PCDB6_MOUSE
ID PCDB6_MOUSE Reviewed; 772 AA.
AC Q91XZ4;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Protocadherin beta-6 {ECO:0000305};
DE Short=PCDH-beta-6 {ECO:0000305};
DE Flags: Precursor;
GN Name=Pcdhb6 {ECO:0000312|MGI:MGI:2136740};
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 X-RAY CRYSTALLOGRAPHY (2.88 ANGSTROMS) OF 29-445 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 AND ASN-417, CALCIUM-BINDING, AND MUTAGENESIS OF HIS-67;
RP ARG-69; LYS-141; GLN-143; SER-145; ARG-185; GLU-317; SER-323; LEU-326 AND
RP SER-368.
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 (PubMed:27161523).
CC Thereby, it is involved in the establishment and maintenance of
CC specific neuronal connections in the brain (PubMed:27161523).
CC {ECO:0000269|PubMed:27161523}.
CC -!- SUBUNIT: Forms homodimers in trans (molecules expressed by two
CC different cells). Forms promiscuous heterodimers in cis (at the plasma
CC membrane of the same cell) with other protocadherins.
CC {ECO:0000269|PubMed:27161523}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27161523};
CC Single-pass type I membrane protein {ECO:0000269|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:5DZX}.
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DR EMBL; AY013788; AAK26077.1; -; mRNA.
DR EMBL; AC020974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS29174.1; -.
DR RefSeq; NP_444361.1; NM_053131.1.
DR PDB; 5DZX; X-ray; 2.88 A; A/B=29-445.
DR PDBsum; 5DZX; -.
DR AlphaFoldDB; Q91XZ4; -.
DR SMR; Q91XZ4; -.
DR STRING; 10090.ENSMUSP00000058592; -.
DR GlyGen; Q91XZ4; 5 sites.
DR iPTMnet; Q91XZ4; -.
DR PhosphoSitePlus; Q91XZ4; -.
DR PaxDb; Q91XZ4; -.
DR PRIDE; Q91XZ4; -.
DR ProteomicsDB; 288111; -.
DR DNASU; 93877; -.
DR Ensembl; ENSMUST00000061717; ENSMUSP00000058592; ENSMUSG00000051678.
DR GeneID; 93877; -.
DR KEGG; mmu:93877; -.
DR UCSC; uc008epr.1; mouse.
DR CTD; 56130; -.
DR MGI; MGI:2136740; Pcdhb6.
DR VEuPathDB; HostDB:ENSMUSG00000051678; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000157793; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR InParanoid; Q91XZ4; -.
DR OMA; ERSNYEM; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q91XZ4; -.
DR TreeFam; TF332299; -.
DR BioGRID-ORCS; 93877; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q91XZ4; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q91XZ4; protein.
DR Bgee; ENSMUSG00000051678; Expressed in cerebellar cortex and 29 other tissues.
DR ExpressionAtlas; Q91XZ4; baseline and differential.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
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:0009988; P:cell-cell recognition; IDA:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA: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; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
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..772
FT /note="Protocadherin beta-6"
FT /evidence="ECO:0000305"
FT /id="PRO_5008429367"
FT TOPO_DOM 31..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..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:27161523"
FT DOMAIN 31..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:5DZX"
FT CARBOHYD 223
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZX"
FT CARBOHYD 225
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZX"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZX"
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:5DZX"
FT MUTAGEN 67
FT /note="H->V: Changed homophilic interaction, being unable
FT to interact with the wild-type protein but able to bind
FT itself;when associated with D-69 and R-368."
FT /evidence="ECO:0000269|PubMed:27161523"
FT MUTAGEN 69
FT /note="R->D: Changed homophilic interaction, being unable
FT to interact with the wild-type protein but able to bind
FT itself;when associated with V-67 and R-368."
FT /evidence="ECO:0000269|PubMed:27161523"
FT MUTAGEN 141
FT /note="K->E: No effect on homophilic interaction. Changed
FT homophilic interaction, being unable to interact with the
FT wild-type protein but able to bind itself; when associated
FT with R-323."
FT /evidence="ECO:0000269|PubMed:27161523"
FT MUTAGEN 143
FT /note="Q->P: Changed homophilic interaction; when
FT associated with F-326."
FT /evidence="ECO:0000269|PubMed:27161523"
FT MUTAGEN 145
FT /note="S->I: Changed homophilic interaction, being unable
FT to interact with the wild-type protein but able to bind
FT itself."
FT /evidence="ECO:0000269|PubMed:27161523"
FT MUTAGEN 185
FT /note="R->N: No effect on homophilic interaction. Changed
FT homophilic interaction, being unable to interact with the
FT wild-type protein but able to bind itself; when associated
FT with K-317."
FT /evidence="ECO:0000269|PubMed:27161523"
FT MUTAGEN 317
FT /note="E->K: Changed homophilic interaction, being unable
FT to interact with the wild-type protein but able to bind
FT itself; when associated with N-185."
FT /evidence="ECO:0000269|PubMed:27161523"
FT MUTAGEN 323
FT /note="S->R: Changed homophilic interaction, being unable
FT to interact with the wild-type protein but able to bind
FT itself; when associated with E-141."
FT /evidence="ECO:0000269|PubMed:27161523"
FT MUTAGEN 326
FT /note="L->F: No effect on homophilic interaction. Changed
FT homophilic interaction; when associated with P-143."
FT /evidence="ECO:0000269|PubMed:27161523"
FT MUTAGEN 368
FT /note="S->R: No effect on homophilic interaction. Changed
FT homophilic interaction, being unable to interact with the
FT wild-type protein but able to bind itself; when associated
FT with V-67 and D-69."
FT /evidence="ECO:0000269|PubMed:27161523"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:5DZX"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:5DZX"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:5DZX"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:5DZX"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:5DZX"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 100..110
FT /evidence="ECO:0007829|PDB:5DZX"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:5DZX"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:5DZX"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 206..220
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:5DZX"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 277..283
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:5DZX"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 299..304
FT /evidence="ECO:0007829|PDB:5DZX"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 312..325
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 327..337
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 345..351
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:5DZX"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 388..396
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 399..406
FT /evidence="ECO:0007829|PDB:5DZX"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 416..428
FT /evidence="ECO:0007829|PDB:5DZX"
FT STRAND 431..441
FT /evidence="ECO:0007829|PDB:5DZX"
SQ SEQUENCE 772 AA; 84280 MW; 21CC99CC7F8C3F87 CRC64;
METTLAKTPE KRQVVFLAIL LLLWEAGSEA IRYSIPEETE SGYLVAHLAK DLGFRVGELA
TRRARIHHRG NKELLQLDVE TGNLLLKEKP DREALCGATE PCVLHFQIIL ENPVQFFQTE
LQLTDINDHS PEFPDTEMLL KIQESTQPAT VFLLKAAQDS DIGSNAVQNY TVSPNLHFHV
VTLSRSDGRK YPELVLDRAL DREEQPELTL ILTALDGGAP PKSGTTTVRI EVVDINDNAP
EFVQSLYSVE VPENSPLDAL VVTVSARDLD AGIHGNVAYS LFQGGGGPQP FVIDEITGEI
RLKGALDFEA TSYYTMEIVA TDSGGLSGKC TVAIQVLDVN DNAPKLTISS LTSSIPENAP
EAVVAVFSVS DPDSGDNGRM VCSIQNELPF LLKPTFENYY TLAAEGPLDR EIREEYNITI
IVSDLGTPRL TTQHTITVQV VDINDNAPAF TQTSYTMFVH ENNNPALHIG TISATDSDSG
SNAHITYSLL PPHDLQLSLA SLVSINADNG QLFALRAMDY EALQAFEFHV VARDGGSPAL
SSQALVRVVV LDDNDNAPFI LYPMQNASAP CTELLPRAAE PGYLVTKVVA VDSDSGQNAW
LSFQLLKATE PGLFSVWAHN GEVRTTRLLS ERDVPKHRLL LLVKDNGEPP RSASVTLHVL
LVDGFSQPYL PLPEVQHDSS QDEDMLTLYL VIALASVSSL FLLSVLLFVG VRLCRRVREA
SLGACSVPEG HFSGHLVDVS GMGTLSQSYQ YEVCLSGDSG TTDFKFLNHY SQ
