ID   PCDG4_PANTR             Reviewed;         931 AA.
AC   Q5DRB6;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Protocadherin gamma-A4;
DE            Short=PCDH-gamma-A4;
DE   Flags: Precursor;
GN   Name=PCDHGA4;
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   AlphaFoldDB; Q5DRB6; -.
DR   SMR; Q5DRB6; -.
DR   STRING; 9598.ENSPTRP00000054373; -.
DR   PaxDb; Q5DRB6; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   InParanoid; Q5DRB6; -.
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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..931
FT                   /note="Protocadherin gamma-A4"
FT                   /id="PRO_0000003955"
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..567
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   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;  100735 MW;  594C21DBE9DB8F7E CRC64;
     MAAPPARPDH TRLLHICLLL GVLVEIRAEQ IRYSVFEEQE EGSVVGNIAK DLGLAPRELA
     ERGVRIVSRG RTQLFALNPR SGTLVTAGRI DREELCDRSP NCVTNLEILL EDTVKILRVE
     VEIIDVNDNP PSFGTEQREI KVAENENPGT RFPLPEAFDP DVGVNSLQGY QLNSNGYFSL
     DVQSGADGIK YPELVLERAL DREEEAVHHL VLTAFDGGDP VRSGTARILI ILVDTNDNAP
     VFTQPEYHVS VHENVPVGTL LLTVKATDPD EGANGDVTYS FRKVRDKISQ LFQLNSLSGD
     ITILGDLDYE DSGFYDIDVE AHDGPGLRAR SKVLVTVLDE NDNAPEVTVT SLTSSVQETS
     SPGTVIALFN VHDSDSGGNG LVTCSIPDNL PFTLEKTYGN YYRLLTHRTL DREEVSEYNI
     TVTATDQGTP PLSTETHISL QVMDINDNPP TFPHASYSAY VPENNPRGAS ILSMTAQDPD
     SGDNARITYS LAEDTFQGAP LSSYVSINSN TGILYALRSF DYEQFRDLQL LVTASDSGDP
     PLSSNVSLSL FVLDQNDNVP EILYPTFPTD DSTGVELAPR SADSGYLVTK VVAVDRDSGQ
     NAWLSYRLLK SSEPGLFAVG LHTGEVRTAR ALLDRDALKQ SLVVVVQDHG QPPLSATVTL
     TVAVADSIPD VLADLGSLKP SADPDDSGLT LYLVVSVAAV SCVFLAFVTV LLALKLRRWH
     KSRLLHAEGS RLSGVPASHF VGVDGVRAFL QTYSHEVSLT ADSRKSHLIF SQPSYADTLI
     SLESCEKSEP LLITQDLLET KGDPNLQQAP PNTDWRFSQA QRPGTSGSQN GDDTGTWPNN
     QFDTEMLQAM ILASASEAAD GSSTLGGGAG TMGLSARYGP QFTLQHVPDY RQNVYIPGSN
     ATLTNAAGKR DGKAPAGGNG NKKKSGKKEK K