Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protocadherin-15

 PCD15_MOUSE             Reviewed;        1943 AA.
Q99PJ1; D6RCH0; E9Q7D7; E9Q7R1; E9Q7R2; F6KJX4; F6KKG6; F6R5Z7;
F6RBV2; F6U3Q6; F6UPC9; F6VPR3; F6WUN7; F6X715; F6XPA1; F6Y0A5;
F6YP25; F6YZQ9; F7ASH0; F7CIN1; F7D5J8; F7DFU0; F8VQ61; H3BKS0;
Q0ZM15; Q0ZM16; Q0ZM18; Q0ZM19; Q0ZM20; Q0ZM21; Q0ZM22; Q0ZM23;
Q0ZM24; Q0ZM25; Q0ZM26; Q0ZM27; Q0ZM28; Q0ZM29; Q0ZM30; Q0ZM31;
Q0ZM32; Q0ZM33; Q0ZM34; Q0ZM35; Q0ZM37; Q2VQG7; Q3URZ1; Q3UTS7;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
26-JUN-2013, sequence version 3.
25-OCT-2017, entry version 142.
RecName: Full=Protocadherin-15;
Flags: Precursor;
Name=Pcdh15;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11138007; DOI=10.1038/83837;
Alagramam K.N., Murcia C.L., Kwon H.Y., Pawlowski K.S., Wright C.G.,
Woychik R.P.;
"The mouse Ames waltzer hearing-loss mutant is caused by mutation of
Pcdh15, a novel protocadherin gene.";
Nat. Genet. 27:99-102(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 24), AND TISSUE SPECIFICITY.
TISSUE=Retina;
PubMed=16799054; DOI=10.1167/iovs.06-0108;
Haywood-Watson R.J. II, Ahmed Z.M., Kjellstrom S., Bush R.A.,
Takada Y., Hampton L.L., Battey J.F., Sieving P.A., Friedman T.B.;
"Ames Waltzer deaf mice have reduced electroretinogram amplitudes and
complex alternative splicing of Pcdh15 transcripts.";
Invest. Ophthalmol. Vis. Sci. 47:3074-3084(2006).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8; 9; 10; 11;
12; 13; 14; 15; 16; 17; 18; 19; 20; 21; 22 AND 23), AND DEVELOPMENTAL
STAGE.
STRAIN=C57BL/6J; TISSUE=Inner ear;
PubMed=16807332; DOI=10.1523/JNEUROSCI.1163-06.2006;
Ahmed Z.M., Goodyear R., Riazuddin S., Lagziel A., Legan P.K.,
Behra M., Burgess S.M., Lilley K.S., Wilcox E.R., Riazuddin S.,
Griffith A.J., Frolenkov G.I., Belyantseva I.A., Richardson G.P.,
Friedman T.B.;
"The tip-link antigen, a protein associated with the transduction
complex of sensory hair cells, is protocadherin-15.";
J. Neurosci. 26:7022-7034(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 21), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1763-1943 (ISOFORMS 1/2/4/5/6/7/8/9).
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1368-1943 (ISOFORMS 25 AND 26),
INTERACTION WITH USH1G, AND SUBCELLULAR LOCATION.
STRAIN=SWR/J; TISSUE=Cochlea;
PubMed=21436032; DOI=10.1073/pnas.1017114108;
Caberlotto E., Michel V., Foucher I., Bahloul A., Goodyear R.J.,
Pepermans E., Michalski N., Perfettini I., Alegria-Prevot O.,
Chardenoux S., Do Cruzeiro M., Hardelin J.P., Richardson G.P.,
Avan P., Weil D., Petit C.;
"Usher type 1G protein sans is a critical component of the tip-link
complex, a structure controlling actin polymerization in
stereocilia.";
Proc. Natl. Acad. Sci. U.S.A. 108:5825-5830(2011).
[7]
PROTEIN SEQUENCE OF 1876-1882, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[8]
TISSUE SPECIFICITY.
PubMed=11429292; DOI=10.1016/S0925-4773(01)00388-4;
Murcia C.L., Woychik R.P.;
"Expression of Pcdh15 in the inner ear, nervous system and various
epithelia of the developing embryo.";
Mech. Dev. 105:163-166(2001).
[9]
INTERACTION WITH MYO7A, AND TISSUE SPECIFICITY.
PubMed=16481439; DOI=10.1523/JNEUROSCI.4251-05.2006;
Senften M., Schwander M., Kazmierczak P., Lillo C., Shin J.B.,
Hasson T., Geleoc G.S., Gillespie P.G., Williams D., Holt J.R.,
Muller U.;
"Physical and functional interaction between protocadherin 15 and
myosin VIIa in mechanosensory hair cells.";
J. Neurosci. 26:2060-2071(2006).
[10]
INTERACTION WITH CDH23, AND TISSUE SPECIFICITY.
PubMed=17805295; DOI=10.1038/nature06091;
Kazmierczak P., Sakaguchi H., Tokita J., Wilson-Kubalek E.M.,
Milligan R.A., Muller U., Kachar B.;
"Cadherin 23 and protocadherin 15 interact to form tip-link filaments
in sensory hair cells.";
Nature 449:87-91(2007).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[12]
SUBCELLULAR LOCATION, AND INTERACTION WITH LHFPL5.
PubMed=23217710; DOI=10.1016/j.cell.2012.10.041;
Xiong W., Grillet N., Elledge H.M., Wagner T.F., Zhao B.,
Johnson K.R., Kazmierczak P., Muller U.;
"TMHS is an integral component of the mechanotransduction machinery of
cochlear hair cells.";
Cell 151:1283-1295(2012).
[13]
IDENTIFICATION IN A COMPLEX WITH LHFPL5 AND PCDH15.
PubMed=25467981; DOI=10.1016/j.neuron.2014.10.041;
Zhao B., Wu Z., Grillet N., Yan L., Xiong W., Harkins-Perry S.,
Mueller U.;
"TMIE is an essential component of the mechanotransduction machinery
of cochlear hair cells.";
Neuron 84:954-967(2014).
[14]
INTERACTION WITH TMC1 AND TMC2.
PubMed=25114259; DOI=10.1073/pnas.1402152111;
Maeda R., Kindt K.S., Mo W., Morgan C.P., Erickson T., Zhao H.,
Clemens-Grisham R., Barr-Gillespie P.G., Nicolson T.;
"Tip-link protein protocadherin 15 interacts with transmembrane
channel-like proteins TMC1 and TMC2.";
Proc. Natl. Acad. Sci. U.S.A. 111:12907-12912(2014).
[15]
INTERACTION WITH TOMT.
PubMed=28504928; DOI=10.7554/eLife.24318;
Cunningham C.L., Wu Z., Jafari A., Zhao B., Schrode K.,
Harkins-Perry S., Lauer A., Mueller U.;
"The murine catecholamine methyltransferase mTOMT is essential for
mechanotransduction by cochlear hair cells.";
Elife 6:0-0(2017).
[16]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 27-259 IN COMPLEX WITH
CALCIUM IONS AND CDH23, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF
ILE-48 AND ARG-139.
PubMed=23135401; DOI=10.1038/nature11590;
Sotomayor M., Weihofen W.A., Gaudet R., Corey D.P.;
"Structure of a force-conveying cadherin bond essential for inner-ear
mechanotransduction.";
Nature 492:128-132(2012).
-!- FUNCTION: Calcium-dependent cell-adhesion protein. Required for
inner ear neuroepithelial cell elaboration and cochlear function.
Probably involved in the maintenance of normal retinal function.
-!- SUBUNIT: Antiparallel heterodimer with CDH23 (PubMed:23135401,
PubMed:17805295). Found in a complex with TMIE and LHFPL5
(PubMed:25467981). Interacts with LHFPL5/TMHS; this interaction is
required for efficient localization to hair bundles
(PubMed:23217710). Interacts with MYO7A (PubMed:16481439).
Interacts with USH1G; this interaction may recruit USH1G to the
plasma membrane (PubMed:21436032). Interacts with TOMT
(PubMed:28504928). Isoforms CD1 and CD3 interact with TMC1 (via N-
terminus) and TMC2 (via N-terminus) (PubMed:25114259).
{ECO:0000269|PubMed:16481439, ECO:0000269|PubMed:17805295,
ECO:0000269|PubMed:21436032, ECO:0000269|PubMed:23135401,
ECO:0000269|PubMed:23217710, ECO:0000269|PubMed:25114259,
ECO:0000269|PubMed:25467981, ECO:0000269|PubMed:28504928}.
-!- INTERACTION:
Q99PF4-1:Cdh23; NbExp=10; IntAct=EBI-6556746, EBI-15656347;
Q9ES64:Ush1c; NbExp=3; IntAct=EBI-6556746, EBI-7418968;
Q9ES64-3:Ush1c; NbExp=2; IntAct=EBI-6556746, EBI-7418919;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21436032,
ECO:0000269|PubMed:23217710}; Single-pass membrane protein
{ECO:0000269|PubMed:21436032, ECO:0000269|PubMed:23217710}.
Note=Efficient localization to the plasma membrane requires the
presence of LHFPL5.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 5: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 6: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 7: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 8: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 9: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 10: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 11: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 12: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 13: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 14: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 15: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 16: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 17: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 18: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 19: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 21: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 22: Secreted {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Isoform 23: Secreted {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=26;
Name=1; Synonyms=CD1-1;
IsoId=Q99PJ1-1; Sequence=Displayed;
Name=2; Synonyms=CD1-2;
IsoId=Q99PJ1-2; Sequence=VSP_046580;
Name=3; Synonyms=CD1-3/5;
IsoId=Q99PJ1-3; Sequence=VSP_046580, VSP_046592, VSP_046594;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=4; Synonyms=CD1-4;
IsoId=Q99PJ1-4; Sequence=VSP_046580, VSP_046602;
Name=5; Synonyms=CD1-6;
IsoId=Q99PJ1-5; Sequence=VSP_046580, VSP_046591;
Name=6; Synonyms=CD1-7;
IsoId=Q99PJ1-6; Sequence=VSP_046580, VSP_046601, VSP_046602;
Name=7; Synonyms=CD1-8;
IsoId=Q99PJ1-7; Sequence=VSP_046580, VSP_046581, VSP_046601,
VSP_046602;
Name=8; Synonyms=CD1-9;
IsoId=Q99PJ1-8; Sequence=VSP_046579;
Name=9; Synonyms=CD1-10;
IsoId=Q99PJ1-9; Sequence=VSP_046579, VSP_046601;
Name=10; Synonyms=CD2-1;
IsoId=Q99PJ1-10; Sequence=VSP_046588, VSP_046605;
Name=11; Synonyms=CD2-2;
IsoId=Q99PJ1-11; Sequence=VSP_046580, VSP_046607, VSP_046609;
Name=12; Synonyms=CD2-3;
IsoId=Q99PJ1-12; Sequence=VSP_046577, VSP_046588, VSP_046607,
VSP_046609;
Name=13; Synonyms=CD2-4;
IsoId=Q99PJ1-13; Sequence=VSP_046580, VSP_046582, VSP_046583;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=14; Synonyms=CD2-5;
IsoId=Q99PJ1-14; Sequence=VSP_046580, VSP_046584, VSP_046585;
Name=15; Synonyms=CD2-6;
IsoId=Q99PJ1-15; Sequence=VSP_046580, VSP_046587, VSP_046593;
Name=16; Synonyms=CD2-7;
IsoId=Q99PJ1-16; Sequence=VSP_046580, VSP_046590, VSP_046596;
Name=17; Synonyms=CD2-8;
IsoId=Q99PJ1-17; Sequence=VSP_046580, VSP_046595, VSP_046597;
Name=18; Synonyms=CD3-1;
IsoId=Q99PJ1-18; Sequence=VSP_046606, VSP_046611;
Name=19; Synonyms=CD3-2;
IsoId=Q99PJ1-19; Sequence=VSP_046580, VSP_046606, VSP_046611;
Name=20; Synonyms=CD3-3;
IsoId=Q99PJ1-20; Sequence=VSP_046576, VSP_046600, VSP_046610;
Name=21; Synonyms=SI-1;
IsoId=Q99PJ1-21; Sequence=VSP_046598, VSP_046599;
Name=22; Synonyms=SI-2;
IsoId=Q99PJ1-22; Sequence=VSP_046580, VSP_046598, VSP_046599;
Name=23; Synonyms=SI-3;
IsoId=Q99PJ1-23; Sequence=VSP_046580, VSP_046589, VSP_046598,
VSP_046599;
Name=24; Synonyms=C;
IsoId=Q99PJ1-24; Sequence=VSP_046578, VSP_046608;
Note=Produced by aberrant splicing sites.;
Name=25;
IsoId=Q99PJ1-25; Sequence=VSP_046603;
Name=26;
IsoId=Q99PJ1-26; Sequence=VSP_046601, VSP_046604;
-!- TISSUE SPECIFICITY: Expressed in brain and sensory epithelium of
the developing inner ear. Expressed in the retina, in the
photoreceptor inner segments, the outer plexiform layer, the inner
nuclei layer and the ganglion cell layer and, more diffusely in
the inner plexiform layer (at protein level). Not detected in the
retinal pigment epithelium (at protein level). Expressed in the
spleen, dorsal root ganglion, dorsal aspect of neural tube, floor
plate and ependymal cells adjacent to the neural canal.
{ECO:0000269|PubMed:11429292, ECO:0000269|PubMed:16481439,
ECO:0000269|PubMed:16799054, ECO:0000269|PubMed:17805295}.
-!- DEVELOPMENTAL STAGE: Highest level of expression is detected at
embryonic day 16. Alternative splicing isoforms have different
spatiotemporal expression patterns. In cochlear cultures at the
equivalent of postnatal day 3, isoforms belonging to the CD1
(isoforms 1 through 9) and CD3 (isoforms 18 through 20) groups are
highly expressed in hair bundles in the basal coils and moderately
in those in the middle of the apical coil; they are hardly
detectable in those at the apical end of the apical coil (at
protein level). At the base of the cultured cochlea, in the more
mature hair bundles, CD3 group isoforms are restricted to the tips
of the shorter stereocilia in both inner and outer hair cells. By
contrast, at the same stage, isoforms belonging to the CD2 group
(isoforms 10 through 17) are highly expressed in hair bundles in
the apex of the cochlea and, at lower levels, in those in the
middle of the apical coil; they are hardly detectable at the base
of the cochlea (at protein level). In mature hair bundles, CD1
group isoforms are distributed fairly evenly along most of the
length of the stereocilia on auditory hair cells, whereas they are
concentrated toward the upper third of the hair bundle in
vestibular hair cells. In both the auditory and the vestibular
organs, these isoforms are excluded from a region at the very tip
of each stereocilium (at protein level). In contrast, CD2 group
isoforms are undetectable in adult cochlear hair cells (at protein
level). These isoforms are expressed in the entire hair bundle of
the immature cells in the sensory epithelium of the early
postnatal vestibule and only in the kinocilium in the more mature
hair bundles (at protein level). CD3 group isoforms are detected
in immature vestibular hair bundles, concentrated toward the tip
of each stereocilium, as early as 15.5 dpc. They also localize to
the tips of the shorter stereocilia in the mature vestibular hair
bundles and are not detected at the tips of the stereocilia in the
tallest row (at protein level). {ECO:0000269|PubMed:16807332}.
-!- DOMAIN: Cadherin repeats 1 and 2 mediate calcium-dependent
heterophilic interaction with CDH23.
{ECO:0000269|PubMed:23135401}.
-!- DOMAIN: Three calcium ions are usually bound at the interface of
each cadherin domain and rigidify the connections, imparting a
strong curvature to the full-length ectodomain.
{ECO:0000269|PubMed:23135401}.
-!- DISEASE: Note=Defects in Pcdh15 are the cause of the Ames waltzer
(av) phenotype. It is characterized by deafness and a balance
disorder, associated with the degeneration of inner ear
neuroepithelia.
-!- SEQUENCE CAUTION:
Sequence=ABC79270.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF281899; AAG53891.1; -; mRNA.
EMBL; AY949849; AAY24693.1; -; mRNA.
EMBL; DQ354396; ABC79259.1; -; mRNA.
EMBL; DQ354397; ABC79260.1; -; mRNA.
EMBL; DQ354398; ABC79261.1; -; mRNA.
EMBL; DQ354399; ABC79262.1; -; mRNA.
EMBL; DQ354400; ABC79263.1; -; mRNA.
EMBL; DQ354401; ABC79264.1; -; mRNA.
EMBL; DQ354402; ABC79265.1; -; mRNA.
EMBL; DQ354403; ABC79266.1; -; mRNA.
EMBL; DQ354404; ABC79267.1; -; mRNA.
EMBL; DQ354405; ABC79268.1; -; mRNA.
EMBL; DQ354406; ABC79269.1; -; mRNA.
EMBL; DQ354407; ABC79270.1; ALT_INIT; mRNA.
EMBL; DQ354408; ABC79271.1; -; mRNA.
EMBL; DQ354409; ABC79272.1; -; mRNA.
EMBL; DQ354410; ABC79273.1; -; mRNA.
EMBL; DQ354411; ABC79274.1; -; mRNA.
EMBL; DQ354412; ABC79275.1; -; mRNA.
EMBL; DQ354413; ABC79276.1; -; mRNA.
EMBL; DQ354414; ABC79277.1; -; mRNA.
EMBL; DQ354415; ABC79278.1; -; mRNA.
EMBL; DQ354416; ABC79279.1; -; mRNA.
EMBL; DQ354417; ABC79280.1; -; mRNA.
EMBL; DQ354418; ABC79281.1; -; mRNA.
EMBL; AK139154; BAE23903.1; -; mRNA.
EMBL; AK141024; BAE24546.1; -; mRNA.
EMBL; AC108392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC119894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC121142; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC121602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC121832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC123032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC123809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC144802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC147721; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC153858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC158800; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC159477; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC186813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC188091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CAAA01110489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; HQ404375; ADP09331.1; -; mRNA.
EMBL; HQ420254; ADT91308.1; -; mRNA.
CCDS; CCDS35934.1; -. [Q99PJ1-1]
CCDS; CCDS48594.1; -. [Q99PJ1-6]
CCDS; CCDS48595.1; -. [Q99PJ1-7]
CCDS; CCDS56711.1; -. [Q99PJ1-10]
CCDS; CCDS56712.1; -. [Q99PJ1-21]
CCDS; CCDS56713.1; -. [Q99PJ1-18]
CCDS; CCDS56714.1; -. [Q99PJ1-22]
CCDS; CCDS56715.1; -. [Q99PJ1-2]
CCDS; CCDS56716.1; -. [Q99PJ1-11]
CCDS; CCDS56717.1; -. [Q99PJ1-19]
CCDS; CCDS56718.1; -. [Q99PJ1-4]
CCDS; CCDS56719.1; -. [Q99PJ1-5]
CCDS; CCDS56720.1; -. [Q99PJ1-8]
CCDS; CCDS56721.1; -. [Q99PJ1-9]
RefSeq; NP_001136207.1; NM_001142735.1. [Q99PJ1-2]
RefSeq; NP_001136208.1; NM_001142736.1. [Q99PJ1-4]
RefSeq; NP_001136209.1; NM_001142737.1. [Q99PJ1-5]
RefSeq; NP_001136210.1; NM_001142738.1. [Q99PJ1-7]
RefSeq; NP_001136211.1; NM_001142739.1. [Q99PJ1-8]
RefSeq; NP_001136212.1; NM_001142740.1. [Q99PJ1-6]
RefSeq; NP_001136213.1; NM_001142741.1. [Q99PJ1-9]
RefSeq; NP_001136214.1; NM_001142742.1. [Q99PJ1-10]
RefSeq; NP_001136215.1; NM_001142743.1. [Q99PJ1-11]
RefSeq; NP_001136218.1; NM_001142746.1. [Q99PJ1-18]
RefSeq; NP_001136219.1; NM_001142747.1. [Q99PJ1-21]
RefSeq; NP_001136220.1; NM_001142748.1. [Q99PJ1-22]
RefSeq; NP_001136232.1; NM_001142760.1. [Q99PJ1-19]
RefSeq; NP_075604.2; NM_023115.3. [Q99PJ1-1]
RefSeq; XP_006513219.1; XM_006513156.3. [Q99PJ1-26]
UniGene; Mm.338933; -.
PDB; 4APX; X-ray; 1.65 A; B=27-259.
PDB; 4AQ8; X-ray; 2.63 A; C/D=27-259.
PDB; 4AQA; X-ray; 1.96 A; B=27-259.
PDB; 4AQE; X-ray; 2.27 A; B=27-259.
PDB; 4AXW; X-ray; 2.23 A; B=27-259.
PDB; 4XXW; X-ray; 2.26 A; A/B=36-259.
PDB; 5KJ4; X-ray; 3.35 A; A/B/C/D=924-1149.
PDBsum; 4APX; -.
PDBsum; 4AQ8; -.
PDBsum; 4AQA; -.
PDBsum; 4AQE; -.
PDBsum; 4AXW; -.
PDBsum; 4XXW; -.
PDBsum; 5KJ4; -.
ProteinModelPortal; Q99PJ1; -.
SMR; Q99PJ1; -.
BioGrid; 198282; 3.
DIP; DIP-42151N; -.
IntAct; Q99PJ1; 3.
MINT; MINT-1895732; -.
STRING; 10090.ENSMUSP00000101066; -.
iPTMnet; Q99PJ1; -.
PhosphoSitePlus; Q99PJ1; -.
PaxDb; Q99PJ1; -.
PRIDE; Q99PJ1; -.
Ensembl; ENSMUST00000092420; ENSMUSP00000090076; ENSMUSG00000052613. [Q99PJ1-6]
Ensembl; ENSMUST00000105424; ENSMUSP00000101064; ENSMUSG00000052613. [Q99PJ1-2]
Ensembl; ENSMUST00000105426; ENSMUSP00000101066; ENSMUSG00000052613. [Q99PJ1-4]
Ensembl; ENSMUST00000105429; ENSMUSP00000101069; ENSMUSG00000052613. [Q99PJ1-5]
Ensembl; ENSMUST00000124046; ENSMUSP00000121130; ENSMUSG00000052613. [Q99PJ1-12]
Ensembl; ENSMUST00000125006; ENSMUSP00000120056; ENSMUSG00000052613. [Q99PJ1-22]
Ensembl; ENSMUST00000125055; ENSMUSP00000114326; ENSMUSG00000052613. [Q99PJ1-3]
Ensembl; ENSMUST00000125517; ENSMUSP00000115399; ENSMUSG00000052613. [Q99PJ1-16]
Ensembl; ENSMUST00000126920; ENSMUSP00000121939; ENSMUSG00000052613. [Q99PJ1-8]
Ensembl; ENSMUST00000129404; ENSMUSP00000117731; ENSMUSG00000052613. [Q99PJ1-9]
Ensembl; ENSMUST00000131321; ENSMUSP00000122911; ENSMUSG00000052613. [Q99PJ1-4]
Ensembl; ENSMUST00000131724; ENSMUSP00000122466; ENSMUSG00000052613. [Q99PJ1-11]
Ensembl; ENSMUST00000134009; ENSMUSP00000120618; ENSMUSG00000052613. [Q99PJ1-23]
Ensembl; ENSMUST00000136096; ENSMUSP00000121534; ENSMUSG00000052613. [Q99PJ1-3]
Ensembl; ENSMUST00000144302; ENSMUSP00000122606; ENSMUSG00000052613. [Q99PJ1-13]
Ensembl; ENSMUST00000146682; ENSMUSP00000134863; ENSMUSG00000052613. [Q99PJ1-20]
Ensembl; ENSMUST00000147189; ENSMUSP00000122940; ENSMUSG00000052613. [Q99PJ1-7]
Ensembl; ENSMUST00000151116; ENSMUSP00000119662; ENSMUSG00000052613. [Q99PJ1-10]
Ensembl; ENSMUST00000152655; ENSMUSP00000118201; ENSMUSG00000052613. [Q99PJ1-17]
Ensembl; ENSMUST00000152819; ENSMUSP00000123647; ENSMUSG00000052613. [Q99PJ1-15]
Ensembl; ENSMUST00000155701; ENSMUSP00000135495; ENSMUSG00000052613. [Q99PJ1-14]
Ensembl; ENSMUST00000177107; ENSMUSP00000135501; ENSMUSG00000052613. [Q99PJ1-18]
Ensembl; ENSMUST00000177420; ENSMUSP00000135849; ENSMUSG00000052613. [Q99PJ1-21]
Ensembl; ENSMUST00000191709; ENSMUSP00000142313; ENSMUSG00000052613. [Q99PJ1-25]
Ensembl; ENSMUST00000191854; ENSMUSP00000141973; ENSMUSG00000052613. [Q99PJ1-19]
Ensembl; ENSMUST00000193361; ENSMUSP00000141792; ENSMUSG00000052613. [Q99PJ1-1]
Ensembl; ENSMUST00000193739; ENSMUSP00000142173; ENSMUSG00000052613. [Q99PJ1-26]
GeneID; 11994; -.
KEGG; mmu:11994; -.
UCSC; uc007fpf.2; mouse. [Q99PJ1-21]
UCSC; uc007fpg.2; mouse. [Q99PJ1-22]
UCSC; uc007fph.2; mouse. [Q99PJ1-10]
UCSC; uc007fpi.2; mouse. [Q99PJ1-8]
UCSC; uc007fpj.2; mouse. [Q99PJ1-9]
UCSC; uc007fpk.2; mouse. [Q99PJ1-1]
UCSC; uc007fpl.2; mouse. [Q99PJ1-4]
UCSC; uc007fpn.2; mouse. [Q99PJ1-6]
UCSC; uc007fpo.2; mouse. [Q99PJ1-17]
UCSC; uc007fpq.2; mouse. [Q99PJ1-20]
UCSC; uc007fpr.2; mouse. [Q99PJ1-11]
UCSC; uc011xfz.1; mouse. [Q99PJ1-23]
UCSC; uc011xgb.1; mouse. [Q99PJ1-7]
UCSC; uc011xgc.1; mouse. [Q99PJ1-5]
UCSC; uc011xgd.1; mouse. [Q99PJ1-15]
UCSC; uc011xge.1; mouse. [Q99PJ1-16]
UCSC; uc011xgf.1; mouse. [Q99PJ1-14]
UCSC; uc011xgg.1; mouse. [Q99PJ1-18]
UCSC; uc011xgh.1; mouse. [Q99PJ1-19]
UCSC; uc033fqa.1; mouse. [Q99PJ1-2]
CTD; 65217; -.
MGI; MGI:1891428; Pcdh15.
eggNOG; KOG3594; Eukaryota.
eggNOG; ENOG410XQHI; LUCA.
GeneTree; ENSGT00890000139339; -.
HOGENOM; HOG000186027; -.
HOVERGEN; HBG053521; -.
InParanoid; Q99PJ1; -.
KO; K16500; -.
OrthoDB; EOG091G0MMW; -.
TreeFam; TF326779; -.
ChiTaRS; Pcdh15; mouse.
PRO; PR:Q99PJ1; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000052613; -.
CleanEx; MM_PCDH15; -.
ExpressionAtlas; Q99PJ1; baseline and differential.
Genevisible; Q99PJ1; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; ISS:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0001750; C:photoreceptor outer segment; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0032420; C:stereocilium; IDA:HGNC.
GO; GO:0032421; C:stereocilium bundle; IDA:MGI.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0051017; P:actin filament bundle assembly; IMP:MGI.
GO; GO:0007015; P:actin filament organization; IMP:MGI.
GO; GO:0007628; P:adult walking behavior; IMP:MGI.
GO; GO:0042491; P:auditory receptor cell differentiation; IMP:MGI.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; IMP:MGI.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
GO; GO:0050973; P:detection of mechanical stimulus involved in equilibrioception; IMP:MGI.
GO; GO:0050910; P:detection of mechanical stimulus involved in sensory perception of sound; IMP:MGI.
GO; GO:0050957; P:equilibrioception; ISO:MGI.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
GO; GO:0048839; P:inner ear development; IMP:MGI.
GO; GO:0060122; P:inner ear receptor stereocilium organization; IMP:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0002009; P:morphogenesis of an epithelium; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
GO; GO:0045494; P:photoreceptor cell maintenance; ISO:MGI.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0060013; P:righting reflex; IMP:MGI.
GO; GO:0050953; P:sensory perception of light stimulus; ISO:MGI.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0001964; P:startle response; IMP:MGI.
GO; GO:0007601; P:visual perception; IMP:MGI.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR030718; Protocadherin-15.
PANTHER; PTHR24028:SF11; PTHR24028:SF11; 3.
Pfam; PF00028; Cadherin; 8.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 11.
SUPFAM; SSF49313; SSF49313; 10.
PROSITE; PS00232; CADHERIN_1; 4.
PROSITE; PS50268; CADHERIN_2; 11.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion;
Cell membrane; Complete proteome; Deafness; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hearing; Membrane; Reference proteome;
Repeat; Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 1943 Protocadherin-15.
/FTId=PRO_0000003999.
TOPO_DOM 27 1381 Extracellular. {ECO:0000255}.
TRANSMEM 1382 1402 Helical. {ECO:0000255}.
TOPO_DOM 1403 1943 Cytoplasmic. {ECO:0000255}.
DOMAIN 45 152 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 153 270 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 283 400 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 401 514 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 515 621 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 622 722 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 724 824 Cadherin 7. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 825 931 Cadherin 8. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 932 1040 Cadherin 9. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1042 1149 Cadherin 10. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1150 1264 Cadherin 11. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
COMPBIAS 1437 1448 Poly-Pro.
COMPBIAS 1772 1778 Poly-Pro.
COMPBIAS 1804 1812 Poly-Pro.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 206 206 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 424 424 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 564 564 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 667 667 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 729 729 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 773 773 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 826 826 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 856 856 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1069 1069 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1089 1089 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1180 1180 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 37 125 {ECO:0000269|PubMed:23135401}.
VAR_SEQ 1 1252 Missing (in isoform 20).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046576.
VAR_SEQ 1 401 Missing (in isoform 12).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046577.
VAR_SEQ 31 600 Missing (in isoform 24).
{ECO:0000303|PubMed:16799054}.
/FTId=VSP_046578.
VAR_SEQ 31 57 Missing (in isoform 8 and isoform 9).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046579.
VAR_SEQ 31 35 Missing (in isoform 2, isoform 3, isoform
4, isoform 5, isoform 6, isoform 7,
isoform 11, isoform 13, isoform 14,
isoform 15, isoform 16, isoform 17,
isoform 19, isoform 22 and isoform 23).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046580.
VAR_SEQ 204 240 Missing (in isoform 7).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046581.
VAR_SEQ 298 331 EELNPILVTPPIQAIDQDRNIQPPSDRPGILYSI -> DFG
SLRSGANSWCQGCGGVHRCPSPWRRLLPRRL (in
isoform 13).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046582.
VAR_SEQ 332 1943 Missing (in isoform 13).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046583.
VAR_SEQ 335 339 TPEDY -> RARES (in isoform 14).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046584.
VAR_SEQ 340 1943 Missing (in isoform 14).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046585.
VAR_SEQ 372 655 AEQDNGHPLPAFASLHIEILDENNQSPYFTMPSYQGYILES
APVGATISESLNLTTPLRIVALDKDIEDTKDPELHLFLNDY
TSVFTVTPTGITRYLTLLQPVDREEQQTYTFLITAFDGVQE
SEPVVVNIRVMDANDNTPTFPEISYDVYVYTDMSPGDSVIQ
LTAVDADEGSNGEISYEILVGGKGDFVINKTTGLVSIAPGV
ELIVGQTYALTVQASDNAPPAERRHSICTVYIEVLPPNNQS
PPRFPQLMYSLEVSEAMRIGAILLNLQATDREGDPITY ->
VEPEKVKKPKVEIREPSEEEVVVTVEKPPAAEPTYPTWKRA
RIFPMIFKKVRGLAEKRGIDLEGEEWRRRLDEEDKDYLQLT
LDQEEATESTVESEEESSDYTEYTETESEFSESETTEESES
ETPSEEAEESSTPESEESESTESEGEKARKNIVLARRRPVV
EEIQEVKGKREEPPVEEEEEPPLEEEERAEEGEESEAAPMD
ESTDLEAQDVPEEGSAESVSMERGVESEESESELSSSSSTS
ESLSGGPWGFQVPEYDRRKDEEPKKSPGANSEGYNTAL
(in isoform 15).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046587.
VAR_SEQ 440 440 D -> DVPPGGVP (in isoform 10 and isoform
12). {ECO:0000303|PubMed:16807332}.
/FTId=VSP_046588.
VAR_SEQ 441 961 Missing (in isoform 23).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046589.
VAR_SEQ 441 725 TKDPELHLFLNDYTSVFTVTPTGITRYLTLLQPVDREEQQT
YTFLITAFDGVQESEPVVVNIRVMDANDNTPTFPEISYDVY
VYTDMSPGDSVIQLTAVDADEGSNGEISYEILVGGKGDFVI
NKTTGLVSIAPGVELIVGQTYALTVQASDNAPPAERRHSIC
TVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAILLNLQA
TDREGDPITYAIENGDPQRVFNLSETTGILSLGKALDREST
DRYILIVTASDGRPDGTSTATVNIVVTDVNDNAPVFDPY
-> VEPEKVKKPKVEIREPSEEEVVVTVEKPPAAEPTYPTW
KRARIFPMIFKKVRGLAEKRGIDLEGEEWRRRLDEEDKDYL
QLTLDQEEATESTVESEEESSDYTEYTETESEFSESETTEE
SESETPSEEAEESSTPESEESESTESEGEKARKNIVLARRR
PVVEEIQEVKGKREEPPVEEEEEPPLEEEERAEEGEESEAA
PMDESTDLEAQDVPEEGSAESVSMERGVESEESESELSSSS
STSESLSGGPWGFQVPEYDRRKDEEPKKSPGANSEGYNTAL
(in isoform 16).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046590.
VAR_SEQ 600 671 RHSICTVYIEVLPPNNQSPPRFPQLMYSLEVSEAMRIGAIL
LNLQATDREGDPITYAIENGDPQRVFNLSET -> S (in
isoform 5).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046591.
VAR_SEQ 645 689 ATDREGDPITYAIENGDPQRVFNLSETTGILSLGKALDRES
TDRY -> HRDSQPREGSRPREHRPLHPHRHSLRWQTGWNL
NCHCEHSGDGRQ (in isoform 3).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046592.
VAR_SEQ 656 1943 Missing (in isoform 15).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046593.
VAR_SEQ 690 1943 Missing (in isoform 3).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046594.
VAR_SEQ 703 986 TSTATVNIVVTDVNDNAPVFDPYLPRNLSVVEEEANAFVGQ
VRATDPDAGINGQVHYSLGNFNNLFRITSNGSIYTAVKLNR
EARDHYELVVVATDGAVHPRHSTLTLYIKVLDIDDNSPVFT
NSTYTVVVEENLPAGTSFLQIEAKDVDLGANVSYRIRSPEV
KHLFALHPFTGELSLLRSLDYEAFPDQEASITFLVEAFDIY
GTMPPGIATVTVIVKDMNDYPPVFSKRIYKGMVAPDAVKGT
PITTVYAEDADPPGMPASRVRYRVDDVQFPYPASIFDV ->
VEPEKVKKPKVEIREPSEEEVVVTVEKPPAAEPTYPTWKRA
RIFPMIFKKVRGLAEKRGIDLEGEEWRRRLDEEDKDYLQLT
LDQEEATESTVESEEESSDYTEYTETESEFSESETTEESES
ETPSEEAEESSTPESEESESTESEGEKARKNIVLARRRPVV
EEIQEVKGKREEPPVEEEEEPPLEEEERAEEGEESEAAPMD
ESTDLEAQDVPEEGSAESVSMERGVESEESESELSSSSSTS
ESLSGGPWGFQVPEYDRRKDEEPKKSPGANSEGYNTAL
(in isoform 17).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046595.
VAR_SEQ 726 1943 Missing (in isoform 16).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046596.
VAR_SEQ 987 1943 Missing (in isoform 17).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046597.
VAR_SEQ 1131 1176 NTAKVYIEIQDENDHPPVFQKKFYIGGVSEDARMFASVLRV
KATDR -> LSVIPCSWRTQVSKSLGLELGVPVSHSVESGT
RTGSSTRAASVPIH (in isoform 21, isoform 22
and isoform 23).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:16807332}.
/FTId=VSP_046598.
VAR_SEQ 1177 1943 Missing (in isoform 21, isoform 22 and
isoform 23).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:16807332}.
/FTId=VSP_046599.
VAR_SEQ 1407 1667 FKVRQAECTKTARIQSAMPAAKPAAPVPAAPAPPPPPPPPP
PGAHLYEELGESAMHNLFLLYHFEQSRGNNSVPEDRSSHRD
GMAFSSSTTESHEPAHVEGPLKESQPNPARTFSFVPDEDNL
STHNPLYMESIGQRSTNSDLQPRTDFEELLAPRTQVKSQSL
RGPREKIQRVWNQSVSFPRRLMWKAPNRPETIDLVEWQITN
QRAECESARCHPSQRGSSNVLLATEDAHESEKEGGHRDTLI
VQQTEQLKSLSSGSS -> GGFAPEHQLLRPSLLKPEELSM
ESGIDPGQEYGQDYYSYEHGYEMPQYGSRRRLLPPAGQEEY
GEVIGEAEEEYEEEEWARKRMIKLVVDREYESSSPGEDSAP
ESQRSRTHKPSGRSNVNGNIYIAQNGSVVRTRRACVADNLK
VPSPGLLGRHLKKLDTLAGTREENVPLNTLFKGPFSTEKAK
RTPTLVTFAPCPVVAEHSAVKPSGTRLKHTAEQESMVDSRL
SRESMEFHGDSAPSDEEELWMGPWNSLHIPMTKL (in
isoform 20).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046600.
VAR_SEQ 1407 1409 Missing (in isoform 6, isoform 7, isoform
9 and isoform 26).
{ECO:0000303|PubMed:16807332,
ECO:0000303|PubMed:21436032}.
/FTId=VSP_046601.
VAR_SEQ 1461 1463 MHN -> I (in isoform 4, isoform 6 and
isoform 7).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046602.
VAR_SEQ 1462 1943 HNLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEP
AHVEGPLKESQPNPARTFSFVPDEDNLSTHNPLYMESIGQR
STNSDLQPRTDFEELLAPRTQVKSQSLRGPREKIQRVWNQS
VSFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQ
RGSSNVLLATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGS
SFSSSWSHFSFSTLPTISRAVELGSEPNVVTSPADCTLELS
PPLRPRILNSLSSKRETPTCASDTEPKRNSFEIAPHPPSIS
APLPHPPLPRPPIAFTTFPLPLSPPNPPPPQLVTFSLPIST
PPTSSLPLPPPLSLPPPPRPPAPRLFPQPPSTSIPSTDSIS
APAAKCTASATHARETTSTTQPPASNPQWGAEPHRHPKGIL
RHVKNLAELEKSVSNMYSHIEKNCPPADPSKLHTFCPAEKT
GMKITHDQSQETLVRVVEGIDVQPHSQSTSL -> YEMPQY
GSRRRLLPPAGQEEYGEVIGEAEEEYEEEEVEPEKVKKPKV
EIREPSEEEVVVTVEKPPAAEPTYPTWKRARIFPMIFKKVR
GLAEKRGIDLEGEEWRRRLDEEDKDYLQLTLDQEEATESTV
ESEEESSDYTEYTETESEFSESETTEESESETPSEEAEESS
TPESEESESTESEGEKARKNIVLARRRPVVEEIQEVKGKRE
EPPVEEEEEPPLEEEERAEEGEESEAAPMDESTDLEAQDVP
EEGSAESVSMERGVESEESESELSSSSSTSESLSGGPWGFQ
VPEYDRRKDEEPKKSPGANSEGYNTAL (in isoform
25). {ECO:0000303|PubMed:21436032}.
/FTId=VSP_046603.
VAR_SEQ 1462 1943 HNLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEP
AHVEGPLKESQPNPARTFSFVPDEDNLSTHNPLYMESIGQR
STNSDLQPRTDFEELLAPRTQVKSQSLRGPREKIQRVWNQS
VSFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQ
RGSSNVLLATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGS
SFSSSWSHFSFSTLPTISRAVELGSEPNVVTSPADCTLELS
PPLRPRILNSLSSKRETPTCASDTEPKRNSFEIAPHPPSIS
APLPHPPLPRPPIAFTTFPLPLSPPNPPPPQLVTFSLPIST
PPTSSLPLPPPLSLPPPPRPPAPRLFPQPPSTSIPSTDSIS
APAAKCTASATHARETTSTTQPPASNPQWGAEPHRHPKGIL
RHVKNLAELEKSVSNMYSHIEKNCPPADPSKLHTFCPAEKT
GMKITHDQSQETLVRVVEGIDVQPHSQSTSL -> YEMPQY
GSRRRLLPPAGQEEYGEVIGEAEEEYEEEEWARKRMIKLVV
DREYESSSPGEDSAPESQRSRTHKPSGRSNVNGNIYIAQNG
SVVRTRRACVADNLKVPSPGLLGRHLKKLDTLAGTREENVP
LNTLFKGPFSTEKAKRTPTLVTFAPCPVVAEHSAVKPSGTR
LKHTAEQESMVDSRLSRESMEFHGDSAPSDEEELWMGPWNS
LHIPMTKL (in isoform 26).
{ECO:0000303|PubMed:21436032}.
/FTId=VSP_046604.
VAR_SEQ 1463 1943 NLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPA
HVEGPLKESQPNPARTFSFVPDEDNLSTHNPLYMESIGQRS
TNSDLQPRTDFEELLAPRTQVKSQSLRGPREKIQRVWNQSV
SFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQR
GSSNVLLATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGSS
FSSSWSHFSFSTLPTISRAVELGSEPNVVTSPADCTLELSP
PLRPRILNSLSSKRETPTCASDTEPKRNSFEIAPHPPSISA
PLPHPPLPRPPIAFTTFPLPLSPPNPPPPQLVTFSLPISTP
PTSSLPLPPPLSLPPPPRPPAPRLFPQPPSTSIPSTDSISA
PAAKCTASATHARETTSTTQPPASNPQWGAEPHRHPKGILR
HVKNLAELEKSVSNMYSHIEKNCPPADPSKLHTFCPAEKTG
MKITHDQSQETLVRVVEGIDVQPHSQSTSL -> KYEMPQY
GSRRRLLPPAGQEEYGEVIGEAEEEYEEEEVEPEKVKKPKV
EIREPSEEEVVVTVEKPPAAEPTYPTWKRARIFPMIFKKVR
GLAEKRGIDLEGEEWRRRLDEEDKDYLQLTLDQEEATESTV
ESEEESSDYTEYTETESEFSESETTEESESETPSEEAEESS
TPESEESESTESEGEKARKNIVLARRRPVVEEIQEVKGKRE
EPPVEEEEEPPLEEEERAEEGEESEAAPMDESTDLEAQDVP
EEGSAESVSMERGVESEESESELSSSSSTSESLSGGPWGFQ
VPEYDRRKDEEPKKSPGANSEGYNTAL (in isoform
10). {ECO:0000303|PubMed:16807332}.
/FTId=VSP_046605.
VAR_SEQ 1463 1682 NLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPA
HVEGPLKESQPNPARTFSFVPDEDNLSTHNPLYMESIGQRS
TNSDLQPRTDFEELLAPRTQVKSQSLRGPREKIQRVWNQSV
SFPRRLMWKAPNRPETIDLVEWQITNQRAECESARCHPSQR
GSSNVLLATEDAHESEKEGGHRDTLIVQQTEQLKSLSSGSS
FSSSWSHFSFSTLPT -> KYEMPQYGSRRRLLPPAGQEEY
GEVIGEAEEEYEEEEWARKRMIKLVVDREYESSSPGEDSAP
ESQRSRTHKPSGRSNVNGNIYIAQNGSVVRTRRACVADNLK
VPSPGLLGRHLKKLDTLAGTREENVPLNTLFKGPFSTEKAK
RTPTLVTFAPCPVVAEHSAVKPSGTRLKHTAEQESMVDSRL
SRESMEFHGDSAPSDEEELWMGPWNSLHIPMTKL (in
isoform 18 and isoform 19).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046606.
VAR_SEQ 1463 1523 NLFLLYHFEQSRGNNSVPEDRSSHRDGMAFSSSTTESHEPA
HVEGPLKESQPNPARTFSFV -> KSYPWNLGLILARNMDK
IITVMSMGMRCPSMEVAVDCCHLLDRRNTAKSLVKLKRNMK
KKR (in isoform 11 and isoform 12).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046607.
VAR_SEQ 1464 1473 Missing (in isoform 24).
{ECO:0000303|PubMed:16799054}.
/FTId=VSP_046608.
VAR_SEQ 1524 1943 Missing (in isoform 11 and isoform 12).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046609.
VAR_SEQ 1668 1943 Missing (in isoform 20).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046610.
VAR_SEQ 1683 1943 Missing (in isoform 18 and isoform 19).
{ECO:0000303|PubMed:16807332}.
/FTId=VSP_046611.
MUTAGEN 48 48 I->A: Strongly reduced interaction with
CDH23. {ECO:0000269|PubMed:23135401}.
MUTAGEN 139 139 R->G: Impaired interaction with CDH23.
{ECO:0000269|PubMed:23135401}.
CONFLICT 608 608 I -> T (in Ref. 1; AAG53891, 2; AAY24693
and 3; ABC79259/ABC79260/ABC79261/
ABC79262/ABC79264/ABC79265/ABC79266/
ABC79267/ABC79268/ABC79269/ABC79270/
ABC79276/ABC79277). {ECO:0000305}.
CONFLICT 901 901 V -> A (in Ref. 1; AAG53891, 2; AAY24693
and 3; ABC79259/ABC79261/ABC79263/
ABC79264/ABC79265/ABC79266/ABC79267/
ABC79268/ABC79269/ABC79270/ABC79276/
ABC79277). {ECO:0000305}.
CONFLICT 1748 1748 S -> F (in Ref. 1; AAG53891, 2; AAY24693
and 3; ABC79259/ABC79261/ABC79263/
ABC79264/ABC79265/ABC79266/ABC79267).
{ECO:0000305}.
CONFLICT 1848 1848 S -> F (in Ref. 1; AAG53891, 2; AAY24693
and 3; ABC79259/ABC79261/ABC79263/
ABC79264/ABC79265/ABC79266/ABC79267).
{ECO:0000305}.
CONFLICT 1859 1859 W -> G (in Ref. 4; BAE24546).
{ECO:0000305}.
TURN 27 30 {ECO:0000244|PDB:4APX}.
HELIX 31 34 {ECO:0000244|PDB:4APX}.
STRAND 38 41 {ECO:0000244|PDB:4APX}.
STRAND 45 52 {ECO:0000244|PDB:4APX}.
STRAND 60 63 {ECO:0000244|PDB:4APX}.
STRAND 67 69 {ECO:0000244|PDB:4APX}.
STRAND 71 75 {ECO:0000244|PDB:4APX}.
STRAND 77 84 {ECO:0000244|PDB:4APX}.
HELIX 86 88 {ECO:0000244|PDB:4APX}.
STRAND 90 93 {ECO:0000244|PDB:4APX}.
TURN 94 97 {ECO:0000244|PDB:4APX}.
STRAND 98 101 {ECO:0000244|PDB:4APX}.
TURN 112 114 {ECO:0000244|PDB:4APX}.
STRAND 118 127 {ECO:0000244|PDB:4APX}.
TURN 128 130 {ECO:0000244|PDB:4APX}.
STRAND 133 143 {ECO:0000244|PDB:4APX}.
STRAND 151 155 {ECO:0000244|PDB:4APX}.
STRAND 157 162 {ECO:0000244|PDB:4APX}.
STRAND 170 172 {ECO:0000244|PDB:4APX}.
TURN 174 179 {ECO:0000244|PDB:4APX}.
STRAND 180 182 {ECO:0000244|PDB:4APX}.
STRAND 184 186 {ECO:0000244|PDB:4AQ8}.
HELIX 187 190 {ECO:0000244|PDB:4APX}.
STRAND 192 197 {ECO:0000244|PDB:4APX}.
HELIX 205 208 {ECO:0000244|PDB:4APX}.
TURN 214 216 {ECO:0000244|PDB:4APX}.
STRAND 219 221 {ECO:0000244|PDB:4APX}.
TURN 227 229 {ECO:0000244|PDB:4APX}.
STRAND 232 241 {ECO:0000244|PDB:4APX}.
HELIX 246 248 {ECO:0000244|PDB:4APX}.
STRAND 251 259 {ECO:0000244|PDB:4APX}.
STRAND 929 932 {ECO:0000244|PDB:5KJ4}.
STRAND 934 940 {ECO:0000244|PDB:5KJ4}.
STRAND 949 952 {ECO:0000244|PDB:5KJ4}.
STRAND 955 957 {ECO:0000244|PDB:5KJ4}.
HELIX 964 966 {ECO:0000244|PDB:5KJ4}.
STRAND 969 973 {ECO:0000244|PDB:5KJ4}.
HELIX 978 983 {ECO:0000244|PDB:5KJ4}.
STRAND 984 986 {ECO:0000244|PDB:5KJ4}.
TURN 988 990 {ECO:0000244|PDB:5KJ4}.
STRAND 992 997 {ECO:0000244|PDB:5KJ4}.
STRAND 1006 1014 {ECO:0000244|PDB:5KJ4}.
STRAND 1022 1031 {ECO:0000244|PDB:5KJ4}.
STRAND 1039 1041 {ECO:0000244|PDB:5KJ4}.
STRAND 1043 1045 {ECO:0000244|PDB:5KJ4}.
STRAND 1059 1062 {ECO:0000244|PDB:5KJ4}.
STRAND 1072 1079 {ECO:0000244|PDB:5KJ4}.
STRAND 1085 1087 {ECO:0000244|PDB:5KJ4}.
TURN 1089 1091 {ECO:0000244|PDB:5KJ4}.
STRAND 1093 1096 {ECO:0000244|PDB:5KJ4}.
TURN 1102 1104 {ECO:0000244|PDB:5KJ4}.
STRAND 1106 1116 {ECO:0000244|PDB:5KJ4}.
HELIX 1117 1121 {ECO:0000244|PDB:5KJ4}.
HELIX 1129 1131 {ECO:0000244|PDB:5KJ4}.
STRAND 1132 1140 {ECO:0000244|PDB:5KJ4}.
SEQUENCE 1943 AA; 214738 MW; 6FD6836082655855 CRC64;
MFLQFAVWKC LPHGILIASL LVVSWGQYDD DWQYEDCKLA RGGPPATIVA IDEESRNGTI
LVDNMLIKGT AGGPDPTIEL SLKDNVDYWV LLDPVKQMLF LNSTGRVLDR DPPMNIHSIV
VQVQCVNKKV GTVIYHEVRI VVRDRNDNSP TFKHESYYAT VNELTPVGTT IFTGFSGDNG
ATDIDDGPNG QIEYVIQYNP EDPTSNDTFE IPLMLTGNVV LRKRLNYEDK TRYYVIIQAN
DRAQNLNERR TTTTTLTVDV LDGDDLGPMF LPCVLVPNTR DCRPLTYQAA IPELRTPEEL
NPILVTPPIQ AIDQDRNIQP PSDRPGILYS ILVGTPEDYP RFFHMHPRTA ELTLLEPVNR
DFHQKFDLVI KAEQDNGHPL PAFASLHIEI LDENNQSPYF TMPSYQGYIL ESAPVGATIS
ESLNLTTPLR IVALDKDIED TKDPELHLFL NDYTSVFTVT PTGITRYLTL LQPVDREEQQ
TYTFLITAFD GVQESEPVVV NIRVMDANDN TPTFPEISYD VYVYTDMSPG DSVIQLTAVD
ADEGSNGEIS YEILVGGKGD FVINKTTGLV SIAPGVELIV GQTYALTVQA SDNAPPAERR
HSICTVYIEV LPPNNQSPPR FPQLMYSLEV SEAMRIGAIL LNLQATDREG DPITYAIENG
DPQRVFNLSE TTGILSLGKA LDRESTDRYI LIVTASDGRP DGTSTATVNI VVTDVNDNAP
VFDPYLPRNL SVVEEEANAF VGQVRATDPD AGINGQVHYS LGNFNNLFRI TSNGSIYTAV
KLNREARDHY ELVVVATDGA VHPRHSTLTL YIKVLDIDDN SPVFTNSTYT VVVEENLPAG
TSFLQIEAKD VDLGANVSYR IRSPEVKHLF ALHPFTGELS LLRSLDYEAF PDQEASITFL
VEAFDIYGTM PPGIATVTVI VKDMNDYPPV FSKRIYKGMV APDAVKGTPI TTVYAEDADP
PGMPASRVRY RVDDVQFPYP ASIFDVEEDS GRVVTRVNLN EEPTTIFKLV VVAFDDGEPV
MSSSATVRIL VLHPGEIPRF TQEEYRPPPV SELAARGTVV GVISAAAINQ SIVYSIVAGN
EEDKFGINNV TGVIYVNSPL DYETRTSYVL RVQADSLEVV LANLRVPSKS NTAKVYIEIQ
DENDHPPVFQ KKFYIGGVSE DARMFASVLR VKATDRDTGN YSAMAYRLII PPIKEGKEGF
VVETYTGLIK TAMLFHNMRR SYFKFQVIAT DDYGKGLSGK ADVLVSVVNQ LDMQVIVSNV
PPTLVEKKIE DLTEILDRYV QEQIPGAKVV VESIGARRHG DAYSLEDYSK CDLTVYAIDP
QTNRAIDRNE LFKFLDGKLL DINKDFQPYY GEGGRILEIR TPEAVTSIKK RGESLGYTEG
ALLALAFIII LCCIPAILVV LVSYRQFKVR QAECTKTARI QSAMPAAKPA APVPAAPAPP
PPPPPPPPGA HLYEELGESA MHNLFLLYHF EQSRGNNSVP EDRSSHRDGM AFSSSTTESH
EPAHVEGPLK ESQPNPARTF SFVPDEDNLS THNPLYMESI GQRSTNSDLQ PRTDFEELLA
PRTQVKSQSL RGPREKIQRV WNQSVSFPRR LMWKAPNRPE TIDLVEWQIT NQRAECESAR
CHPSQRGSSN VLLATEDAHE SEKEGGHRDT LIVQQTEQLK SLSSGSSFSS SWSHFSFSTL
PTISRAVELG SEPNVVTSPA DCTLELSPPL RPRILNSLSS KRETPTCASD TEPKRNSFEI
APHPPSISAP LPHPPLPRPP IAFTTFPLPL SPPNPPPPQL VTFSLPISTP PTSSLPLPPP
LSLPPPPRPP APRLFPQPPS TSIPSTDSIS APAAKCTASA THARETTSTT QPPASNPQWG
AEPHRHPKGI LRHVKNLAEL EKSVSNMYSH IEKNCPPADP SKLHTFCPAE KTGMKITHDQ
SQETLVRVVE GIDVQPHSQS TSL


Related products :

Catalog number Product name Quantity
EIAAB30019 Homo sapiens,Human,PCDH11,PCDH11Y,PCDH22,PCDHY,PCDH-Y,Protocadherin on the Y chromosome,Protocadherin prostate cancer,Protocadherin-11,Protocadherin-11 Y-linked,Protocadherin-22,Protocadherin-PC
EIAAB30017 Homo sapiens,Human,KIAA1326,PCDH11,PCDH11X,PCDHX,PCDH-X,Protocadherin on the X chromosome,Protocadherin-11,Protocadherin-11 X-linked,Protocadherin-S
EIAAB30018 PCDH11,PCDH11X,PCDHX,PCDH-X,Pig,Protocadherin on the X chromosome,Protocadherin-11,Protocadherin-11 X-linked,Sus scrofa
EIAAB30116 Homo sapiens,Human,PC-43,PCDH2,PCDH-gamma-C3,PCDHGC3,Protocadherin gamma-C3,Protocadherin-2,Protocadherin-43
EIAAB30054 Homo sapiens,Human,PCDH17,PCDH68,PCH68,Protocadherin-17,Protocadherin-68
EIAAB30123 Arcadlin,Mouse,Mus musculus,Papc,Paraxial protocadherin,Pcdh8,Protocadherin-8
U1615h CLIA Cadherin-like protein 1,Homo sapiens,Human,PC42,PCDH1,Protocadherin-1,Protocadherin-42 96T
E1615h ELISA kit Cadherin-like protein 1,Homo sapiens,Human,PC42,PCDH1,Protocadherin-1,Protocadherin-42 96T
EIAAB30120 BHPCDH,BH-Pcdh,Brain-heart protocadherin,Homo sapiens,Human,PCDH7,Protocadherin-7
E1615h ELISA Cadherin-like protein 1,Homo sapiens,Human,PC42,PCDH1,Protocadherin-1,Protocadherin-42 96T
EIAAB30061 Homo sapiens,Human,PCDH20,Protocadherin-13,Protocadherin-20
EIAAB06485 Cadherin-related family member 2,CDHR2,Homo sapiens,Human,PCDH24,PCLKC,PC-LKC,Protocadherin LKC,Protocadherin-24
EIAAB30093 Homo sapiens,Human,KIAA1621,PCDH3X,PCDHB16,PCDH-beta-16,Protocadherin beta-16,Protocadherin-3X
EIAAB30085 Homo sapiens,Human,PCDH3H,PCDHB9,PCDH-beta-9,Protocadherin beta-9,Protocadherin-3H
EIAAB30084 Homo sapiens,Human,PCDH3I,PCDHB8,PCDH-beta-8,Protocadherin beta-8,Protocadherin-3I
EIAAB06480 Cadherin-related family member 1,Cdhr1,Kiaa1775,MT-protocadherin,Pcdh21,Photoreceptor cadherin,prCAD,Prcad,Protocadherin-21,Rat,Rattus norvegicus
EIAAB30062 Cadherin-27,Cadherin-like protein CDHJ,Cadherin-like protein VR8,CDH27,CDHJ,DCHS2,Homo sapiens,Human,PCDH23,PCDHJ,Protein dachsous homolog 2,Protocadherin PCDHJ,Protocadherin-23
5081 Protocadherin 18 0.1 mg
5071 Protocadherin 12 0.5 mg
42-252 Protocadherin X Antibody 0.1 mg
5081 Protocadherin 18 0.5 mg
CD63 Protocadherin-10 (C-Fc-His tag) 500
C629 Protocadherin-10 (C-His tag) 500
5071 Protocadherin 12 0.1 mg
C629 Protocadherin-10 (C-His tag) lmg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur