PCDB8_PANTR
ID PCDB8_PANTR Reviewed; 801 AA.
AC Q5DRC6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Protocadherin beta-8 {ECO:0000305};
DE Short=PCDH-beta-8 {ECO:0000305};
DE Flags: Precursor;
GN Name=PCDHB8 {ECO:0000250|UniProtKB:Q9UN66};
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:Q91XZ2}.
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:Q91XZ2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q91XZ2};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q91XZ2}.
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:Q91XZ2}.
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DR AlphaFoldDB; Q5DRC6; -.
DR SMR; Q5DRC6; -.
DR STRING; 9598.ENSPTRP00000060233; -.
DR PaxDb; Q5DRC6; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q5DRC6; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
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; 5.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
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..29
FT /evidence="ECO:0000250|UniProtKB:Q91XZ2"
FT CHAIN 30..801
FT /note="Protocadherin beta-8"
FT /id="PRO_0000003929"
FT TOPO_DOM 30..691
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q91XZ2"
FT TRANSMEM 692..710
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 711..801
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91XZ2"
FT DOMAIN 36..134
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 139..243
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 248..348
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 353..452
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 457..562
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 569..672
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..103
FT /evidence="ECO:0000250|UniProtKB:Q91XZ2"
SQ SEQUENCE 801 AA; 87540 MW; C10677B65F0871ED CRC64;
MEASGKLICR QRQVLFSFLL LGLSLAGAAE PRSYSVVEET EGSSFVTNLA KDLGLEQREF
SRRGVRVVSR GNKLHLQLNQ ETGDLLLNEK LDREDLCGHT EPCVLRFQVL LESPFEFFQA
ELQVIDINDH SPVFLDKQML VKVSESSPPG TAFPLKNAED LDVGQNNIEN YIISPNSYFR
VLTRKRSDGR KYPELVLDKA LDREEEAELR LTLTALDGGS PPRSGTAQVY IEVVDVNDNA
PEFEQPFYRV QISEDSPISF LVVKVSATDV DTGVNGEISY SLFQASDEIS KTFKVDFLTG
EIRLKKQLDF EKFQSYEVNI EARDAGGFSG KCTVLIQVID VNDHAPEVTM SAFTSPIPEN
APETVVALFS VSDLDSGENG KISCSIQEDL PFLLKSSVGN FYTLLTETPL DRESRAEYNV
TITVTDLGTP GLTTHLNMTV LVSDVNDNAP AFTQASYTLF VRENNSPALH IGSVSATDRD
SGTNAQVTYS LLPPQNPHLP LASLVSINTD NGHLFALRSL DYEALQAFEF RVGASDRGSP
ALSSEALVRV LVLDANDNSP FVLYPLQNSS APCTELVPRA AEPGYLVTKV VAVDGDSGQN
AWLSYQLLKA TEPGLFGVWA HNGEVRTARL LSERDAAKQR LVVLVKDNGE PPCSATATLH
VLLVDGFSQP YLPLPEAAPA QGQADSLTVY LVVALASVSS LFLFSVLLFV AVRLCRRSRA
ASVGRCSVPE GPFPGHLVDV RGTGSLSQNY QYEVCLAGGS GTNEFQFLKP VLPNIQGHSF
GPEMEQNSNF RNGFGFSLQL K
