Full text data of PCDH1
PCDH1
[Confidence: low (only semi-automatic identification from reviews)]
Protocadherin-1 (Cadherin-like protein 1; Protocadherin-42; PC42; Flags: Precursor)
Protocadherin-1 (Cadherin-like protein 1; Protocadherin-42; PC42; Flags: Precursor)
UniProt
Q08174
ID PCDH1_HUMAN Reviewed; 1060 AA.
AC Q08174; Q8IUP2;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Protocadherin-1;
DE AltName: Full=Cadherin-like protein 1;
DE AltName: Full=Protocadherin-42;
DE Short=PC42;
DE Flags: Precursor;
GN Name=PCDH1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-1060 (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 980-1060 (ISOFORM 2), AND VARIANT PRO-25.
RC TISSUE=Brain;
RX PubMed=8508762;
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
RT central nervous system.";
RL EMBO J. 12:2249-2256(1993).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-949 AND SER-962, AND
RP 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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-305; ASN-813 AND ASN-818,
RP AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-918; SER-962 AND
RP SER-984, AND MASS 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 be involved in cell-cell interaction processes and
CC in cell adhesion.
CC -!- SUBCELLULAR LOCATION: Cell junction. Cell membrane; Single-pass
CC type I membrane protein (Probable). Note=Found at cell-cell
CC boundaries and probably at cell-matrix boundaries.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q08174-1; Sequence=Displayed;
CC Name=2; Synonyms=PC42-8;
CC IsoId=Q08174-2; Sequence=VSP_000703;
CC Note=Ref.4 (AAA36418) sequence is in conflict in position:
CC 1156:V->M;
CC Name=3;
CC IsoId=Q08174-3; Sequence=VSP_035772;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and neuro-glial
CC cells.
CC -!- DEVELOPMENTAL STAGE: Highest expression in adults.
CC -!- SIMILARITY: Contains 7 cadherin domains.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-23 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36419.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. N-terminal sequence identical to a region of chromosome 8;
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; AC094107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61902.1; -; Genomic_DNA.
DR EMBL; BC035812; AAH35812.1; -; mRNA.
DR EMBL; L11369; AAA36418.1; -; mRNA.
DR EMBL; L11370; AAA36419.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001265542.1; NM_001278613.1.
DR RefSeq; NP_001265544.1; NM_001278615.1.
DR RefSeq; NP_002578.2; NM_002587.4.
DR RefSeq; NP_115796.2; NM_032420.3.
DR UniGene; Hs.79769; -.
DR ProteinModelPortal; Q08174; -.
DR SMR; Q08174; 54-812.
DR IntAct; Q08174; 3.
DR MINT; MINT-1185829; -.
DR PhosphoSite; Q08174; -.
DR DMDM; 215273864; -.
DR PaxDb; Q08174; -.
DR PRIDE; Q08174; -.
DR DNASU; 5097; -.
DR Ensembl; ENST00000287008; ENSP00000287008; ENSG00000156453.
DR Ensembl; ENST00000394536; ENSP00000378043; ENSG00000156453.
DR Ensembl; ENST00000456271; ENSP00000403497; ENSG00000156453.
DR GeneID; 5097; -.
DR KEGG; hsa:5097; -.
DR UCSC; uc003llq.3; human.
DR CTD; 5097; -.
DR GeneCards; GC05M141232; -.
DR HGNC; HGNC:8655; PCDH1.
DR HPA; HPA047720; -.
DR HPA; HPA050538; -.
DR MIM; 603626; gene.
DR neXtProt; NX_Q08174; -.
DR PharmGKB; PA32994; -.
DR eggNOG; NOG118788; -.
DR HOGENOM; HOG000234535; -.
DR HOVERGEN; HBG053523; -.
DR KO; K16498; -.
DR OMA; FPDVGHL; -.
DR OrthoDB; EOG7WMCHN; -.
DR ChiTaRS; PCDH1; human.
DR GeneWiki; PCDH1; -.
DR GenomeRNAi; 5097; -.
DR NextBio; 19664; -.
DR PRO; PR:Q08174; -.
DR ArrayExpress; Q08174; -.
DR Bgee; Q08174; -.
DR CleanEx; HS_PCDH1; -.
DR Genevestigator; Q08174; -.
DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR Gene3D; 2.60.40.60; -; 7.
DR InterPro; IPR002126; Cadherin.
DR InterPro; IPR015919; Cadherin-like.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR013585; Protocadherin.
DR Pfam; PF00028; Cadherin; 6.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF08374; Protocadherin; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell junction;
KW Cell membrane; Complete proteome; Glycoprotein; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 57 Potential.
FT CHAIN 58 1060 Protocadherin-1.
FT /FTId=PRO_0000354078.
FT TOPO_DOM 58 852 Extracellular (Potential).
FT TRANSMEM 853 873 Helical; (Potential).
FT TOPO_DOM 874 1060 Cytoplasmic (Potential).
FT DOMAIN 58 168 Cadherin 1.
FT DOMAIN 169 280 Cadherin 2.
FT DOMAIN 281 387 Cadherin 3.
FT DOMAIN 396 506 Cadherin 4.
FT DOMAIN 507 612 Cadherin 5.
FT DOMAIN 613 715 Cadherin 6.
FT DOMAIN 718 844 Cadherin 7.
FT MOD_RES 918 918 Phosphoserine.
FT MOD_RES 949 949 Phosphoserine.
FT MOD_RES 962 962 Phosphoserine.
FT MOD_RES 984 984 Phosphoserine.
FT CARBOHYD 305 305 N-linked (GlcNAc...).
FT CARBOHYD 403 403 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 618 618 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 662 662 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 813 813 N-linked (GlcNAc...).
FT CARBOHYD 818 818 N-linked (GlcNAc...).
FT VAR_SEQ 207 218 Missing (in isoform 3).
FT /FTId=VSP_035772.
FT VAR_SEQ 1034 1060 VGQPFQLSTPQPLPHPYHGAIWTEVWE -> LPHRRVTFSA
FT TSQAQELQDPSQHSYYDSGLEESETPSSKSSSGPRLGPLAL
FT PEDHYERTTPDGSIGEMEHPENDLRPLPDVAMTGTCTRECS
FT EFGHSDTCWMPGQSSPSRRTKSSALKLSTFVPYQDRGGQEP
FT AGAGSPSPPEDRNTKTAPVRLLPSYSAFSHSSHDSCKDSAT
FT LEEIPLTQTSDFPPAATPASAQTAKREIYL (in
FT isoform 2).
FT /FTId=VSP_000703.
FT VARIANT 15 15 L -> F (in dbSNP:rs12517385).
FT /FTId=VAR_047530.
FT VARIANT 25 25 H -> P (in dbSNP:rs12515587).
FT /FTId=VAR_047531.
FT VARIANT 514 514 A -> T (in dbSNP:rs3822357).
FT /FTId=VAR_047532.
FT CONFLICT 147 147 G -> A (in Ref. 4; AAA36419).
FT CONFLICT 262 262 S -> T (in Ref. 4; AAA36419).
SQ SEQUENCE 1060 AA; 114743 MW; 0F4F24F3EE607D04 CRC64;
MDSGAGGRRC PEAALLILGP PRMEHLRHSP GPGGQRLLLP SMLLALLLLL APSPGHATRV
VYKVPEEQPP NTLIGSLAAD YGFPDVGHLY KLEVGAPYLR VDGKTGDIFT TETSIDREGL
RECQNQLPGD PCILEFEVSI TDLVQNGSPR LLEGQIEVQD INDNTPNFAS PVITLAIPEN
TNIGSLFPIP LASDRDAGPN GVASYELQAG PEAQELFGLQ VAEDQEEKQP QLIVMGNLDR
ERWDSYDLTI KVQDGGSPPR ASSALLRVTV LDTNDNAPKF ERPSYEAELS ENSPIGHSVI
QVKANDSDQG ANAEIEYTFH QAPEVVRRLL RLDRNTGLIT VQGPVDREDL STLRFSVLAK
DRGTNPKSAR AQVVVTVKDM NDNAPTIEIR GIGLVTHQDG MANISEDVAE ETAVALVQVS
DRDEGENAAV TCVVAGDVPF QLRQASETGS DSKKKYFLQT TTPLDYEKVK DYTIEIVAVD
SGNPPLSSTN SLKVQVVDVN DNAPVFTQSV TEVAFPENNK PGEVIAEITA SDADSGSNAE
LVYSLEPEPA AKGLFTISPE TGEIQVKTSL DREQRESYEL KVVAADRGSP SLQGTATVLV
NVLDCNDNDP KFMLSGYNFS VMENMPALSP VGMVTVIDGD KGENAQVQLS VEQDNGDFVI
QNGTGTILSS LSFDREQQST YTFQLKAVDG GVPPRSAYVG VTINVLDEND NAPYITAPSN
TSHKLLTPQT RLGETVSQVA AEDFDSGVNA ELIYSIAGGN PYGLFQIGSH SGAITLEKEI
ERRHHGLHRL VVKVSDRGKP PRYGTALVHL YVNETLANRT LLETLLGHSL DTPLDIDIAG
DPEYERSKQR GNILFGVVAG VVAVALLIAL AVLVRYCRQR EAKSGYQAGK KETKDLYAPK
PSGKASKGNK SKGKKSKSPK PVKPVEDEDE AGLQKSLKFN LMSDAPGDSP RIHLPLNYPP
GSPDLGRHYR SNSPLPSIQL QPQSPSASKK HQVVQDLPPA NTFVGTGDTT STGSEQYSDY
SYRTNPPKYP SKQVGQPFQL STPQPLPHPY HGAIWTEVWE
//
ID PCDH1_HUMAN Reviewed; 1060 AA.
AC Q08174; Q8IUP2;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 25-NOV-2008, sequence version 2.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=Protocadherin-1;
DE AltName: Full=Cadherin-like protein 1;
DE AltName: Full=Protocadherin-42;
DE Short=PC42;
DE Flags: Precursor;
GN Name=PCDH1;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-1060 (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 980-1060 (ISOFORM 2), AND VARIANT PRO-25.
RC TISSUE=Brain;
RX PubMed=8508762;
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
RT central nervous system.";
RL EMBO J. 12:2249-2256(1993).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-949 AND SER-962, AND
RP 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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-305; ASN-813 AND ASN-818,
RP AND MASS SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of
RT multiple enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-918; SER-962 AND
RP SER-984, AND MASS 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 be involved in cell-cell interaction processes and
CC in cell adhesion.
CC -!- SUBCELLULAR LOCATION: Cell junction. Cell membrane; Single-pass
CC type I membrane protein (Probable). Note=Found at cell-cell
CC boundaries and probably at cell-matrix boundaries.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q08174-1; Sequence=Displayed;
CC Name=2; Synonyms=PC42-8;
CC IsoId=Q08174-2; Sequence=VSP_000703;
CC Note=Ref.4 (AAA36418) sequence is in conflict in position:
CC 1156:V->M;
CC Name=3;
CC IsoId=Q08174-3; Sequence=VSP_035772;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Highly expressed in the brain and neuro-glial
CC cells.
CC -!- DEVELOPMENTAL STAGE: Highest expression in adults.
CC -!- SIMILARITY: Contains 7 cadherin domains.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-23 is the initiator.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36419.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. N-terminal sequence identical to a region of chromosome 8;
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; AC094107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61902.1; -; Genomic_DNA.
DR EMBL; BC035812; AAH35812.1; -; mRNA.
DR EMBL; L11369; AAA36418.1; -; mRNA.
DR EMBL; L11370; AAA36419.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001265542.1; NM_001278613.1.
DR RefSeq; NP_001265544.1; NM_001278615.1.
DR RefSeq; NP_002578.2; NM_002587.4.
DR RefSeq; NP_115796.2; NM_032420.3.
DR UniGene; Hs.79769; -.
DR ProteinModelPortal; Q08174; -.
DR SMR; Q08174; 54-812.
DR IntAct; Q08174; 3.
DR MINT; MINT-1185829; -.
DR PhosphoSite; Q08174; -.
DR DMDM; 215273864; -.
DR PaxDb; Q08174; -.
DR PRIDE; Q08174; -.
DR DNASU; 5097; -.
DR Ensembl; ENST00000287008; ENSP00000287008; ENSG00000156453.
DR Ensembl; ENST00000394536; ENSP00000378043; ENSG00000156453.
DR Ensembl; ENST00000456271; ENSP00000403497; ENSG00000156453.
DR GeneID; 5097; -.
DR KEGG; hsa:5097; -.
DR UCSC; uc003llq.3; human.
DR CTD; 5097; -.
DR GeneCards; GC05M141232; -.
DR HGNC; HGNC:8655; PCDH1.
DR HPA; HPA047720; -.
DR HPA; HPA050538; -.
DR MIM; 603626; gene.
DR neXtProt; NX_Q08174; -.
DR PharmGKB; PA32994; -.
DR eggNOG; NOG118788; -.
DR HOGENOM; HOG000234535; -.
DR HOVERGEN; HBG053523; -.
DR KO; K16498; -.
DR OMA; FPDVGHL; -.
DR OrthoDB; EOG7WMCHN; -.
DR ChiTaRS; PCDH1; human.
DR GeneWiki; PCDH1; -.
DR GenomeRNAi; 5097; -.
DR NextBio; 19664; -.
DR PRO; PR:Q08174; -.
DR ArrayExpress; Q08174; -.
DR Bgee; Q08174; -.
DR CleanEx; HS_PCDH1; -.
DR Genevestigator; Q08174; -.
DR GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR Gene3D; 2.60.40.60; -; 7.
DR InterPro; IPR002126; Cadherin.
DR InterPro; IPR015919; Cadherin-like.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR InterPro; IPR013585; Protocadherin.
DR Pfam; PF00028; Cadherin; 6.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF08374; Protocadherin; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 7.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell adhesion; Cell junction;
KW Cell membrane; Complete proteome; Glycoprotein; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1 57 Potential.
FT CHAIN 58 1060 Protocadherin-1.
FT /FTId=PRO_0000354078.
FT TOPO_DOM 58 852 Extracellular (Potential).
FT TRANSMEM 853 873 Helical; (Potential).
FT TOPO_DOM 874 1060 Cytoplasmic (Potential).
FT DOMAIN 58 168 Cadherin 1.
FT DOMAIN 169 280 Cadherin 2.
FT DOMAIN 281 387 Cadherin 3.
FT DOMAIN 396 506 Cadherin 4.
FT DOMAIN 507 612 Cadherin 5.
FT DOMAIN 613 715 Cadherin 6.
FT DOMAIN 718 844 Cadherin 7.
FT MOD_RES 918 918 Phosphoserine.
FT MOD_RES 949 949 Phosphoserine.
FT MOD_RES 962 962 Phosphoserine.
FT MOD_RES 984 984 Phosphoserine.
FT CARBOHYD 305 305 N-linked (GlcNAc...).
FT CARBOHYD 403 403 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 618 618 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 662 662 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 813 813 N-linked (GlcNAc...).
FT CARBOHYD 818 818 N-linked (GlcNAc...).
FT VAR_SEQ 207 218 Missing (in isoform 3).
FT /FTId=VSP_035772.
FT VAR_SEQ 1034 1060 VGQPFQLSTPQPLPHPYHGAIWTEVWE -> LPHRRVTFSA
FT TSQAQELQDPSQHSYYDSGLEESETPSSKSSSGPRLGPLAL
FT PEDHYERTTPDGSIGEMEHPENDLRPLPDVAMTGTCTRECS
FT EFGHSDTCWMPGQSSPSRRTKSSALKLSTFVPYQDRGGQEP
FT AGAGSPSPPEDRNTKTAPVRLLPSYSAFSHSSHDSCKDSAT
FT LEEIPLTQTSDFPPAATPASAQTAKREIYL (in
FT isoform 2).
FT /FTId=VSP_000703.
FT VARIANT 15 15 L -> F (in dbSNP:rs12517385).
FT /FTId=VAR_047530.
FT VARIANT 25 25 H -> P (in dbSNP:rs12515587).
FT /FTId=VAR_047531.
FT VARIANT 514 514 A -> T (in dbSNP:rs3822357).
FT /FTId=VAR_047532.
FT CONFLICT 147 147 G -> A (in Ref. 4; AAA36419).
FT CONFLICT 262 262 S -> T (in Ref. 4; AAA36419).
SQ SEQUENCE 1060 AA; 114743 MW; 0F4F24F3EE607D04 CRC64;
MDSGAGGRRC PEAALLILGP PRMEHLRHSP GPGGQRLLLP SMLLALLLLL APSPGHATRV
VYKVPEEQPP NTLIGSLAAD YGFPDVGHLY KLEVGAPYLR VDGKTGDIFT TETSIDREGL
RECQNQLPGD PCILEFEVSI TDLVQNGSPR LLEGQIEVQD INDNTPNFAS PVITLAIPEN
TNIGSLFPIP LASDRDAGPN GVASYELQAG PEAQELFGLQ VAEDQEEKQP QLIVMGNLDR
ERWDSYDLTI KVQDGGSPPR ASSALLRVTV LDTNDNAPKF ERPSYEAELS ENSPIGHSVI
QVKANDSDQG ANAEIEYTFH QAPEVVRRLL RLDRNTGLIT VQGPVDREDL STLRFSVLAK
DRGTNPKSAR AQVVVTVKDM NDNAPTIEIR GIGLVTHQDG MANISEDVAE ETAVALVQVS
DRDEGENAAV TCVVAGDVPF QLRQASETGS DSKKKYFLQT TTPLDYEKVK DYTIEIVAVD
SGNPPLSSTN SLKVQVVDVN DNAPVFTQSV TEVAFPENNK PGEVIAEITA SDADSGSNAE
LVYSLEPEPA AKGLFTISPE TGEIQVKTSL DREQRESYEL KVVAADRGSP SLQGTATVLV
NVLDCNDNDP KFMLSGYNFS VMENMPALSP VGMVTVIDGD KGENAQVQLS VEQDNGDFVI
QNGTGTILSS LSFDREQQST YTFQLKAVDG GVPPRSAYVG VTINVLDEND NAPYITAPSN
TSHKLLTPQT RLGETVSQVA AEDFDSGVNA ELIYSIAGGN PYGLFQIGSH SGAITLEKEI
ERRHHGLHRL VVKVSDRGKP PRYGTALVHL YVNETLANRT LLETLLGHSL DTPLDIDIAG
DPEYERSKQR GNILFGVVAG VVAVALLIAL AVLVRYCRQR EAKSGYQAGK KETKDLYAPK
PSGKASKGNK SKGKKSKSPK PVKPVEDEDE AGLQKSLKFN LMSDAPGDSP RIHLPLNYPP
GSPDLGRHYR SNSPLPSIQL QPQSPSASKK HQVVQDLPPA NTFVGTGDTT STGSEQYSDY
SYRTNPPKYP SKQVGQPFQL STPQPLPHPY HGAIWTEVWE
//
MIM
603626
*RECORD*
*FIELD* NO
603626
*FIELD* TI
*603626 PROTOCADHERIN 1; PCDH1
;;PC42
*FIELD* TX
CLONING
Cadherins are a group of integral membrane proteins that mediate
read morecalcium-dependent cell-cell adhesion. See 601120. By PCR of rat, mouse,
and human neural cell cDNA with degenerate primers based on conserved
regions of the cadherin extracellular domain, Sano et al. (1993)
isolated partial cDNAs encoding pc42 and pc43 (PCDH2; 603627). They used
the partial cDNAs to screen a human brain library and recovered cDNAs
corresponding to the entire coding sequence of both genes. Like typical
cadherins, both pc42 and pc43 contain an N-terminal extracellular
domain, a transmembrane domain, and a C-terminal cytoplasmic region. The
extracellular domains of pc42 and pc43 contain 7 and 6 repeats,
respectively, of a subdomain that is very similar to those of cadherins,
but with characteristic properties. The cytoplasmic domains of pc42 and
pc43 share no homology with those of cadherins. The authors isolated
partial cDNAs encoding proteins with the protocadherin repeats from
Xenopus, Drosophila, and C. elegans. Since pc42 and pc43 are more
closely related to one another than to classic cadherins, and because of
the existence of similar proteins in distantly related organisms, Sano
et al. (1993) suggested the name 'protocadherins' for this family of
proteins.
Sano et al. (1993) reported that pc42 migrated at 170 kD on Western
blots of extracts of mammalian cells expressing the protein.
Immunofluorescence microscopy localized pc42 to the periphery of cells,
primarily in cell-cell contact sites. Cells expressing pc42 showed cell
aggregation activity.
MAPPING
By analysis of somatic cell hybrids, Del Mastro et al. (1995) mapped the
pc42 gene to 5q32-q33. Sago et al. (1995) noted that the mouse Pcdh1,
Pcdh2, and Pcdh3 genes form a cluster on chromosome 18.
*FIELD* RF
1. Del Mastro, R. G.; Wang, L.; Simmons, A. D.; Gallardo, T. D.; Clines,
G. A.; Ashley, J. A.; Hilliard, C. J.; Wasmuth, J. J.; McPherson,
J. D.; Lovett, M.: Human chromosome-specific cDNA libraries: new
tools for gene identification and genome annotation. Genome Res. 5:
185-194, 1995.
2. Sago, H.; Kitagawa, M.; Obata, S.; Mori, N.; Taketani, S.; Rochelle,
J. M.; Seldin, M. F.; Davidson, M.; St. John, T.; Suzuki, S. T.:
Cloning, expression, and chromosomal localization of a novel cadherin-related
protein, protocadherin-3. Genomics 29: 631-640, 1995.
3. Sano, K.; Tanihara, H.; Heimark, R. L.; Obata, S.; Davidson, M.;
St. John, T.; Taketani, S.; Suzuki, S.: Protocadherins: a large family
of cadherin-related molecules in central nervous system. EMBO J. 12:
2249-2256, 1993.
*FIELD* CD
Rebekah S. Rasooly: 3/10/1999
*FIELD* ED
alopez: 04/09/2012
alopez: 3/10/1999
*RECORD*
*FIELD* NO
603626
*FIELD* TI
*603626 PROTOCADHERIN 1; PCDH1
;;PC42
*FIELD* TX
CLONING
Cadherins are a group of integral membrane proteins that mediate
read morecalcium-dependent cell-cell adhesion. See 601120. By PCR of rat, mouse,
and human neural cell cDNA with degenerate primers based on conserved
regions of the cadherin extracellular domain, Sano et al. (1993)
isolated partial cDNAs encoding pc42 and pc43 (PCDH2; 603627). They used
the partial cDNAs to screen a human brain library and recovered cDNAs
corresponding to the entire coding sequence of both genes. Like typical
cadherins, both pc42 and pc43 contain an N-terminal extracellular
domain, a transmembrane domain, and a C-terminal cytoplasmic region. The
extracellular domains of pc42 and pc43 contain 7 and 6 repeats,
respectively, of a subdomain that is very similar to those of cadherins,
but with characteristic properties. The cytoplasmic domains of pc42 and
pc43 share no homology with those of cadherins. The authors isolated
partial cDNAs encoding proteins with the protocadherin repeats from
Xenopus, Drosophila, and C. elegans. Since pc42 and pc43 are more
closely related to one another than to classic cadherins, and because of
the existence of similar proteins in distantly related organisms, Sano
et al. (1993) suggested the name 'protocadherins' for this family of
proteins.
Sano et al. (1993) reported that pc42 migrated at 170 kD on Western
blots of extracts of mammalian cells expressing the protein.
Immunofluorescence microscopy localized pc42 to the periphery of cells,
primarily in cell-cell contact sites. Cells expressing pc42 showed cell
aggregation activity.
MAPPING
By analysis of somatic cell hybrids, Del Mastro et al. (1995) mapped the
pc42 gene to 5q32-q33. Sago et al. (1995) noted that the mouse Pcdh1,
Pcdh2, and Pcdh3 genes form a cluster on chromosome 18.
*FIELD* RF
1. Del Mastro, R. G.; Wang, L.; Simmons, A. D.; Gallardo, T. D.; Clines,
G. A.; Ashley, J. A.; Hilliard, C. J.; Wasmuth, J. J.; McPherson,
J. D.; Lovett, M.: Human chromosome-specific cDNA libraries: new
tools for gene identification and genome annotation. Genome Res. 5:
185-194, 1995.
2. Sago, H.; Kitagawa, M.; Obata, S.; Mori, N.; Taketani, S.; Rochelle,
J. M.; Seldin, M. F.; Davidson, M.; St. John, T.; Suzuki, S. T.:
Cloning, expression, and chromosomal localization of a novel cadherin-related
protein, protocadherin-3. Genomics 29: 631-640, 1995.
3. Sano, K.; Tanihara, H.; Heimark, R. L.; Obata, S.; Davidson, M.;
St. John, T.; Taketani, S.; Suzuki, S.: Protocadherins: a large family
of cadherin-related molecules in central nervous system. EMBO J. 12:
2249-2256, 1993.
*FIELD* CD
Rebekah S. Rasooly: 3/10/1999
*FIELD* ED
alopez: 04/09/2012
alopez: 3/10/1999