ID PCDH8_MOUSE Reviewed; 1070 AA.
AC Q7TSK3; Q05BD0; Q8C824; Q9JKP3;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 24-JAN-2024, entry version 145.
DE RecName: Full=Protocadherin-8;
DE AltName: Full=Arcadlin;
DE AltName: Full=Paraxial protocadherin;
DE Flags: Precursor;
GN Name=Pcdh8; Synonyms=Papc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Yamamoto A., Kemp C.R., De Robertis E.M.;
RT "Mouse PAPC.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Embryonic 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 [5]
RP FUNCTION.
RX PubMed=17988630; DOI=10.1016/j.neuron.2007.08.020;
RA Yasuda S., Tanaka H., Sugiura H., Okamura K., Sakaguchi T., Tran U.,
RA Takemiya T., Mizoguchi A., Yagita Y., Sakurai T., De Robertis E.M.,
RA Yamagata K.;
RT "Activity-induced protocadherin arcadlin regulates dendritic spine number
RT by triggering N-cadherin endocytosis via TAO2beta and p38 MAP kinases.";
RL Neuron 56:456-471(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein (By similarity). May
CC play a role in activity-induced synaptic reorganization underlying long
CC term memory (By similarity). Could be involved in CDH2 internalization
CC through TAOK2/p38 MAPK pathway (By similarity). In hippocampal neurons,
CC may play a role in the down-regulation of dendritic spines, maybe
CC through its action on CDH2 endocytosis. {ECO:0000250,
CC ECO:0000269|PubMed:17988630}.
CC -!- SUBUNIT: The N-terminal extracellular domain forms homophilic
CC interactions; these interactions activate p38 MAPK via TAOK2 and
CC trigger endocytosis. Interacts with CDH2; this interaction may lead to
CC CDH2 cointernalization. Interacts with CDH11. Interacts with TAOK2.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Cell projection, dendrite
CC {ECO:0000250}. Presynaptic cell membrane. Postsynaptic cell membrane
CC {ECO:0000250}. Note=Expressed in neuronal cell bodies and dendrites.
CC Localized to excitatory, but not with inhibitory, synapses.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7TSK3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TSK3-2; Sequence=VSP_040562;
CC Name=3;
CC IsoId=Q7TSK3-3; Sequence=VSP_040563, VSP_040564;
CC -!- MISCELLANEOUS: [Isoform 3]: Due to intron retention. {ECO:0000305}.
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DR EMBL; AF231125; AAF63319.1; -; mRNA.
DR EMBL; AK048638; BAC33404.1; -; mRNA.
DR EMBL; CH466535; EDL35755.1; -; Genomic_DNA.
DR EMBL; BC052388; AAH52388.1; -; mRNA.
DR EMBL; BC053008; AAH53008.1; -; mRNA.
DR CCDS; CCDS27303.1; -. [Q7TSK3-1]
DR CCDS; CCDS79349.1; -. [Q7TSK3-2]
DR RefSeq; NP_001036191.1; NM_001042726.3. [Q7TSK3-2]
DR RefSeq; NP_067518.2; NM_021543.4. [Q7TSK3-1]
DR AlphaFoldDB; Q7TSK3; -.
DR SMR; Q7TSK3; -.
DR BioGRID; 202045; 5.
DR IntAct; Q7TSK3; 1.
DR STRING; 10090.ENSMUSP00000045333; -.
DR GlyCosmos; Q7TSK3; 1 site, No reported glycans.
DR GlyGen; Q7TSK3; 1 site.
DR iPTMnet; Q7TSK3; -.
DR PhosphoSitePlus; Q7TSK3; -.
DR MaxQB; Q7TSK3; -.
DR PaxDb; 10090-ENSMUSP00000045333; -.
DR ProteomicsDB; 288113; -. [Q7TSK3-1]
DR ProteomicsDB; 288114; -. [Q7TSK3-2]
DR ProteomicsDB; 288115; -. [Q7TSK3-3]
DR Antibodypedia; 24243; 162 antibodies from 22 providers.
DR DNASU; 18530; -.
DR Ensembl; ENSMUST00000039568.11; ENSMUSP00000045333.6; ENSMUSG00000036422.11. [Q7TSK3-1]
DR Ensembl; ENSMUST00000195355.2; ENSMUSP00000141417.2; ENSMUSG00000036422.11. [Q7TSK3-2]
DR GeneID; 18530; -.
DR KEGG; mmu:18530; -.
DR UCSC; uc007uti.3; mouse. [Q7TSK3-1]
DR UCSC; uc007utj.3; mouse. [Q7TSK3-2]
DR UCSC; uc029smd.1; mouse. [Q7TSK3-3]
DR AGR; MGI:1306800; -.
DR CTD; 5100; -.
DR MGI; MGI:1306800; Pcdh8.
DR VEuPathDB; HostDB:ENSMUSG00000036422; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000155219; -.
DR HOGENOM; CLU_006480_1_2_1; -.
DR InParanoid; Q7TSK3; -.
DR OMA; GESSCHF; -.
DR OrthoDB; 4259465at2759; -.
DR PhylomeDB; Q7TSK3; -.
DR TreeFam; TF352008; -.
DR BioGRID-ORCS; 18530; 3 hits in 78 CRISPR screens.
DR PRO; PR:Q7TSK3; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q7TSK3; Protein.
DR Bgee; ENSMUSG00000036422; Expressed in anterior amygdaloid area and 137 other cell types or tissues.
DR Genevisible; Q7TSK3; MM.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; ISO:MGI.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
DR GO; GO:0099179; P:regulation of synaptic membrane adhesion; ISO:MGI.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR CDD; cd11304; Cadherin_repeat; 6.
DR Gene3D; 2.60.40.60; Cadherins; 6.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR PANTHER; PTHR24028; CADHERIN-87A; 1.
DR PANTHER; PTHR24028:SF46; PROTOCADHERIN-8; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; Cadherin-like; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Cell projection; Glycoprotein; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..1070
FT /note="Protocadherin-8"
FT /id="PRO_0000404296"
FT TOPO_DOM 30..747
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 748..768
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 769..1070
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..135
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 136..245
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 247..354
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 393..497
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 498..609
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 615..721
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 716..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..928
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1053
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3ZE55"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 779..875
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_040562"
FT VAR_SEQ 876..966
FT /note="PYGASPGFGKEPAAPPVAVWKGHSFNTISGREAEKFSGKDSGKGDSDFNDSD
FT SDISGDALKKDLINHMQSGLWACTAECKILGHSDRCWSP -> VRPSFGWAPPSVLCGQ
FT AGRRETGGVRVGSHREMFNLSHLLFCVLSNPHTFPPPPFPAAALRCLSRLREGACCAPC
FT YSLEGSFIQHHLGPRS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040563"
FT VAR_SEQ 967..1070
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040564"
FT CONFLICT 58
FT /note="S -> F (in Ref. 1; AAF63319)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="V -> A (in Ref. 1; AAF63319)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="R -> TG (in Ref. 1; AAF63319)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="D -> G (in Ref. 2; BAC33404)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="Q -> H (in Ref. 1; AAF63319)"
FT /evidence="ECO:0000305"
FT CONFLICT 403
FT /note="E -> Q (in Ref. 1; AAF63319)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="S -> P (in Ref. 4; AAH52388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1070 AA; 113260 MW; FFC2D87D63F6856E CRC64;
MSPAKRWGSP CLFPLQLFSL CWVLSVAQSK TVRYSTFEED APGTVIGTLA EDLHMKVSGD
TSFRLMKQFN SSLLRVREGD GQLTVGDAGL DRERLCGPSP 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 APEISITPLA
APGAPATSPF AAAAAAAALG GADAASSTGS GTQEAGITSL VPEGAARESL VALVSTSDRD
SGANGQVRCA LYGHEHFRLQ PAYAGSYLVV TAASLDRERI AEYNLTLVAE DRGTPPLRTV
RPYTVRVGDE NDNAPIFTKP VYEVSVRENN PPGAYLATVA ARDPDVGRNG QVTYRLVEAE
VGRSGEAVST YVSVDPATGA IYALRSFDYE TLRQLDVRVQ ASDGGSPQLS SNALVQVRVL
DQNDHSPILV HPAPANGSLE VAVPGRSTKD TAVARIQARD ADEGANGELA FDLLQQEPRE
AFSIGRHTGE IMLTGDLSQE PPGRVFKALL VISDGGRPPL TTTATVSFVV TAGGGSAVPA
SSGSPEHSRP PGSRLAPSGP SLQWDTPLIV IIVLAGSCTL LLAAIIAIAT TCNRRKKEVR
KGGALREERP GAAGGGASAP GSPDETARGT GPRPNMFDVL TFPGSGKAPF GSPAADAPPP
AVAAAEVPGS EGGSATGESA CHFEGQQRLR GAHAEPYGAS PGFGKEPAAP PVAVWKGHSF
NTISGREAEK FSGKDSGKGD SDFNDSDSDI SGDALKKDLI NHMQSGLWAC TAECKILGHS
DRCWSPSCAG PNVHPPPHPP AQMSTFCKST SLPRDPLRRD NYYQAQLPKT VGLQSVYEKV
LHRDYDRTVT LLSPPRPGRL PDLQEIGVPL YESPPGSRYV SPKKGINENV
//
