PCDG6_PANTR
ID PCDG6_PANTR Reviewed; 932 AA.
AC Q5DRB4;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Protocadherin gamma-A6;
DE Short=PCDH-gamma-A6;
DE Flags: Precursor;
GN Name=PCDHGA6;
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; Q5DRB4; -.
DR SMR; Q5DRB4; -.
DR InParanoid; Q5DRB4; -.
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..932
FT /note="Protocadherin gamma-A6"
FT /id="PRO_0000003959"
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 803..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 806..841
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 81
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; 100851 MW; 9CC3EC90FDCAD8D4 CRC64;
MAPPQRHPQR SEQVLLLTLL GTLWGAAAAQ IRYSIPEELE KGSFVGNIVK DLGLEPQELA
EHGVRIVSRG RMQLFSLNPR NGSLVTAGRI DREELCAQSP RCLVSFNILV EDKLNLYPVE
VEIVDINDNT PRFLKEELEV KILENAAPSS RFPLMEVYDP DVGMNSLQGF KLSGNSYFSV
DVQSEAHGPK YPELVLEGTL DREGEAVYRL VLTAMDGGDP VRSSIAQILV TVLDVNDNTP
VFTQPVYRVS VPENLPVGTP VLAVTATDQD EGVHGEVTYS FVKITEKISQ IFCLNVLTGE
ISTSANLDYE DSSFYELGVE ARDGPGLRDR AKVLITILDV NDNVPEVVVT SGSRTIAESA
PPGTVIALFQ VFDRDSGLNG LVTCSIPRSL PFELEKSVGN YYRLVTNAAL DREEVFLYNI
TVTATDKGTP PLSTETIISL NVADTNDNPP TFPHSSYSVY VLENNPRGAS IFSVNALDPD
VDQNAQVSYS LAEDTLQGAP LSSYVSINSD TGILYALRSF DYEQLRDLQL WVTASDSGDP
PLSSNVSLSL FVLDQNDNAP EILYPALPTD GSTGVELAPR SAEPGYLVTK VVAVDRDSGQ
NAWLSYRLLK ASEPGLFSVG LHTGEVRTAR ALLDRDALKQ SLVVAVQDHG QPPLSATVTL
TVAVADRIPD ILADLGSLEP SAKPNDSDLT LYLVVAVAAV SCVFLAFVIV LLALRLQRWH
KSRLLQASGG GLASMPGSHF VGVDGVRAFL QTYSHEVSLT ADSRKSHLIF PQPNYADTLI
NQESYEKSEP LLITQDLLET KGDPRQLQQA PPNTDWRFSQ AQRPGTSGSQ NGDDTGTWPN
NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS
NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK
