PCDG5_PANTR
ID PCDG5_PANTR Reviewed; 931 AA.
AC Q5DRB5;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Protocadherin gamma-A5;
DE Short=PCDH-gamma-A5;
DE Flags: Precursor;
GN Name=PCDHGA5;
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_001076032.1; NM_001082563.2.
DR AlphaFoldDB; Q5DRB5; -.
DR SMR; Q5DRB5; -.
DR GeneID; 100034683; -.
DR KEGG; ptr:100034683; -.
DR CTD; 56110; -.
DR InParanoid; Q5DRB5; -.
DR OrthoDB; 213724at2759; -.
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 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..931
FT /note="Protocadherin gamma-A5"
FT /id="PRO_0000003957"
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..931
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..683
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 800..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 811..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ SEQUENCE 931 AA; 100894 MW; C4D6BC537666B166 CRC64;
MASPPRGWGC GELLLPFMLL GTLCEPGSGQ IRYSMPEELD KGSFVGNIAK DLGLEPQELA
QRGVRIVSRG RTQLFALNPR SGSLVTAGRI DREELCAQSP LCVVNFNILV ENKMKIYGVE
VEIIDINDNF PRFRDEELKV KVNENAAAGT RLVLPFARDA DVGVNSLRSY QLSSNLHFSL
DVVIGTDGQK YPELVLEQPL DREKETVHDL LLTALDGGDP VLSGTTHIRV TVLDANDNAP
LFTPSEYSVS VPENIPVGTR LLMLTATDPD EGINGKLTYS FRNEEEKISE TFQLDSNLGE
ISTLQSLDYE ESRFYLMEVV AQDGGALVAS AKVVVTVQDV NDNAPEVILT SLTSSLSEDC
LPGTVIALFS VHDGDSGENG EIACSIPRNL PFKLEKSVDN YYHLVTTRDL DREETSDYNI
TLTVMDHGTP PLSTESHIPL KVADVNDNPP NFPQASYSTS VPENNPRGVS IFSVTAHDPD
SGDNARVTYS LAEDTFQGAP LSSYVSINSD TGVLYALRSF DYEQLRDLQL WVTASDSGNP
PLSSNVSLSL FVLDQNDNTP EILYPALPTD GSTGVELAPR SAEPGYLVTK VVAVDKDSGQ
NAWLSYRLLK ASEPGLFAVG LHTGEVRTAR ALLDRDALKQ SLVVAVEDHG QPPLSATVTV
TVAVADRIPD ILADLGSIKT PIDPEDLDLT LYLVVAVAAV SCVFLAFVIV LLVLRLRRWH
KSRLLQAEGS RLAGVPASHF VGVDGVRAFL QTYSHEVSLT ADSRKSHLIF PQPNYADTLL
SEESCEKSEP LLMSDKVDAN KEERRVQQAP PNTDWRFSQA QRPGTSGSQN GDDTGTWPNN
QFDTEMLQAM ILASASEAAD GSSTLGGGAG TMGLSARYGP QFTLQHVPDY RQNVYIPGSN
ATLTNAAGKR DGKAPAGGNG NKKKSGKKEK K
