PCDH7_HUMAN
ID PCDH7_HUMAN Reviewed; 1069 AA.
AC O60245; O60246; O60247; Q4W5C4;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Protocadherin-7;
DE AltName: Full=Brain-heart protocadherin;
DE Short=BH-Pcdh;
DE Flags: Precursor;
GN Name=PCDH7; Synonyms=BHPCDH;
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] (ISOFORMS A AND B).
RX PubMed=9615233; DOI=10.1006/geno.1998.5271;
RA Yoshida K., Yoshitomo-Nakagawa K., Seki N., Sasaki M., Sugano S.;
RT "Cloning, expression analysis, and chromosomal localization of BH-
RT protocadherin (PCDH7), a novel member of the cadherin superfamily.";
RL Genomics 49:458-461(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-989 AND SER-1011, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-989, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-989, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [7]
RP STRUCTURE BY NMR OF 302-413.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the third cadherin domain from human protocadherin
RT 7.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=BH-Pcdh-a;
CC IsoId=O60245-1; Sequence=Displayed;
CC Name=B; Synonyms=BH-Pcdh-b;
CC IsoId=O60245-2; Sequence=VSP_000704;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in brain and heart and at
CC lower levels in various other tissues.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25196.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AB006755; BAA25194.1; -; mRNA.
DR EMBL; AB006756; BAA25195.1; -; mRNA.
DR EMBL; AB006757; BAA25196.1; ALT_SEQ; mRNA.
DR EMBL; AC097716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC098595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110766; AAY40944.1; -; Genomic_DNA.
DR EMBL; AC112239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS33971.1; -. [O60245-1]
DR PIR; T00041; T00041.
DR PIR; T00042; T00042.
DR RefSeq; NP_002580.2; NM_002589.2. [O60245-1]
DR RefSeq; NP_115832.1; NM_032456.2. [O60245-2]
DR PDB; 2YST; NMR; -; A=302-413.
DR PDBsum; 2YST; -.
DR AlphaFoldDB; O60245; -.
DR SMR; O60245; -.
DR BioGRID; 111132; 110.
DR IntAct; O60245; 36.
DR MINT; O60245; -.
DR STRING; 9606.ENSP00000441802; -.
DR GlyGen; O60245; 7 sites.
DR iPTMnet; O60245; -.
DR PhosphoSitePlus; O60245; -.
DR SwissPalm; O60245; -.
DR BioMuta; PCDH7; -.
DR EPD; O60245; -.
DR jPOST; O60245; -.
DR MassIVE; O60245; -.
DR MaxQB; O60245; -.
DR PaxDb; O60245; -.
DR PeptideAtlas; O60245; -.
DR PRIDE; O60245; -.
DR ProteomicsDB; 49279; -. [O60245-1]
DR ProteomicsDB; 49280; -. [O60245-2]
DR Antibodypedia; 2149; 371 antibodies from 26 providers.
DR DNASU; 5099; -.
DR Ensembl; ENST00000361762.3; ENSP00000355243.2; ENSG00000169851.15. [O60245-1]
DR Ensembl; ENST00000543491.2; ENSP00000441802.2; ENSG00000169851.15. [O60245-2]
DR GeneID; 5099; -.
DR KEGG; hsa:5099; -.
DR UCSC; uc003gsk.2; human. [O60245-1]
DR CTD; 5099; -.
DR DisGeNET; 5099; -.
DR GeneCards; PCDH7; -.
DR HGNC; HGNC:8659; PCDH7.
DR HPA; ENSG00000169851; Tissue enhanced (brain).
DR MIM; 602988; gene.
DR neXtProt; NX_O60245; -.
DR OpenTargets; ENSG00000169851; -.
DR PharmGKB; PA33006; -.
DR VEuPathDB; HostDB:ENSG00000169851; -.
DR eggNOG; ENOG502QVM0; Eukaryota.
DR GeneTree; ENSGT00940000157221; -.
DR InParanoid; O60245; -.
DR OMA; LAQKHYG; -.
DR OrthoDB; 97260at2759; -.
DR PhylomeDB; O60245; -.
DR PathwayCommons; O60245; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR SignaLink; O60245; -.
DR BioGRID-ORCS; 5099; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; PCDH7; human.
DR EvolutionaryTrace; O60245; -.
DR GeneWiki; PCDH7; -.
DR GenomeRNAi; 5099; -.
DR Pharos; O60245; Tbio.
DR PRO; PR:O60245; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O60245; protein.
DR Bgee; ENSG00000169851; Expressed in endothelial cell and 188 other tissues.
DR ExpressionAtlas; O60245; baseline and differential.
DR Genevisible; O60245; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
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; 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; 7.
DR SUPFAM; SSF49313; SSF49313; 7.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 7.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1069
FT /note="Protocadherin-7"
FT /id="PRO_0000003992"
FT TOPO_DOM 29..879
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 880..900
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 901..1069
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 29..143
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 144..308
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 309..415
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 424..535
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 536..639
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 640..742
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 745..862
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 182..242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 747
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 822
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 840
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 845
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1059..1069
FT /note="MRLHPYITVFG -> VRCIPNIFKYPREG (in isoform B)"
FT /evidence="ECO:0000303|PubMed:9615233"
FT /id="VSP_000704"
FT CONFLICT 25
FT /note="L -> F (in Ref. 1; BAA25194/BAA25195/BAA25196)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="N -> K (in Ref. 1; BAA25194/BAA25195/BAA25196)"
FT /evidence="ECO:0000305"
FT CONFLICT 834
FT /note="L -> V (in Ref. 1; BAA25194/BAA25195/BAA25196)"
FT /evidence="ECO:0000305"
FT STRAND 309..318
FT /evidence="ECO:0007829|PDB:2YST"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:2YST"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:2YST"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:2YST"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2YST"
FT TURN 362..364
FT /evidence="ECO:0007829|PDB:2YST"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:2YST"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:2YST"
FT STRAND 379..387
FT /evidence="ECO:0007829|PDB:2YST"
FT TURN 391..394
FT /evidence="ECO:0007829|PDB:2YST"
FT STRAND 397..406
FT /evidence="ECO:0007829|PDB:2YST"
SQ SEQUENCE 1069 AA; 116071 MW; 6150CAF0599D5DAF CRC64;
MLRMRTAGWA RGWCLGCCLL LPLSLSLAAA KQLLRYRLAE EGPADVRIGN VASDLGIVTG
SGEVTFSLES GSEYLKIDNL TGELSTSERR IDREKLPQCQ MIFDENECFL DFEVSVIGPS
QSWVDLFEGQ VIVLDINDNT PTFPSPVLTL TVEENRPVGT LYLLPTATDR DFGRNGIERY
ELLQEPGGGG SGGESRRAGA ADSAPYPGGG GNGASGGGSG GSKRRLDASE GGGGTNPGGR
SSVFELQVAD TPDGEKQPQL IVKGALDREQ RDSYELTLRV RDGGDPPRSS QAILRVLITD
VNDNSPRFEK SVYEADLAEN SAPGTPILQL RAADLDVGVN GQIEYVFGAA TESVRRLLRL
DETSGWLSVL HRIDREEVNQ LRFTVMARDR GQPPKTDKAT VVLNIKDEND NVPSIEIRKI
GRIPLKDGVA NVAEDVLVDT PIALVQVSDR DQGENGVVTC TVVGDVPFQL KPASDTEGDQ
NKKKYFLHTS TPLDYEATRE FNVVIVAVDS GSPSLSSNNS LIVKVGDTND NPPMFGQSVV
EVYFPENNIP GERVATVLAT DADSGKNAEI AYSLDSSVMG IFAIDPDSGD ILVNTVLDRE
QTDRYEFKVN AKDKGIPVLQ GSTTVIVQVA DKNDNDPKFM QDVFTFYVKE NLQPNSPVGM
VTVMDADKGR NAEMSLYIEE NNNIFSIEND TGTIYSTMSF DREHQTTYTF RVKAVDGGDP
PRSATATVSL FVMDENDNAP TVTLPKNISY TLLPPSSNVR TVVATVLATD SDDGINADLN
YSIVGGNPFK LFEIDPTSGV VSLVGKLTQK HYGLHRLVVQ VNDSGQPSQS TTTLVHVFVN
ESVSNATAID SQIARSLHIP LTQDIAGDPS YEISKQRLSI VIGVVAGIMT VILIILIVVM
ARYCRSKNKN GYEAGKKDHE DFFTPQQHDK SKKPKKDKKN KKSKQPLYSS IVTVEASKPN
GQRYDSVNEK LSDSPSMGRY RSVNGGPGSP DLARHYKSSS PLPTVQLHPQ SPTAGKKHQA
VQDLPPANTF VGAGDNISIG SDHCSEYSCQ TNNKYSKQMR LHPYITVFG
