PCDB6_PANTR
ID PCDB6_PANTR Reviewed; 794 AA.
AC Q5DRC8;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protocadherin beta-6 {ECO:0000305};
DE Short=PCDH-beta-6 {ECO:0000305};
DE Flags: Precursor;
GN Name=PCDHB6 {ECO:0000250|UniProtKB:Q9Y5E3};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2]
RP IDENTIFICATION.
RX PubMed=15744052; DOI=10.1534/genetics.104.037606;
RA Wu Q.;
RT "Comparative genomics and diversifying selection of the clustered
RT vertebrate protocadherin genes.";
RL Genetics 169:2179-2188(2005).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein involved in cells
CC self-recognition and non-self discrimination. Thereby, it is involved
CC in the establishment and maintenance of specific neuronal connections
CC in the brain. {ECO:0000250|UniProtKB:Q91XZ4}.
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:0000250|UniProtKB:Q91XZ4}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91XZ4};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q91XZ4}.
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. This is a head-to-tail interaction, the cadherin
CC 1 domain interacting with the cadherin 4 domain and the cadherin 2
CC domain interacting the cadherin 3 domain of the other protocadherin.
CC The cadherin 6 domain mediates promiscuous interactions with
CC protocadherins on the same cell membrane. Each cadherin domain binds
CC three calcium ions. {ECO:0000250|UniProtKB:Q91XZ4}.
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DR RefSeq; NP_001013027.1; NM_001013009.3.
DR AlphaFoldDB; Q5DRC8; -.
DR SMR; Q5DRC8; -.
DR STRING; 9598.ENSPTRP00000029635; -.
DR PaxDb; Q5DRC8; -.
DR Ensembl; ENSPTRT00000032075; ENSPTRP00000029635; ENSPTRG00000017335.
DR GeneID; 462130; -.
DR KEGG; ptr:462130; -.
DR CTD; 56130; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000163433; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR InParanoid; Q5DRC8; -.
DR OMA; MLWGEVG; -.
DR OrthoDB; 300321at2759; -.
DR TreeFam; TF332299; -.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000017335; Expressed in dorsolateral prefrontal cortex and 14 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0009988; P:cell-cell recognition; ISS:UniProtKB.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProt.
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 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; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 5.
PE 3: Inferred from homology;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Membrane; Metal-binding; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..27
FT /evidence="ECO:0000250|UniProtKB:Q91XZ4"
FT CHAIN 28..794
FT /note="Protocadherin beta-6"
FT /id="PRO_0000003925"
FT TOPO_DOM 28..688
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q91XZ4"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..794
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91XZ4"
FT DOMAIN 34..132
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 137..241
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 246..345
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 350..449
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 454..559
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 566..669
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 773..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 416
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 565
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 95..101
FT /evidence="ECO:0000250|UniProtKB:Q91XZ4"
SQ SEQUENCE 794 AA; 87365 MW; 36284776747AB129 CRC64;
MMQTKVQNKK RQVAFFILLM LWGEVGSESI QYSVLEETES GTFVANLTKD LGLRVGELAS
RGARVVFKGN RQHLQFDPQT HDLLLNEKLD REELCGSTEL CVLPFQVLLE NPLQFFQASL
RVRDINDHAP EFPAREMLLK ISEITMPGKI FPLKMAHDLD TGSNGLQRYT ISSNPHFHVL
TRNRSEGRKF PELVLDKPLD REEQPQLRLT LIALDGGSPP RSGTSEIQIQ VLDINDNVPE
FAEELYEAQV PENNPLGSLV ITVSARDLDA GSFGKVSYAL FQVDDVNQPF EINAITGEIR
LRKALDFEEI QSYDLDVEAT DGGGLSGKCS LLVRVLDVND NAPELTMSFF ISPIPENLPE
IIVAVFSVSD ADSGHNQQVI CSIENNLPFL LRPTVENFYT LVTEGALDRE SRAEYNITIT
VTDLGTPRLK TQQSITVQVS DVNDNAPAFT QTSYTLFVRE NNSPALHIGS VSATDRDSGI
NAQVTYSLLP PQDPHLPLAS LVSINADNGH LFALRSLDYE ALQAFEFRVG ATDRGSPALS
SEALVRVLVL DANDNSPFVL YPLQNGSAPC TELVPRAAEP GYLVTKVVAV DGDSGQNAWL
SYQLLKATEL GLFGVWAHNG EVRTARLLSE RDAAKHRLVV LVKDNGEPPR SATATLHVLL
VDGFSQPYLP LPEAAPAPAQ ADLLTVYLVV ALASVSSLFL FSVLLFVAVR LCRRSRAASV
GRCSVPEGPF PEHLVDVNGT GTLSQSYQYK VCLTGGSETN EFKFLKPIMP NFPPQGTERE
MEETPTSRNS FPFS
