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   13-FEB-2019, entry version 167.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 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.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-989, AND IDENTIFICATION
RP   BY 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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-989, AND IDENTIFICATION
RP   BY 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
RT   protocadherin 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
CC       at 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   CCDS; CCDS75116.1; -. [O60245-2]
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   UniGene; Hs.479439; -.
DR   PDB; 2YST; NMR; -; A=302-413.
DR   PDBsum; 2YST; -.
DR   ProteinModelPortal; O60245; -.
DR   SMR; O60245; -.
DR   BioGrid; 111132; 45.
DR   IntAct; O60245; 15.
DR   STRING; 9606.ENSP00000441802; -.
DR   iPTMnet; O60245; -.
DR   PhosphoSitePlus; O60245; -.
DR   SwissPalm; O60245; -.
DR   BioMuta; PCDH7; -.
DR   EPD; O60245; -.
DR   jPOST; O60245; -.
DR   MaxQB; O60245; -.
DR   PaxDb; O60245; -.
DR   PeptideAtlas; O60245; -.
DR   PRIDE; O60245; -.
DR   ProteomicsDB; 49279; -.
DR   ProteomicsDB; 49280; -. [O60245-2]
DR   Ensembl; ENST00000361762; ENSP00000355243; ENSG00000169851. [O60245-1]
DR   Ensembl; ENST00000543491; ENSP00000441802; ENSG00000169851. [O60245-2]
DR   GeneID; 5099; -.
DR   KEGG; hsa:5099; -.
DR   UCSC; uc003gsk.2; human. [O60245-1]
DR   CTD; 5099; -.
DR   DisGeNET; 5099; -.
DR   EuPathDB; HostDB:ENSG00000169851.15; -.
DR   GeneCards; PCDH7; -.
DR   H-InvDB; HIX0024543; -.
DR   HGNC; HGNC:8659; PCDH7.
DR   HPA; HPA011866; -.
DR   HPA; HPA046521; -.
DR   MIM; 602988; gene.
DR   neXtProt; NX_O60245; -.
DR   OpenTargets; ENSG00000169851; -.
DR   PharmGKB; PA33006; -.
DR   eggNOG; ENOG410II7Q; Eukaryota.
DR   eggNOG; ENOG410XPHP; LUCA.
DR   GeneTree; ENSGT00940000157221; -.
DR   HOGENOM; HOG000234535; -.
DR   HOVERGEN; HBG053523; -.
DR   InParanoid; O60245; -.
DR   KO; K16498; -.
DR   OMA; LHPYITV; -.
DR   OrthoDB; 97260at2759; -.
DR   PhylomeDB; O60245; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   ChiTaRS; PCDH7; human.
DR   EvolutionaryTrace; O60245; -.
DR   GeneWiki; PCDH7; -.
DR   GenomeRNAi; 5099; -.
DR   PRO; PR:O60245; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000169851; Expressed in 204 organ(s), highest expression level in primary visual cortex.
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   GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
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;
KW   Cell membrane; Complete proteome; Glycoprotein; Membrane;
KW   Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   CHAIN        29   1069       Protocadherin-7.
FT                                /FTId=PRO_0000003992.
FT   TOPO_DOM     29    879       Extracellular. {ECO:0000255}.
FT   TRANSMEM    880    900       Helical. {ECO:0000255}.
FT   TOPO_DOM    901   1069       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       29    143       Cadherin 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      144    308       Cadherin 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      309    415       Cadherin 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      424    535       Cadherin 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      536    639       Cadherin 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      640    742       Cadherin 6. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   DOMAIN      745    862       Cadherin 7. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00043}.
FT   MOD_RES     989    989       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES    1011   1011       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   CARBOHYD     79     79       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    689    689       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    747    747       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    780    780       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    822    822       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    840    840       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    845    845       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ    1059   1069       MRLHPYITVFG -> VRCIPNIFKYPREG (in isoform
FT                                B). {ECO:0000303|PubMed:9615233}.
FT                                /FTId=VSP_000704.
FT   CONFLICT     25     25       L -> F (in Ref. 1; BAA25194/BAA25195/
FT                                BAA25196). {ECO:0000305}.
FT   CONFLICT    518    518       N -> K (in Ref. 1; BAA25194/BAA25195/
FT                                BAA25196). {ECO:0000305}.
FT   CONFLICT    834    834       L -> V (in Ref. 1; BAA25194/BAA25195/
FT                                BAA25196). {ECO:0000305}.
FT   STRAND      309    318       {ECO:0000244|PDB:2YST}.
FT   STRAND      326    329       {ECO:0000244|PDB:2YST}.
FT   STRAND      335    338       {ECO:0000244|PDB:2YST}.
FT   HELIX       354    357       {ECO:0000244|PDB:2YST}.
FT   STRAND      358    360       {ECO:0000244|PDB:2YST}.
FT   TURN        362    364       {ECO:0000244|PDB:2YST}.
FT   STRAND      366    369       {ECO:0000244|PDB:2YST}.
FT   TURN        375    377       {ECO:0000244|PDB:2YST}.
FT   STRAND      379    387       {ECO:0000244|PDB:2YST}.
FT   TURN        391    394       {ECO:0000244|PDB:2YST}.
FT   STRAND      397    406       {ECO:0000244|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
//