Full text data of PKP3
PKP3
[Confidence: low (only semi-automatic identification from reviews)]
Plakophilin-3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Plakophilin-3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y446
ID PKP3_HUMAN Reviewed; 797 AA.
AC Q9Y446; Q53EX8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Plakophilin-3;
GN Name=PKP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon carcinoma;
RX PubMed=10374265;
RA Schmidt A., Langbein L., Praetzel S., Rode M., Rackwitz H.-R.,
RA Franke W.W.;
RT "Plakophilin 3 -- a novel cell-type-specific desmosomal plaque
RT protein.";
RL Differentiation 64:291-306(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10381383;
RA Bonne S., van Hengel J., Nollet F., Kools P., van Roy F.;
RT "Plakophilin-3, a novel armadillo-like protein present in nuclei and
RT desmosomes of epithelial cells.";
RL J. Cell Sci. 112:2265-2276(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-238; SER-240;
RP SER-313 AND SER-314, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238; SER-313 AND
RP SER-314, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May play a role in junctional plaques.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cell junction, desmosome.
CC Note=Nuclear and associated with desmosomes.
CC -!- TISSUE SPECIFICITY: Found in desmosomes of most simple and
CC stratified epithelia. Not found in foreskin fibroblasts and
CC various sarcoma-derived cell lines. Beside dendritic reticular
CC cells of lymphatic follicles not found in non-epithelial
CC desmosome-bearing tissues.
CC -!- SIMILARITY: Belongs to the beta-catenin family.
CC -!- SIMILARITY: Contains 8 ARM repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Z98265; CAB44310.1; -; mRNA.
DR EMBL; AF053719; AAF23050.1; -; mRNA.
DR EMBL; AK223511; BAD97231.1; -; mRNA.
DR EMBL; BC000081; AAH00081.1; -; mRNA.
DR RefSeq; NP_009114.1; NM_007183.2.
DR UniGene; Hs.534395; -.
DR ProteinModelPortal; Q9Y446; -.
DR SMR; Q9Y446; 318-781.
DR IntAct; Q9Y446; 4.
DR MINT; MINT-3975143; -.
DR STRING; 9606.ENSP00000331678; -.
DR PhosphoSite; Q9Y446; -.
DR DMDM; 20139301; -.
DR PaxDb; Q9Y446; -.
DR PeptideAtlas; Q9Y446; -.
DR PRIDE; Q9Y446; -.
DR DNASU; 11187; -.
DR Ensembl; ENST00000331563; ENSP00000331678; ENSG00000184363.
DR GeneID; 11187; -.
DR KEGG; hsa:11187; -.
DR UCSC; uc001lpc.3; human.
DR CTD; 11187; -.
DR GeneCards; GC11P000394; -.
DR HGNC; HGNC:9025; PKP3.
DR HPA; CAB012993; -.
DR MIM; 605561; gene.
DR neXtProt; NX_Q9Y446; -.
DR PharmGKB; PA33358; -.
DR eggNOG; NOG246597; -.
DR HOGENOM; HOG000115567; -.
DR HOVERGEN; HBG106682; -.
DR InParanoid; Q9Y446; -.
DR OMA; NARNKDE; -.
DR OrthoDB; EOG7RFTGQ; -.
DR PhylomeDB; Q9Y446; -.
DR SignaLink; Q9Y446; -.
DR ChiTaRS; PKP3; human.
DR GeneWiki; PKP3; -.
DR GenomeRNAi; 11187; -.
DR NextBio; 42581; -.
DR PRO; PR:Q9Y446; -.
DR ArrayExpress; Q9Y446; -.
DR Bgee; Q9Y446; -.
DR CleanEx; HS_PKP3; -.
DR Genevestigator; Q9Y446; -.
DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR028434; Plakophilin-3.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR PANTHER; PTHR10372:SF1; PTHR10372:SF1; 1.
DR Pfam; PF00514; Arm; 1.
DR SMART; SM00185; ARM; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Complete proteome; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1 797 Plakophilin-3.
FT /FTId=PRO_0000064287.
FT REPEAT 305 348 ARM 1.
FT REPEAT 351 390 ARM 2.
FT REPEAT 393 432 ARM 3.
FT REPEAT 449 487 ARM 4.
FT REPEAT 491 536 ARM 5.
FT REPEAT 596 637 ARM 6.
FT REPEAT 645 684 ARM 7.
FT REPEAT 689 730 ARM 8.
FT MOD_RES 180 180 Phosphoserine.
FT MOD_RES 238 238 Phosphoserine.
FT MOD_RES 240 240 Phosphoserine.
FT MOD_RES 313 313 Phosphoserine.
FT MOD_RES 314 314 Phosphoserine.
FT CONFLICT 719 719 V -> A (in Ref. 3; BAD97231).
FT CONFLICT 730 730 V -> G (in Ref. 3; BAD97231).
SQ SEQUENCE 797 AA; 87082 MW; D43C7E77FA805E7E CRC64;
MQDGNFLLSA LQPEAGVCSL ALPSDLQLDR RGAEGPEAER LRAARVQEQV RARLLQLGQQ
PRHNGAAEPE PEAETARGTS RGQYHTLQAG FSSRSQGLSG DKTSGFRPIA KPAYSPASWS
SRSAVDLSCS RRLSSAHNGG SAFGAAGYGG AQPTPPMPTR PVSFHERGGV GSRADYDTLS
LRSLRLGPGG LDDRYSLVSE QLEPAATSTY RAFAYERQAS SSSSRAGGLD WPEATEVSPS
RTIRAPAVRT LQRFQSSHRS RGVGGAVPGA VLEPVARAPS VRSLSLSLAD SGHLPDVHGF
NSYGSHRTLQ RLSSGFDDID LPSAVKYLMA SDPNLQVLGA AYIQHKCYSD AAAKKQARSL
QAVPRLVKLF NHANQEVQRH ATGAMRNLIY DNADNKLALV EENGIFELLR TLREQDDELR
KNVTGILWNL SSSDHLKDRL ARDTLEQLTD LVLSPLSGAG GPPLIQQNAS EAEIFYNATG
FLRNLSSASQ ATRQKMRECH GLVDALVTSI NHALDAGKCE DKSVENAVCV LRNLSYRLYD
EMPPSALQRL EGRGRRDLAG APPGEVVGCF TPQSRRLREL PLAADALTFA EVSKDPKGLE
WLWSPQIVGL YNRLLQRCEL NRHTTEAAAG ALQNITAGDR RWAGVLSRLA LEQERILNPL
LDRVRTADHH QLRSLTGLIR NLSRNARNKD EMSTKVVSHL IEKLPGSVGE KSPPAEVLVN
IIAVLNNLVV ASPIAARDLL YFDGLRKLIF IKKKRDSPDS EKSSRAASSL LANLWQYNKL
HRDFRAKGYR KEDFLGP
//
ID PKP3_HUMAN Reviewed; 797 AA.
AC Q9Y446; Q53EX8;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 108.
DE RecName: Full=Plakophilin-3;
GN Name=PKP3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon carcinoma;
RX PubMed=10374265;
RA Schmidt A., Langbein L., Praetzel S., Rode M., Rackwitz H.-R.,
RA Franke W.W.;
RT "Plakophilin 3 -- a novel cell-type-specific desmosomal plaque
RT protein.";
RL Differentiation 64:291-306(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10381383;
RA Bonne S., van Hengel J., Nollet F., Kools P., van Roy F.;
RT "Plakophilin-3, a novel armadillo-like protein present in nuclei and
RT desmosomes of epithelial cells.";
RL J. Cell Sci. 112:2265-2276(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-238; SER-240;
RP SER-313 AND SER-314, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238; SER-313 AND
RP SER-314, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-314, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May play a role in junctional plaques.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cell junction, desmosome.
CC Note=Nuclear and associated with desmosomes.
CC -!- TISSUE SPECIFICITY: Found in desmosomes of most simple and
CC stratified epithelia. Not found in foreskin fibroblasts and
CC various sarcoma-derived cell lines. Beside dendritic reticular
CC cells of lymphatic follicles not found in non-epithelial
CC desmosome-bearing tissues.
CC -!- SIMILARITY: Belongs to the beta-catenin family.
CC -!- SIMILARITY: Contains 8 ARM repeats.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; Z98265; CAB44310.1; -; mRNA.
DR EMBL; AF053719; AAF23050.1; -; mRNA.
DR EMBL; AK223511; BAD97231.1; -; mRNA.
DR EMBL; BC000081; AAH00081.1; -; mRNA.
DR RefSeq; NP_009114.1; NM_007183.2.
DR UniGene; Hs.534395; -.
DR ProteinModelPortal; Q9Y446; -.
DR SMR; Q9Y446; 318-781.
DR IntAct; Q9Y446; 4.
DR MINT; MINT-3975143; -.
DR STRING; 9606.ENSP00000331678; -.
DR PhosphoSite; Q9Y446; -.
DR DMDM; 20139301; -.
DR PaxDb; Q9Y446; -.
DR PeptideAtlas; Q9Y446; -.
DR PRIDE; Q9Y446; -.
DR DNASU; 11187; -.
DR Ensembl; ENST00000331563; ENSP00000331678; ENSG00000184363.
DR GeneID; 11187; -.
DR KEGG; hsa:11187; -.
DR UCSC; uc001lpc.3; human.
DR CTD; 11187; -.
DR GeneCards; GC11P000394; -.
DR HGNC; HGNC:9025; PKP3.
DR HPA; CAB012993; -.
DR MIM; 605561; gene.
DR neXtProt; NX_Q9Y446; -.
DR PharmGKB; PA33358; -.
DR eggNOG; NOG246597; -.
DR HOGENOM; HOG000115567; -.
DR HOVERGEN; HBG106682; -.
DR InParanoid; Q9Y446; -.
DR OMA; NARNKDE; -.
DR OrthoDB; EOG7RFTGQ; -.
DR PhylomeDB; Q9Y446; -.
DR SignaLink; Q9Y446; -.
DR ChiTaRS; PKP3; human.
DR GeneWiki; PKP3; -.
DR GenomeRNAi; 11187; -.
DR NextBio; 42581; -.
DR PRO; PR:Q9Y446; -.
DR ArrayExpress; Q9Y446; -.
DR Bgee; Q9Y446; -.
DR CleanEx; HS_PKP3; -.
DR Genevestigator; Q9Y446; -.
DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR028434; Plakophilin-3.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR PANTHER; PTHR10372:SF1; PTHR10372:SF1; 1.
DR Pfam; PF00514; Arm; 1.
DR SMART; SM00185; ARM; 3.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Complete proteome; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1 797 Plakophilin-3.
FT /FTId=PRO_0000064287.
FT REPEAT 305 348 ARM 1.
FT REPEAT 351 390 ARM 2.
FT REPEAT 393 432 ARM 3.
FT REPEAT 449 487 ARM 4.
FT REPEAT 491 536 ARM 5.
FT REPEAT 596 637 ARM 6.
FT REPEAT 645 684 ARM 7.
FT REPEAT 689 730 ARM 8.
FT MOD_RES 180 180 Phosphoserine.
FT MOD_RES 238 238 Phosphoserine.
FT MOD_RES 240 240 Phosphoserine.
FT MOD_RES 313 313 Phosphoserine.
FT MOD_RES 314 314 Phosphoserine.
FT CONFLICT 719 719 V -> A (in Ref. 3; BAD97231).
FT CONFLICT 730 730 V -> G (in Ref. 3; BAD97231).
SQ SEQUENCE 797 AA; 87082 MW; D43C7E77FA805E7E CRC64;
MQDGNFLLSA LQPEAGVCSL ALPSDLQLDR RGAEGPEAER LRAARVQEQV RARLLQLGQQ
PRHNGAAEPE PEAETARGTS RGQYHTLQAG FSSRSQGLSG DKTSGFRPIA KPAYSPASWS
SRSAVDLSCS RRLSSAHNGG SAFGAAGYGG AQPTPPMPTR PVSFHERGGV GSRADYDTLS
LRSLRLGPGG LDDRYSLVSE QLEPAATSTY RAFAYERQAS SSSSRAGGLD WPEATEVSPS
RTIRAPAVRT LQRFQSSHRS RGVGGAVPGA VLEPVARAPS VRSLSLSLAD SGHLPDVHGF
NSYGSHRTLQ RLSSGFDDID LPSAVKYLMA SDPNLQVLGA AYIQHKCYSD AAAKKQARSL
QAVPRLVKLF NHANQEVQRH ATGAMRNLIY DNADNKLALV EENGIFELLR TLREQDDELR
KNVTGILWNL SSSDHLKDRL ARDTLEQLTD LVLSPLSGAG GPPLIQQNAS EAEIFYNATG
FLRNLSSASQ ATRQKMRECH GLVDALVTSI NHALDAGKCE DKSVENAVCV LRNLSYRLYD
EMPPSALQRL EGRGRRDLAG APPGEVVGCF TPQSRRLREL PLAADALTFA EVSKDPKGLE
WLWSPQIVGL YNRLLQRCEL NRHTTEAAAG ALQNITAGDR RWAGVLSRLA LEQERILNPL
LDRVRTADHH QLRSLTGLIR NLSRNARNKD EMSTKVVSHL IEKLPGSVGE KSPPAEVLVN
IIAVLNNLVV ASPIAARDLL YFDGLRKLIF IKKKRDSPDS EKSSRAASSL LANLWQYNKL
HRDFRAKGYR KEDFLGP
//
MIM
605561
*RECORD*
*FIELD* NO
605561
*FIELD* TI
*605561 PLAKOPHILIN 3; PKP3
*FIELD* TX
DESCRIPTION
Desmosomal plaque proteins are members of the 'armadillo-repeat'
read moremultigene family and have important functions in cytoskeleton/cell
membrane interactions. For additional general information on desmosomal
proteins, see 601975 and 125647.
CLONING
Using recombinant DNA and immunologic techniques, Schmidt et al. (1999)
identified a novel desmosomal plaque protein, which they called
plakophilin-3 (PKP3). A PKP3 cDNA, cloned from a size-selected cDNA
library from a CaCo-2 cell line, encodes a deduced 797-amino acid
protein with a calculated molecular mass of 87.081 kD. PKP3 shows
homology to the other known plakophilins, PKP1 (601975) and PKP2
(602861). Each contains a basic 'head' domain showing relatively great
sequence diversity, except for a markedly conserved portion near the N
terminus, followed by at least 9 'arm-repeat' units in which homology
reaches about 70%, compared to an overall homology of about 35% between
PKP3 and the other 2 plakophilins. Northern blot analysis detected an
approximately 2.9-kb PKP3 transcript in cells of stratified and
single-layered epithelia. Immunofluorescence and immunoelectron
microscopy studies localized PKP3 to desmosomes of most simple and
almost all stratified epithelia and cell lines derived therefrom, with
the exception of hepatocytes and hepatocellular carcinoma cells.
MAPPING
By fluorescence in situ hybridization, Schmidt et al. (1999) mapped the
PKP3 gene to chromosome 11p15.
*FIELD* RF
1. Schmidt, A.; Langbein, L.; Pratzel, S.; Rode, M.; Rackwitz, H.-R.;
Franke, W. W.: Plakophilin 3--a novel cell-type-specific desmosomal
plaque protein. Differentiation 64: 291-306, 1999.
*FIELD* CD
Carol A. Bocchini: 1/18/2001
*FIELD* ED
carol: 07/13/2009
mcapotos: 1/18/2001
carol: 1/18/2001
*RECORD*
*FIELD* NO
605561
*FIELD* TI
*605561 PLAKOPHILIN 3; PKP3
*FIELD* TX
DESCRIPTION
Desmosomal plaque proteins are members of the 'armadillo-repeat'
read moremultigene family and have important functions in cytoskeleton/cell
membrane interactions. For additional general information on desmosomal
proteins, see 601975 and 125647.
CLONING
Using recombinant DNA and immunologic techniques, Schmidt et al. (1999)
identified a novel desmosomal plaque protein, which they called
plakophilin-3 (PKP3). A PKP3 cDNA, cloned from a size-selected cDNA
library from a CaCo-2 cell line, encodes a deduced 797-amino acid
protein with a calculated molecular mass of 87.081 kD. PKP3 shows
homology to the other known plakophilins, PKP1 (601975) and PKP2
(602861). Each contains a basic 'head' domain showing relatively great
sequence diversity, except for a markedly conserved portion near the N
terminus, followed by at least 9 'arm-repeat' units in which homology
reaches about 70%, compared to an overall homology of about 35% between
PKP3 and the other 2 plakophilins. Northern blot analysis detected an
approximately 2.9-kb PKP3 transcript in cells of stratified and
single-layered epithelia. Immunofluorescence and immunoelectron
microscopy studies localized PKP3 to desmosomes of most simple and
almost all stratified epithelia and cell lines derived therefrom, with
the exception of hepatocytes and hepatocellular carcinoma cells.
MAPPING
By fluorescence in situ hybridization, Schmidt et al. (1999) mapped the
PKP3 gene to chromosome 11p15.
*FIELD* RF
1. Schmidt, A.; Langbein, L.; Pratzel, S.; Rode, M.; Rackwitz, H.-R.;
Franke, W. W.: Plakophilin 3--a novel cell-type-specific desmosomal
plaque protein. Differentiation 64: 291-306, 1999.
*FIELD* CD
Carol A. Bocchini: 1/18/2001
*FIELD* ED
carol: 07/13/2009
mcapotos: 1/18/2001
carol: 1/18/2001