PCDG2_PANTR
ID PCDG2_PANTR Reviewed; 932 AA.
AC Q5DRB8;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Protocadherin gamma-A2;
DE Short=PCDH-gamma-A2;
DE Flags: Precursor;
GN Name=PCDHGA2;
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_001076037.1; NM_001082568.2.
DR AlphaFoldDB; Q5DRB8; -.
DR SMR; Q5DRB8; -.
DR GeneID; 100034677; -.
DR KEGG; ptr:100034677; -.
DR CTD; 56113; -.
DR OrthoDB; 190510at2759; -.
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 InterPro; IPR030725; PCDHGA2/A3.
DR PANTHER; PTHR24028:SF134; PTHR24028:SF134; 1.
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..932
FT /note="Protocadherin gamma-A2"
FT /id="PRO_0000003951"
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 798..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"
FT CARBOHYD 685
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 932 AA; 101485 MW; 2A49C3C515325116 CRC64;
MAALQKLPHC RKLFLLCFLL ATLWEARAGQ IRYSVREEID RGSFVGNIAK DLGLEPLALA
EQGVRIVSRG RSQLFALNPR SGSLVTANRI DREELCAQSA PCLLNFNILL EDKLTIYSVE
VEITDINDNA PRFGVEELEL KISETTTPGF RIPLKNAHDA DVGENALQKY ALNPNDHFSL
DVRSGADGNK YPELVLERAL DREEEAVHHL VLVASDGGDP VLSGTSRICV KVLDANDNAP
VFTQPEYRIS IPENTPVGTR ILTVTATDAD EGYYAQVVYF LEKSPGETSE VFELKSTSGE
LTIIKDLDYE DATFHEIDIE AQDGPGLLTR AKVIVTVLDV NDNAPEFYMT SATSSVSEDS
LPGTIIGLFN VHDRDSGQNA FTTCSLPENL PFKLEKSVDN YYRLVTTRAL DREQFSFYNI
TLTAKDGGNP SLSTDAHILL QVADINDNAP AFSRTSYSTY IPENNPRGAS VFSVTAHDPD
SNDNAHVTYS FVEDTVQGAP LSSYISINSD TGVLYALRSF DYEQLRDLQV WVIARDSGNP
PLSSNVSLSL FVLDQNDNPP EILYPAFPTD GSTGVELAPR SAEPGYLVTK VVAVDRDSGQ
NAWLSYHLLK ASEPGLFSVG LHTGEVRTAR ALLDRDALKQ SLVVAVQDHG QPPLSATVTL
TVAVADRIPD ILADLGSLEP SAKPNDSDLT LYLVVAVAAV SCVFLAFVIV LLAHRLRRWH
KSRLLQASGG SLTGMQSSHF VGVDGVRAFL QTYSHEVSLT ADSRKSHLIF PQPNYADTLI
SQESCEKKDF LSAPQSLLEE EREETFSQQA PPNTDWRFSQ AQRPGTSGSQ NGDDTGTWPN
NQFDTEMLQA MILASASEAA DGSSTLGGGA GTMGLSARYG PQFTLQHVPD YRQNVYIPGS
NATLTNAAGK RDGKAPAGGN GNKKKSGKKE KK
