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Protocadherin beta-8 (PCDH-beta-8)

 PCDB8_MOUSE             Reviewed;         779 AA.
Q91XZ2;
30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
28-FEB-2018, entry version 113.
RecName: Full=Protocadherin beta-8 {ECO:0000305};
Short=PCDH-beta-8 {ECO:0000305};
Flags: Precursor;
Name=Pcdhb8 {ECO:0000312|MGI:MGI:2136742};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=11230163; DOI=10.1101/gr.167301;
Wu Q., Zhang T., Cheng J.-F., Kim Y., Grimwood J., Schmutz J.,
Dickson M., Noonan J.P., Zhang M.Q., Myers R.M., Maniatis T.;
"Comparative DNA sequence analysis of mouse and human protocadherin
gene clusters.";
Genome Res. 11:389-404(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 29-446 OF HOMODIMER IN
COMPLEX WITH CALCIUM, PROTEIN SEQUENCE OF 29-35, FUNCTION, SUBUNIT,
SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, DISULFIDE BONDS, GLYCOSYLATION
AT ASN-169; SER-223; THR-225; THR-227 AND ASN-417, AND
CALCIUM-BINDING.
PubMed=27161523; DOI=10.1016/j.neuron.2016.04.004;
Goodman K.M., Rubinstein R., Thu C.A., Bahna F., Mannepalli S.,
Ahlsen G., Rittenhouse C., Maniatis T., Honig B., Shapiro L.;
"Structural basis of diverse homophilic recognition by clustered
alpha- and beta-protocadherins.";
Neuron 90:709-723(2016).
-!- FUNCTION: Calcium-dependent cell-adhesion protein involved in
cells self-recognition and non-self discrimination (Probable).
Thereby, it is involved in the establishment and maintenance of
specific neuronal connections in the brain (PubMed:27161523).
{ECO:0000305|PubMed:27161523}.
-!- SUBUNIT: Forms homodimers in trans (molecules expressed by two
different cells) (PubMed:27161523). Forms promiscuous heterodimers
in cis (at the plasma membrane of the same cell) with other
protocadherins (PubMed:27161523). {ECO:0000269|PubMed:27161523}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:27161523};
Single-pass type I membrane protein {ECO:0000305|PubMed:27161523}.
-!- DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-
interaction, the interaction with an identical protocadherin
expressed by a neighboring cell (PubMed:27161523). This is a head-
to-tail interaction, the cadherin 1 domain interacting with the
cadherin 4 domain and the cadherin 2 domain interacting the
cadherin 3 domain of the other protocadherin (PubMed:27161523).
The cadherin 6 domain mediates promiscuous interactions with
protocadherins on the same cell membrane (PubMed:27161523). Each
cadherin domain binds three calcium ions (PubMed:27161523).
{ECO:0000269|PubMed:27161523, ECO:0000312|PDB:5DZY}.
-----------------------------------------------------------------------
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EMBL; AY013790; AAK26079.1; -; mRNA.
EMBL; AC020974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466528; EDL10163.1; -; Genomic_DNA.
EMBL; BC127160; AAI27161.1; -; mRNA.
CCDS; CCDS29175.1; -.
RefSeq; NP_444363.1; NM_053133.1.
UniGene; Mm.348052; -.
PDB; 5DZY; X-ray; 2.90 A; A/B/C/D/E/F=29-446.
PDBsum; 5DZY; -.
ProteinModelPortal; Q91XZ2; -.
SMR; Q91XZ2; -.
STRING; 10090.ENSMUSP00000054371; -.
iPTMnet; Q91XZ2; -.
PhosphoSitePlus; Q91XZ2; -.
PaxDb; Q91XZ2; -.
Ensembl; ENSMUST00000051163; ENSMUSP00000054371; ENSMUSG00000045876.
GeneID; 93879; -.
KEGG; mmu:93879; -.
UCSC; uc008ept.1; mouse.
CTD; 56128; -.
MGI; MGI:2136742; Pcdhb8.
eggNOG; KOG3594; Eukaryota.
eggNOG; ENOG410XQHI; LUCA.
GeneTree; ENSGT00910000143986; -.
HOVERGEN; HBG054878; -.
KO; K16494; -.
OMA; HVVTHNR; -.
OrthoDB; EOG091G024L; -.
PhylomeDB; Q91XZ2; -.
TreeFam; TF332299; -.
PRO; PR:Q91XZ2; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000045876; -.
ExpressionAtlas; Q91XZ2; baseline and differential.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IC:UniProtKB.
GO; GO:0007416; P:synapse assembly; IBA:GO_Central.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR032455; Cadherin_C.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR013164; Cadherin_N.
Pfam; PF00028; Cadherin; 5.
Pfam; PF08266; Cadherin_2; 1.
Pfam; PF16492; Cadherin_C_2; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 5.
SUPFAM; SSF49313; SSF49313; 5.
PROSITE; PS00232; CADHERIN_1; 4.
PROSITE; PS50268; CADHERIN_2; 5.
1: Evidence at protein level;
3D-structure; Calcium; Cell adhesion; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Membrane; Metal-binding; Reference proteome; Repeat;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 28 {ECO:0000269|PubMed:27161523}.
CHAIN 29 779 Protocadherin beta-8. {ECO:0000305}.
/FTId=PRO_5008429396.
TOPO_DOM 29 690 Extracellular.
{ECO:0000305|PubMed:27161523}.
TRANSMEM 691 711 Helical. {ECO:0000255}.
TOPO_DOM 712 779 Cytoplasmic.
{ECO:0000305|PubMed:27161523}.
DOMAIN 75 133 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 134 242 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 243 346 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 347 450 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 451 560 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 575 675 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27161523,
ECO:0000312|PDB:5DZY}.
CARBOHYD 223 223 O-linked (Man) serine.
{ECO:0000269|PubMed:27161523,
ECO:0000312|PDB:5DZY}.
CARBOHYD 225 225 O-linked (Man) threonine.
{ECO:0000269|PubMed:27161523,
ECO:0000312|PDB:5DZY}.
CARBOHYD 227 227 O-linked (Man) threonine.
{ECO:0000269|PubMed:27161523,
ECO:0000312|PDB:5DZY}.
CARBOHYD 417 417 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:27161523,
ECO:0000312|PDB:5DZY}.
CARBOHYD 566 566 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
DISULFID 96 102 {ECO:0000269|PubMed:27161523,
ECO:0000312|PDB:5DZY}.
STRAND 32 36 {ECO:0000244|PDB:5DZY}.
STRAND 44 46 {ECO:0000244|PDB:5DZY}.
HELIX 48 52 {ECO:0000244|PDB:5DZY}.
HELIX 58 61 {ECO:0000244|PDB:5DZY}.
STRAND 65 67 {ECO:0000244|PDB:5DZY}.
STRAND 75 78 {ECO:0000244|PDB:5DZY}.
TURN 79 82 {ECO:0000244|PDB:5DZY}.
STRAND 83 88 {ECO:0000244|PDB:5DZY}.
HELIX 92 95 {ECO:0000244|PDB:5DZY}.
TURN 96 98 {ECO:0000244|PDB:5DZY}.
STRAND 103 110 {ECO:0000244|PDB:5DZY}.
TURN 111 114 {ECO:0000244|PDB:5DZY}.
STRAND 115 124 {ECO:0000244|PDB:5DZY}.
STRAND 134 143 {ECO:0000244|PDB:5DZY}.
STRAND 151 153 {ECO:0000244|PDB:5DZY}.
HELIX 163 165 {ECO:0000244|PDB:5DZY}.
STRAND 166 172 {ECO:0000244|PDB:5DZY}.
STRAND 176 183 {ECO:0000244|PDB:5DZY}.
TURN 186 188 {ECO:0000244|PDB:5DZY}.
STRAND 191 196 {ECO:0000244|PDB:5DZY}.
TURN 202 204 {ECO:0000244|PDB:5DZY}.
STRAND 206 220 {ECO:0000244|PDB:5DZY}.
STRAND 223 233 {ECO:0000244|PDB:5DZY}.
STRAND 241 243 {ECO:0000244|PDB:5DZY}.
STRAND 245 252 {ECO:0000244|PDB:5DZY}.
STRAND 260 263 {ECO:0000244|PDB:5DZY}.
HELIX 272 274 {ECO:0000244|PDB:5DZY}.
STRAND 278 282 {ECO:0000244|PDB:5DZY}.
STRAND 285 287 {ECO:0000244|PDB:5DZY}.
STRAND 291 293 {ECO:0000244|PDB:5DZY}.
TURN 295 297 {ECO:0000244|PDB:5DZY}.
STRAND 299 304 {ECO:0000244|PDB:5DZY}.
TURN 308 310 {ECO:0000244|PDB:5DZY}.
STRAND 313 321 {ECO:0000244|PDB:5DZY}.
STRAND 323 325 {ECO:0000244|PDB:5DZY}.
STRAND 327 337 {ECO:0000244|PDB:5DZY}.
STRAND 345 351 {ECO:0000244|PDB:5DZY}.
STRAND 353 355 {ECO:0000244|PDB:5DZY}.
STRAND 363 370 {ECO:0000244|PDB:5DZY}.
HELIX 375 377 {ECO:0000244|PDB:5DZY}.
STRAND 380 383 {ECO:0000244|PDB:5DZY}.
STRAND 386 396 {ECO:0000244|PDB:5DZY}.
STRAND 399 406 {ECO:0000244|PDB:5DZY}.
TURN 410 412 {ECO:0000244|PDB:5DZY}.
STRAND 414 424 {ECO:0000244|PDB:5DZY}.
STRAND 426 428 {ECO:0000244|PDB:5DZY}.
STRAND 431 440 {ECO:0000244|PDB:5DZY}.
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


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