PCDA5_PANTR
ID PCDA5_PANTR Reviewed; 936 AA.
AC Q5DRE7;
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 alpha-5;
DE Short=PCDH-alpha-5;
DE Flags: Precursor;
GN Name=PCDHA5;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; Q5DRE7; -.
DR SMR; Q5DRE7; -.
DR STRING; 9598.ENSPTRP00000058286; -.
DR PaxDb; Q5DRE7; -.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q5DRE7; -.
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; 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; 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..936
FT /note="Protocadherin alpha-5"
FT /id="PRO_0000003893"
FT TOPO_DOM 29..696
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..936
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 33..132
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 156..241
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 242..349
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 350..454
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 455..564
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 580..677
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 773..776
FT /note="PXXP 1"
FT REPEAT 785..788
FT /note="PXXP 2"
FT REPEAT 818..821
FT /note="PXXP 3"
FT REPEAT 873..876
FT /note="PXXP 4"
FT REPEAT 877..890
FT /note="PXXP 5"
FT REGION 759..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..890
FT /note="5 X 4 AA repeats of P-X-X-P"
FT REGION 815..875
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..791
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 921..936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 936 AA; 101914 MW; 26236087AC70B078 CRC64;
MVYSRRGSLG SRLLLLWLLL AYWKAGSGQL HYSIPEEAKH GTFVGRIAQD LGLELAELVP
RLFRVASKGR GDLLEVNLQN GILFVNSRID REELCRRRAE CSIHLEVIVD RPLQVFHVEV
AVKDINDNPP RFSRQEQTLF ILESRMPDSR FPLEGASDLD IGANAQLRYR LNPNEYFDLD
VKTNEEETNF LELVLRKSLD REETQEHRLL VIATDGGKPE LTGTVQLLIN VLDANDNAPE
FDKSIYNVRL LENAPSGTLV IKLNASDADE GINKEIVYFF SNLVLDDVKS KFIINSNTGE
IKVNGELDYE DCNSYEINID AVDKSTFPLS GHCKVVVKLL DVNDNTPEMA ITTLFLPVKE
DAPLSTVIAL ITVSDRDSGA NGPVTCSLMP HVPFKLVSTF KNYYSLVLDS ALDRESLSVY
ELVVTARDGG SPSLWATASV SVEVADVNDT LRAFAQPQYT VFVKENNPPG CHIFTVSARD
ADAQENALVS YSLVERRVGE RPLSSYVSVH AESGKVYALQ PLDHEEVELL QFQVSARDAG
VPPLGSNVTL QVFVLDENDN APALLAPRVG GTGGAVSELV PRSVGAGHVV AKVRAVDPDS
GYNAWLSYEL QPAPGSARIP FRVGLYTGEI STTRSLDETE APRHRLLVLV KDHGEPPLTA
TATVLVSLVE SGQAPKASSR ASAGAVGPEA ALVDVNVYLI IAICAVSSLL VLTLLLYTAL
RCSAQPTEAV CTRGKPTLVC SSAVGSWSYS QQRRQRVCSG EAPPKTDLMA FSPSLPQGPT
STDNPRQPNP DWRYSASLRA GMHSSVHLEE AGILRAGPGG PDQQWPTVSS ATPEPEAGEV
SPPVGAGVNS NSWTFKYGPG NPKQSGPGEL PDKFIIPGSP AIISIRQEPA NSQIDKSDFI
TFGKKEETKK KKKKKKGNKT QEKKEKGNST TDNSDQ
