PCDG8_PANTR
ID PCDG8_PANTR Reviewed; 932 AA.
AC Q5DRB2;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protocadherin gamma-A8;
DE Short=PCDH-gamma-A8;
DE Flags: Precursor;
GN Name=PCDHGA8;
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_001026791.2; NM_001031620.3.
DR AlphaFoldDB; Q5DRB2; -.
DR SMR; Q5DRB2; -.
DR Ensembl; ENSPTRT00000061828; ENSPTRP00000054371; ENSPTRG00000017346.
DR GeneID; 471673; -.
DR KEGG; ptr:471673; -.
DR CTD; 9708; -.
DR GeneTree; ENSGT00940000162232; -.
DR InParanoid; Q5DRB2; -.
DR OrthoDB; 260275at2759; -.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000017346; Expressed in dorsolateral prefrontal cortex and 21 other tissues.
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 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..29
FT /evidence="ECO:0000255"
FT CHAIN 30..932
FT /note="Protocadherin gamma-A8"
FT /id="PRO_0000003963"
FT TOPO_DOM 30..692
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 693..713
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 714..932
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..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 804..841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..932
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
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 932 AA; 101535 MW; 21DEB9D0B768E1EC CRC64;
MAAPQSRPRR GELILLCALL GTLWEIGRGQ IRYSVPEETD KGSFVGNISK DLGLDPRELA
KHGVRIVSRG RTQLFALNPR SGSLVTAGRI DREELCAQSP RCLININILV EDKGKLFGIE
IEIVDINDNN PKFQVEDLEV KINEIAVPGA RYPLPEAVDP DVGVNSLQSY QLSPNHHFSL
DVQTGDNGAI NPELVLERAL DREEEAAHHL VLTASDGGEP RRSSTVRIHV TVLDTNDNAP
VFPHPIYRVK VLENMPPGTR LLTVTASDPD EGINGKVAYK FRKINEKQTP LFQLNENTGE
ISIAKSLDYE ECSFYEMEIQ AEDVGALLGR TKLLISVEDV NDNRPEVIIT SLFSPVLENS
LPGTVIAFLS VHDQDSGKNG QVVCHTRDNL PFKLEKSIDN YYRLVTRKYL DRENVSIYNI
TVMASDLGTP PLSTETQIAL HVADINDNPP TFPHASYSAY ILENNLRGAS IFSLTAHDPD
SQENAQVTYS VTEDTLQGAP LSSYISINSD TGVLYALQSF DYEQIRDLQL LVTASDSGDP
PLSSNVSLSL FVLDQNDNAP EILYPTLPTD GSTGLELAPR SAEPGYLVTK VVAVDRDSGQ
NAWLSYRLLK ASEPGLFSVG LHTGEVRTAR ALLDRDALKQ SLVVAVQDHG QPPLSATVTL
TVAVADSIPE VLTELGSLKP SVDPNDSSLT LYLVVAVAAI SCVFLAFVAV LLGLRLRRWH
KSHLLQDSSG RLVGVPASHF VGVEEVQAFL QTYSQEVSLT ADSRKSHLIF PQPNYADTLI
SQESCEKNDS LLTSVDFHEY KNEADHGQQA PPNTDWRFSQ AQRPGTSGSQ NGDDTGTWPN
NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS
NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK
