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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
 
 
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