PCDH3_RAT
ID PCDH3_RAT Reviewed; 797 AA.
AC Q63418;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Protocadherin-3;
DE Flags: Precursor;
GN Name=Pcdh3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8575755; DOI=10.1006/geno.1995.9956;
RA Sago H., Kitagawa M., Obata S., Mori N., Taketani S., Rochelle J.M.,
RA Seldin M.F., Davidson M.K., John T., Suzuki S.T.;
RT "Cloning, expression, and chromosomal localization of a novel cadherin-
RT related protein, protocadherin-3.";
RL Genomics 29:631-640(1995).
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 -!- TISSUE SPECIFICITY: Expressed in brain.
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DR EMBL; L43592; AAC42079.1; -; mRNA.
DR RefSeq; NP_775122.1; NM_173099.1.
DR AlphaFoldDB; Q63418; -.
DR SMR; Q63418; -.
DR STRING; 10116.ENSRNOP00000045459; -.
DR GlyGen; Q63418; 4 sites.
DR iPTMnet; Q63418; -.
DR PhosphoSitePlus; Q63418; -.
DR SwissPalm; Q63418; -.
DR PaxDb; Q63418; -.
DR PRIDE; Q63418; -.
DR GeneID; 25133; -.
DR KEGG; rno:25133; -.
DR UCSC; RGD:3266; rat.
DR CTD; 56124; -.
DR RGD; 3266; Pcdh3.
DR eggNOG; KOG3594; Eukaryota.
DR InParanoid; Q63418; -.
DR OrthoDB; 300321at2759; -.
DR PhylomeDB; Q63418; -.
DR PRO; PR:Q63418; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
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 InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR032455; Cadherin_C.
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 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 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..797
FT /note="Protocadherin-3"
FT /id="PRO_0000003947"
FT TOPO_DOM 31..691
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 692..712
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 713..797
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 138..242
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 247..346
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 351..450
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 455..560
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 567..670
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 797 AA; 87474 MW; 42E279E6C6117861 CRC64;
METALAKIPQ QRQVFFLTIL SLLWKSSSEA IRYSMPEETE SGYMVANLAK DLGIRVGELS
SRGAQIHYKG NKELLQLDAE TGNLFLKEKL DRELLCGETE PCVLNFQIIL ENPMQFFQTE
LQLTDINDHS PEFPNKKMLL TIPESAHPGT VFPLKAARDS DIGSNAVQNY TVNPNLHFHV
VTHSRTDGRK YPELVLDRAL DREEQPELTL ILTALDGGAP SRSGTTTVHI EVVDINDNSP
QFVQSLYKVQ VPENNPLNAF VVTVSATDLD AGVYGNVTYS LFQGYGVFQP FVIDEITGEI
HLSKELDFEE ISNHNIEIAA TDGGGLSGKC TVAVQVLDVN DNAPELTIRK LTVLVPENSA
ETVVAVFSVS DSDSGDNGRM VCSIPNNIPF LLKPTFENYY TLVTEGPLDR ENRAEYNITI
TVSDLGTPRL TTQHTITVQV SDINDNAPAF TQTSYTMFVH ENNSPALHIG TISATDSDSG
SNAHITYSLL PPDDPQLALD SLISINVDNG QLFALRALDY EALQSFEFYV GATDGGSPAL
SSQTLVRMVV LDDNDNAPFV LYPLQNASAP CTELLPRAAE PGYLITKVVA VDRDSGQNAW
LSFQLLKATE PGLFSVWAHN GEVRTTRLLS ERDAQKHKLL LLVKDNGDPL RSANVTLHVL
VVDGFSQPYL PLAEVAQDSM QDNYDVLTLY LVIALASVSS LFLLSVVLFV GVRLCRRARE
ASLGDYSVPE GHFPSHLVDV SGAGTLSQSY QYEVCLNGGT RTNEFNFLKP LFPILPTQAA
AAEERENAVV HNSVGFY