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Protocadherin-7 (Brain-heart protocadherin) (BH-Pcdh)

 PCDH7_HUMAN             Reviewed;        1069 AA.
O60245; O60246; O60247; Q4W5C4;
05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
28-JUL-2009, sequence version 2.
28-MAR-2018, entry version 160.
RecName: Full=Protocadherin-7;
AltName: Full=Brain-heart protocadherin;
Short=BH-Pcdh;
Flags: Precursor;
Name=PCDH7; Synonyms=BHPCDH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
PubMed=9615233; DOI=10.1006/geno.1998.5271;
Yoshida K., Yoshitomo-Nakagawa K., Seki N., Sasaki M., Sugano S.;
"Cloning, expression analysis, and chromosomal localization of BH-
protocadherin (PCDH7), a novel member of the cadherin superfamily.";
Genomics 49:458-461(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-989 AND SER-1011, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-989, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-989, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[7]
STRUCTURE BY NMR OF 302-413.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the third cadherin domain from human
protocadherin 7.";
Submitted (OCT-2007) to the PDB data bank.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A; Synonyms=BH-Pcdh-a;
IsoId=O60245-1; Sequence=Displayed;
Name=B; Synonyms=BH-Pcdh-b;
IsoId=O60245-2; Sequence=VSP_000704;
-!- TISSUE SPECIFICITY: Expressed predominantly in brain and heart and
at lower levels in various other tissues.
-!- SEQUENCE CAUTION:
Sequence=BAA25196.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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EMBL; AB006755; BAA25194.1; -; mRNA.
EMBL; AB006756; BAA25195.1; -; mRNA.
EMBL; AB006757; BAA25196.1; ALT_SEQ; mRNA.
EMBL; AC097716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC098595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC110766; AAY40944.1; -; Genomic_DNA.
EMBL; AC112239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS33971.1; -. [O60245-1]
CCDS; CCDS75116.1; -. [O60245-2]
PIR; T00041; T00041.
PIR; T00042; T00042.
RefSeq; NP_002580.2; NM_002589.2. [O60245-1]
RefSeq; NP_115832.1; NM_032456.2. [O60245-2]
UniGene; Hs.479439; -.
PDB; 2YST; NMR; -; A=302-413.
PDBsum; 2YST; -.
ProteinModelPortal; O60245; -.
SMR; O60245; -.
BioGrid; 111132; 45.
IntAct; O60245; 15.
STRING; 9606.ENSP00000441802; -.
iPTMnet; O60245; -.
PhosphoSitePlus; O60245; -.
BioMuta; PCDH7; -.
MaxQB; O60245; -.
PaxDb; O60245; -.
PeptideAtlas; O60245; -.
PRIDE; O60245; -.
Ensembl; ENST00000361762; ENSP00000355243; ENSG00000169851. [O60245-1]
Ensembl; ENST00000543491; ENSP00000441802; ENSG00000169851. [O60245-2]
GeneID; 5099; -.
KEGG; hsa:5099; -.
UCSC; uc003gsk.2; human. [O60245-1]
CTD; 5099; -.
DisGeNET; 5099; -.
EuPathDB; HostDB:ENSG00000169851.15; -.
GeneCards; PCDH7; -.
H-InvDB; HIX0024543; -.
HGNC; HGNC:8659; PCDH7.
HPA; HPA011866; -.
HPA; HPA046521; -.
MIM; 602988; gene.
neXtProt; NX_O60245; -.
OpenTargets; ENSG00000169851; -.
PharmGKB; PA33006; -.
eggNOG; ENOG410II7Q; Eukaryota.
eggNOG; ENOG410XPHP; LUCA.
GeneTree; ENSGT00910000143986; -.
HOGENOM; HOG000234535; -.
HOVERGEN; HBG053523; -.
InParanoid; O60245; -.
KO; K16498; -.
OMA; WCLGCCL; -.
OrthoDB; EOG091G011P; -.
PhylomeDB; O60245; -.
Reactome; R-HSA-114608; Platelet degranulation.
ChiTaRS; PCDH7; human.
EvolutionaryTrace; O60245; -.
GeneWiki; PCDH7; -.
GenomeRNAi; 5099; -.
PRO; PR:O60245; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000169851; -.
CleanEx; HS_PCDH7; -.
ExpressionAtlas; O60245; baseline and differential.
Genevisible; O60245; HS.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR013164; Cadherin_N.
InterPro; IPR013585; Protocadherin.
Pfam; PF00028; Cadherin; 6.
Pfam; PF08266; Cadherin_2; 1.
Pfam; PF08374; Protocadherin; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 7.
SUPFAM; SSF49313; SSF49313; 8.
PROSITE; PS00232; CADHERIN_1; 6.
PROSITE; PS50268; CADHERIN_2; 7.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion;
Cell membrane; Complete proteome; Glycoprotein; Membrane;
Phosphoprotein; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 1069 Protocadherin-7.
/FTId=PRO_0000003992.
TOPO_DOM 29 879 Extracellular. {ECO:0000255}.
TRANSMEM 880 900 Helical. {ECO:0000255}.
TOPO_DOM 901 1069 Cytoplasmic. {ECO:0000255}.
DOMAIN 29 143 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 144 308 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 309 415 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 424 535 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 536 639 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 640 742 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 745 862 Cadherin 7. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
MOD_RES 989 989 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1011 1011 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 689 689 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 747 747 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 780 780 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 822 822 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 840 840 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 845 845 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1059 1069 MRLHPYITVFG -> VRCIPNIFKYPREG (in isoform
B). {ECO:0000303|PubMed:9615233}.
/FTId=VSP_000704.
CONFLICT 25 25 L -> F (in Ref. 1; BAA25194/BAA25195/
BAA25196). {ECO:0000305}.
CONFLICT 518 518 N -> K (in Ref. 1; BAA25194/BAA25195/
BAA25196). {ECO:0000305}.
CONFLICT 834 834 L -> V (in Ref. 1; BAA25194/BAA25195/
BAA25196). {ECO:0000305}.
STRAND 309 318 {ECO:0000244|PDB:2YST}.
STRAND 326 329 {ECO:0000244|PDB:2YST}.
STRAND 335 338 {ECO:0000244|PDB:2YST}.
HELIX 354 357 {ECO:0000244|PDB:2YST}.
STRAND 358 360 {ECO:0000244|PDB:2YST}.
TURN 362 364 {ECO:0000244|PDB:2YST}.
STRAND 366 369 {ECO:0000244|PDB:2YST}.
TURN 375 377 {ECO:0000244|PDB:2YST}.
STRAND 379 387 {ECO:0000244|PDB:2YST}.
TURN 391 394 {ECO:0000244|PDB:2YST}.
STRAND 397 406 {ECO:0000244|PDB:2YST}.
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


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