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Protein crumbs (95F)

 CRB_DROME               Reviewed;        2146 AA.
P10040; Q0KI19; Q8MSX5; Q9VC97;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 3.
18-JUL-2018, entry version 203.
RecName: Full=Protein crumbs;
AltName: Full=95F;
Flags: Precursor;
Name=crb; ORFNames=CG6383;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR
LOCATION, AND DISRUPTION PHENOTYPE.
STRAIN=Oregon-R; TISSUE=Embryo;
PubMed=2344615; DOI=10.1016/0092-8674(90)90189-L;
Tepass U., Theres C., Knust E.;
"Crumbs encodes an EGF-like protein expressed on apical membranes of
Drosophila epithelial cells and required for organization of
epithelia.";
Cell 61:787-799(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1578-2146.
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1661-1952.
TISSUE=Embryo;
PubMed=3107986;
Knust E., Dietrich U., Tepass U., Bremer K.A., Weigel D., Vaessin H.,
Campos-Ortega J.A.;
"EGF homologous sequences encoded in the genome of Drosophila
melanogaster, and their relation to neurogenic genes.";
EMBO J. 6:761-766(1987).
[6]
FUNCTION, AND INTERACTION WITH PATJ.
PubMed=10102271; DOI=10.1016/S0092-8674(00)80593-0;
Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.;
"Discs Lost, a novel multi-PDZ domain protein, establishes and
maintains epithelial polarity.";
Cell 96:833-845(1999).
[7]
ERRATUM.
Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.;
Cell 115:765-766(2003).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PATJ.
PubMed=11076972; DOI=10.1083/jcb.151.4.891;
Tanentzapf G., Smith C., McGlade J., Tepass U.;
"Apical, lateral, and basal polarization cues contribute to the
development of the follicular epithelium during Drosophila
oogenesis.";
J. Cell Biol. 151:891-904(2000).
[9]
IDENTIFICATION IN A SAC COMPLEX WITH PATJ AND SDT.
PubMed=11740560; DOI=10.1038/414638a;
Bachmann A., Schneider M., Theilenberg E., Grawe F., Knust E.;
"Drosophila Stardust is a partner of Crumbs in the control of
epithelial cell polarity.";
Nature 414:638-643(2001).
[10]
FUNCTION, AND INTERACTION WITH THE PAR-6 COMPLEX.
PubMed=12900452; DOI=10.1242/dev.00648;
Nam S.-C., Choi K.-W.;
"Interaction of Par-6 and Crumbs complexes is essential for
photoreceptor morphogenesis in Drosophila.";
Development 130:4363-4372(2003).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1100, AND IDENTIFICATION
BY MASS SPECTROMETRY.
STRAIN=Oregon-R; TISSUE=Head;
PubMed=17893096; DOI=10.1093/glycob/cwm097;
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
Panin V.;
"Identification of N-glycosylated proteins from the central nervous
system of Drosophila melanogaster.";
Glycobiology 17:1388-1403(2007).
[12]
FUNCTION, INTERACTION WITH THE CGX COMPLEX, SUBCELLULAR LOCATION, AND
DISRUPTION PHENOTYPE.
PubMed=25065591; DOI=10.1038/onc.2014.202;
Yeom E., Hong S.T., Choi K.W.;
"Crumbs interacts with Xpd for nuclear division control in
Drosophila.";
Oncogene 34:2777-2789(2015).
-!- FUNCTION: Plays a central role in cell polarity establishment
(PubMed:2344615, PubMed:12900452, PubMed:10102271,
PubMed:11740560). Participates in the assembly, positioning and
maintenance of adherens junctions via its interaction with the SAC
complex (PubMed:11740560, PubMed:12900452, PubMed:10102271,
PubMed:11076972). Controls the coalescence of the spots of zonula
adherens (ZA) into a adhesive ring around the cells
(PubMed:11740560). It may act as a signal (PubMed:2344615).
Involved in morphogenesis of the photoreceptor rhabdomere, for
positioning and growth of rhabdomere and AJ during the crucial
period of photoreceptor extension along the proximodistal axis of
the retina (PubMed:12900452). Component of the crb-galla-Xpd (CGX)
complex which is essential for proper mitotic chromosome
segregation in early embryos (PubMed:25065591). The CGX complex is
also required for cell proliferation in developing wing disks
(PubMed:25065591). In the CGX complex, acts with galla-1 or galla-
2 to recruit Xpd and thus form the functional complex.
{ECO:0000269|PubMed:10102271, ECO:0000269|PubMed:11076972,
ECO:0000269|PubMed:11740560, ECO:0000269|PubMed:12900452,
ECO:0000269|PubMed:2344615, ECO:0000269|PubMed:25065591}.
-!- SUBUNIT: Component of the SAC complex, a complex composed of crb,
Patj and sdt (PubMed:11740560, PubMed:10102271, PubMed:11076972).
May interact with the par-6 complex, which is composed of par-6,
baz and aPKC, via its interaction with Patj (PubMed:12900452,
PubMed:10102271, PubMed:11076972). Interacts with other proteins
with Patj and sdt via its short cytoplasmic tail
(PubMed:11740560). Component of the CGX complex composed of crb,
galla (galla-1 or galla-2) and Xpd (PubMed:25065591). Able to
interact independently (via intracellular domain) with galla-1,
galla-2 and Xpd (PubMed:25065591). {ECO:0000269|PubMed:10102271,
ECO:0000269|PubMed:11076972, ECO:0000269|PubMed:11740560,
ECO:0000269|PubMed:12900452, ECO:0000269|PubMed:25065591}.
-!- INTERACTION:
A1Z9X0:aPKC; NbExp=3; IntAct=EBI-672928, EBI-160861;
Q07436:ex; NbExp=2; IntAct=EBI-672928, EBI-192660;
Q9NB04:Patj; NbExp=2; IntAct=EBI-672928, EBI-442573;
-!- SUBCELLULAR LOCATION: Apical cell membrane
{ECO:0000269|PubMed:11076972, ECO:0000269|PubMed:2344615}; Single-
pass type I membrane protein {ECO:0000269|PubMed:11076972,
ECO:0000269|PubMed:2344615}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:25065591}. Note=Specifically localized to the
apical membrane (PubMed:11076972, PubMed:2344615). Expressed in a
mesh punctate pattern that overlaps with metaphase spindle
microtubules (PubMed:25065591). {ECO:0000269|PubMed:11076972,
ECO:0000269|PubMed:2344615, ECO:0000269|PubMed:25065591}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A;
IsoId=P10040-1; Sequence=Displayed;
Name=B;
IsoId=P10040-2; Sequence=VSP_031870;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated in the cytoplasmic domain. {ECO:0000305}.
-!- DISRUPTION PHENOTYPE: Flies show severe disruptions in the
organization of ectodermally derived epithelia and leading in some
cases to cell death in these tissues (PubMed:2344615). RNAi-
mediated knockdown in germline cells results in severe chromosomal
and spindle microtubule defects such as chromosome bridges, bent
chromosomes, monopolar spindles and fusion with one or more
neighboring spindles (PubMed:25065591).
{ECO:0000269|PubMed:2344615, ECO:0000269|PubMed:25065591}.
-!- SIMILARITY: Belongs to the Crumbs protein family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAM49878.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; M33753; AAA28428.1; -; mRNA.
EMBL; AE014297; AAF56276.1; -; Genomic_DNA.
EMBL; AE014297; ABI31202.1; -; Genomic_DNA.
EMBL; AY118509; AAM49878.1; ALT_INIT; mRNA.
EMBL; X05144; CAA28793.1; -; mRNA.
PIR; A35672; A35672.
PIR; B26637; B26637.
RefSeq; NP_001036751.1; NM_001043286.2. [P10040-2]
RefSeq; NP_524480.2; NM_079756.3. [P10040-1]
UniGene; Dm.2365; -.
PDB; 4WSI; X-ray; 2.95 A; X/Y=2110-2146.
PDB; 4YL8; X-ray; 1.50 A; B=2110-2146.
PDBsum; 4WSI; -.
PDBsum; 4YL8; -.
ProteinModelPortal; P10040; -.
SMR; P10040; -.
BioGrid; 67824; 54.
DIP; DIP-40915N; -.
IntAct; P10040; 11.
MINT; P10040; -.
STRING; 7227.FBpp0293268; -.
TCDB; 9.B.87.1.11; the selenoprotein p receptor (selp-receptor) family.
iPTMnet; P10040; -.
PaxDb; P10040; -.
PRIDE; P10040; -.
EnsemblMetazoa; FBtr0084603; FBpp0083987; FBgn0259685. [P10040-1]
EnsemblMetazoa; FBtr0111008; FBpp0110307; FBgn0259685. [P10040-2]
GeneID; 42896; -.
KEGG; dme:Dmel_CG6383; -.
CTD; 42896; -.
FlyBase; FBgn0259685; crb.
eggNOG; KOG1217; Eukaryota.
eggNOG; ENOG410XP6K; LUCA.
GeneTree; ENSGT00910000144018; -.
InParanoid; P10040; -.
KO; K16681; -.
OMA; YFNGSAY; -.
OrthoDB; EOG091G001C; -.
PhylomeDB; P10040; -.
SignaLink; P10040; -.
GenomeRNAi; 42896; -.
PRO; PR:P10040; -.
Proteomes; UP000000803; Chromosome 3R.
Bgee; FBgn0259685; -.
ExpressionAtlas; P10040; baseline and differential.
Genevisible; P10040; DM.
GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
GO; GO:0016327; C:apicolateral plasma membrane; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0016028; C:rhabdomere; IDA:FlyBase.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0035003; C:subapical complex; TAS:FlyBase.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005080; F:protein kinase C binding; IPI:FlyBase.
GO; GO:0030507; F:spectrin binding; TAS:FlyBase.
GO; GO:0034332; P:adherens junction organization; IMP:FlyBase.
GO; GO:0046665; P:amnioserosa maintenance; IMP:FlyBase.
GO; GO:0003383; P:apical constriction; IMP:FlyBase.
GO; GO:0045176; P:apical protein localization; IMP:FlyBase.
GO; GO:0106036; P:assembly of apicomedial cortex actomyosin; IMP:FlyBase.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0061336; P:cell morphogenesis involved in Malpighian tubule morphogenesis; IMP:FlyBase.
GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase.
GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
GO; GO:0046664; P:dorsal closure, amnioserosa morphology change; IMP:FlyBase.
GO; GO:0035088; P:establishment or maintenance of apical/basal cell polarity; IMP:FlyBase.
GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:FlyBase.
GO; GO:0016332; P:establishment or maintenance of polarity of embryonic epithelium; IMP:FlyBase.
GO; GO:0016334; P:establishment or maintenance of polarity of follicular epithelium; IMP:FlyBase.
GO; GO:0035002; P:liquid clearance, open tracheal system; IGI:FlyBase.
GO; GO:0035090; P:maintenance of apical/basal cell polarity; IMP:FlyBase.
GO; GO:0007443; P:Malpighian tubule morphogenesis; IMP:FlyBase.
GO; GO:0061024; P:membrane organization; IMP:FlyBase.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; IGI:FlyBase.
GO; GO:0046621; P:negative regulation of organ growth; IMP:FlyBase.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IGI:FlyBase.
GO; GO:0007399; P:nervous system development; IMP:FlyBase.
GO; GO:0098813; P:nuclear chromosome segregation; IMP:FlyBase.
GO; GO:0048477; P:oogenesis; IMP:FlyBase.
GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
GO; GO:0045494; P:photoreceptor cell maintenance; IMP:FlyBase.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:FlyBase.
GO; GO:0035332; P:positive regulation of hippo signaling; IMP:FlyBase.
GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
GO; GO:0045570; P:regulation of imaginal disc growth; IMP:FlyBase.
GO; GO:0033157; P:regulation of intracellular protein transport; IMP:FlyBase.
GO; GO:0032880; P:regulation of protein localization; IMP:FlyBase.
GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
GO; GO:0061541; P:rhabdomere morphogenesis; IMP:FlyBase.
GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
GO; GO:0035239; P:tube morphogenesis; IMP:FlyBase.
GO; GO:0045186; P:zonula adherens assembly; IMP:FlyBase.
GO; GO:0045218; P:zonula adherens maintenance; IMP:FlyBase.
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; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR001791; Laminin_G.
Pfam; PF00008; EGF; 17.
Pfam; PF07645; EGF_CA; 2.
Pfam; PF12661; hEGF; 4.
Pfam; PF00054; Laminin_G_1; 2.
Pfam; PF02210; Laminin_G_2; 1.
SMART; SM00181; EGF; 28.
SMART; SM00179; EGF_CA; 23.
SMART; SM00282; LamG; 3.
SUPFAM; SSF49899; SSF49899; 5.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS00010; ASX_HYDROXYL; 16.
PROSITE; PS00022; EGF_1; 25.
PROSITE; PS01186; EGF_2; 17.
PROSITE; PS50026; EGF_3; 27.
PROSITE; PS01187; EGF_CA; 13.
PROSITE; PS50025; LAM_G_DOMAIN; 3.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
Developmental protein; Differentiation; Disulfide bond;
EGF-like domain; Glycoprotein; Membrane; Mitosis; Phosphoprotein;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 88
CHAIN 89 2146 Protein crumbs.
/FTId=PRO_0000007499.
TOPO_DOM 89 2082 Extracellular. {ECO:0000255}.
TRANSMEM 2083 2109 Helical. {ECO:0000255}.
TOPO_DOM 2110 2146 Cytoplasmic. {ECO:0000255}.
DOMAIN 265 301 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 304 341 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 346 384 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 386 423 EGF-like 4; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 425 461 EGF-like 5; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 462 498 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 543 579 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 609 644 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 646 683 EGF-like 9; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 685 721 EGF-like 10; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 723 759 EGF-like 11; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 761 798 EGF-like 12; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 800 836 EGF-like 13; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 838 900 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 902 938 EGF-like 15; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 940 976 EGF-like 16; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 978 1019 EGF-like 17. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1021 1203 Laminin G-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1205 1241 EGF-like 18. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1248 1483 Laminin G-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1479 1515 EGF-like 19. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1555 1757 Laminin G-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00122}.
DOMAIN 1758 1792 EGF-like 20. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1794 1830 EGF-like 21; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1832 1868 EGF-like 22; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1871 1909 EGF-like 23. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1912 1948 EGF-like 24. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1950 1987 EGF-like 25; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 1989 2027 EGF-like 26; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 2028 2068 EGF-like 27. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 196 196 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 236 236 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 334 334 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 398 398 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 548 548 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 563 563 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 734 734 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 744 744 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 858 858 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 882 882 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 974 974 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1006 1006 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1100 1100 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17893096}.
CARBOHYD 1112 1112 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1136 1136 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1190 1190 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1243 1243 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1253 1253 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1352 1352 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1361 1361 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1439 1439 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1452 1452 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1543 1543 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1737 1737 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1749 1749 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1806 1806 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1846 1846 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1882 1882 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1891 1891 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1897 1897 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2027 2027 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2033 2033 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2066 2066 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 269 280 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 274 289 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 291 300 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 308 319 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 313 329 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 331 340 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 350 361 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 355 372 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 374 383 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 390 401 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 395 410 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 412 422 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 429 440 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 434 449 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 451 460 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 466 477 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 471 486 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 488 497 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 547 560 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 554 567 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 569 578 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 611 622 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 616 632 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 634 643 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 650 662 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 657 671 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 673 682 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 689 700 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 694 709 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 711 720 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 727 738 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 732 747 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 749 758 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 765 776 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 770 785 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 787 797 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 804 815 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 809 824 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 826 835 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 842 853 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 847 888 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 890 899 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 906 917 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 911 926 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 928 937 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 944 955 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 950 964 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 966 975 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 982 993 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 987 1007 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1009 1018 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1171 1203 {ECO:0000255|PROSITE-ProRule:PRU00122}.
DISULFID 1209 1220 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1214 1229 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1231 1240 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1483 1494 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1488 1503 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1505 1514 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1713 1757 {ECO:0000255|PROSITE-ProRule:PRU00122}.
DISULFID 1760 1771 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1765 1780 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1782 1791 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1798 1809 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1803 1818 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1820 1829 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1836 1847 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1841 1856 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1858 1867 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1875 1886 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1880 1900 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1916 1927 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1921 1936 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1938 1947 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1954 1965 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1959 1974 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1976 1986 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 1993 2006 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2000 2015 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2017 2026 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2032 2044 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2038 2056 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 2058 2067 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VAR_SEQ 526 526 G -> ASDMEPLTPLELDILDATLCPSEKKKRYISPEWLKR
KRCELKLS (in isoform B). {ECO:0000305}.
/FTId=VSP_031870.
CONFLICT 1661 1673 VDPTPAFSTDIDQ -> WWIRRQLFPRTSTK (in Ref.
5; CAA28793). {ECO:0000305}.
CONFLICT 1719 1719 V -> L (in Ref. 1; AAA28428).
{ECO:0000305}.
CONFLICT 1952 1952 N -> K (in Ref. 5; CAA28793).
{ECO:0000305}.
STRAND 2116 2119 {ECO:0000244|PDB:4YL8}.
TURN 2121 2123 {ECO:0000244|PDB:4YL8}.
HELIX 2131 2135 {ECO:0000244|PDB:4WSI}.
SEQUENCE 2146 AA; 233572 MW; 8E23B9E32B761115 CRC64;
MAKIANASLS QQQKQRQAET ATTTTTTVAA SVETATTTAR SRDRTKSAAQ ITSHLLKRAI
SVYSSPQWIP LFILIYLATD VASVAVPTKE AYFNGSTYLR LTTPMPIWDH SAISFRSCRG
GEILAQQYNK NSIVISVLND FLQISLAGPA VHGPNNRLDV KLPYQLLDNR WHTLQFKYEY
GNLYLHVDRA ASIFANSTYN SQFLTNQDIG YKDAILILGN SFSGCLLDGP GLQFVNNSTV
QNVVFGHCPL TPGPCSDHDL FTRLPDNFCL NDPCMGHGTC SSSPEGYECR CTARYSGKNC
QKDNGSPCAK NPCENGGSCL ENSRGDYQCF CDPNHSGQHC ETEVNIHPLC QTNPCLNNGA
CVVIGGSGAL TCECPKGYAG ARCEVDTDEC ASQPCQNNGS CIDRINGFSC DCSGTGYTGA
FCQTNVDECD KNPCLNGGRC FDTYGWYTCQ CLDGWGGEIC DRPMTCQTQQ CLNGGTCLDK
PIGFQCLCPP EYTGELCQIA PSCAQQCPID SECVGGKCVC KPGSSGYNCQ TSTGDGASAL
ALTPINCNAT NGKCLNGGTC SMNGTHCYCA VGYSGDRCEK AENCSPLNCQ EPMVCVQNQC
LCPENKVCNQ CATQPCQNGG ECVDLPNGDY ECKCTRGWTG RTCGNDVDEC TLHPKICGNG
ICKNEKGSYK CYCTPGFTGV HCDSDVDECL SFPCLNGATC HNKINAYECV CQPGYEGENC
EVDIDECGSN PCSNGSTCID RINNFTCNCI PGMTGRICDI DIDDCVGDPC LNGGQCIDQL
GGFRCDCSGT GYEGENCELN IDECLSNPCT NGAKCLDRVK DYFCDCHNGY KGKNCEQDIN
ECESNPCQYN GNCLERSNIT LYQMSRITDL PKVFSQPFSF ENASGYECVC VPGIIGKNCE
ININECDSNP CSKHGNCNDG IGTYTCECEP GFEGTHCEIN IDECDRYNPC QRGTCYDQID
DYDCDCDANY GGKNCSVLLK GCDQNPCLNG GACLPYLINE VTHLYNCTCE NGFQGDKCEK
TTTLSMVATS LISVTTEREE GYDINLQFRT TLPNGVLAFG TTGEKNEPVS YILELINGRL
NLHSSLLNKW EGVFIGSKLN DSNWHKVFVA INTSHLVLSA NDEQAIFPVG SYETANNSQP
SFPRTYLGGT IPNLKSYLRH LTHQPSAFVG CMQDIMVNGK WIFPDEQDAN ISYTKLENVQ
SGCPRTEQCK PNPCHSNGEC TDLWHTFACH CPRPFFGHTC QHNMTAATFG HENTTHSAVI
VETTDVARRA IRSILDISMF IRTREPTGQV FYLGTDPRKA PTKNIGDSYV AAKLHGGELL
VKMQFSGTPE AYTVGGQKLD NGYNHLIEVV RNQTLVQVKL NGTEYFRKTL STTGLLDAQV
LYLGGPAPTR ESLLGATTEP GIIPVPGAGI PIEDTTVPKE ADDSRDYFKG IIQDVKVSNG
SLNLIVEMYS LNVTDVQVNA KPLGAVTIDR ASVLPGEVSD DLCRKNPCLH NAECRNTWND
YTCKCPNGYK GKNCQEIEFC QHVTCPGQSL CQNLDDGYEC VTNTTFTGQE RSPLAFFYFQ
EQQSDDIVSE ASPKQTLKPV IDIAFRTRAG GTLLYIDNVD GFFEIGVNGG RVTITWKLSA
LHFGESARFE KENTDGEWSR IYLRAHNSKL EGGWKGWESM VDPTPAFSTD IDQAAFQSLI
ATSTQVYLGG MPESRQARGS TLSAQQGSQF KGCVGEARVG DLLLPYFSMA ELYSRTNVSV
QQKAQFRLNA TRPEEGCILC FQSDCKNDGF CQSPSDEYAC TCQPGFEGDD CGTDIDECLN
TECLNNGTCI NQVAAFFCQC QPGFEGQHCE QNIDECADQP CHNGGNCTDL IASYVCDCPE
DYMGPQCDVL KQMTCENEPC RNGSTCQNGF NASTGNNFTC TCVPGFEGPL CDIPFCEITP
CDNGGLCLTT GAVPMCKCSL GYTGRLCEQD INECESNPCQ NGGQCKDLVG RYECDCQGTG
FEGIRCENDI DECNMEGDYC GGLGRCFNKP GSFQCICQKP YCGAYCNFTD PCNATDLCSN
GGRCVESCGA KPDYYCECPE GFAGKNCTAP ITAKEDGPST TDIAIIVIPV VVVLLLIAGA
LLGTFLVMAR NKRATRGTYS PSAQEYCNPR LEMDNVLKPP PEERLI


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