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PCDG7_PANTR
ID   PCDG7_PANTR             Reviewed;         932 AA.
AC   Q5DRB3;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Protocadherin gamma-A7;
DE            Short=PCDH-gamma-A7;
DE   Flags: Precursor;
GN   Name=PCDHGA7;
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_001076025.1; NM_001082556.1.
DR   AlphaFoldDB; Q5DRB3; -.
DR   SMR; Q5DRB3; -.
DR   GeneID; 100034686; -.
DR   KEGG; ptr:100034686; -.
DR   CTD; 56108; -.
DR   OrthoDB; 222156at2759; -.
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; 4.
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..932
FT                   /note="Protocadherin gamma-A7"
FT                   /id="PRO_0000003961"
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..932
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          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        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   932 AA;  101557 MW;  90572373A9911FA8 CRC64;
     MAAQPRGGDC RGFVLLSILL GTPWEAWAGR ILYSVSEETD KGSFVGDIAK DLGLEPRELA
     ERGVRIISRG RTQLFALNQR SGSLVTAGRI DREEICAQSA RCLVNFNILM EDKMNLYPID
     VEIIDINDNV PRFLTEEINV KIMENTAPGV RFPLSEAGDP DVGTNSLQSY QLSPNRHFSL
     AVQSGDDGTK YPELVLERVL DREEERVHHL VLTASDGGDP PRSSTAHIQV TVVDVNDHTP
     VFSLPQYQVT VPENVPVGTR LLTVHAIDLD EGVNGEVTYS FRKITPKLPQ MFHLNSLTGE
     ISTLEGLDYE ETAFYEMEVQ AQDGPGSLTK AKVLITVLDV NDNAPEVTMT SLSSSIPEDT
     PLGTVIALFY LQDRDSGKNG EVTCTIPENL PFKLEKSIDN YYRLVTTKNL DRETLSLYNI
     TLKATDGGTP PLSRETHIFM QVADTNDNPP TFPHSSYSVY IAENNPRGAS IFLVTAQDHD
     SEDNAQITYS LAEDTIQGAP VSSYVSINSD TGVLYALQSF DYEQLRELQL RVTAHDSGDP
     PLSSNMSLSL FVLDQNDNPP EILYPALPTD GSTGMELAPR SAEPGYLVTK VVAVDKDSGQ
     NAWLSYLLLK ASEPGLFAVG LYTGEVRTAR ALLDRDALKQ SLVVAVQDHG QPPLSATVTL
     TVAVADSIPE VLADLGSLEP SDGPYNYDLT LYLVVAVAAV SCVFLAFVLV LLALRLRRWH
     KSRLLQASEG GLASVPTSHF VGMDRVQAFL QTYSHEVSLT ADSRKSHLIF PQPNYVDMLI
     SQESCEKNDS LLTSVDFQEC KDDVPSIQQA PPNTDWRFSQ AQRPGTSGSQ NGDDTGTWPN
     NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS
     NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK
 
 
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