PCDB8_MOUSE
ID PCDB8_MOUSE Reviewed; 779 AA.
AC Q91XZ2;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Protocadherin beta-8 {ECO:0000305};
DE Short=PCDH-beta-8 {ECO:0000305};
DE Flags: Precursor;
GN Name=Pcdhb8 {ECO:0000312|MGI:MGI:2136742};
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].
RC TISSUE=Brain;
RX PubMed=11230163; DOI=10.1101/gr.167301;
RA Wu Q., Zhang T., Cheng J.-F., Kim Y., Grimwood J., Schmutz J., Dickson M.,
RA Noonan J.P., Zhang M.Q., Myers R.M., Maniatis T.;
RT "Comparative DNA sequence analysis of mouse and human protocadherin gene
RT clusters.";
RL Genome Res. 11:389-404(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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].
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 X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 29-446 OF HOMODIMER IN COMPLEX
RP WITH CALCIUM, PROTEIN SEQUENCE OF 29-35, FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, TOPOLOGY, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION AT ASN-169;
RP SER-223; THR-225; THR-227 AND ASN-417, AND CALCIUM-BINDING.
RX PubMed=27161523; DOI=10.1016/j.neuron.2016.04.004;
RA Goodman K.M., Rubinstein R., Thu C.A., Bahna F., Mannepalli S., Ahlsen G.,
RA Rittenhouse C., Maniatis T., Honig B., Shapiro L.;
RT "Structural basis of diverse homophilic recognition by clustered alpha- and
RT beta-protocadherins.";
RL Neuron 90:709-723(2016).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein involved in cells
CC self-recognition and non-self discrimination (Probable). Thereby, it is
CC involved in the establishment and maintenance of specific neuronal
CC connections in the brain (PubMed:27161523).
CC {ECO:0000305|PubMed:27161523}.
CC -!- SUBUNIT: Forms homodimers in trans (molecules expressed by two
CC different cells) (PubMed:27161523). Forms promiscuous heterodimers in
CC cis (at the plasma membrane of the same cell) with other protocadherins
CC (PubMed:27161523). {ECO:0000269|PubMed:27161523}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:27161523};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:27161523}.
CC -!- DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-
CC interaction, the interaction with an identical protocadherin expressed
CC by a neighboring cell (PubMed:27161523). This is a head-to-tail
CC interaction, the cadherin 1 domain interacting with the cadherin 4
CC domain and the cadherin 2 domain interacting the cadherin 3 domain of
CC the other protocadherin (PubMed:27161523). The cadherin 6 domain
CC mediates promiscuous interactions with protocadherins on the same cell
CC membrane (PubMed:27161523). Each cadherin domain binds three calcium
CC ions (PubMed:27161523). {ECO:0000269|PubMed:27161523,
CC ECO:0000312|PDB:5DZY}.
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DR EMBL; AY013790; AAK26079.1; -; mRNA.
DR EMBL; AC020974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466528; EDL10163.1; -; Genomic_DNA.
DR EMBL; BC127160; AAI27161.1; -; mRNA.
DR CCDS; CCDS29175.1; -.
DR RefSeq; NP_444363.1; NM_053133.1.
DR PDB; 5DZY; X-ray; 2.90 A; A/B/C/D/E/F=29-446.
DR PDBsum; 5DZY; -.
DR AlphaFoldDB; Q91XZ2; -.
DR SMR; Q91XZ2; -.
DR STRING; 10090.ENSMUSP00000054371; -.
DR GlyGen; Q91XZ2; 6 sites.
DR iPTMnet; Q91XZ2; -.
DR PhosphoSitePlus; Q91XZ2; -.
DR PaxDb; Q91XZ2; -.
DR PRIDE; Q91XZ2; -.
DR ProteomicsDB; 288112; -.
DR DNASU; 93879; -.
DR Ensembl; ENSMUST00000051163; ENSMUSP00000054371; ENSMUSG00000045876.
DR GeneID; 93879; -.
DR KEGG; mmu:93879; -.
DR UCSC; uc008ept.1; mouse.
DR CTD; 56128; -.
DR MGI; MGI:2136742; Pcdhb8.
DR VEuPathDB; HostDB:ENSMUSG00000045876; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000157793; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR InParanoid; Q91XZ2; -.
DR OMA; RIHYKGD; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q91XZ2; -.
DR TreeFam; TF332299; -.
DR BioGRID-ORCS; 93879; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q91XZ2; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q91XZ2; protein.
DR Bgee; ENSMUSG00000045876; Expressed in epibranchial ganglion and 40 other tissues.
DR ExpressionAtlas; Q91XZ2; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IC:UniProtKB.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR032455; Cadherin_C.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR030730; PCDHB5/6/8.
DR PANTHER; PTHR24028:SF90; PTHR24028:SF90; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF16492; Cadherin_C_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 5.
DR SUPFAM; SSF49313; SSF49313; 5.
DR PROSITE; PS00232; CADHERIN_1; 4.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Cell adhesion; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Membrane;
KW Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000269|PubMed:27161523"
FT CHAIN 29..779
FT /note="Protocadherin beta-8"
FT /evidence="ECO:0000305"
FT /id="PRO_5008429396"
FT TOPO_DOM 29..690
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:27161523"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..779
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27161523"
FT DOMAIN 75..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 134..242
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 243..346
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 347..450
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 451..560
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 575..675
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZY"
FT CARBOHYD 223
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZY"
FT CARBOHYD 225
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZY"
FT CARBOHYD 227
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZY"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZY"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 96..102
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZY"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5DZY"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:5DZY"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:5DZY"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:5DZY"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:5DZY"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:5DZY"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5DZY"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:5DZY"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:5DZY"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 206..220
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 223..233
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:5DZY"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:5DZY"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:5DZY"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 327..337
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:5DZY"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 386..396
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 399..406
FT /evidence="ECO:0007829|PDB:5DZY"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 414..424
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:5DZY"
FT STRAND 431..440
FT /evidence="ECO:0007829|PDB:5DZY"
SQ SEQUENCE 779 AA; 84766 MW; 64BE9D2C7BDBB2EC CRC64;
METALTKTPE KRQVIFLAIL LLLWEASSEA ISYSMPEETE SGYLVANLAQ DLGLRVGELT
TRGARIHHNG NKELLQLDAE RGNLLLKEKP DREALCGATE PCVLHFQIIL ENPVQFFQTD
LQFTDINDHF PEFPDTEMLL KIQEIAQPGT VFPLKAAQDP DIGSNAVQNY TVSPNLHFHV
VTLSRSDDRK YPELVLDRAL DREEQPELTL ILTALDGGAP PKSGTTTVRI EVVDINDNAP
QFLQSLYAVE VPENSPLNAL VVTVSARDLD AGIHGNVAYS LFQGGGGPQP FVIDEITGEI
RLKGALDFEA TSYYTMEIVA TDSGGLSGKC TVAIQVLDVN DNAPKLTISS LTSSIPENAP
EAVVAVFSVS DPDSGDNGRM VCSIQNGLPF LLKPTFKNFY TLVTERPLDR ESNAEYNITI
TVSDLGTPRL TTQHTITVQV SDINDNAPAF TQTSYTLFVH ENNSPALHIG TISATDSDSG
SNGLIIYSLL PPHDQQLGLA SLISINSDNG QLFALRALDY EALQAFEFHV GATDRGSPAL
SSEALVRVVV LDDNDNAPFV LYPLQNASAP CTELLPRAAE PGYLITKVVA VDRDSGQNAW
LSFQLLKATE PGLFSVWAHN GEVRTTRLLS ERDAPKHRLL LLVKDNGEPL RSASVMLQVL
VVDGFSQPYL PLPEVALNPT QEEDMLTLYL VIALASVSSL FLLSVLLFVG VKLCKKAREA
SLADCSIPEG HFPSHLVDVS GAGTLSQSYH YEVCLTEDSG TSDFKFMNPI IPSSLLQDS
