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Protein

Protein crumbs

Gene

crb

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a central role in cell polarity establishment. Participates in the assembly, positioning and maintenance of adherens junctions via its interaction with the SAC complex. Controls the coalescence of the spots of zonula adherens (ZA) into a adhesive ring around the cells. It may act as a signal. 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.1 Publication

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • protein kinase C binding Source: FlyBase
  • spectrin binding Source: FlyBase

GO - Biological processi

  • adherens junction organization Source: FlyBase
  • cell-cell junction assembly Source: FlyBase
  • cell morphogenesis involved in Malpighian tubule morphogenesis Source: FlyBase
  • centrosome localization Source: FlyBase
  • compound eye morphogenesis Source: FlyBase
  • compound eye photoreceptor development Source: FlyBase
  • dorsal closure, amnioserosa morphology change Source: FlyBase
  • establishment of epithelial cell apical/basal polarity Source: FlyBase
  • establishment or maintenance of apical/basal cell polarity Source: FlyBase
  • establishment or maintenance of cell polarity Source: FlyBase
  • establishment or maintenance of epithelial cell apical/basal polarity Source: FlyBase
  • establishment or maintenance of polarity of embryonic epithelium Source: FlyBase
  • establishment or maintenance of polarity of follicular epithelium Source: FlyBase
  • liquid clearance, open tracheal system Source: FlyBase
  • maintenance of apical/basal cell polarity Source: FlyBase
  • Malpighian tubule morphogenesis Source: FlyBase
  • membrane organization Source: FlyBase
  • morphogenesis of an epithelium Source: FlyBase
  • morphogenesis of a polarized epithelium Source: FlyBase
  • negative regulation of Notch signaling pathway Source: FlyBase
  • negative regulation of organ growth Source: FlyBase
  • negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: FlyBase
  • nervous system development Source: FlyBase
  • nuclear chromosome segregation Source: FlyBase
  • oogenesis Source: FlyBase
  • open tracheal system development Source: FlyBase
  • photoreceptor cell maintenance Source: FlyBase
  • positive regulation of cell proliferation Source: FlyBase
  • positive regulation of phosphorylation Source: FlyBase
  • protein localization Source: FlyBase
  • protein stabilization Source: FlyBase
  • regulation of hippo signaling Source: FlyBase
  • regulation of imaginal disc growth Source: FlyBase
  • regulation of intracellular protein transport Source: FlyBase
  • regulation of protein localization Source: FlyBase
  • rhabdomere development Source: FlyBase
  • rhabdomere morphogenesis Source: FlyBase
  • salivary gland development Source: FlyBase
  • salivary gland morphogenesis Source: FlyBase
  • tube morphogenesis Source: FlyBase
  • zonula adherens assembly Source: FlyBase
  • zonula adherens maintenance Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation

Enzyme and pathway databases

SignaLinkiP10040.

Protein family/group databases

TCDBi9.B.87.1.11. the selenoprotein p receptor (selp-receptor) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein crumbs
Alternative name(s):
95F
Gene namesi
Name:crb
ORF Names:CG6383
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0259685. crb.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini89 – 20821994ExtracellularSequence analysisAdd
BLAST
Transmembranei2083 – 210927HelicalSequence analysisAdd
BLAST
Topological domaini2110 – 214637CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: FlyBase
  • apicolateral plasma membrane Source: FlyBase
  • cell-cell adherens junction Source: FlyBase
  • integral component of membrane Source: FlyBase
  • plasma membrane Source: FlyBase
  • rhabdomere Source: FlyBase
  • septate junction Source: FlyBase
  • subapical complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Flies show severe disruptions in the organization of ectodermally derived epithelia and leading in some cases to cell death in these tissues.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 8888Add
BLAST
Chaini89 – 21462058Protein crumbsPRO_0000007499Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi94 – 941N-linked (GlcNAc...)Sequence analysis
Glycosylationi196 – 1961N-linked (GlcNAc...)Sequence analysis
Glycosylationi236 – 2361N-linked (GlcNAc...)Sequence analysis
Glycosylationi237 – 2371N-linked (GlcNAc...)Sequence analysis
Disulfide bondi269 ↔ 280By similarity
Disulfide bondi274 ↔ 289By similarity
Disulfide bondi291 ↔ 300By similarity
Disulfide bondi308 ↔ 319By similarity
Disulfide bondi313 ↔ 329By similarity
Disulfide bondi331 ↔ 340By similarity
Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence analysis
Disulfide bondi350 ↔ 361By similarity
Disulfide bondi355 ↔ 372By similarity
Disulfide bondi374 ↔ 383By similarity
Disulfide bondi390 ↔ 401By similarity
Disulfide bondi395 ↔ 410By similarity
Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence analysis
Disulfide bondi412 ↔ 422By similarity
Disulfide bondi429 ↔ 440By similarity
Disulfide bondi434 ↔ 449By similarity
Disulfide bondi451 ↔ 460By similarity
Disulfide bondi466 ↔ 477By similarity
Disulfide bondi471 ↔ 486By similarity
Disulfide bondi488 ↔ 497By similarity
Disulfide bondi503 ↔ 513By similarity
Disulfide bondi507 ↔ 518By similarity
Disulfide bondi520 ↔ 529By similarity
Disulfide bondi547 ↔ 560By similarity
Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi554 ↔ 567By similarity
Glycosylationi563 – 5631N-linked (GlcNAc...)Sequence analysis
Disulfide bondi569 ↔ 578By similarity
Disulfide bondi584 ↔ 595By similarity
Disulfide bondi589 ↔ 600By similarity
Disulfide bondi602 ↔ 608By similarity
Disulfide bondi611 ↔ 622By similarity
Disulfide bondi616 ↔ 632By similarity
Disulfide bondi634 ↔ 643By similarity
Disulfide bondi650 ↔ 662By similarity
Disulfide bondi657 ↔ 671By similarity
Disulfide bondi673 ↔ 682By similarity
Disulfide bondi689 ↔ 700By similarity
Disulfide bondi694 ↔ 709By similarity
Disulfide bondi711 ↔ 720By similarity
Disulfide bondi727 ↔ 738By similarity
Disulfide bondi732 ↔ 747By similarity
Glycosylationi734 – 7341N-linked (GlcNAc...)Sequence analysis
Glycosylationi744 – 7441N-linked (GlcNAc...)Sequence analysis
Disulfide bondi749 ↔ 758By similarity
Disulfide bondi765 ↔ 776By similarity
Disulfide bondi770 ↔ 785By similarity
Disulfide bondi787 ↔ 797By similarity
Disulfide bondi804 ↔ 815By similarity
Disulfide bondi809 ↔ 824By similarity
Disulfide bondi826 ↔ 835By similarity
Disulfide bondi842 ↔ 853By similarity
Disulfide bondi847 ↔ 888By similarity
Glycosylationi858 – 8581N-linked (GlcNAc...)Sequence analysis
Glycosylationi882 – 8821N-linked (GlcNAc...)Sequence analysis
Disulfide bondi890 ↔ 899By similarity
Disulfide bondi906 ↔ 917By similarity
Disulfide bondi911 ↔ 926By similarity
Disulfide bondi928 ↔ 937By similarity
Disulfide bondi944 ↔ 955By similarity
Disulfide bondi950 ↔ 964By similarity
Disulfide bondi966 ↔ 975By similarity
Glycosylationi974 – 9741N-linked (GlcNAc...)Sequence analysis
Disulfide bondi982 ↔ 993By similarity
Disulfide bondi987 ↔ 1007By similarity
Glycosylationi1006 – 10061N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1009 ↔ 1018By similarity
Glycosylationi1100 – 11001N-linked (GlcNAc...)1 Publication
Glycosylationi1112 – 11121N-linked (GlcNAc...)Sequence analysis
Glycosylationi1136 – 11361N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1171 ↔ 1203By similarity
Glycosylationi1190 – 11901N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1209 ↔ 1220By similarity
Disulfide bondi1214 ↔ 1229By similarity
Disulfide bondi1231 ↔ 1240By similarity
Glycosylationi1243 – 12431N-linked (GlcNAc...)Sequence analysis
Glycosylationi1253 – 12531N-linked (GlcNAc...)Sequence analysis
Glycosylationi1352 – 13521N-linked (GlcNAc...)Sequence analysis
Glycosylationi1361 – 13611N-linked (GlcNAc...)Sequence analysis
Glycosylationi1439 – 14391N-linked (GlcNAc...)Sequence analysis
Glycosylationi1452 – 14521N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1483 ↔ 1494By similarity
Disulfide bondi1488 ↔ 1503By similarity
Disulfide bondi1505 ↔ 1514By similarity
Glycosylationi1543 – 15431N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1713 ↔ 1757By similarity
Glycosylationi1737 – 17371N-linked (GlcNAc...)Sequence analysis
Glycosylationi1749 – 17491N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1760 ↔ 1771By similarity
Disulfide bondi1765 ↔ 1780By similarity
Disulfide bondi1782 ↔ 1791By similarity
Disulfide bondi1798 ↔ 1809By similarity
Disulfide bondi1803 ↔ 1818By similarity
Glycosylationi1806 – 18061N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1820 ↔ 1829By similarity
Disulfide bondi1836 ↔ 1847By similarity
Disulfide bondi1841 ↔ 1856By similarity
Glycosylationi1846 – 18461N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1858 ↔ 1867By similarity
Disulfide bondi1875 ↔ 1886By similarity
Disulfide bondi1880 ↔ 1900By similarity
Glycosylationi1882 – 18821N-linked (GlcNAc...)Sequence analysis
Glycosylationi1891 – 18911N-linked (GlcNAc...)Sequence analysis
Glycosylationi1897 – 18971N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1916 ↔ 1927By similarity
Disulfide bondi1921 ↔ 1936By similarity
Disulfide bondi1938 ↔ 1947By similarity
Disulfide bondi1954 ↔ 1965By similarity
Disulfide bondi1959 ↔ 1974By similarity
Disulfide bondi1976 ↔ 1986By similarity
Disulfide bondi1993 ↔ 2006By similarity
Disulfide bondi2000 ↔ 2015By similarity
Disulfide bondi2017 ↔ 2026By similarity
Glycosylationi2027 – 20271N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2032 ↔ 2044By similarity
Glycosylationi2033 – 20331N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2038 ↔ 2056By similarity
Disulfide bondi2058 ↔ 2067By similarity
Glycosylationi2066 – 20661N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Phosphorylated in the cytoplasmic domain.Curated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP10040.

Expressioni

Gene expression databases

BgeeiP10040.
GenevisibleiP10040. DM.

Interactioni

Subunit structurei

Component of the SAC complex, a complex composed of crb, Patj and sdt. May interact with the par-6 complex, which is composed of par-6, baz and aPKC, via its interaction with Patj. Interacts with other proteins with Patj and sdt via its short cytoplasmic tail.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
aPKCA1Z9X03EBI-672928,EBI-160861

GO - Molecular functioni

  • protein kinase C binding Source: FlyBase
  • spectrin binding Source: FlyBase

Protein-protein interaction databases

BioGridi67824. 8 interactions.
DIPiDIP-40915N.
IntActiP10040. 8 interactions.
MINTiMINT-89007.
STRINGi7227.FBpp0293268.

Structurei

Secondary structure

1
2146
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2116 – 21194Combined sources
Turni2121 – 21233Combined sources
Helixi2131 – 21355Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WSIX-ray2.95X/Y2110-2146[»]
4YL8X-ray1.50B2110-2146[»]
ProteinModelPortaliP10040.
SMRiP10040. Positions 2110-2146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini265 – 30137EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini304 – 34138EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini346 – 38439EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini386 – 42338EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini425 – 46137EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini462 – 49837EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini499 – 53032EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini543 – 57937EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini580 – 60930EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini607 – 64438EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini646 – 68338EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini685 – 72137EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini723 – 75937EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini761 – 79838EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini800 – 83637EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini838 – 90063EGF-like 16PROSITE-ProRule annotationAdd
BLAST
Domaini902 – 93837EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini940 – 97637EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini978 – 101942EGF-like 19PROSITE-ProRule annotationAdd
BLAST
Domaini1021 – 1203183Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini1205 – 124137EGF-like 20PROSITE-ProRule annotationAdd
BLAST
Domaini1248 – 1478231Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini1479 – 151537EGF-like 21PROSITE-ProRule annotationAdd
BLAST
Domaini1555 – 1755201Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini1756 – 179237EGF-like 22PROSITE-ProRule annotationAdd
BLAST
Domaini1794 – 183037EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1832 – 186837EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1871 – 191242EGF-like 25PROSITE-ProRule annotationAdd
BLAST
Domaini1912 – 194837EGF-like 26PROSITE-ProRule annotationAdd
BLAST
Domaini1950 – 198738EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1989 – 202739EGF-like 28; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2028 – 206841EGF-like 29PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the Crumbs protein family.Curated
Contains 29 EGF-like domains.PROSITE-ProRule annotation
Contains 3 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
ENOG410XP6K. LUCA.
GeneTreeiENSGT00810000125346.
InParanoidiP10040.
KOiK16681.
OrthoDBiEOG7FBRGQ.
PhylomeDBiP10040.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00008. EGF. 18 hits.
PF07645. EGF_CA. 2 hits.
PF00054. Laminin_G_1. 2 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 28 hits.
SM00179. EGF_CA. 23 hits.
SM00282. LamG. 3 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
SSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 16 hits.
PS00022. EGF_1. 25 hits.
PS01186. EGF_2. 17 hits.
PS50026. EGF_3. 27 hits.
PS01187. EGF_CA. 13 hits.
PS50025. LAM_G_DOMAIN. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P10040-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAKIANASLS QQQKQRQAET ATTTTTTVAA SVETATTTAR SRDRTKSAAQ
60 70 80 90 100
ITSHLLKRAI SVYSSPQWIP LFILIYLATD VASVAVPTKE AYFNGSTYLR
110 120 130 140 150
LTTPMPIWDH SAISFRSCRG GEILAQQYNK NSIVISVLND FLQISLAGPA
160 170 180 190 200
VHGPNNRLDV KLPYQLLDNR WHTLQFKYEY GNLYLHVDRA ASIFANSTYN
210 220 230 240 250
SQFLTNQDIG YKDAILILGN SFSGCLLDGP GLQFVNNSTV QNVVFGHCPL
260 270 280 290 300
TPGPCSDHDL FTRLPDNFCL NDPCMGHGTC SSSPEGYECR CTARYSGKNC
310 320 330 340 350
QKDNGSPCAK NPCENGGSCL ENSRGDYQCF CDPNHSGQHC ETEVNIHPLC
360 370 380 390 400
QTNPCLNNGA CVVIGGSGAL TCECPKGYAG ARCEVDTDEC ASQPCQNNGS
410 420 430 440 450
CIDRINGFSC DCSGTGYTGA FCQTNVDECD KNPCLNGGRC FDTYGWYTCQ
460 470 480 490 500
CLDGWGGEIC DRPMTCQTQQ CLNGGTCLDK PIGFQCLCPP EYTGELCQIA
510 520 530 540 550
PSCAQQCPID SECVGGKCVC KPGSSGYNCQ TSTGDGASAL ALTPINCNAT
560 570 580 590 600
NGKCLNGGTC SMNGTHCYCA VGYSGDRCEK AENCSPLNCQ EPMVCVQNQC
610 620 630 640 650
LCPENKVCNQ CATQPCQNGG ECVDLPNGDY ECKCTRGWTG RTCGNDVDEC
660 670 680 690 700
TLHPKICGNG ICKNEKGSYK CYCTPGFTGV HCDSDVDECL SFPCLNGATC
710 720 730 740 750
HNKINAYECV CQPGYEGENC EVDIDECGSN PCSNGSTCID RINNFTCNCI
760 770 780 790 800
PGMTGRICDI DIDDCVGDPC LNGGQCIDQL GGFRCDCSGT GYEGENCELN
810 820 830 840 850
IDECLSNPCT NGAKCLDRVK DYFCDCHNGY KGKNCEQDIN ECESNPCQYN
860 870 880 890 900
GNCLERSNIT LYQMSRITDL PKVFSQPFSF ENASGYECVC VPGIIGKNCE
910 920 930 940 950
ININECDSNP CSKHGNCNDG IGTYTCECEP GFEGTHCEIN IDECDRYNPC
960 970 980 990 1000
QRGTCYDQID DYDCDCDANY GGKNCSVLLK GCDQNPCLNG GACLPYLINE
1010 1020 1030 1040 1050
VTHLYNCTCE NGFQGDKCEK TTTLSMVATS LISVTTEREE GYDINLQFRT
1060 1070 1080 1090 1100
TLPNGVLAFG TTGEKNEPVS YILELINGRL NLHSSLLNKW EGVFIGSKLN
1110 1120 1130 1140 1150
DSNWHKVFVA INTSHLVLSA NDEQAIFPVG SYETANNSQP SFPRTYLGGT
1160 1170 1180 1190 1200
IPNLKSYLRH LTHQPSAFVG CMQDIMVNGK WIFPDEQDAN ISYTKLENVQ
1210 1220 1230 1240 1250
SGCPRTEQCK PNPCHSNGEC TDLWHTFACH CPRPFFGHTC QHNMTAATFG
1260 1270 1280 1290 1300
HENTTHSAVI VETTDVARRA IRSILDISMF IRTREPTGQV FYLGTDPRKA
1310 1320 1330 1340 1350
PTKNIGDSYV AAKLHGGELL VKMQFSGTPE AYTVGGQKLD NGYNHLIEVV
1360 1370 1380 1390 1400
RNQTLVQVKL NGTEYFRKTL STTGLLDAQV LYLGGPAPTR ESLLGATTEP
1410 1420 1430 1440 1450
GIIPVPGAGI PIEDTTVPKE ADDSRDYFKG IIQDVKVSNG SLNLIVEMYS
1460 1470 1480 1490 1500
LNVTDVQVNA KPLGAVTIDR ASVLPGEVSD DLCRKNPCLH NAECRNTWND
1510 1520 1530 1540 1550
YTCKCPNGYK GKNCQEIEFC QHVTCPGQSL CQNLDDGYEC VTNTTFTGQE
1560 1570 1580 1590 1600
RSPLAFFYFQ EQQSDDIVSE ASPKQTLKPV IDIAFRTRAG GTLLYIDNVD
1610 1620 1630 1640 1650
GFFEIGVNGG RVTITWKLSA LHFGESARFE KENTDGEWSR IYLRAHNSKL
1660 1670 1680 1690 1700
EGGWKGWESM VDPTPAFSTD IDQAAFQSLI ATSTQVYLGG MPESRQARGS
1710 1720 1730 1740 1750
TLSAQQGSQF KGCVGEARVG DLLLPYFSMA ELYSRTNVSV QQKAQFRLNA
1760 1770 1780 1790 1800
TRPEEGCILC FQSDCKNDGF CQSPSDEYAC TCQPGFEGDD CGTDIDECLN
1810 1820 1830 1840 1850
TECLNNGTCI NQVAAFFCQC QPGFEGQHCE QNIDECADQP CHNGGNCTDL
1860 1870 1880 1890 1900
IASYVCDCPE DYMGPQCDVL KQMTCENEPC RNGSTCQNGF NASTGNNFTC
1910 1920 1930 1940 1950
TCVPGFEGPL CDIPFCEITP CDNGGLCLTT GAVPMCKCSL GYTGRLCEQD
1960 1970 1980 1990 2000
INECESNPCQ NGGQCKDLVG RYECDCQGTG FEGIRCENDI DECNMEGDYC
2010 2020 2030 2040 2050
GGLGRCFNKP GSFQCICQKP YCGAYCNFTD PCNATDLCSN GGRCVESCGA
2060 2070 2080 2090 2100
KPDYYCECPE GFAGKNCTAP ITAKEDGPST TDIAIIVIPV VVVLLLIAGA
2110 2120 2130 2140
LLGTFLVMAR NKRATRGTYS PSAQEYCNPR LEMDNVLKPP PEERLI
Length:2,146
Mass (Da):233,572
Last modified:June 21, 2005 - v3
Checksum:i8E23B9E32B761115
GO
Isoform B (identifier: P10040-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     526-526: G → ASDMEPLTPLELDILDATLCPSEKKKRYISPEWLKRKRCELKLS

Note: No experimental confirmation available.
Show »
Length:2,189
Mass (Da):238,643
Checksum:i89C31579A5DDDA38
GO

Sequence cautioni

The sequence AAM49878.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1661 – 167313VDPTP…TDIDQ → WWIRRQLFPRTSTK in CAA28793 (PubMed:3107986).CuratedAdd
BLAST
Sequence conflicti1719 – 17191V → L in AAA28428 (PubMed:2344615).Curated
Sequence conflicti1952 – 19521N → K in CAA28793 (PubMed:3107986).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei526 – 5261G → ASDMEPLTPLELDILDATLC PSEKKKRYISPEWLKRKRCE LKLS in isoform B. CuratedVSP_031870

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33753 mRNA. Translation: AAA28428.1.
AE014297 Genomic DNA. Translation: AAF56276.1.
AE014297 Genomic DNA. Translation: ABI31202.1.
AY118509 mRNA. Translation: AAM49878.1. Different initiation.
X05144 mRNA. Translation: CAA28793.1.
PIRiA35672.
B26637.
RefSeqiNP_001036751.1. NM_001043286.2. [P10040-2]
NP_524480.2. NM_079756.3. [P10040-1]
UniGeneiDm.2365.

Genome annotation databases

EnsemblMetazoaiFBtr0084603; FBpp0083987; FBgn0259685. [P10040-1]
GeneIDi42896.
KEGGidme:Dmel_CG6383.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33753 mRNA. Translation: AAA28428.1.
AE014297 Genomic DNA. Translation: AAF56276.1.
AE014297 Genomic DNA. Translation: ABI31202.1.
AY118509 mRNA. Translation: AAM49878.1. Different initiation.
X05144 mRNA. Translation: CAA28793.1.
PIRiA35672.
B26637.
RefSeqiNP_001036751.1. NM_001043286.2. [P10040-2]
NP_524480.2. NM_079756.3. [P10040-1]
UniGeneiDm.2365.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WSIX-ray2.95X/Y2110-2146[»]
4YL8X-ray1.50B2110-2146[»]
ProteinModelPortaliP10040.
SMRiP10040. Positions 2110-2146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67824. 8 interactions.
DIPiDIP-40915N.
IntActiP10040. 8 interactions.
MINTiMINT-89007.
STRINGi7227.FBpp0293268.

Protein family/group databases

TCDBi9.B.87.1.11. the selenoprotein p receptor (selp-receptor) family.

Proteomic databases

PaxDbiP10040.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084603; FBpp0083987; FBgn0259685. [P10040-1]
GeneIDi42896.
KEGGidme:Dmel_CG6383.

Organism-specific databases

CTDi42896.
FlyBaseiFBgn0259685. crb.

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
ENOG410XP6K. LUCA.
GeneTreeiENSGT00810000125346.
InParanoidiP10040.
KOiK16681.
OrthoDBiEOG7FBRGQ.
PhylomeDBiP10040.

Enzyme and pathway databases

SignaLinkiP10040.

Miscellaneous databases

GenomeRNAii42896.
PROiP10040.

Gene expression databases

BgeeiP10040.
GenevisibleiP10040. DM.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00008. EGF. 18 hits.
PF07645. EGF_CA. 2 hits.
PF00054. Laminin_G_1. 2 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 28 hits.
SM00179. EGF_CA. 23 hits.
SM00282. LamG. 3 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
SSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 16 hits.
PS00022. EGF_1. 25 hits.
PS01186. EGF_2. 17 hits.
PS50026. EGF_3. 27 hits.
PS01187. EGF_CA. 13 hits.
PS50025. LAM_G_DOMAIN. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Crumbs encodes an EGF-like protein expressed on apical membranes of Drosophila epithelial cells and required for organization of epithelia."
    Tepass U., Theres C., Knust E.
    Cell 61:787-799(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: Oregon-R.
    Tissue: Embryo.
  2. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1578-2146.
    Strain: Berkeley.
    Tissue: Embryo.
  5. "EGF homologous sequences encoded in the genome of Drosophila melanogaster, and their relation to neurogenic genes."
    Knust E., Dietrich U., Tepass U., Bremer K.A., Weigel D., Vaessin H., Campos-Ortega J.A.
    EMBO J. 6:761-766(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1661-1952.
    Tissue: Embryo.
  6. "Discs Lost, a novel multi-PDZ domain protein, establishes and maintains epithelial polarity."
    Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.
    Cell 96:833-845(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PATJ.
  7. Erratum
    Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.
    Cell 115:765-766(2003)
  8. "Apical, lateral, and basal polarization cues contribute to the development of the follicular epithelium during Drosophila oogenesis."
    Tanentzapf G., Smith C., McGlade J., Tepass U.
    J. Cell Biol. 151:891-904(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PATJ.
  9. "Drosophila Stardust is a partner of Crumbs in the control of epithelial cell polarity."
    Bachmann A., Schneider M., Theilenberg E., Grawe F., Knust E.
    Nature 414:638-643(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A SAC COMPLEX WITH PATJ AND SDT.
  10. "Interaction of Par-6 and Crumbs complexes is essential for photoreceptor morphogenesis in Drosophila."
    Nam S.-C., Choi K.-W.
    Development 130:4363-4372(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THE PAR-6 COMPLEX.
  11. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
    Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
    Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1100, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Oregon-R.
    Tissue: Head.

Entry informationi

Entry nameiCRB_DROME
AccessioniPrimary (citable) accession number: P10040
Secondary accession number(s): Q0KI19, Q8MSX5, Q9VC97
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: June 21, 2005
Last modified: July 6, 2016
This is version 183 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.