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Protein

Protein dachsous

Gene

ds

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

Functioni

Involved in morphogenesis. May also be involved in cell adhesion.1 Publication1 Publication

GO - Molecular functioni

  • cadherin binding Source: FlyBase
  • calcium ion binding Source: FlyBase
  • cell adhesion molecule binding Source: FlyBase
  • receptor activity Source: FlyBase
  • signal transducer activity Source: FlyBase

GO - Biological processi

  • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: FlyBase
  • cell-cell adhesion mediated by cadherin Source: FlyBase
  • cell morphogenesis involved in differentiation Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • equator specification Source: FlyBase
  • establishment of cell polarity Source: FlyBase
  • establishment of epithelial cell apical/basal polarity Source: FlyBase
  • establishment of imaginal disc-derived wing hair orientation Source: FlyBase
  • establishment of ommatidial planar polarity Source: UniProtKB
  • establishment of planar polarity Source: FlyBase
  • establishment of tissue polarity Source: FlyBase
  • eye morphogenesis Source: FlyBase
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: FlyBase
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: FlyBase
  • imaginal disc-derived leg morphogenesis Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • microtubule cytoskeleton organization involved in establishment of planar polarity Source: FlyBase
  • ommatidial rotation Source: FlyBase
  • peptide cross-linking Source: UniProtKB
  • regulation of establishment of planar polarity Source: FlyBase
  • regulation of tube length, open tracheal system Source: FlyBase
  • signal transduction Source: GOC
  • single organismal cell-cell adhesion Source: FlyBase
  • wing disc pattern formation Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Protein dachsous
Alternative name(s):
Adherin
Gene namesi
Name:ds
ORF Names:CG17941
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0000497. ds.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 30453025ExtracellularSequence analysisAdd
BLAST
Transmembranei3046 – 306621HelicalSequence analysisAdd
BLAST
Topological domaini3067 – 3503437CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: FlyBase
  • integral component of plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi236 – 2361S → A: Decreased phosphorylation by fj. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 35033483Protein dachsousPRO_0000004009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence analysis
Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence analysis
Modified residuei236 – 2361Phosphoserine1 Publication
Glycosylationi245 – 2451N-linked (GlcNAc...)Sequence analysis
Glycosylationi381 – 3811N-linked (GlcNAc...)Sequence analysis
Glycosylationi416 – 4161N-linked (GlcNAc...)Sequence analysis
Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence analysis
Glycosylationi594 – 5941N-linked (GlcNAc...)Sequence analysis
Glycosylationi743 – 7431N-linked (GlcNAc...)Sequence analysis
Glycosylationi966 – 9661N-linked (GlcNAc...)Sequence analysis
Glycosylationi991 – 9911N-linked (GlcNAc...)Sequence analysis
Glycosylationi1006 – 10061N-linked (GlcNAc...)Sequence analysis
Glycosylationi1029 – 10291N-linked (GlcNAc...)Sequence analysis
Glycosylationi1143 – 11431N-linked (GlcNAc...)Sequence analysis
Glycosylationi1236 – 12361N-linked (GlcNAc...)Sequence analysis
Glycosylationi1453 – 14531N-linked (GlcNAc...)Sequence analysis
Glycosylationi1479 – 14791N-linked (GlcNAc...)Sequence analysis
Glycosylationi1524 – 15241N-linked (GlcNAc...)Sequence analysis
Glycosylationi1553 – 15531N-linked (GlcNAc...)Sequence analysis
Glycosylationi1700 – 17001N-linked (GlcNAc...)Sequence analysis
Glycosylationi1884 – 18841N-linked (GlcNAc...)Sequence analysis
Glycosylationi1940 – 19401N-linked (GlcNAc...)Sequence analysis
Glycosylationi2115 – 21151N-linked (GlcNAc...)Sequence analysis
Glycosylationi2211 – 22111N-linked (GlcNAc...)Sequence analysis
Glycosylationi2212 – 22121N-linked (GlcNAc...)Sequence analysis
Glycosylationi2421 – 24211N-linked (GlcNAc...)Sequence analysis
Glycosylationi2511 – 25111N-linked (GlcNAc...)Sequence analysis
Glycosylationi2520 – 25201N-linked (GlcNAc...)Sequence analysis
Glycosylationi2547 – 25471N-linked (GlcNAc...)Sequence analysis
Glycosylationi2588 – 25881N-linked (GlcNAc...)Sequence analysis
Glycosylationi2678 – 26781N-linked (GlcNAc...)Sequence analysis
Glycosylationi2845 – 28451N-linked (GlcNAc...)Sequence analysis
Glycosylationi2967 – 29671N-linked (GlcNAc...)Sequence analysis
Modified residuei3465 – 34651Phosphoserine1 Publication
Modified residuei3469 – 34691Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by fj on Ser/Thr of cadherin domains.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ24292.
PRIDEiQ24292.

PTM databases

iPTMnetiQ24292.

Expressioni

Tissue specificityi

Expressed in embryonic ectoderm. In larvae, expression is restricted to imaginal disks and brain.1 Publication

Developmental stagei

Expressed throughout embryogenesis where it is first detected during gastrulation. Also expressed in larvae and adults.1 Publication

Gene expression databases

BgeeiQ24292.
ExpressionAtlasiQ24292. differential.
GenevisibleiQ24292. DM.

Interactioni

GO - Molecular functioni

  • cadherin binding Source: FlyBase
  • cell adhesion molecule binding Source: FlyBase

Protein-protein interaction databases

BioGridi59500. 6 interactions.
DIPiDIP-49190N.
IntActiQ24292. 4 interactions.
MINTiMINT-898703.
STRINGi7227.FBpp0077708.

Structurei

3D structure databases

ProteinModelPortaliQ24292.
SMRiQ24292. Positions 60-2115, 2207-3025.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 121100Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini122 – 233112Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini234 – 340107Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini345 – 451107Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini452 – 558107Cadherin 5PROSITE-ProRule annotationAdd
BLAST
Domaini559 – 662104Cadherin 6PROSITE-ProRule annotationAdd
BLAST
Domaini663 – 774112Cadherin 7PROSITE-ProRule annotationAdd
BLAST
Domaini775 – 878104Cadherin 8PROSITE-ProRule annotationAdd
BLAST
Domaini879 – 983105Cadherin 9PROSITE-ProRule annotationAdd
BLAST
Domaini984 – 1100117Cadherin 10PROSITE-ProRule annotationAdd
BLAST
Domaini1101 – 1203103Cadherin 11PROSITE-ProRule annotationAdd
BLAST
Domaini1205 – 1312108Cadherin 12PROSITE-ProRule annotationAdd
BLAST
Domaini1313 – 1432120Cadherin 13PROSITE-ProRule annotationAdd
BLAST
Domaini1433 – 1549117Cadherin 14PROSITE-ProRule annotationAdd
BLAST
Domaini1556 – 1666111Cadherin 15PROSITE-ProRule annotationAdd
BLAST
Domaini1667 – 1794128Cadherin 16PROSITE-ProRule annotationAdd
BLAST
Domaini1796 – 1899104Cadherin 17PROSITE-ProRule annotationAdd
BLAST
Domaini1900 – 2004105Cadherin 18PROSITE-ProRule annotationAdd
BLAST
Domaini2005 – 2111107Cadherin 19PROSITE-ProRule annotationAdd
BLAST
Domaini2114 – 2269156Cadherin 20PROSITE-ProRule annotationAdd
BLAST
Domaini2270 – 2375106Cadherin 21PROSITE-ProRule annotationAdd
BLAST
Domaini2375 – 2479105Cadherin 22PROSITE-ProRule annotationAdd
BLAST
Domaini2489 – 2595107Cadherin 23PROSITE-ProRule annotationAdd
BLAST
Domaini2596 – 2699104Cadherin 24PROSITE-ProRule annotationAdd
BLAST
Domaini2701 – 2809109Cadherin 25PROSITE-ProRule annotationAdd
BLAST
Domaini2810 – 2916107Cadherin 26PROSITE-ProRule annotationAdd
BLAST
Domaini2919 – 3028110Cadherin 27PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 27 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1219. Eukaryota.
ENOG410XPEI. LUCA.
InParanoidiQ24292.
KOiK16507.
OrthoDBiEOG75TM9Z.
PhylomeDBiQ24292.

Family and domain databases

Gene3Di2.60.40.60. 27 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
[Graphical view]
PfamiPF00028. Cadherin. 23 hits.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 27 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 27 hits.
PROSITEiPS00232. CADHERIN_1. 20 hits.
PS50268. CADHERIN_2. 27 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q24292-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRSSLLILL AIVLLGSSQA ASHDQERERK LEVFEGVAVD YQIGYIGDFG
60 70 80 90 100
GIDSGPPYII VAEAGVETDL AIDRATGEIR TKVKLDRETR ASYSLVAIPL
110 120 130 140 150
SGRNIRVLVT VKDENDNAPT FPQTSMHIEF PENTPREVKR TLLPARDLDL
160 170 180 190 200
EPYNTQRYNI VSGNVNDAFR LSSHRERDGV LYLDLQISGF LDRETTPGYS
210 220 230 240 250
LLIEALDGGT PPLRGFMTVN ITIQDVNDNQ PIFNQSRYFA TVPENATVGT
260 270 280 290 300
SVLQVYASDT DADENGLVEY AINRRQSDKE QMFRIDPRTG AIYINKALDF
310 320 330 340 350
ETKELHELVV VAKDHGEQPL ETTAFVSIRV TDVNDNQPTI NVIFLSDDAS
360 370 380 390 400
PKISESAQPG EFVARISVHD PDSKTEYANV NVTLNGGDGH FALTTRDNSI
410 420 430 440 450
YLVIVHLPLD REIVSNYTLS VVATDKGTPP LHASKSIFLR ITDVNDNPPE
460 470 480 490 500
FEQDLYHANV MEVADPGTSV LQVLAHDRDE GLNSALTYSL AETPETHAQW
510 520 530 540 550
FQIDPQTGLI TTRSHIDCET EPVPQLTVVA RDGGVPPLSS TATVLVTIHD
560 570 580 590 600
VNDNEPIFDQ SFYNVSVAEN EPVGRCILKV SASDPDCGVN AMVNYTIGEG
610 620 630 640 650
FKHLTEFEVR SASGEICIAG ELDFERRSSY EFPVLATDRG GLSTTAMIKM
660 670 680 690 700
QLTDVNDNRP VFYPREYKVS LRESPKASSQ ASSTPIVAVV ATDPDYGNFG
710 720 730 740 750
QVSYRIVAGN EAGIFRIDRS TGEIFVVRPD MLSVRTQPMH MLNISATDGG
760 770 780 790 800
NLRSNADAVV FLSIIDAMQR PPIFEKARYN YYVKEDIPRG TVVGSVIAAS
810 820 830 840 850
GDVAHRSPVR YSIYSGDPDG YFSIETNSGN IRIAKPLDHE AKSQVLLNIQ
860 870 880 890 900
ATLGEPPVYG HTQVNIEVED VNDNAPEFEA SMVRISVPES AELGAPLYAA
910 920 930 940 950
HAHDKDSGSS GQVTYSLVKE SGKGLFAIDA RSGHLILSQH LDYESSQRHT
960 970 980 990 1000
LIVTATDGGV PSLSTNLTIL VDVQDVNDNP PVFEKDEYSV NVSESRSINA
1010 1020 1030 1040 1050
QIIQVNASDL DTGNNARITY RIVDAGVDNV TNSISSSDVS QHFGIFPNSG
1060 1070 1080 1090 1100
WIYLRAPLDR ETRDRYQLTV LATDNGTPAA HAKTRVIVRV LDANDNDPKF
1110 1120 1130 1140 1150
QKSKYEFRIE ENLRRGSVVG VVTASDLDLG ENAAIRYSLL PINSSFQVHP
1160 1170 1180 1190 1200
VTGEISTREP LDRELRELYD LVVEARDQGT PVRSARVPVR IHVSDVNDNA
1210 1220 1230 1240 1250
PEIADPQEDV VSVREEQPPG TEVVRVRAVD RDHGQNASIT YSIVKGRDSD
1260 1270 1280 1290 1300
GHGLFSIDPT SGVIRTRVVL DHEERSIYRL GVAASDGGNP PRETVRMLRV
1310 1320 1330 1340 1350
EVLDLNDNRP TFTSSSLVFR VREDAALGHV VGSISPIERP ADVVRNSVEE
1360 1370 1380 1390 1400
SFEDLRVTYT LNPLTKDLIE AAFDIDRHSG NLVVARLLDR EVQSEFRLEI
1410 1420 1430 1440 1450
RALDTTASNN PQSSAITVKI EVADVNDNAP EWPQDPIDLQ VSEATPVGTI
1460 1470 1480 1490 1500
IHNFTATDAD TGTNGDLQYR LIRYFPQLNE SQEQAMSLFR MDSLTGALSL
1510 1520 1530 1540 1550
QAPLDFEAVQ EYLLIVQALD QSSNVTERLQ TSVTVRLRIL DANDHAPHFV
1560 1570 1580 1590 1600
SPNSSGGKTA SLFISDATRI GEVVAHIVAV DEDSGDNGQL TYEITGGNGE
1610 1620 1630 1640 1650
GRFRINSQTG IIELVKSLPP ATEDVEKGGR FNLIIGAKDH GQPEPKKSSL
1660 1670 1680 1690 1700
NLHLIVQGSH NNPPRFLQAV YRATILENVP SGSFVLQVTA KSLHGAENAN
1710 1720 1730 1740 1750
LSYEIPAGVA NDLFHVDWQR GIITTRGQFD RESQASYVLP VYVRDANRQS
1760 1770 1780 1790 1800
TLSSSAVRKQ RSSDSIGDTS NGQHFDVATI YITVGDVNDN SPEFRPGSCY
1810 1820 1830 1840 1850
GLSVPENSEP GVIHTVVASD LDEGPNADLI YSITGGNLGN KFSIDSSSGE
1860 1870 1880 1890 1900
LSARPLDREQ HSRYTLQIQA SDRGQPKSRQ GHCNITIFVE DQNDNAPRFK
1910 1920 1930 1940 1950
LSKYTGSVQE DAPLGTSVVQ ISAVDADLGV NARLVYSLAN ETQWQFAIDG
1960 1970 1980 1990 2000
QSGLITTVGK LDRELQASYN FMVLATDGGR YEVRSATVPV QINVLDINDN
2010 2020 2030 2040 2050
RPIFERYPYI GQVPALIQPG QTLLKVQALD ADLGANAEIV YSLNAENSAV
2060 2070 2080 2090 2100
SAKFRINPST GALSASQSLA SESGKLLHLE VVARDKGNPP QSSLGLIELL
2110 2120 2130 2140 2150
IGEAPQGTPV LRFQNETYRV MLKENSPSGT RLLQVVALRS DGRRQKVQFS
2160 2170 2180 2190 2200
FGAGNEDGIL SLDSLSGEIR VNKPHLLDYD RFSTPSMSAL SRGRALHYEE
2210 2220 2230 2240 2250
EIDESSEEDP NNSTRSQRAL TSSSFALTNS QPNEIRVVLV ARTADAPFLA
2260 2270 2280 2290 2300
SYAELVIELE DENDNSPKFS QKQFVATVSE GNNKGTFVAQ VHAFDSDAGS
2310 2320 2330 2340 2350
NARLRYHIVD GNHDNAFVIE PAFSGIVRTN IVLDREIRDI YKLKIIATDE
2360 2370 2380 2390 2400
GVPQMTGTAT IRVQIVDVND NQPTFPPNNL VTVSEATELG AVITSISAND
2410 2420 2430 2440 2450
VDTYPALTYR LGAESTVDIE NMSIFALDRY SGKLVLKRRL DYELQQEYEL
2460 2470 2480 2490 2500
DVIASDAAHE ARTVLTVRVN DENDNAPVFL AQQPPAYFAI LPAISEISES
2510 2520 2530 2540 2550
LSVDFDLLTV NATDADSEGN NSKVIYIIEP AQEGFSVHPS NGVVSVNMSR
2560 2570 2580 2590 2600
LQPAVSSSGD YFVRIIAKDA GKPALKSSTL LRVQANDNGS GRSQFLQNQY
2610 2620 2630 2640 2650
RAQISEAAPL GSVVLQLGQD ALDQSLAIIA GNEESAFELL QSKAIVLVKP
2660 2670 2680 2690 2700
LDRERNDLYK LRLVLSHPHG PPLISSLNSS SGISVIITIL DANDNFPIFD
2710 2720 2730 2740 2750
RSAKYEAEIS ELAPLRYSIA QLQAIDADQE NTPNSEVVYD ITSGNDEHMF
2760 2770 2780 2790 2800
TIDLVTGVLF VNNRLDYDSG AKSYELIIRA CDSHHQRPLC SLQPFRLELH
2810 2820 2830 2840 2850
DENDNEPKFP LTEYVHFLAE NEPVGSSVFR AHASDLDKGP FGQLNYSIGP
2860 2870 2880 2890 2900
APSDESSWKM FRVDSESGLV TSAFVFDYEQ RQRYDMELLA SDMGGKKASV
2910 2920 2930 2940 2950
AVRVEIESRD EFTPQFTERT YRFVLPAAVA LPQGYVVGQV TATDSDSGPD
2960 2970 2980 2990 3000
GRVVYQLSAP HSHFKVNRSS GAVLIKRKLK LDGDGDGNLY MDGRDISLVI
3010 3020 3030 3040 3050
SASSGRHNSL SSMAVVEIAL DPLAHPGTNL ASAGGSSSGS IGDWAIGLLV
3060 3070 3080 3090 3100
AFLLVLCAAA GIFLFIHMRS RKPRNAVKPH LATDNAGVGN TNSYVDPSAF
3110 3120 3130 3140 3150
DTIPIRGSIS GGAAGAASGQ FAPPKYDEIP PFGAHAGSSG AATTSELSGS
3160 3170 3180 3190 3200
EQSGSSGRGS AEDDGEDEEI RMINEGPLHH RNGGAGAGSD DGRISDISVQ
3210 3220 3230 3240 3250
NTQEYLARLG IVDHDPSGAG GGASSMAGSS HPMHLYHDDD ATARSDITNL
3260 3270 3280 3290 3300
IYAKLNDVTG AGSEIGSSAD DAGTTAGSIG TIGTAITHGH GVMSSYGEVP
3310 3320 3330 3340 3350
VPVPVVVGGS NVGGSLSSIV HSEEELTGSY NWDYLLDWGP QYQPLAHVFS
3360 3370 3380 3390 3400
EIARLKDDTL SEHSGSGASS SAKSKHSSSH SSAGAGSVVL KPPPSAPPTH
3410 3420 3430 3440 3450
IPPPLLTNVA PRAINLPMRL PPHLSLAPAH LPRSPIGHEA SGSFSTSSAM
3460 3470 3480 3490 3500
SPSFSPSLSP LATRSPSISP LGAGPPTHLP HVSLPRHGHA PQPSQRGNVG

TRM
Length:3,503
Mass (Da):379,780
Last modified:October 1, 2002 - v3
Checksum:i975B09F059F7EEF5
GO

Sequence cautioni

The sequence AAF51468.3 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1070 – 10701V → I in AAA79329 (PubMed:7601355).Curated
Sequence conflicti1490 – 14901R → S in AAA79329 (PubMed:7601355).Curated
Sequence conflicti1636 – 16361G → S in AAA79329 (PubMed:7601355).Curated
Sequence conflicti1692 – 16921S → P in AAA79329 (PubMed:7601355).Curated
Sequence conflicti1804 – 18041V → I in AAA79329 (PubMed:7601355).Curated
Sequence conflicti2029 – 20291L → I in AAA79329 (PubMed:7601355).Curated
Sequence conflicti2210 – 22101P → A in AAA79329 (PubMed:7601355).Curated
Sequence conflicti2289 – 22891A → S in AAA79329 (PubMed:7601355).Curated
Sequence conflicti2536 – 25361S → T in AAA79329 (PubMed:7601355).Curated
Sequence conflicti2862 – 28621R → Q in AAA79329 (PubMed:7601355).Curated
Sequence conflicti3038 – 30381S → G in AAA79329 (PubMed:7601355).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08811 mRNA. Translation: AAA79329.2.
AE014134 Genomic DNA. Translation: AAF51468.3. Different initiation.
RefSeqiNP_001285551.1. NM_001298622.1.
NP_523446.2. NM_078722.3.

Genome annotation databases

GeneIDi33245.
KEGGidme:Dmel_CG17941.
UCSCiCG17941-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L08811 mRNA. Translation: AAA79329.2.
AE014134 Genomic DNA. Translation: AAF51468.3. Different initiation.
RefSeqiNP_001285551.1. NM_001298622.1.
NP_523446.2. NM_078722.3.

3D structure databases

ProteinModelPortaliQ24292.
SMRiQ24292. Positions 60-2115, 2207-3025.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59500. 6 interactions.
DIPiDIP-49190N.
IntActiQ24292. 4 interactions.
MINTiMINT-898703.
STRINGi7227.FBpp0077708.

PTM databases

iPTMnetiQ24292.

Proteomic databases

PaxDbiQ24292.
PRIDEiQ24292.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi33245.
KEGGidme:Dmel_CG17941.
UCSCiCG17941-RA. d. melanogaster.

Organism-specific databases

CTDi109661.
FlyBaseiFBgn0000497. ds.

Phylogenomic databases

eggNOGiKOG1219. Eukaryota.
ENOG410XPEI. LUCA.
InParanoidiQ24292.
KOiK16507.
OrthoDBiEOG75TM9Z.
PhylomeDBiQ24292.

Miscellaneous databases

GenomeRNAii33245.
NextBioi782633.
PROiQ24292.

Gene expression databases

BgeeiQ24292.
ExpressionAtlasiQ24292. differential.
GenevisibleiQ24292. DM.

Family and domain databases

Gene3Di2.60.40.60. 27 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
[Graphical view]
PfamiPF00028. Cadherin. 23 hits.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 27 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 27 hits.
PROSITEiPS00232. CADHERIN_1. 20 hits.
PS50268. CADHERIN_2. 27 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Dachsous encodes a member of the cadherin superfamily that controls imaginal disc morphogenesis in Drosophila."
    Clark H.F., Brentrup D., Schneitz K., Bieber A., Goodman C., Noll M.
    Genes Dev. 9:1530-1542(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Tissue: Embryo.
  2. Noll M.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "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.
  4. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3465 AND SER-3469, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  6. "Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin domains."
    Ishikawa H.O., Takeuchi H., Haltiwanger R.S., Irvine K.D.
    Science 321:401-404(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-236, MUTAGENESIS OF SER-236.

Entry informationi

Entry nameiDS_DROME
AccessioniPrimary (citable) accession number: Q24292
Secondary accession number(s): Q9VPS4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: October 1, 2002
Last modified: January 20, 2016
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. 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.