PCDB1_PANTR
ID PCDB1_PANTR Reviewed; 818 AA.
AC Q5DRE0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Protocadherin beta-1;
DE Short=PCDH-beta-1;
DE Flags: Precursor;
GN Name=PCDHB1;
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: Potential calcium-dependent cell-adhesion protein. May be
CC involved in the establishment and maintenance of specific neuronal
CC connections in the brain.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
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DR RefSeq; NP_001019304.1; NM_001024133.2.
DR AlphaFoldDB; Q5DRE0; -.
DR SMR; Q5DRE0; -.
DR STRING; 9598.ENSPTRP00000029631; -.
DR PaxDb; Q5DRE0; -.
DR Ensembl; ENSPTRT00000032070; ENSPTRP00000029631; ENSPTRG00000017330.
DR GeneID; 471658; -.
DR KEGG; ptr:471658; -.
DR CTD; 29930; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000162745; -.
DR HOGENOM; CLU_006480_3_2_1; -.
DR InParanoid; Q5DRE0; -.
DR OMA; ERDPMMQ; -.
DR OrthoDB; 300321at2759; -.
DR TreeFam; TF332299; -.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000017330; Expressed in pituitary gland.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 InterPro; IPR030723; PCDHB1.
DR PANTHER; PTHR24028:SF12; PTHR24028:SF12; 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; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 3: Inferred from homology;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..818
FT /note="Protocadherin beta-1"
FT /id="PRO_0000003915"
FT TOPO_DOM 29..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..818
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 138..242
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 243..347
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 348..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 577..672
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 789..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 818 AA; 90571 MW; 70AEF1ADC40BEE1C CRC64;
MAGTRRKSLQ NRQVGSLLIF LCISVGGATT IRYSVAEEME SGSFVANVAK DLGLEVGKLA
ARGARLVSEG NKMHFRLHRK TGDLFVKEKL DRESLCGKAD PCVLHFEVVL VEPLQSFRAE
VRVFDINDNA PVFLNKEPLL KIPESTPLGS RFPLQSAQDL DVGLNGLQNY TLSANGYFHL
HTRFRSHGPK YAELVLNKPL DREKQPEVNL TITAVDGGSP PKSGTAHIHV VVLDVNDHVP
QFSRLVYRAQ VSENSPNGSL VATVTAVDLD EGTNKAITYS LAQNPEAILK TFQIDPQNGE
VRLRGPLDFE AIETYDIDIQ ATDGGGLSAH SKVLVEVVDV NDNPPEVMVS SVSSPLPEDS
PPQTVVALFT IRDRDIRVGG KVTCFLREDL PFVIKPTFGN SYSLVTDRSL DREEVSGYNI
TLVAMDTGPP SLSAETMIEV LISDVNDNPP IFREDSYILT VRENNSPAVF IGKVHAEDLD
LGENAQITYS LLPPKNGDLS VFAYISINSD NGKLYALRTM DYEAIQDFQF VVKATDGGFL
SLSSQVTVRV VVLDDNDNRP MILYPLQNGT LPCNDLVPRS AEAGYLVTKV VAVDGDSGQN
SWLSYHLLKA TDLGLFSVQR QNGEIHTLRQ ISERDPMMQK LIILVQDHGQ PALSTTVSLN
ILLVDGFSEP YLQFQDPTRH SRKVNPSTKY LVISLVILSF LFLLSVIVIF IIHVYQKIKY
REKFTIQEHF YDDCNFSNNL VQGQGNGSLS RPCPYEMCSA TGTGNSEFRF LKRFMPNFPF
PHATGEIKME AGSSLPPNSD RNKSQRLEGH DQVSDDYM
