GENTAUR Molecular Products.

 PCDH8_RAT               Reviewed;        1069 AA.
 D3ZE55; A1A5N4; Q9WVR2;
 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
 08-FEB-2011, sequence version 2.
 05-DEC-2018, entry version 60.
 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; ENSGT00940000155219; -.
 HOVERGEN; HBG054878; -.
 InParanoid; D3ZE55; -.
 KO; K16499; -.
 OMA; GPALQWD; -.
 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:0098978; C:glutamatergic synapse; IDA:SynGO.
 GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
 GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
 GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
 GO; GO:0098685; C:Schaffer collateral - CA1 synapse; EXP:SynGO.
 GO; GO:0045202; C:synapse; IDA:SynGO.
 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:0050804; P:modulation of chemical synaptic transmission; EXP:SynGO.
 GO; GO:0016331; P:morphogenesis of embryonic epithelium; IEA:Ensembl.
 GO; GO:0099179; P:regulation of synaptic membrane adhesion; IDA:SynGO.
 GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
 InterPro; IPR002126; Cadherin-like_dom.
 InterPro; IPR015919; Cadherin-like_sf.
 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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