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Protein

Protein crumbs

Gene

crb

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

Functioni

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.6 Publications

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
  • amnioserosa maintenance Source: FlyBase
  • apical constriction Source: FlyBase
  • apical protein localization Source: FlyBase
  • assembly of apicomedial cortex actomyosin Source: FlyBase
  • cell-cell junction assembly Source: FlyBase
  • cell division Source: UniProtKB-KW
  • 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 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

Keywordsi

Molecular functionDevelopmental protein
Biological processCell cycle, Cell division, Differentiation, Mitosis

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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0259685 crb

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini89 – 2082ExtracellularSequence analysisAdd BLAST1994
Transmembranei2083 – 2109HelicalSequence analysisAdd BLAST27
Topological domaini2110 – 2146CytoplasmicSequence analysisAdd BLAST37

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoskeleton, 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 (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).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 88Add BLAST88
ChainiPRO_000000749989 – 2146Protein crumbsAdd BLAST2058

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi94N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi196N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi236N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi237N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi269 ↔ 280PROSITE-ProRule annotation
Disulfide bondi274 ↔ 289PROSITE-ProRule annotation
Disulfide bondi291 ↔ 300PROSITE-ProRule annotation
Disulfide bondi308 ↔ 319PROSITE-ProRule annotation
Disulfide bondi313 ↔ 329PROSITE-ProRule annotation
Disulfide bondi331 ↔ 340PROSITE-ProRule annotation
Glycosylationi334N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi350 ↔ 361PROSITE-ProRule annotation
Disulfide bondi355 ↔ 372PROSITE-ProRule annotation
Disulfide bondi374 ↔ 383PROSITE-ProRule annotation
Disulfide bondi390 ↔ 401PROSITE-ProRule annotation
Disulfide bondi395 ↔ 410PROSITE-ProRule annotation
Glycosylationi398N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi412 ↔ 422PROSITE-ProRule annotation
Disulfide bondi429 ↔ 440PROSITE-ProRule annotation
Disulfide bondi434 ↔ 449PROSITE-ProRule annotation
Disulfide bondi451 ↔ 460PROSITE-ProRule annotation
Disulfide bondi466 ↔ 477PROSITE-ProRule annotation
Disulfide bondi471 ↔ 486PROSITE-ProRule annotation
Disulfide bondi488 ↔ 497PROSITE-ProRule annotation
Disulfide bondi547 ↔ 560PROSITE-ProRule annotation
Glycosylationi548N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi554 ↔ 567PROSITE-ProRule annotation
Glycosylationi563N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi569 ↔ 578PROSITE-ProRule annotation
Disulfide bondi611 ↔ 622PROSITE-ProRule annotation
Disulfide bondi616 ↔ 632PROSITE-ProRule annotation
Disulfide bondi634 ↔ 643PROSITE-ProRule annotation
Disulfide bondi650 ↔ 662PROSITE-ProRule annotation
Disulfide bondi657 ↔ 671PROSITE-ProRule annotation
Disulfide bondi673 ↔ 682PROSITE-ProRule annotation
Disulfide bondi689 ↔ 700PROSITE-ProRule annotation
Disulfide bondi694 ↔ 709PROSITE-ProRule annotation
Disulfide bondi711 ↔ 720PROSITE-ProRule annotation
Disulfide bondi727 ↔ 738PROSITE-ProRule annotation
Disulfide bondi732 ↔ 747PROSITE-ProRule annotation
Glycosylationi734N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi744N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi749 ↔ 758PROSITE-ProRule annotation
Disulfide bondi765 ↔ 776PROSITE-ProRule annotation
Disulfide bondi770 ↔ 785PROSITE-ProRule annotation
Disulfide bondi787 ↔ 797PROSITE-ProRule annotation
Disulfide bondi804 ↔ 815PROSITE-ProRule annotation
Disulfide bondi809 ↔ 824PROSITE-ProRule annotation
Disulfide bondi826 ↔ 835PROSITE-ProRule annotation
Disulfide bondi842 ↔ 853PROSITE-ProRule annotation
Disulfide bondi847 ↔ 888PROSITE-ProRule annotation
Glycosylationi858N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi882N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi890 ↔ 899PROSITE-ProRule annotation
Disulfide bondi906 ↔ 917PROSITE-ProRule annotation
Disulfide bondi911 ↔ 926PROSITE-ProRule annotation
Disulfide bondi928 ↔ 937PROSITE-ProRule annotation
Disulfide bondi944 ↔ 955PROSITE-ProRule annotation
Disulfide bondi950 ↔ 964PROSITE-ProRule annotation
Disulfide bondi966 ↔ 975PROSITE-ProRule annotation
Glycosylationi974N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi982 ↔ 993PROSITE-ProRule annotation
Disulfide bondi987 ↔ 1007PROSITE-ProRule annotation
Glycosylationi1006N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1009 ↔ 1018PROSITE-ProRule annotation
Glycosylationi1100N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1112N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1136N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1171 ↔ 1203PROSITE-ProRule annotation
Glycosylationi1190N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1209 ↔ 1220PROSITE-ProRule annotation
Disulfide bondi1214 ↔ 1229PROSITE-ProRule annotation
Disulfide bondi1231 ↔ 1240PROSITE-ProRule annotation
Glycosylationi1243N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1253N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1352N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1361N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1439N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1452N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1483 ↔ 1494PROSITE-ProRule annotation
Disulfide bondi1488 ↔ 1503PROSITE-ProRule annotation
Disulfide bondi1505 ↔ 1514PROSITE-ProRule annotation
Glycosylationi1543N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1713 ↔ 1757PROSITE-ProRule annotation
Glycosylationi1737N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1749N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1760 ↔ 1771PROSITE-ProRule annotation
Disulfide bondi1765 ↔ 1780PROSITE-ProRule annotation
Disulfide bondi1782 ↔ 1791PROSITE-ProRule annotation
Disulfide bondi1798 ↔ 1809PROSITE-ProRule annotation
Disulfide bondi1803 ↔ 1818PROSITE-ProRule annotation
Glycosylationi1806N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1820 ↔ 1829PROSITE-ProRule annotation
Disulfide bondi1836 ↔ 1847PROSITE-ProRule annotation
Disulfide bondi1841 ↔ 1856PROSITE-ProRule annotation
Glycosylationi1846N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1858 ↔ 1867PROSITE-ProRule annotation
Disulfide bondi1875 ↔ 1886PROSITE-ProRule annotation
Disulfide bondi1880 ↔ 1900PROSITE-ProRule annotation
Glycosylationi1882N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1891N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1897N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1916 ↔ 1927PROSITE-ProRule annotation
Disulfide bondi1921 ↔ 1936PROSITE-ProRule annotation
Disulfide bondi1938 ↔ 1947PROSITE-ProRule annotation
Disulfide bondi1954 ↔ 1965PROSITE-ProRule annotation
Disulfide bondi1959 ↔ 1974PROSITE-ProRule annotation
Disulfide bondi1976 ↔ 1986PROSITE-ProRule annotation
Disulfide bondi1993 ↔ 2006PROSITE-ProRule annotation
Disulfide bondi2000 ↔ 2015PROSITE-ProRule annotation
Disulfide bondi2017 ↔ 2026PROSITE-ProRule annotation
Glycosylationi2027N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2032 ↔ 2044PROSITE-ProRule annotation
Glycosylationi2033N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2038 ↔ 2056PROSITE-ProRule annotation
Disulfide bondi2058 ↔ 2067PROSITE-ProRule annotation
Glycosylationi2066N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Phosphorylated in the cytoplasmic domain.Curated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP10040
PRIDEiP10040

PTM databases

iPTMnetiP10040

Expressioni

Gene expression databases

BgeeiFBgn0259685
ExpressionAtlasiP10040 differential
GenevisibleiP10040 DM

Interactioni

Subunit structurei

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).5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi67824, 54 interactors
DIPiDIP-40915N
IntActiP10040, 11 interactors
MINTiP10040
STRINGi7227.FBpp0293268

Structurei

Secondary structure

12146
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2116 – 2119Combined sources4
Turni2121 – 2123Combined sources3
Helixi2131 – 2135Combined sources5

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini265 – 301EGF-like 1PROSITE-ProRule annotationAdd BLAST37
Domaini304 – 341EGF-like 2PROSITE-ProRule annotationAdd BLAST38
Domaini346 – 384EGF-like 3PROSITE-ProRule annotationAdd BLAST39
Domaini386 – 423EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini425 – 461EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini462 – 498EGF-like 6PROSITE-ProRule annotationAdd BLAST37
Domaini543 – 579EGF-like 7PROSITE-ProRule annotationAdd BLAST37
Domaini609 – 644EGF-like 8PROSITE-ProRule annotationAdd BLAST36
Domaini646 – 683EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini685 – 721EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini723 – 759EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini761 – 798EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini800 – 836EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini838 – 900EGF-like 14PROSITE-ProRule annotationAdd BLAST63
Domaini902 – 938EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini940 – 976EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini978 – 1019EGF-like 17PROSITE-ProRule annotationAdd BLAST42
Domaini1021 – 1203Laminin G-like 1PROSITE-ProRule annotationAdd BLAST183
Domaini1205 – 1241EGF-like 18PROSITE-ProRule annotationAdd BLAST37
Domaini1248 – 1483Laminin G-like 2PROSITE-ProRule annotationAdd BLAST236
Domaini1479 – 1515EGF-like 19PROSITE-ProRule annotationAdd BLAST37
Domaini1555 – 1757Laminin G-like 3PROSITE-ProRule annotationAdd BLAST203
Domaini1758 – 1792EGF-like 20PROSITE-ProRule annotationAdd BLAST35
Domaini1794 – 1830EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1832 – 1868EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1871 – 1909EGF-like 23PROSITE-ProRule annotationAdd BLAST39
Domaini1912 – 1948EGF-like 24PROSITE-ProRule annotationAdd BLAST37
Domaini1950 – 1987EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini1989 – 2027EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini2028 – 2068EGF-like 27PROSITE-ProRule annotationAdd BLAST41

Sequence similaritiesi

Belongs to the Crumbs protein family.Curated

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG1217 Eukaryota
ENOG410XP6K LUCA
GeneTreeiENSGT00910000144018
InParanoidiP10040
KOiK16681
OMAiYFNGSAY
OrthoDBiEOG091G001C
PhylomeDBiP10040

Family and domain databases

InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
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_cys_sf
IPR001791 Laminin_G
PfamiView protein in Pfam
PF00008 EGF, 17 hits
PF07645 EGF_CA, 2 hits
PF12661 hEGF, 4 hits
PF00054 Laminin_G_1, 2 hits
PF02210 Laminin_G_2, 1 hit
SMARTiView protein in SMART
SM00181 EGF, 28 hits
SM00179 EGF_CA, 23 hits
SM00282 LamG, 3 hits
SUPFAMiSSF49899 SSF49899, 5 hits
SSF57184 SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS00010 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

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 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1661 – 1673VDPTP…TDIDQ → WWIRRQLFPRTSTK in CAA28793 (PubMed:3107986).CuratedAdd BLAST13
Sequence conflicti1719V → L in AAA28428 (PubMed:2344615).Curated1
Sequence conflicti1952N → K in CAA28793 (PubMed:3107986).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_031870526G → ASDMEPLTPLELDILDATLC PSEKKKRYISPEWLKRKRCE LKLS in isoform B. Curated1

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]
FBtr0111008; FBpp0110307; FBgn0259685 [P10040-2]
GeneIDi42896
KEGGidme:Dmel_CG6383

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiCRB_DROME
AccessioniPrimary (citable) accession number: P10040
Secondary accession number(s): Q0KI19, Q8MSX5, Q9VC97
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: June 21, 2005
Last modified: March 28, 2018
This is version 201 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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