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

Cadherin-related family member 5 (Mu-protocadherin) (Mucin and cadherin-like protein) (Mucin-like protocadherin) (MLPCDH)

 CDHR5_HUMAN             Reviewed;         845 AA.
Q9HBB8; C9J7X1; Q9H746; Q9HAU3; Q9HBB5; Q9HBB6; Q9HBB7; Q9NX86;
Q9NXI9;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
31-JAN-2018, entry version 147.
RecName: Full=Cadherin-related family member 5 {ECO:0000305};
AltName: Full=Mu-protocadherin {ECO:0000312|EMBL:AAG33495.1};
AltName: Full=Mucin and cadherin-like protein {ECO:0000303|PubMed:11031102};
AltName: Full=Mucin-like protocadherin {ECO:0000303|PubMed:24725409};
Short=MLPCDH {ECO:0000303|PubMed:24725409};
Flags: Precursor;
Name=CDHR5 {ECO:0000312|HGNC:HGNC:7521};
Synonyms=MUCDHL {ECO:0000303|PubMed:11031102},
MUPCDH {ECO:0000312|HGNC:HGNC:7521};
ORFNames=UNQ2781/PRO7168 {ECO:0000312|EMBL:AAQ88734.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAG16731.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANTS
PRO-165; SER-357; SER-521 AND SER-702.
PubMed=11031102; DOI=10.1006/geno.2000.6339;
Paris M.J., Williams B.R.G.;
"Characterization of a 500-kb contig spanning the region between c-Ha-
Ras and MUC2 on chromosome 11p15.5.";
Genomics 69:196-202(2000).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS SER-357;
SER-521 AND SER-702.
TISSUE=Kidney {ECO:0000312|EMBL:AAG33495.1};
Soleiman A., Krieger S., Haase A., Hantusch B.;
"Cloning and characterization of human mu-protocadherin.";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND VARIANTS
SER-357 AND SER-702.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS SER-357; SER-521 AND SER-702.
TISSUE=Colon mucosa {ECO:0000312|EMBL:BAA91021.1}, and
Ileal mucosa {ECO:0000312|EMBL:BAA91130.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6] {ECO:0000305}
TISSUE SPECIFICITY.
PubMed=12167596; DOI=10.1152/ajprenal.00012.2002;
Goldberg M., Wei M., Tycko B., Falikovich I., Warburton D.;
"Identification and expression analysis of the human mu-protocadherin
gene in fetal and adult kidneys.";
Am. J. Physiol. 283:F454-F463(2002).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-81 AND ASN-308.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[8]
FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH MYO7B AND
USH1C, MUTAGENESIS OF ARG-109 AND ILE-845, REGION, AND TISSUE
SPECIFICITY.
PubMed=24725409; DOI=10.1016/j.cell.2014.01.067;
Crawley S.W., Shifrin D.A. Jr., Grega-Larson N.E., McConnell R.E.,
Benesh A.E., Mao S., Zheng Y., Zheng Q.Y., Nam K.T., Millis B.A.,
Kachar B., Tyska M.J.;
"Intestinal brush border assembly driven by protocadherin-based
intermicrovillar adhesion.";
Cell 157:433-446(2014).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-810; SER-817; SER-819
AND SER-821, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
IDENTIFICATION OF THE IMAC COMPLEX.
PubMed=26812018; DOI=10.1016/j.devcel.2015.12.022;
Crawley S.W., Weck M.L., Grega-Larson N.E., Shifrin D.A. Jr.,
Tyska M.J.;
"ANKS4B is essential for intermicrovillar adhesion complex
formation.";
Dev. Cell 36:190-200(2016).
-!- FUNCTION: Intermicrovillar adhesion molecule that forms, via its
extracellular domain, calcium-dependent heterophilic complexes
with CDHR2 on adjacent microvilli. Thereby, controls the packing
of microvilli at the apical membrane of epithelial cells. Through
its cytoplasmic domain, interacts with microvillus cytoplasmic
proteins to form the intermicrovillar adhesion complex/IMAC. This
complex plays a central role in microvilli and epithelial brush
border differentiation. {ECO:0000269|PubMed:24725409}.
-!- SUBUNIT: Part of the IMAC/intermicrovillar adhesion
complex/intermicrovillar tip-link complex composed of ANKS4B,
MYO7B, USH1C, CDHR2 and CDHR5 (PubMed:26812018). Interacts (via
cytoplasmic domain) with USH1C and MYO7B; required for proper
localization of CDHR5 to microvilli tips and its function in brush
border differentiation (PubMed:24725409).
{ECO:0000269|PubMed:24725409, ECO:0000269|PubMed:26812018}.
-!- INTERACTION:
Q9BYE9:CDHR2; NbExp=3; IntAct=EBI-9540729, EBI-493793;
Q9Y6N9-1:USH1C; NbExp=2; IntAct=EBI-9540696, EBI-9541226;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:24725409}; Single-pass type I membrane protein
{ECO:0000269|PubMed:24725409}. Cell projection, microvillus
membrane {ECO:0000269|PubMed:24725409}; Single-pass type I
membrane protein {ECO:0000269|PubMed:24725409}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1 {ECO:0000269|PubMed:11031102, ECO:0000305};
Synonyms=MUCDHL-FL {ECO:0000303|PubMed:11031102}, MLPCDH-L
{ECO:0000303|PubMed:24725409};
IsoId=Q9HBB8-1; Sequence=Displayed;
Name=2 {ECO:0000305}; Synonyms=MLPCDH-S
{ECO:0000303|PubMed:24725409};
IsoId=Q9HBB8-2; Sequence=VSP_050693;
Name=3;
IsoId=Q9HBB8-4; Sequence=VSP_050692;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highest expression in kidney, liver, colon and
small intestine. In kidney, expressed apically along brush border
of proximal convoluted tubule but not in cortical collecting
ducts. Isoform 1 is expressed primarily in adult small intestine
and colon. Isoform 2 is highly expressed in fetal liver
(PubMed:12167596). Expressed in duodenum with higher expression in
enterocytes along the villus axis and lower expression in crypts
(at protein level) (PubMed:24725409).
{ECO:0000269|PubMed:12167596, ECO:0000269|PubMed:24725409}.
-!- PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:Q9JIK1}.
-!- SEQUENCE CAUTION:
Sequence=AAG16730.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAG16732.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
Sequence=BAA91021.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA91021.1; Type=Frameshift; Positions=763; Evidence={ECO:0000305};
Sequence=BAA91021.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
Sequence=BAB15052.1; Type=Frameshift; Positions=458; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=A tighter mesh - Issue
178 of April 2016;
URL="https://web.expasy.org/spotlight/back_issues/178/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF258674; AAG16730.1; ALT_SEQ; Genomic_DNA.
EMBL; AF258674; AAG16731.1; -; Genomic_DNA.
EMBL; AF258675; AAG16732.1; ALT_SEQ; mRNA.
EMBL; AF258676; AAG16733.1; -; mRNA.
EMBL; AF276242; AAG30821.1; -; mRNA.
EMBL; AF301909; AAG33495.1; -; mRNA.
EMBL; AY358368; AAQ88734.1; -; mRNA.
EMBL; AK000226; BAA91021.1; ALT_SEQ; mRNA.
EMBL; AK000384; BAA91130.1; -; mRNA.
EMBL; AK025012; BAB15052.1; ALT_FRAME; mRNA.
EMBL; AP006284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS7707.1; -. [Q9HBB8-1]
CCDS; CCDS7708.1; -. [Q9HBB8-2]
RefSeq; NP_001165439.1; NM_001171968.1.
RefSeq; NP_068743.2; NM_021924.4.
RefSeq; NP_112554.2; NM_031264.3.
UniGene; Hs.165619; -.
ProteinModelPortal; Q9HBB8; -.
BioGrid; 119810; 11.
IntAct; Q9HBB8; 3.
MINT; MINT-4999634; -.
STRING; 9606.ENSP00000351118; -.
iPTMnet; Q9HBB8; -.
PhosphoSitePlus; Q9HBB8; -.
BioMuta; CDHR5; -.
DMDM; 296439399; -.
MaxQB; Q9HBB8; -.
PaxDb; Q9HBB8; -.
PeptideAtlas; Q9HBB8; -.
PRIDE; Q9HBB8; -.
Ensembl; ENST00000349570; ENSP00000345726; ENSG00000099834. [Q9HBB8-2]
Ensembl; ENST00000358353; ENSP00000351118; ENSG00000099834. [Q9HBB8-1]
Ensembl; ENST00000397542; ENSP00000380676; ENSG00000099834. [Q9HBB8-1]
GeneID; 53841; -.
KEGG; hsa:53841; -.
UCSC; uc001lqj.3; human. [Q9HBB8-1]
CTD; 53841; -.
DisGeNET; 53841; -.
EuPathDB; HostDB:ENSG00000099834.18; -.
GeneCards; CDHR5; -.
HGNC; HGNC:7521; CDHR5.
HPA; CAB025004; -.
HPA; HPA009081; -.
HPA; HPA009173; -.
MIM; 606839; gene.
neXtProt; NX_Q9HBB8; -.
OpenTargets; ENSG00000099834; -.
PharmGKB; PA165543311; -.
eggNOG; KOG3594; Eukaryota.
eggNOG; ENOG410XQHI; LUCA.
GeneTree; ENSGT00390000001008; -.
HOVERGEN; HBG052536; -.
InParanoid; Q9HBB8; -.
KO; K16505; -.
OMA; GTSQPMP; -.
OrthoDB; EOG091G0HDO; -.
PhylomeDB; Q9HBB8; -.
TreeFam; TF350567; -.
ChiTaRS; CDHR5; human.
GeneWiki; MUPCDH; -.
GenomeRNAi; 53841; -.
PRO; PR:Q9HBB8; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000099834; -.
CleanEx; HS_MUPCDH; -.
ExpressionAtlas; Q9HBB8; baseline and differential.
Genevisible; Q9HBB8; HS.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
GO; GO:0005905; C:clathrin-coated pit; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031528; C:microvillus membrane; IDA:UniProtKB.
GO; GO:0044214; C:spanning component of plasma membrane; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0050839; F:cell adhesion molecule binding; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; ISS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
GO; GO:0090675; P:intermicrovillar adhesion; IMP:UniProtKB.
GO; GO:0032532; P:regulation of microvillus length; IMP:UniProtKB.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR030326; Mucdhl.
PANTHER; PTHR45160; PTHR45160; 1.
SMART; SM00112; CA; 3.
SUPFAM; SSF49313; SSF49313; 3.
PROSITE; PS00232; CADHERIN_1; 1.
PROSITE; PS50268; CADHERIN_2; 4.
1: Evidence at protein level;
Alternative splicing; Calcium; Cell membrane; Cell projection;
Complete proteome; Differentiation; Glycoprotein; Membrane;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 845 Cadherin-related family member 5.
/FTId=PRO_0000004012.
TOPO_DOM 26 669 Extracellular. {ECO:0000255}.
TRANSMEM 670 690 Helical. {ECO:0000255}.
TOPO_DOM 691 845 Cytoplasmic. {ECO:0000255}.
DOMAIN 71 124 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043, ECO:0000305}.
DOMAIN 125 237 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043, ECO:0000305}.
DOMAIN 249 354 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043, ECO:0000305}.
DOMAIN 355 459 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043, ECO:0000305}.
REPEAT 540 570 1. {ECO:0000305}.
REPEAT 571 601 2. {ECO:0000305}.
REPEAT 602 631 3. {ECO:0000305}.
REPEAT 632 645 4; truncated.
REGION 540 645 4 X 31 AA approximate tandem repeats.
REGION 691 845 Mediates interaction with USH1C and MYO7B
and is required for proper localization
to microvilli tips and function in
microvilli organization.
{ECO:0000269|PubMed:24725409}.
MOD_RES 770 770 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VHF2}.
MOD_RES 810 810 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 817 817 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 819 819 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 81 81 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 198 198 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 308 308 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 405 405 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 526 526 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
VAR_SEQ 460 653 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2}.
/FTId=VSP_050693.
VAR_SEQ 460 465 Missing (in isoform 3).
{ECO:0000303|PubMed:12975309}.
/FTId=VSP_050692.
VARIANT 165 165 Q -> P (in dbSNP:rs2740374).
{ECO:0000269|PubMed:11031102}.
/FTId=VAR_060412.
VARIANT 357 357 R -> S (in dbSNP:rs2246614).
{ECO:0000269|PubMed:11031102,
ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.2}.
/FTId=VAR_017920.
VARIANT 389 389 D -> N (in dbSNP:rs2306066).
/FTId=VAR_017921.
VARIANT 521 521 P -> S (in dbSNP:rs2740375).
{ECO:0000269|PubMed:11031102,
ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.2}.
/FTId=VAR_060413.
VARIANT 702 702 C -> S (in dbSNP:rs2740379).
{ECO:0000269|PubMed:11031102,
ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.2}.
/FTId=VAR_059192.
MUTAGEN 109 109 R->G: Loss of binding to CDHR2.
{ECO:0000269|PubMed:24725409}.
MUTAGEN 845 845 I->R: Loss of interaction with USH1C.
{ECO:0000269|PubMed:24725409}.
CONFLICT 313 313 R -> S (in Ref. 4; BAA91021).
{ECO:0000305}.
CONFLICT 373 373 V -> A (in Ref. 4; BAB15052).
{ECO:0000305}.
CONFLICT 476 476 S -> G (in Ref. 2; AAG33495 and 4;
BAA91021). {ECO:0000305}.
CONFLICT 498 498 G -> E (in Ref. 2; AAG33495 and 4;
BAA91021). {ECO:0000305}.
CONFLICT 571 571 A -> V (in Ref. 1; AAG16733, 2; AAG33495
and 4; BAA91021). {ECO:0000305}.
CONFLICT 807 807 N -> S (in Ref. 2; AAG30821/AAG33495 and
4; BAA91130). {ECO:0000305}.
SEQUENCE 845 AA; 88223 MW; FD872A8D67AF6677 CRC64;
MGSWALLWPP LLFTGLLVRP PGTMAQAQYC SVNKDIFEVE ENTNVTEPLV DIHVPEGQEV
TLGALSTPFA FRIQGNQLFL NVTPDYEEKS LLEAQLLCQS GGTLVTQLRV FVSVLDVNDN
APEFPFKTKE IRVEEDTKVN STVIPETQLQ AEDRDKDDIL FYTLQEMTAG ASDYFSLVSV
NRPALRLDRP LDFYERPNMT FWLLVRDTPG ENVEPSHTAT ATLVLNVVPA DLRPPWFLPC
TFSDGYVCIQ AQYHGAVPTG HILPSPLVLR PGPIYAEDGD RGINQPIIYS IFRGNVNGTF
IIHPDSGNLT VARSVPSPMT FLLLVKGQQA DLARYSVTQV TVEAVAAAGS PPRFPQRLYR
GTVARGAGAG VVVKDAAAPS QPLRIQAQDP EFSDLNSAIT YRITNHSHFR MEGEVVLTTT
TLAQAGAFYA EVEAHNTVTS GTATTVIEIQ VSEQEPPSTD VPPSPEAGGT TGPWTSTTSE
VPRPPEPSQG PSTTSSGGGT GPHPPSGTTL RPPTSSTPGG PPGAENSTSH QPATPGGDTA
QTPKPGTSQP MPPGVGTSTS HQPATPSGGT AQTPEPGTSQ PMPPSMGTST SHQPATPGGG
TAQTPEAGTS QPMPPGMGTS TSHQPTTPGG GTAQTPEPGT SQPMPLSKST PSSGGGPSED
KRFSVVDMAA LGGVLGALLL LALLGLAVLV HKHYGPRLKC CCGKAPEPQP QGFDNQAFLP
DHKANWAPVP SPTHDPKPAE APMPAEPAPP GPASPGGAPE PPAAARAGGS PTAVRSILTK
ERRPEGGYKA VWFGEDIGTE ADVVVLNAPT LDVDGASDSG SGDEGEGAGR GGGPYDAPGG
DDSYI


Related products :

Catalog number Product name Quantity
EIAAB06490 Cadherin-related family member 5,Cdhr5,Mouse,Mucdhl,Mucin and cadherin-like protein,Mupcdh,Mu-protocadherin,Mus musculus
EIAAB06491 Cadherin-related family member 5,Cdhr5,GP100,Mucdhl,Mucin and cadherin-like protein,Mupcdh,Mu-protocadherin,Rat,Rattus norvegicus
EIAAB06489 Cadherin-related family member 5,CDHR5,Homo sapiens,Human,MUCDHL,Mucin and cadherin-like protein,MUPCDH,Mu-protocadherin,UNQ2781_PRO7168
EIAAB06480 Cadherin-related family member 1,Cdhr1,Kiaa1775,MT-protocadherin,Pcdh21,Photoreceptor cadherin,prCAD,Prcad,Protocadherin-21,Rat,Rattus norvegicus
EIAAB06485 Cadherin-related family member 2,CDHR2,Homo sapiens,Human,PCDH24,PCLKC,PC-LKC,Protocadherin LKC,Protocadherin-24
EIAAB14451 Cadherin family member 7,Cadherin-related tumor suppressor homolog,CDHF7,FAT,FAT1,Homo sapiens,Human,Protein fat homolog,Protocadherin Fat 1
EIAAB06482 Bos taurus,Bovine,Cadherin-related family member 1,CDHR1,PCDH21,Photoreceptor cadherin,prCAD,PRCAD,Protocadherin-21
EIAAB06483 Cadherin-related family member 1,Cdhr1,Kiaa1775,Mouse,Mus musculus,Pcdh21,Photoreceptor cadherin,prCAD,Prcad,Protocadherin-21
EIAAB06484 Cadherin-related family member 1,CDHR1,Homo sapiens,Human,KIAA1775,PCDH21,Photoreceptor cadherin,prCAD,PRCAD,Protocadherin-21
EIAAB14459 Cadherin family member 14,CDHF14,FAT tumor suppressor homolog 4,FAT4,FATJ,Fat-like cadherin protein FAT-J,hFat4,Homo sapiens,Human,Nbla00548,Protocadherin Fat 4
EIAAB06481 Cadherin-related family member 1,CDHR1,Chicken,Gallus gallus,PCDH21,Photoreceptor cadherin,prCAD,PRCAD,Protocadherin-21
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
EIAAB30053 Cadherin-19,Cadherin-25,CDH19,CDH25,DCHS1,FIB1,Fibroblast cadherin-1,Homo sapiens,Human,KIAA1773,PCDH16,Protein dachsous homolog 1,Protocadherin-16
26-204 PCDH12 belongs to the protocadherin protein family, a subfamily of the cadherin superfamily. It consists of an extracellular domain containing 6 cadherin repeats, a transmembrane domain and a cytoplas 0.05 mg
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
E1615h ELISA Cadherin-like protein 1,Homo sapiens,Human,PC42,PCDH1,Protocadherin-1,Protocadherin-42 96T
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
EIAAB06486 Cadherin-like protein 28,Cadherin-related family member 3,Cdh28,Cdhr3,Mouse,Mus musculus
EIAAB30049 Homo sapiens,Human,PCDH12,Protocadherin-12,UNQ395_PRO731,Vascular cadherin-2,Vascular endothelial cadherin-2,VE-cad-2,VE-cadherin-2
EIAAB06487 Cadherin-like protein 28,Cadherin-related family member 3,CDH28,CDHR3,Homo sapiens,Human
EIAAB14456 Cadherin family member 15,CDHF15,FAT tumor suppressor homolog 3,FAT3,hFat3,Homo sapiens,Human,KIAA1989,Protocadherin Fat 3
EIAAB06488 Cadherin-like protein 29,Cadherin-related family member 4,CDH29,CDHR4,Homo sapiens,Human,UNQ9392_PRO34300
EIAAB30050 Mouse,Mus musculus,Pcdh12,Protocadherin-12,Vascular cadherin-2,Vascular endothelial cadherin-2,VE-cad-2,VE-cadherin-2
EIAAB14452 Cadherin family member 8,CDHF8,FAT2,hFat2,Homo sapiens,Human,KIAA0811,MEGF1,Multiple EGF-like domains protein 1,Multiple epidermal growth factor-like domains protein 1,Protocadherin Fat 2


 

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