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Protein crumbs homolog 2 (Crumbs-like protein 2)

 CRUM2_HUMAN             Reviewed;        1285 AA.
Q5IJ48; A2A3N4; Q0QD46; Q5JS41; Q5JS43; Q6ZTA9; Q6ZWI6;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-APR-2018, entry version 131.
RecName: Full=Protein crumbs homolog 2 {ECO:0000305};
AltName: Full=Crumbs-like protein 2;
Flags: Precursor;
Name=CRB2 {ECO:0000312|HGNC:HGNC:18688};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANTS LEU-46; LEU-97; LEU-116; THR-145; ALA-159; ASP-187; THR-351;
GLN-534; TRP-610; ALA-709; GLN-746 AND MET-1110.
PubMed=15851977;
van den Hurk J.A.J.M., Rashbass P., Roepman R., Davis J.,
Voesenek K.E.J., Arends M.L., Zonneveld M.N., van Roekel M.H.G.,
Cameron K., Rohrschneider K., Heckenlively J.R., Koenekoop R.K.,
Hoyng C.B., Cremers F.P.M., den Hollander A.I.;
"Characterization of the crumbs homolog 2 (CRB2) gene and analysis of
its role in retinitis pigmentosa and Leber congenital amaurosis.";
Mol. Vis. 11:263-273(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
VARIANTS ASN-90; THR-145; ALA-159 AND ALA-709.
TISSUE=Cerebellum;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
TISSUE=Retina;
Roni V., Carpio R., Wissinger B.;
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[5]
INVOLVEMENT IN FSGS9, VARIANTS FSGS9 SER-620; CYS-628; SER-629 AND
GLN-1249, AND CHARACTERIZATION OF VARIANTS FSGS9 SER-620 AND SER-629.
PubMed=25557779; DOI=10.1016/j.ajhg.2014.11.014;
Ebarasi L., Ashraf S., Bierzynska A., Gee H.Y., McCarthy H.J.,
Lovric S., Sadowski C.E., Pabst W., Vega-Warner V., Fang H.,
Koziell A., Simpson M.A., Dursun I., Serdaroglu E., Levy S.,
Saleem M.A., Hildebrandt F., Majumdar A.;
"Defects of CRB2 cause steroid-resistant nephrotic syndrome.";
Am. J. Hum. Genet. 96:153-161(2015).
[6]
INVOLVEMENT IN VMCKD, AND VARIANTS VMCKD TRP-633; ALA-643 AND LYS-800.
PubMed=25557780; DOI=10.1016/j.ajhg.2014.11.013;
Slavotinek A., Kaylor J., Pierce H., Cahr M., DeWard S.J.,
Schneidman-Duhovny D., Alsadah A., Salem F., Schmajuk G., Mehta L.;
"CRB2 mutations produce a phenotype resembling congenital nephrosis,
Finnish type, with cerebral ventriculomegaly and raised alpha-
fetoprotein.";
Am. J. Hum. Genet. 96:162-169(2015).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 4-9 IN COMPLEX WITH DYRK1A.
Structural genomics consortium (SGC);
"The crystal structure of the human dual specificity tyrosine-
phosphorylation-regulated kinase 1A.";
Submitted (AUG-2009) to the PDB data bank.
-!- FUNCTION: Apical polarity protein that plays a central role during
the epithelial-to-mesenchymal transition (EMT) at gastrulation,
when newly specified mesodermal cells move inside the embryo. Acts
by promoting cell ingression, the process by which cells leave the
epithelial epiblast and move inside the embryo to form a new
tissue layer. The anisotropic distribution of CRB2 and
MYH10/myosin-IIB at cell edges define which cells will ingress:
cells with high apical CRB2 are probably extruded from the
epiblast by neighboring cells with high levels of apical
MYH10/myosin-IIB. Also required for maintenance of the apical
polarity complex during development of the cortex.
{ECO:0000250|UniProtKB:Q80YA8}.
-!- SUBCELLULAR LOCATION: Isoform 1: Apical cell membrane
{ECO:0000250|UniProtKB:Q80YA8}; Single-pass type I membrane
protein {ECO:0000255}. Note=O-glucosylation is required for
localization at the apical plasma membrane.
{ECO:0000250|UniProtKB:Q80YA8}.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted {ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q5IJ48-1; Sequence=Displayed;
Name=2;
IsoId=Q5IJ48-2; Sequence=VSP_014739, VSP_014740;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q5IJ48-3; Sequence=VSP_014737, VSP_014738;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in retina, fetal eye and brain. Also
expressed in kidney, ARPE-19 and RPE/choroid cell lines, and at
low levels in lung, placenta, and heart.
{ECO:0000269|PubMed:15851977}.
-!- PTM: O-glucosylated by POGLUT1 at Ser-267; consists of an O-
glucose trisaccharide, in which the O-glucose is elongated by the
addition of two xylose residues. O-glucosylation is required for
localization at the plasma membrane.
{ECO:0000250|UniProtKB:Q80YA8}.
-!- DISEASE: Focal segmental glomerulosclerosis 9 (FSGS9)
[MIM:616220]: A renal pathology defined by the presence of
segmental sclerosis in glomeruli and resulting in proteinuria,
reduced glomerular filtration rate and progressive decline in
renal function. Renal insufficiency often progresses to end-stage
renal disease, a highly morbid state requiring either dialysis
therapy or kidney transplantation. {ECO:0000269|PubMed:25557779}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Ventriculomegaly with cystic kidney disease (VMCKD)
[MIM:219730]: A severe autosomal recessive developmental disorder
manifesting in utero. It is characterized by cerebral
ventriculomegaly, echogenic kidneys, microscopic renal tubular
cysts and findings of congenital nephrosis.
{ECO:0000269|PubMed:25557780}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the Crumbs protein family. {ECO:0000305}.
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EMBL; AY720432; AAU14134.1; -; mRNA.
EMBL; AK123000; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK126775; BAC86684.1; -; mRNA.
EMBL; AL445489; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL365504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; DQ426866; ABD90532.1; -; mRNA.
CCDS; CCDS6852.2; -. [Q5IJ48-1]
RefSeq; NP_775960.4; NM_173689.6. [Q5IJ48-1]
RefSeq; XP_005251991.1; XM_005251934.2. [Q5IJ48-3]
UniGene; Hs.568340; -.
UniGene; Hs.710092; -.
PDB; 2WO6; X-ray; 2.50 A; C=4-9.
PDBsum; 2WO6; -.
ProteinModelPortal; Q5IJ48; -.
SMR; Q5IJ48; -.
BioGrid; 130332; 2.
STRING; 9606.ENSP00000362734; -.
iPTMnet; Q5IJ48; -.
PhosphoSitePlus; Q5IJ48; -.
BioMuta; CRB2; -.
DMDM; 116241316; -.
EPD; Q5IJ48; -.
PaxDb; Q5IJ48; -.
PeptideAtlas; Q5IJ48; -.
PRIDE; Q5IJ48; -.
Ensembl; ENST00000359999; ENSP00000353092; ENSG00000148204. [Q5IJ48-2]
Ensembl; ENST00000373631; ENSP00000362734; ENSG00000148204. [Q5IJ48-1]
Ensembl; ENST00000460253; ENSP00000435279; ENSG00000148204. [Q5IJ48-3]
GeneID; 286204; -.
KEGG; hsa:286204; -.
UCSC; uc004bnw.3; human. [Q5IJ48-1]
CTD; 286204; -.
DisGeNET; 286204; -.
EuPathDB; HostDB:ENSG00000148204.11; -.
GeneCards; CRB2; -.
H-InvDB; HIX0008365; -.
HGNC; HGNC:18688; CRB2.
HPA; HPA043674; -.
MalaCards; CRB2; -.
MIM; 219730; phenotype.
MIM; 609720; gene.
MIM; 616220; phenotype.
neXtProt; NX_Q5IJ48; -.
OpenTargets; ENSG00000148204; -.
PharmGKB; PA134910460; -.
eggNOG; KOG1217; Eukaryota.
eggNOG; ENOG410XP6K; LUCA.
GeneTree; ENSGT00910000144018; -.
HOVERGEN; HBG080001; -.
InParanoid; Q5IJ48; -.
KO; K16681; -.
OMA; PFCGQNT; -.
OrthoDB; EOG091G00O4; -.
PhylomeDB; Q5IJ48; -.
TreeFam; TF316224; -.
EvolutionaryTrace; Q5IJ48; -.
GenomeRNAi; 286204; -.
PRO; PR:Q5IJ48; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000148204; -.
CleanEx; HS_CRB2; -.
Genevisible; Q5IJ48; HS.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045121; C:membrane raft; IC:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0019899; F:enzyme binding; IMP:UniProtKB.
GO; GO:0072358; P:cardiovascular system development; ISS:UniProtKB.
GO; GO:0055111; P:ingression involved in gastrulation with mouth forming second; ISS:UniProtKB.
GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; ISS:UniProtKB.
GO; GO:0001707; P:mesoderm formation; ISS:UniProtKB.
GO; GO:0010951; P:negative regulation of endopeptidase activity; IMP:UniProtKB.
GO; GO:0014028; P:notochord formation; ISS:UniProtKB.
GO; GO:0030513; P:positive regulation of BMP signaling pathway; ISS:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0010470; P:regulation of gastrulation; ISS:UniProtKB.
GO; GO:0001756; P:somitogenesis; ISS:UniProtKB.
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; PF00008; EGF; 9.
Pfam; PF12661; hEGF; 1.
Pfam; PF02210; Laminin_G_2; 1.
SMART; SM00181; EGF; 15.
SMART; SM00179; EGF_CA; 12.
SMART; SM00282; LamG; 3.
SUPFAM; SSF49899; SSF49899; 3.
PROSITE; PS00010; ASX_HYDROXYL; 7.
PROSITE; PS00022; EGF_1; 14.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 15.
PROSITE; PS01187; EGF_CA; 5.
PROSITE; PS50025; LAM_G_DOMAIN; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell membrane;
Complete proteome; Developmental protein; Disease mutation;
Disulfide bond; EGF-like domain; Gastrulation; Glycoprotein; Membrane;
Polymorphism; Reference proteome; Repeat; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 1285 Protein crumbs homolog 2. {ECO:0000255}.
/FTId=PRO_0000007502.
TRANSMEM 1225 1245 Helical. {ECO:0000255}.
DOMAIN 67 106 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 108 144 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 146 182 EGF-like 3; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 184 221 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 223 259 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 261 318 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 320 356 EGF-like 7; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 358 394 EGF-like 8; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 396 436 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 431 603 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 605 641 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 647 805 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 807 843 EGF-like 11. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 871 1054 Laminin G-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1056 1092 EGF-like 12. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1094 1130 EGF-like 13. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1134 1171 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1173 1209 EGF-like 15. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 267 267 O-linked (Glc...) serine.
{ECO:0000250|UniProtKB:Q80YA8}.
CARBOHYD 438 438 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 478 478 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 669 669 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 690 690 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 786 786 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 800 800 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 836 836 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 886 886 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 926 926 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1009 1009 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1141 1141 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1158 1158 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 71 82 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 76 94 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 96 105 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 112 123 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 117 132 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 134 143 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 150 161 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 155 170 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 172 181 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 188 199 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 193 208 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 210 220 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 227 238 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 232 247 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 249 258 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 265 276 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 270 306 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 308 317 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 324 335 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 329 344 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 346 355 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 362 373 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 367 382 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 384 393 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 400 411 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 405 424 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 426 435 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 579 603 {ECO:0000255|PROSITE-ProRule:PRU00122}.
DISULFID 609 620 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 614 629 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 631 640 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 766 805 {ECO:0000255|PROSITE-ProRule:PRU00122}.
DISULFID 811 822 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 816 831 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 833 842 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1013 1054 {ECO:0000255|PROSITE-ProRule:PRU00122}.
DISULFID 1060 1071 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1065 1080 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1082 1091 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1098 1108 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1103 1118 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1120 1129 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1138 1150 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1144 1159 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1161 1170 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1177 1188 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1182 1197 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1199 1208 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VAR_SEQ 1 332 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_014737.
VAR_SEQ 333 351 GHCQDLPNGFQCHCPDGYA -> MAMEPGALWTFLGHLWLL
A (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_014738.
VAR_SEQ 1131 1176 LPVPSKECSLNVTCLDGSPCEGGSPAANCSCLEGLAGQRCQ
VPTLP -> WDGWAGGWAANAPWGYGGAEKSARSVDESLPF
PGPHVLICDMRRTV (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_014739.
VAR_SEQ 1177 1285 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_014740.
VARIANT 46 46 P -> L (in dbSNP:rs73571404).
{ECO:0000269|PubMed:15851977}.
/FTId=VAR_022984.
VARIANT 90 90 T -> N (in dbSNP:rs2808415).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_048974.
VARIANT 97 97 V -> L. {ECO:0000269|PubMed:15851977}.
/FTId=VAR_022985.
VARIANT 116 116 P -> L (in dbSNP:rs542211566).
{ECO:0000269|PubMed:15851977}.
/FTId=VAR_022986.
VARIANT 145 145 M -> T (in dbSNP:rs1105223).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15851977}.
/FTId=VAR_022987.
VARIANT 159 159 G -> A (in dbSNP:rs1105222).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15851977}.
/FTId=VAR_022988.
VARIANT 187 187 E -> D. {ECO:0000269|PubMed:15851977}.
/FTId=VAR_022989.
VARIANT 351 351 A -> T (in dbSNP:rs199679542).
{ECO:0000269|PubMed:15851977}.
/FTId=VAR_022990.
VARIANT 534 534 R -> Q. {ECO:0000269|PubMed:15851977}.
/FTId=VAR_022991.
VARIANT 610 610 R -> W (in dbSNP:rs145286619).
{ECO:0000269|PubMed:15851977}.
/FTId=VAR_022992.
VARIANT 620 620 C -> S (in FSGS9; loss of function
mutation; dbSNP:rs879255250).
{ECO:0000269|PubMed:25557779}.
/FTId=VAR_073266.
VARIANT 628 628 R -> C (in FSGS9; dbSNP:rs202128397).
{ECO:0000269|PubMed:25557779}.
/FTId=VAR_073267.
VARIANT 629 629 C -> S (in FSGS9; moderate loss of
function mutation; dbSNP:rs879255252).
{ECO:0000269|PubMed:25557779}.
/FTId=VAR_073268.
VARIANT 633 633 R -> W (in VMCKD; dbSNP:rs730880377).
{ECO:0000269|PubMed:25557780}.
/FTId=VAR_073269.
VARIANT 643 643 E -> A (in VMCKD; dbSNP:rs730880300).
{ECO:0000269|PubMed:25557780}.
/FTId=VAR_073270.
VARIANT 709 709 V -> A (in dbSNP:rs2488602).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15851977}.
/FTId=VAR_061153.
VARIANT 746 746 H -> Q (in dbSNP:rs757353722).
{ECO:0000269|PubMed:15851977}.
/FTId=VAR_022993.
VARIANT 800 800 N -> K (in VMCKD; dbSNP:rs765676223).
{ECO:0000269|PubMed:25557780}.
/FTId=VAR_073271.
VARIANT 1110 1110 T -> M (in dbSNP:rs73571431).
{ECO:0000269|PubMed:15851977}.
/FTId=VAR_022994.
VARIANT 1249 1249 R -> Q (in FSGS9; dbSNP:rs147412276).
{ECO:0000269|PubMed:25557779}.
/FTId=VAR_073272.
CONFLICT 430 430 T -> A (in Ref. 2; BAC86684).
{ECO:0000305}.
CONFLICT 969 969 T -> A (in Ref. 2; AK123000/BAC86684).
{ECO:0000305}.
CONFLICT 1153 1153 G -> R (in Ref. 2; BAC86684).
{ECO:0000305}.
CONFLICT 1239 1239 Missing (in Ref. 2; BAC86684).
{ECO:0000305}.
SEQUENCE 1285 AA; 134265 MW; C5B7E9D7A91CD703 CRC64;
MALARPGTPD PQALASVLLL LLWAPALSLL AGTVPSEPPS ACASDPCAPG TECQATESGG
YTCGPMEPRG CATQPCHHGA LCVPQGPDPT GFRCYCVPGF QGPRCELDID ECASRPCHHG
ATCRNLADRY ECHCPLGYAG VTCEMEVDEC ASAPCLHGGS CLDGVGSFRC VCAPGYGGTR
CQLDLDECQS QPCAHGGTCH DLVNGFRCDC AGTGYEGTHC EREVLECASA PCEHNASCLE
GLGSFRCLCW PGYSGELCEV DEDECASSPC QHGGRCLQRS DPALYGGVQA AFPGAFSFRH
AAGFLCHCPP GFEGADCGVE VDECASRPCL NGGHCQDLPN GFQCHCPDGY AGPTCEEDVD
ECLSDPCLHG GTCSDTVAGY ICRCPETWGG RDCSVQLTGC QGHTCPLAAT CIPIFESGVH
SYVCHCPPGT HGPFCGQNTT FSVMAGSPIQ ASVPAGGPLG LALRFRTTLP AGTLATRNDT
KESLELALVA ATLQATLWSY STTVLVLRLP DLALNDGHWH QVEVVLHLAT LELRLWHEGC
PARLCVASGP VALASTASAT PLPAGISSAQ LGDATFAGCL QDVRVDGHLL LPEDLGENVL
LGCERREQCR PLPCVHGGSC VDLWTHFRCD CARPHRGPTC ADEIPAATFG LGGAPSSASF
LLQELPGPNL TVSFLLRTRE SAGLLLQFAN DSAAGLTVFL SEGRIRAEVP GSPAVVLPGR
WDDGLRHLVM LSFGPDQLQD LGQHVHVGGR LLAADSQPWG GPFRGCLQDL RLDGCHLPFF
PLPLDNSSQP SELGGRQSWN LTAGCVSEDM CSPDPCFNGG TCLVTWNDFH CTCPANFTGP
TCAQQLWCPG QPCLPPATCE EVPDGFVCVA EATFREGPPA AFSGHNASSG RLLGGLSLAF
RTRDSEAWLL RAAAGALEGV WLAVRNGSLA GGVRGGHGLP GAVLPIPGPR VADGAWHRVR
LAMERPAATT SRWLLWLDGA ATPVALRGLA SDLGFLQGPG AVRILLAENF TGCLGRVALG
GLPLPLARPR PGAAPGAREH FASWPGTPAP ILGCRGAPVC APSPCLHDGA CRDLFDAFAC
ACGPGWEGPR CEAHVDPCHS APCARGRCHT HPDGRFECRC PPGFGGPRCR LPVPSKECSL
NVTCLDGSPC EGGSPAANCS CLEGLAGQRC QVPTLPCEAN PCLNGGTCRA AGGVSECICN
ARFSGQFCEV AKGLPLPLPF PLLEVAVPAA CACLLLLLLG LLSGILAARK RRQSEGTYSP
SQQEVAGARL EMDSVLKVPP EERLI


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