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

Protocadherin Fat 1 (Cadherin family member 7) (Cadherin-related tumor suppressor homolog) (Protein fat homolog) [Cleaved into: Protocadherin Fat 1, nuclear form]

 FAT1_HUMAN              Reviewed;        4588 AA.
Q14517;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
31-MAY-2011, sequence version 2.
28-FEB-2018, entry version 174.
RecName: Full=Protocadherin Fat 1;
AltName: Full=Cadherin family member 7;
AltName: Full=Cadherin-related tumor suppressor homolog;
AltName: Full=Protein fat homolog;
Contains:
RecName: Full=Protocadherin Fat 1, nuclear form;
Flags: Precursor;
Name=FAT1; Synonyms=CDHF7, FAT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lymphocyte;
PubMed=8586420; DOI=10.1006/geno.1995.9884;
Dunne J., Hanby A.M., Poulsom R., Jones T.A., Sheer D., Chin W.G.,
Da S.M., Zhao Q., Beverley P.C.L., Owen M.J.;
"Molecular cloning and tissue expression of FAT, the human homologue
of the Drosophila fat gene that is located on chromosome 4q34-q35 and
encodes a putative adhesion molecule.";
Genomics 30:207-223(1995).
[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]
SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
PubMed=15922730; DOI=10.1016/j.yexcr.2005.03.006;
Magg T., Schreiner D., Solis G.P., Bade E.G., Hofer H.W.;
"Processing of the human protocadherin Fat1 and translocation of its
cytoplasmic domain to the nucleus.";
Exp. Cell Res. 307:100-108(2005).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[5]
INTERACTION WITH ATN1 AND RERE.
PubMed=19131340; DOI=10.1074/jbc.M809333200;
Hou R., Sibinga N.E.;
"Atrophin proteins interact with the Fat1 cadherin and regulate
migration and orientation in vascular smooth muscle cells.";
J. Biol. Chem. 284:6955-6965(2009).
[6]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3415; ASN-3422 AND
ASN-3716.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-3716.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
VARIANTS SER-902; VAL-1393 AND SER-3732.
PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179;
Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G.,
Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.;
"Homozygous missense mutation in the LMAN2L gene segregates with
intellectual disability in a large consanguineous Pakistani family.";
J. Med. Genet. 53:138-144(2016).
-!- FUNCTION: Plays an essential role for cellular polarization,
directed cell migration and modulating cell-cell contact.
{ECO:0000250}.
-!- SUBUNIT: Interacts (via the C-terminus 4300-4400 AA) with ATN1.
Interacts with RERE. Interacts (via EVH1 domains) with ENAH (By
similarity). Interacts (via cytoplasmic domain) with CTNNB1 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q8N8S7:ENAH; NbExp=2; IntAct=EBI-1171918, EBI-2834410;
Q9NSC5:HOMER3; NbExp=4; IntAct=EBI-1171918, EBI-748420;
Q99JP6:Homer3 (xeno); NbExp=2; IntAct=EBI-1171918, EBI-6272061;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15922730};
Single-pass type I membrane protein {ECO:0000269|PubMed:15922730}.
Nucleus {ECO:0000269|PubMed:15922730}. Cytoplasm, perinuclear
region {ECO:0000269|PubMed:15922730}.
-!- TISSUE SPECIFICITY: Expressed in many epithelial and some
endothelial and smooth muscle cells.
-!- DOMAIN: A PTB-like motif (DNXYH sequence) is required for the
targeting to the leading edge. This motif represents a minimal
protein-protein interaction core motif that is not regulated by
tyrosine phosphorylation (By similarity). {ECO:0000250}.
-!- PTM: Undergoes proteolytic cleavage. The extracellular domain is
cleaved off and the cytoplasmic domain (about 400 AA) shuttles to
the nucleus. {ECO:0000269|PubMed:15922730}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FAT1ID40533ch4q35.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X87241; CAA60685.1; -; mRNA.
EMBL; AC107050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC110761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS47177.1; -.
RefSeq; NP_005236.2; NM_005245.3.
RefSeq; XP_006714202.1; XM_006714139.2.
UniGene; Hs.481371; -.
ProteinModelPortal; Q14517; -.
SMR; Q14517; -.
BioGrid; 108489; 52.
IntAct; Q14517; 24.
MINT; Q14517; -.
STRING; 9606.ENSP00000406229; -.
iPTMnet; Q14517; -.
PhosphoSitePlus; Q14517; -.
BioMuta; FAT1; -.
DMDM; 334302792; -.
EPD; Q14517; -.
MaxQB; Q14517; -.
PaxDb; Q14517; -.
PeptideAtlas; Q14517; -.
PRIDE; Q14517; -.
Ensembl; ENST00000441802; ENSP00000406229; ENSG00000083857.
GeneID; 2195; -.
KEGG; hsa:2195; -.
UCSC; uc003izf.4; human.
CTD; 2195; -.
DisGeNET; 2195; -.
EuPathDB; HostDB:ENSG00000083857.13; -.
GeneCards; FAT1; -.
HGNC; HGNC:3595; FAT1.
HPA; HPA001869; -.
HPA; HPA023882; -.
MIM; 600976; gene.
neXtProt; NX_Q14517; -.
OpenTargets; ENSG00000083857; -.
PharmGKB; PA164719952; -.
eggNOG; KOG1219; Eukaryota.
eggNOG; ENOG410XPEI; LUCA.
GeneTree; ENSGT00760000118805; -.
HOGENOM; HOG000046499; -.
HOVERGEN; HBG005641; -.
InParanoid; Q14517; -.
KO; K16506; -.
TreeFam; TF316403; -.
ChiTaRS; FAT1; human.
GeneWiki; FAT_(gene); -.
GenomeRNAi; 2195; -.
PRO; PR:Q14517; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000083857; -.
CleanEx; HS_FAT1; -.
ExpressionAtlas; Q14517; baseline and differential.
Genevisible; Q14517; HS.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0030175; C:filopodium; IEA:Ensembl.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0007015; P:actin filament organization; ISS:UniProtKB.
GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0007163; P:establishment or maintenance of cell polarity; ISS:UniProtKB.
GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
InterPro; IPR002126; Cadherin.
InterPro; IPR015919; Cadherin-like.
InterPro; IPR020894; Cadherin_CS.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR001791; Laminin_G.
Pfam; PF00028; Cadherin; 29.
Pfam; PF00008; EGF; 2.
Pfam; PF02210; Laminin_G_2; 1.
PRINTS; PR00205; CADHERIN.
SMART; SM00112; CA; 34.
SMART; SM00181; EGF; 5.
SMART; SM00179; EGF_CA; 4.
SMART; SM00282; LamG; 1.
SUPFAM; SSF49313; SSF49313; 33.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00232; CADHERIN_1; 17.
PROSITE; PS50268; CADHERIN_2; 33.
PROSITE; PS00022; EGF_1; 4.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 5.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS50025; LAM_G_DOMAIN; 1.
1: Evidence at protein level;
Calcium; Cell adhesion; Cell membrane; Complete proteome; Cytoplasm;
Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Nucleus;
Polymorphism; Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 4588 Protocadherin Fat 1.
/FTId=PRO_0000004017.
CHAIN ? 4588 Protocadherin Fat 1, nuclear form.
/FTId=PRO_0000408559.
TOPO_DOM 22 4181 Extracellular. {ECO:0000255}.
TRANSMEM 4182 4202 Helical. {ECO:0000255}.
TOPO_DOM 4203 4588 Cytoplasmic. {ECO:0000255}.
DOMAIN 35 149 Cadherin 1. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 150 257 Cadherin 2. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 368 463 Cadherin 3. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 464 569 Cadherin 4. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 570 673 Cadherin 5. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 718 822 Cadherin 6. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 823 927 Cadherin 7. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 928 1034 Cadherin 8. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1035 1139 Cadherin 9. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1140 1245 Cadherin 10. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1246 1357 Cadherin 11. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1359 1456 Cadherin 12. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1457 1562 Cadherin 13. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1563 1667 Cadherin 14. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1668 1765 Cadherin 15. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1766 1879 Cadherin 16. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1880 1979 Cadherin 17. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 1980 2081 Cadherin 18. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2082 2182 Cadherin 19. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2183 2283 Cadherin 20. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2284 2390 Cadherin 21. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2391 2492 Cadherin 22. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2493 2596 Cadherin 23. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2597 2703 Cadherin 24. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2704 2809 Cadherin 25. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2810 2918 Cadherin 26. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 2919 3023 Cadherin 27. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3024 3125 Cadherin 28. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3126 3230 Cadherin 29. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3231 3335 Cadherin 30. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3336 3440 Cadherin 31. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3441 3545 Cadherin 32. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3546 3647 Cadherin 33. {ECO:0000255|PROSITE-
ProRule:PRU00043}.
DOMAIN 3790 3827 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3829 4009 Laminin G-like. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 4013 4050 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4052 4088 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4089 4125 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4127 4163 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
MOTIF 4204 4214 Nuclear localization signal.
{ECO:0000255}.
MOTIF 4378 4382 PTB-like motif. {ECO:0000250}.
CARBOHYD 40 40 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 333 333 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 660 660 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 740 740 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 791 791 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 998 998 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1426 1426 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1551 1551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1748 1748 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1864 1864 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1902 1902 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1940 1940 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1991 1991 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2325 2325 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2464 2464 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3324 3324 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3415 3415 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 3422 3422 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 3444 3444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3613 3613 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3640 3640 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3716 3716 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 4152 4152 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 3794 3805 {ECO:0000250}.
DISULFID 3799 3816 {ECO:0000250}.
DISULFID 3818 3826 {ECO:0000250}.
DISULFID 3976 4009 {ECO:0000250}.
DISULFID 4017 4028 {ECO:0000250}.
DISULFID 4022 4038 {ECO:0000250}.
DISULFID 4040 4049 {ECO:0000250}.
DISULFID 4056 4067 {ECO:0000250}.
DISULFID 4061 4076 {ECO:0000250}.
DISULFID 4078 4087 {ECO:0000250}.
DISULFID 4093 4104 {ECO:0000250}.
DISULFID 4098 4113 {ECO:0000250}.
DISULFID 4115 4124 {ECO:0000250}.
DISULFID 4131 4142 {ECO:0000250}.
DISULFID 4136 4151 {ECO:0000250}.
DISULFID 4153 4162 {ECO:0000250}.
VARIANT 131 131 A -> V (in dbSNP:rs3733415).
/FTId=VAR_055590.
VARIANT 902 902 R -> S (in dbSNP:rs555992573).
{ECO:0000269|PubMed:26566883}.
/FTId=VAR_076441.
VARIANT 1330 1330 N -> S (in dbSNP:rs874111).
/FTId=VAR_055591.
VARIANT 1393 1393 I -> V (in dbSNP:rs753226094).
{ECO:0000269|PubMed:26566883}.
/FTId=VAR_076442.
VARIANT 1564 1564 A -> T (in dbSNP:rs2304867).
/FTId=VAR_055592.
VARIANT 1605 1605 N -> D (in dbSNP:rs6836935).
/FTId=VAR_055593.
VARIANT 3732 3732 N -> S (in dbSNP:rs373241719).
{ECO:0000269|PubMed:26566883}.
/FTId=VAR_076443.
VARIANT 3800 3800 P -> H (in dbSNP:rs11731738).
/FTId=VAR_055594.
CONFLICT 322 322 G -> D (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 404 404 S -> R (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 482 482 V -> I (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 614 614 F -> L (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 862 862 V -> L (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 1064 1064 R -> G (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 1273 1273 H -> R (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 1351 1351 P -> Q (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 1526 1529 HQHT -> SPAH (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 1604 1604 G -> GNIG (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 2006 2006 N -> S (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 2054 2054 T -> I (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 2385 2385 D -> G (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 2618 2619 VL -> S (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 2718 2718 I -> V (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 3113 3113 L -> V (in Ref. 1; CAA60685).
{ECO:0000305}.
CONFLICT 4059 4059 K -> N (in Ref. 1; CAA60685).
{ECO:0000305}.
SEQUENCE 4588 AA; 506273 MW; 1896223E46E3B892 CRC64;
MGRHLALLLL LLLLFQHFGD SDGSQRLEQT PLQFTHLEYN VTVQENSAAK TYVGHPVKMG
VYITHPAWEV RYKIVSGDSE NLFKAEEYIL GDFCFLRIRT KGGNTAILNR EVKDHYTLIV
KALEKNTNVE ARTKVRVQVL DTNDLRPLFS PTSYSVSLPE NTAIRTSIAR VSATDADIGT
NGEFYYSFKD RTDMFAIHPT SGVIVLTGRL DYLETKLYEM EILAADRGMK LYGSSGISSM
AKLTVHIEQA NECAPVITAV TLSPSELDRD PAYAIVTVDD CDQGANGDIA SLSIVAGDLL
QQFRTVRSFP GSKEYKVKAI GGIDWDSHPF GYNLTLQAKD KGTPPQFSSV KVIHVTSPQF
KAGPVKFEKD VYRAEISEFA PPNTPVVMVK AIPAYSHLRY VFKSTPGKAK FSLNYNTGLI
SILEPVKRQQ AAHFELEVTT SDRKASTKVL VKVLGANSNP PEFTQTAYKA AFDENVPIGT
TVMSLSAVDP DEGENGYVTY SIANLNHVPF AIDHFTGAVS TSENLDYELM PRVYTLRIRA
SDWGLPYRRE VEVLATITLN NLNDNTPLFE KINCEGTIPR DLGVGEQITT VSAIDADELQ
LVQYQIEAGN ELDFFSLNPN SGVLSLKRSL MDGLGAKVSF HSLRITATDG ENFATPLYIN
ITVAASHKLV NLQCEETGVA KMLAEKLLQA NKLHNQGEVE DIFFDSHSVN AHIPQFRSTL
PTGIQVKENQ PVGSSVIFMN STDLDTGFNG KLVYAVSGGN EDSCFMIDME TGMLKILSPL
DRETTDKYTL NITVYDLGIP QKAAWRLLHV VVVDANDNPP EFLQESYFVE VSEDKEVHSE
IIQVEATDKD LGPNGHVTYS IVTDTDTFSI DSVTGVVNIA RPLDRELQHE HSLKIEARDQ
AREEPQLFST VVVKVSLEDV NDNPPTFIPP NYRVKVREDL PEGTVIMWLE AHDPDLGQSG
QVRYSLLDHG EGNFDVDKLS GAVRIVQQLD FEKKQVYNLT VRAKDKGKPV SLSSTCYVEV
EVVDVNENLH PPVFSSFVEK GTVKEDAPVG SLVMTVSAHD EDARRDGEIR YSIRDGSGVG
VFKIGEETGV IETSDRLDRE STSHYWLTVF ATDQGVVPLS SFIEIYIEVE DVNDNAPQTS
EPVYYPEIME NSPKDVSVVQ IEAFDPDSSS NDKLMYKITS GNPQGFFSIH PKTGLITTTS
RKLDREQQDE HILEVTVTDN GSPPKSTIAR VIVKILDEND NKPQFLQKFY KIRLPEREKP
DRERNARREP LYHVIATDKD EGPNAEISYS IEDGNEHGKF FIEPKTGVVS SKRFSAAGEY
DILSIKAVDN GRPQKSSTTR LHIEWISKPK PSLEPISFEE SFFTFTVMES DPVAHMIGVI
SVEPPGIPLW FDITGGNYDS HFDVDKGTGT IIVAKPLDAE QKSNYNLTVE ATDGTTTILT
QVFIKVIDTN DHRPQFSTSK YEVVIPEDTA PETEILQISA VDQDEKNKLI YTLQSSRDPL
SLKKFRLDPA TGSLYTSEKL DHEAVHQHTL TVMVRDQDVP VKRNFARIVV NVSDTNDHAP
WFTASSYKGR VYESAAVGSV VLQVTALDKD KGKNAEVLYS IESGNIGNSF MIDPVLGSIK
TAKELDRSNQ AEYDLMVKAT DKGSPPMSEI TSVRIFVTIA DNASPKFTSK EYSVELSETV
SIGSFVGMVT AHSQSSVVYE IKDGNTGDAF DINPHSGTII TQKALDFETL PIYTLIIQGT
NMAGLSTNTT VLVHLQDEND NAPVFMQAEY TGLISESASI NSVVLTDRNV PLVIRAADAD
KDSNALLVYH IVEPSVHTYF AIDSSTGAIH TVLSLDYEET SIFHFTVQVH DMGTPRLFAE
YAANVTVHVI DINDCPPVFA KPLYEASLLL PTYKGVKVIT VNATDADSSA FSQLIYSITE
GNIGEKFSMD YKTGALTVQN TTQLRSRYEL TVRASDGRFA GLTSVKINVK ESKESHLKFT
QDVYSAVVKE NSTEAETLAV ITAIGNPINE PLFYHILNPD RRFKISRTSG VLSTTGTPFD
REQQEAFDVV VEVTEEHKPS AVAHVVVKVI VEDQNDNAPV FVNLPYYAVV KVDTEVGHVI
RYVTAVDRDS GRNGEVHYYL KEHHEHFQIG PLGEISLKKQ FELDTLNKEY LVTVVAKDGG
NPAFSAEVIV PITVMNKAMP VFEKPFYSAE IAESIQVHSP VVHVQANSPE GLKVFYSITD
GDPFSQFTIN FNTGVINVIA PLDFEAHPAY KLSIRATDSL TGAHAEVFVD IIVDDINDNP
PVFAQQSYAV TLSEASVIGT SVVQVRATDS DSEPNRGISY QMFGNHSKSH DHFHVDSSTG
LISLLRTLDY EQSRQHTIFV RAVDGGMPTL SSDVIVTVDV TDLNDNPPLF EQQIYEARIS
EHAPHGHFVT CVKAYDADSS DIDKLQYSIL SGNDHKHFVI DSATGIITLS NLHRHALKPF
YSLNLSVSDG VFRSSTQVHV TVIGGNLHSP AFLQNEYEVE LAENAPLHTL VMEVKTTDGD
SGIYGHVTYH IVNDFAKDRF YINERGQIFT LEKLDRETPA EKVISVRLMA KDAGGKVAFC
TVNVILTDDN DNAPQFRATK YEVNIGSSAA KGTSVVKVLA SDADEGSNAD ITYAIEADSE
SVKENLEINK LSGVITTKES LIGLENEFFT FFVRAVDNGS PSKESVVLVY VKILPPEMQL
PKFSEPFYTF TVSEDVPIGT EIDLIRAEHS GTVLYSLVKG NTPESNRDES FVIDRQSGRL
KLEKSLDHET TKWYQFSILA RCTQDDHEMV ASVDVSIQVK DANDNSPVFE SSPYEAFIVE
NLPGGSRVIQ IRASDADSGT NGQVMYSLDQ SQSVEVIESF AINMETGWIT TLKELDHEKR
DNYQIKVVAS DHGEKIQLSS TAIVDVTVTD VNDSPPRFTA EIYKGTVSED DPQGGVIAIL
STTDADSEEI NRQVTYFITG GDPLGQFAVE TIQNEWKVYV KKPLDREKRD NYLLTITATD
GTFSSKAIVE VKVLDANDNS PVCEKTLYSD TIPEDVLPGK LIMQISATDA DIRSNAEITY
TLLGSGAEKF KLNPDTGELK TSTPLDREEQ AVYHLLVRAT DGGGRFCQAS IVLTLEDVND
NAPEFSADPY AITVFENTEP GTLLTRVQAT DADAGLNRKI LYSLIDSADG QFSINELSGI
IQLEKPLDRE LQAVYTLSLK AVDQGLPRRL TATGTVIVSV LDINDNPPVF EYREYGATVS
EDILVGTEVL QVYAASRDIE ANAEITYSII SGNEHGKFSI DSKTGAVFII ENLDYESSHE
YYLTVEATDG GTPSLSDVAT VNVNVTDIND NTPVFSQDTY TTVISEDAVL EQSVITVMAD
DADGPSNSHI HYSIIDGNQG SSFTIDPVRG EVKVTKLLDR ETISGYTLTV QASDNGSPPR
VNTTTVNIDV SDVNDNAPVF SRGNYSVIIQ ENKPVGFSVL QLVVTDEDSS HNGPPFFFTI
VTGNDEKAFE VNPQGVLLTS SAIKRKEKDH YLLQVKVADN GKPQLSSLTY IDIRVIEESI
YPPAILPLEI FITSSGEEYS GGVIGKIHAT DQDVYDTLTY SLDPQMDNLF SVSSTGGKLI
AHKKLDIGQY LLNVSVTDGK FTTVADITVH IRQVTQEMLN HTIAIRFANL TPEEFVGDYW
RNFQRALRNI LGVRRNDIQI VSLQSSEPHP HLDVLLFVEK PGSAQISTKQ LLHKINSSVT
DIEEIIGVRI LNVFQKLCAG LDCPWKFCDE KVSVDESVMS THSTARLSFV TPRHHRAAVC
LCKEGRCPPV HHGCEDDPCP EGSECVSDPW EEKHTCVCPS GRFGQCPGSS SMTLTGNSYV
KYRLTENENK LEMKLTMRLR TYSTHAVVMY ARGTDYSILE IHHGRLQYKF DCGSGPGIVS
VQSIQVNDGQ WHAVALEVNG NYARLVLDQV HTASGTAPGT LKTLNLDNYV FFGGHIRQQG
TRHGRSPQVG NGFRGCMDSI YLNGQELPLN SKPRSYAHIE ESVDVSPGCF LTATEDCASN
PCQNGGVCNP SPAGGYYCKC SALYIGTHCE ISVNPCSSKP CLYGGTCVVD NGGFVCQCRG
LYTGQRCQLS PYCKDEPCKN GGTCFDSLDG AVCQCDSGFR GERCQSDIDE CSGNPCLHGA
LCENTHGSYH CNCSHEYRGR HCEDAAPNQY VSTPWNIGLA EGIGIVVFVA GIFLLVVVFV
LCRKMISRKK KHQAEPKDKH LGPATAFLQR PYFDSKLNKN IYSDIPPQVP VRPISYTPSI
PSDSRNNLDR NSFEGSAIPE HPEFSTFNPE SVHGHRKAVA VCSVAPNLPP PPPSNSPSDS
DSIQKPSWDF DYDTKVVDLD PCLSKKPLEE KPSQPYSARE SLSEVQSLSS FQSESCDDNG
YHWDTSDWMP SVPLPDIQEF PNYEVIDEQT PLYSADPNAI DTDYYPGGYD IESDFPPPPE
DFPAADELPP LPPEFSNQFE SIHPPRDMPA AGSLGSSSRN RQRFNLNQYL PNFYPLDMSE
PQTKGTGENS TCREPHAPYP PGYQRHFEAP AVESMPMSVY ASTASCSDVS ACCEVESEVM
MSDYESGDDG HFEEVTIPPL DSQQHTEV


Related products :

Catalog number Product name Quantity
EIAAB14451 Cadherin family member 7,Cadherin-related tumor suppressor homolog,CDHF7,FAT,FAT1,Homo sapiens,Human,Protein fat homolog,Protocadherin Fat 1
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
EIAAB14456 Cadherin family member 15,CDHF15,FAT tumor suppressor homolog 3,FAT3,hFat3,Homo sapiens,Human,KIAA1989,Protocadherin Fat 3
EIAAB14458 FAT tumor suppressor homolog 4,Fat4,Fatj,Fat-like cadherin protein FAT-J,Mouse,Mus musculus,Protocadherin Fat 4
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
EIAAB06490 Cadherin-related family member 5,Cdhr5,Mouse,Mucdhl,Mucin and cadherin-like protein,Mupcdh,Mu-protocadherin,Mus musculus
EIAAB06485 Cadherin-related family member 2,CDHR2,Homo sapiens,Human,PCDH24,PCLKC,PC-LKC,Protocadherin LKC,Protocadherin-24
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
EIAAB30053 Cadherin-19,Cadherin-25,CDH19,CDH25,DCHS1,FIB1,Fibroblast cadherin-1,Homo sapiens,Human,KIAA1773,PCDH16,Protein dachsous homolog 1,Protocadherin-16
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
EIAAB06481 Cadherin-related family member 1,CDHR1,Chicken,Gallus gallus,PCDH21,Photoreceptor cadherin,prCAD,PRCAD,Protocadherin-21
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
BPA1053 FAT tumor suppressor homolog 4 _ Protocadherin Fat 4 Polyclonal Antibodie 100 μg
BPA1053 FAT tumor suppressor homolog 4 Protocadherin Fat 4 Polyclonal Antibodie 100 μg
E1615h ELISA kit Cadherin-like protein 1,Homo sapiens,Human,PC42,PCDH1,Protocadherin-1,Protocadherin-42 96T
U1615h CLIA 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
EIAAB14457 FAT tumor suppressor homolog 3,Fat3,Protocadherin Fat 3,Rat,Rattus norvegicus
BPA1053 FAT tumor suppressor homolog 4 _ Protocadherin Fat 4, Polyclonal primary Antibodies 100 μg
'BPA1053 FAT tumor suppressor homolog 4 Protocadherin Fat 4 IgG antibody Ab host: Rabbit 0.1 mg
EIAAB06750 Cadherin EGF LAG seven-pass G-type receptor 2,Cadherin family member 10,CDHF10,CELSR2,EGFL2,EGF-like protein 2,Epidermal growth factor-like protein 2,Flamingo homolog 3,Homo sapiens,Human,KIAA0279,MEG


 

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