PCDG1_PANTR
ID PCDG1_PANTR Reviewed; 931 AA.
AC Q5DRC2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Protocadherin gamma-A1;
DE Short=PCDH-gamma-A1;
DE Flags: Precursor;
GN Name=PCDHGA1;
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_001076024.1; NM_001082555.1.
DR AlphaFoldDB; Q5DRC2; -.
DR SMR; Q5DRC2; -.
DR GeneID; 100034676; -.
DR KEGG; ptr:100034676; -.
DR CTD; 56114; -.
DR InParanoid; Q5DRC2; -.
DR OrthoDB; 223098at2759; -.
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; 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; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR030736; PCDHGA1.
DR PANTHER; PTHR24028:SF108; PTHR24028:SF108; 1.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF16492; Cadherin_C_2; 1.
DR Pfam; PF15974; Cadherin_tail; 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..931
FT /note="Protocadherin gamma-A1"
FT /id="PRO_0000003949"
FT TOPO_DOM 29..692
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..931
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..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..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 453..562
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 570..682
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 801..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 265
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 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 931 AA; 101543 MW; 4796C738F0D4AE57 CRC64;
MKIQKKLTGC SRLMLLCLSL ELLLEAGAGN IHYSVPEETD KGSFVGNIAK DLGLQPQELA
DRGVRIVSRG RMPLFALNPR SGSLITARRI DREELCAQSM PCLVSFNILV EDKMKLFPVE
VEIIDINDNT PQFQLEELEF QMNEITTPGT RISLPFGQDL DVGMNSLQSY QLSSNPHFSL
DVQQGADGPQ HPEMVLQSPL DREEEAVHHL ILTASDGGEP VRSGTLRIYI QVVDANDNPP
AFTQAQYHIN VPENVPLGTQ LLMVNATDPD EGANGEVTYS FHNVDHRVAQ IFHLDSYTGE
ISNKEPLDFE EYKMYSMEVQ AQDGAGLMAK AKVLIKVLDV NDNTPEVTIT SVTTAVPENF
PPGTIIALIS VHDQDSGDNG CTTCFIPGNL PFKLEKLVDN YYRLVTERTL DRELISGYNI
TITAIDQGTP ALSTETHISL LVTDINDNSP VFHQDSYSAY IPENNPRGAS IFSVRAHDLD
SNENAQITYS LIEDTIQGAP LSAYLSINSD TGVLYALRSF DYEQFRNLQL KVMARDSGDP
PLSSNVSLSL FVLDQNDNPP EILYPALPTD DSTGVELAPR SAEPGYLVTK VVAVDRDSGQ
NAWLSYRLLK ASEPGLFSVG LHTGEVRTAR ALLDRDALKQ SLVVAVQDHG QPPLSATVTL
TVAVADRIPD ILADLGSLEP SAKPNDSDLT LYLVVAVAAV SCVFLAFVIV LLAHRLRRWH
KSRLLQASGG SLTGMQSSHF VGVDGVRAFL QTYSHEVSLT ADSRKSHLIF PQPNYADTLI
SQESCEKKDF LSAPQSLLED KKEPFSQQAP PNTDWRFSQA QRPGTSGSQN GDDTGTWPNN
QFDTEMLQAM ILASASEAAD GSSTLGGGAG TMGLSARYGP QFTLQHVPDY RQNVYIPGSN
ATLTNAAGKR DGKAPAGGNG NKKKSGKKEK K
