PCDGK_HUMAN
ID PCDGK_HUMAN Reviewed; 934 AA.
AC Q9UN70; O60622; Q08192; Q9Y5C4;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Protocadherin gamma-C3;
DE Short=PCDH-gamma-C3;
DE AltName: Full=Protocadherin-2;
DE AltName: Full=Protocadherin-43;
DE Short=PC-43;
DE Flags: Precursor;
GN Name=PCDHGC3; Synonyms=PCDH2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8508762; DOI=10.1002/j.1460-2075.1993.tb05878.x;
RA Sano K., Tanihara H., Heimark R.L., Obata S., Davidson M., St John T.,
RA Taketani S., Suzuki S.;
RT "Protocadherins: a large family of cadherin-related molecules in central
RT nervous system.";
RL EMBO J. 12:2249-2256(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RX PubMed=9360932; DOI=10.1126/science.278.5341.1315;
RA Lynch E.D., Lee M.K., Morrow J.E., Welcsh P.L., Leon P.E., King M.-C.;
RT "Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of
RT the Drosophila gene diaphanous.";
RL Science 278:1315-1318(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=10380929; DOI=10.1016/s0092-8674(00)80789-8;
RA Wu Q., Maniatis T.;
RT "A striking organization of a large family of human neural cadherin-like
RT cell adhesion genes.";
RL Cell 97:779-790(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UN70-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=Q9UN70-2; Sequence=VSP_008698, VSP_008699;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36421.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. The C-terminus matches chromosome 8 region.; Evidence={ECO:0000305};
CC Sequence=AAA75391.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 2]:
CC Sequence=AAA36420.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L11371; AAA36420.1; ALT_FRAME; mRNA.
DR EMBL; L11372; AAA36421.1; ALT_SEQ; mRNA.
DR EMBL; L11373; AAA75391.1; ALT_FRAME; mRNA.
DR EMBL; AF052685; AAC08350.1; -; Genomic_DNA.
DR EMBL; AF052683; AAC08350.1; JOINED; Genomic_DNA.
DR EMBL; AF052684; AAC08350.1; JOINED; Genomic_DNA.
DR EMBL; AF152337; AAD43731.1; -; mRNA.
DR EMBL; AF152524; AAD43784.1; -; mRNA.
DR EMBL; BC019299; AAH19299.1; -; mRNA.
DR EMBL; BC026218; AAH26218.1; -; mRNA.
DR CCDS; CCDS4261.1; -. [Q9UN70-1]
DR CCDS; CCDS75348.1; -. [Q9UN70-2]
DR RefSeq; NP_002579.2; NM_002588.3. [Q9UN70-1]
DR RefSeq; NP_115778.1; NM_032402.1. [Q9UN70-2]
DR AlphaFoldDB; Q9UN70; -.
DR SMR; Q9UN70; -.
DR BioGRID; 111131; 52.
DR IntAct; Q9UN70; 36.
DR STRING; 9606.ENSP00000312070; -.
DR GlyGen; Q9UN70; 7 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UN70; -.
DR PhosphoSitePlus; Q9UN70; -.
DR BioMuta; PCDHGC3; -.
DR DMDM; 37999813; -.
DR EPD; Q9UN70; -.
DR jPOST; Q9UN70; -.
DR MassIVE; Q9UN70; -.
DR MaxQB; Q9UN70; -.
DR PaxDb; Q9UN70; -.
DR PeptideAtlas; Q9UN70; -.
DR PRIDE; Q9UN70; -.
DR ProteomicsDB; 85253; -. [Q9UN70-1]
DR ProteomicsDB; 85254; -. [Q9UN70-2]
DR ABCD; Q9UN70; 1 sequenced antibody.
DR Antibodypedia; 35055; 334 antibodies from 29 providers.
DR DNASU; 5098; -.
DR Ensembl; ENST00000308177.5; ENSP00000312070.3; ENSG00000240184.7. [Q9UN70-1]
DR Ensembl; ENST00000611950.1; ENSP00000481219.1; ENSG00000240184.7. [Q9UN70-2]
DR GeneID; 5098; -.
DR KEGG; hsa:5098; -.
DR MANE-Select; ENST00000308177.5; ENSP00000312070.3; NM_002588.4; NP_002579.2.
DR UCSC; uc003lku.2; human. [Q9UN70-1]
DR CTD; 5098; -.
DR DisGeNET; 5098; -.
DR GeneCards; PCDHGC3; -.
DR HGNC; HGNC:8716; PCDHGC3.
DR HPA; ENSG00000240184; Tissue enhanced (brain).
DR MIM; 603627; gene.
DR MIM; 604968; gene.
DR neXtProt; NX_Q9UN70; -.
DR OpenTargets; ENSG00000240184; -.
DR PharmGKB; PA33064; -.
DR VEuPathDB; HostDB:ENSG00000240184; -.
DR eggNOG; KOG3594; Eukaryota.
DR GeneTree; ENSGT00940000164266; -.
DR HOGENOM; CLU_006480_3_0_1; -.
DR InParanoid; Q9UN70; -.
DR OMA; PEGTHCK; -.
DR PhylomeDB; Q9UN70; -.
DR TreeFam; TF332299; -.
DR PathwayCommons; Q9UN70; -.
DR SignaLink; Q9UN70; -.
DR SIGNOR; Q9UN70; -.
DR BioGRID-ORCS; 5098; 20 hits in 1022 CRISPR screens.
DR GeneWiki; PCDHGC3; -.
DR GenomeRNAi; 5098; -.
DR Pharos; Q9UN70; Tbio.
DR PRO; PR:Q9UN70; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UN70; protein.
DR Bgee; ENSG00000240184; Expressed in right frontal lobe and 96 other tissues.
DR ExpressionAtlas; Q9UN70; baseline and differential.
DR Genevisible; Q9UN70; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; NAS:UniProtKB.
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:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; IEA:UniProt.
DR GO; GO:0050808; P:synapse organization; IEA:Ensembl.
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; IPR030728; PCDHGC3.
DR PANTHER; PTHR24028:SF70; PTHR24028:SF70; 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 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..934
FT /note="Protocadherin gamma-C3"
FT /id="PRO_0000003985"
FT TOPO_DOM 32..693
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 715..934
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..135
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 136..244
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 245..352
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 353..457
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 458..567
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 572..685
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 804..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..843
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 424
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 615
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 811..863
FT /note="QAPPNTDWRFSQAQRPGTSGSQNGDDTGTWPNNQFDTEMLQAMILASASEAA
FT D -> VRFSKSCLTLLVLFYSYIILRKEWSCFFSDEDVFLVMHSHFQLALPRSKLVPL
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10380929"
FT /id="VSP_008698"
FT VAR_SEQ 864..934
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10380929"
FT /id="VSP_008699"
FT CONFLICT 67
FT /note="R -> P (in Ref. 1; AAA75391)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="V -> L (in Ref. 1; AAA75391)"
FT /evidence="ECO:0000305"
FT CONFLICT 366..367
FT /note="PL -> S (in Ref. 1; AAA75391)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="L -> F (in Ref. 1; AAA75391)"
FT /evidence="ECO:0000305"
FT CONFLICT 768..769
FT /note="RS -> PG (in Ref. 2; AAC08350)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 934 AA; 101077 MW; 1C8E1EADD485AB10 CRC64;
MVPEAWRSGL VSTGRVVGVL LLLGALNKAS TVIHYEIPEE REKGFAVGNV VANLGLDLGS
LSARRFRVVS GASRRFFEVN RETGEMFVND RLDREELCGT LPSCTVTLEL VVENPLELFS
VEVVIQDIND NNPAFPTQEM KLEISEAVAP GTRFPLESAH DPDVGSNSLQ TYELSRNEYF
ALRVQTREDS TKYAELVLER ALDREREPSL QLVLTALDGG TPALSASLPI HIKVLDANDN
APVFNQSLYR ARVLEDAPSG TRVVQVLATD LDEGPNGEII YSFGSHNRAG VRQLFALDLV
TGMLTIKGRL DFEDTKLHEI YIQAKDKGAN PEGAHCKVLV EVVDVNDNAP EITVTSVYSP
VPEDAPLGTV IALLSVTDLD AGENGLVTCE VPPGLPFSLT SSLKNYFTLK TSADLDRETV
PEYNLSITAR DAGTPSLSAL TIVRVQVSDI NDNPPQSSQS SYDVYIEENN LPGAPILNLS
VWDPDAPQNA RLSFFLLEQG AETGLVGRYF TINRDNGIVS SLVPLDYEDR REFELTAHIS
DGGTPVLATN ISVNIFVTDR NDNAPQVLYP RPGGSSVEML PRGTSAGHLV SRVVGWDADA
GHNAWLSYSL LGSPNQSLFA IGLHTGQIST ARPVQDTDSP RQTLTVLIKD NGEPSLSTTA
TLTVSVTEDS PEARAEFPSG SAPREQKKNL TFYLLLSLIL VSVGFVVTVF GVIIFKVYKW
KQSRDLYRAP VSSLYRTPGP SLHADAVRGG LMSPHLYHQV YLTTDSRRSD PLLKKPGAAS
PLASRQNTLR SCDPVFYRQV LGAESAPPGQ QAPPNTDWRF SQAQRPGTSG SQNGDDTGTW
PNNQFDTEML QAMILASASE AADGSSTLGG GAGTMGLSAR YGPQFTLQHV PDYRQNVYIP
GSNATLTNAA GKRDGKAPAG GNGNKKKSGK KEKK
