PCDA2_PANTR
ID PCDA2_PANTR Reviewed; 948 AA.
AC Q5DRF0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Protocadherin alpha-2;
DE Short=PCDH-alpha-2;
DE Flags: Precursor;
GN Name=PCDHA2;
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 RefSeq; NP_001076052.1; NM_001082583.2.
DR AlphaFoldDB; Q5DRF0; -.
DR SMR; Q5DRF0; -.
DR Ensembl; ENSPTRT00000066652; ENSPTRP00000058232; ENSPTRG00000017328.
DR GeneID; 100034708; -.
DR KEGG; ptr:100034708; -.
DR CTD; 56146; -.
DR GeneTree; ENSGT00940000160554; -.
DR OrthoDB; 300321at2759; -.
DR Proteomes; UP000002277; Chromosome 5.
DR Bgee; ENSPTRG00000017328; Expressed in cerebellum and 18 other tissues.
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; 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..22
FT /evidence="ECO:0000250"
FT CHAIN 23..948
FT /note="Protocadherin alpha-2"
FT /id="PRO_0000003887"
FT TOPO_DOM 23..697
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..948
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 157..242
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 243..350
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 351..455
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 456..565
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 588..678
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 734..737
FT /note="PXXP 1"
FT REPEAT 797..800
FT /note="PXXP 2"
FT REPEAT 830..833
FT /note="PXXP 3"
FT REPEAT 871..874
FT /note="PXXP 4"
FT REPEAT 889..892
FT /note="PXXP 5"
FT REGION 734..892
FT /note="5 X 4 AA repeats of P-X-X-P"
FT REGION 755..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..948
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 948 AA; 101940 MW; 06DA6E076FA94821 CRC64;
MASSIRRGLG AWTRLLSLLL LAAWEVGSGQ LRYSVPEEAK HGTFVGRIAQ DLGLELAELV
PRLFRVASKR HGDLLEVNLQ NGILFVNSRI DREELCGRSA ECSIHLEVIV DRPLQVFHVE
VEVKDINDNP PVFPMTVKTI RFPESRLLDS RFPLEGASDA DIGVNALLSY KLSSSEFFFL
DIQTNDELSE SLSLVLGKSL DREETAEVNL LLVATDGGKP ELTGTVQILI KVLDVNDNEP
TFAQSVYKVK LLENTANGTL VVKLNASDAD EGSNSEIVYS LGSDVSSTIQ TKFTIDPISG
EIRTKGKLDY EEAKSYEIQV TATDKGTPSM SGHCKISLKL VDINDNTPEV SITSLSLPIS
ENASLGTVIA LITVSDRDSG TNGHVTCSLT PHVPFKLVST FKNYYSLVLD SALDRESVSA
YELVVTARDG GSPSLWATTS VSIEVADVND NAPAFAQPEY TVFVKENNPP GCHIFTVSAW
DADAQENALV SYSLVERRVG ERALSSYVSV HAESGKVYAL QPLDHEEVEL LQFQVTARDA
GVPPLGSNVT LQVFVLDEND NAPALLAPRA GTAAGAVSEL VPWSVGAGHV VAKVRAVDAD
SGYNAWLSYE LQLGTGSARI PFRVGLYTGE ISTTRALDEA DSPRHRLLVL VKDHGEPALT
ATATVLVSLV ESGQAPKASS RAWVGAAGSE ATLVDVNVYL IIAICAVSSL LVLTVLLYTA
LRCSVPATEG ARAPGKPTLV CSSAVGSWSY SQQRRQRVCS GEDPPKTDLM AFSPSLSQGP
DSAEEKQLSE SEYVGKPRQP NPDWRYSASL RAGMHSSVHL EEAGILRAGP GGPDQQWPTV
SSATPEPEAG EVSPPVGAGV NSNSWTFKYG PGNPKQSGPG ELPDKFIIPG SPAIISIRQE
PANSQIDKSD FITFGKKEET KKKKKKKKGN KTQEKKEKGN STTDNSDQ
