSRNOG00000013101; Expressed in 3 organ(s), highest expression level in Ammon's horn.
Genevisible; D3ZE55; RN.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0007268; P:chemical synaptic transmission; IDA:RGD.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
GO; GO:0007616; P:long-term memory; TAS:RGD.
GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; IBA:GO_Central.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR013164; Cadherin_N.
InterPro; IPR030711; Protocadherin-8.
PANTHER; PTHR24028:SF46; PTHR24028:SF46; 1.
Pfam; PF00028; Cadherin; 5.
Pfam; PF08266; Cadherin_2; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 6.
SUPFAM; SSF49313; SSF49313; 6.
PROSITE; PS00232; CADHERIN_1; 5.
PROSITE; PS50268; CADHERIN_2; 6.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Complete proteome; Glycoprotein;
Membrane; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Repeat; Signal; Synapse; Transmembrane;
Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 1069 Protocadherin-8.
/FTId=PRO_0000404297.
TOPO_DOM 30 747 Extracellular. {ECO:0000255}.
TRANSMEM 748 768 Helical. {ECO:0000255}.
TOPO_DOM 769 1069 Cytoplasmic. {ECO:0000255}.
DOMAIN 30 135 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 136 245 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 247 354 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 393 497 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 498 609 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 615 721 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
MOD_RES 1052 1052 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 616 616 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 779 875 Missing (in isoform 2).
{ECO:0000303|PubMed:10383464}.
/FTId=VSP_040565.
CONFLICT 351 351 A -> P (in Ref. 1; BAA82442).
{ECO:0000305}.
SEQUENCE 1069 AA; 113191 MW; 307DB9763F69D7D3 CRC64;
MSPVKRWGSP CLFPLQLFSL CWVLSVAQSK TVRYSTFEED APGTVIGTLA EDLHMKVSGD
TSFRLMKQFN SSLLRVREGD GQLTVGDAGL DRERLCGQSP QCVLAFDVVS FSQEQFRLVH
VEVEVRDVND HAPRFPRAQI PVEVSESAPV GTRIPLEVPV DEDVGANGLQ SVRLAEPHSP
FRVELQTRAD GAQCADLVLL QELDRESQAS YSLELVAQDG GRPPRSATAA LSVRVLDAND
HSPAFPQGAV AEVELAEDAP VGSLLLDLDA ADPDEGPNGD VVFTFGARTP PEARHLFRLD
PRSGRLTLAG QVDYERQDTY ELDVRAQDRG PGPRTATCKV IVRIRDVNDN APDISITPLA
APGAPATSPF AAAAAAAALG GADAASSAGS GTQETGVTSL VPEGAARESL VALVSTSDRD
SGANGQVRCA LYGHEHFRLQ PAYAGSYLVV TAASLDRERI AEYNLTLVAE DRGAPPLRTV
RPYTVRVGDE NDNAPLFTKP VYEVSVRENN PPGAYLATVA ARDPDLGRNG QVTYRLVEAE
VGRSGEAVST YVSVDPATGA IYALRSFDYE TLRQLDVRVQ ASDGGSPQLS SNALVQVRVL
DQNDHSPVLV HPAPANGSLE VAVPGRSTKD TAVARIQARD ADEGANGELA FDLLQQEPRE
AFSIGRHTGE IVLTGDLSQE PPGRVFKALL VISDGGRPPL TTTATVSFVV TAGGGSAVPA
SAGSPEHFRP PGSRLAPSGP SLQWDTPLIV IIVLAGSCTL LLAAIIAIAT TCNRRKKEVR
KGGALREERP GAAGGGASAP GSPDETARGT GPRPNMFDVL TFPGSGKAPF GSPAADAPPP
AVAAAEVPGS EGGSATGESA CHFEGQQRLR GAHAEPYSAS PGFGKEPAPP VAVWKGHSFN
TISGREAEKF SGKDSGKGDS DFNDSDSDIS GDALKKDLIN HMQSGLWACT AECKILGHSD
RCWSPSCAGP NTHPPPHPPA QMSTFCKSTS LPRDPLRRDN YYQAQLPKTV GLQSVYEKVL
HRDYDRTVTL LSPPRPGRLP DLQEIGVPLY ESPPGGRYVS PKKGTNENV


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