Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O15943 (CADN_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neural-cadherin
Alternative name(s):
Cadherin-N
Short name=dN-cadherin
Gene names
Name:CadN
ORF Names:CG7100
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length3097 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. May associate with arm neural isoform andparticipate in the transmission of developmental information.

Subcellular location

Cell membrane; Single-pass type I membrane protein Potential.

Tissue specificity

In the embryo, the protein first appears in the mesoderm at stage 9 and is present in the myoblasts and muscle fibers by stage 12 and stage 14, respectively. At stage 12 the protein is also located in the axons of the entire CNS, but not in the glial cells. In third instar larvae protein is expressed in the CNS neuropile, photoreceptor axons and precursors of adult muscles.

Domain

Three calcium ions are usually bound at the interface of each cadherin domain and rigidify the connections, imparting a strong curvature to the full-length ectodomain By similarity.

Sequence similarities

Contains 16 cadherin domains.

Contains 3 EGF-like domains.

Contains 2 laminin G-like domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processR7 cell development

Inferred from mutant phenotype PubMed 17320070PubMed 18400161PubMed 18978776PubMed 21835342. Source: FlyBase

R8 cell development

Inferred from mutant phenotype PubMed 17320070PubMed 18400161. Source: FlyBase

axon extension

Inferred from mutant phenotype PubMed 19766621. Source: FlyBase

axon extension involved in axon guidance

Inferred from mutant phenotype PubMed 15735641. Source: FlyBase

axon guidance

Inferred from mutant phenotype PubMed 18516287PubMed 19766621PubMed 21835342. Source: FlyBase

axon target recognition

Inferred from mutant phenotype PubMed 11395005. Source: FlyBase

axonal fasciculation

Traceable author statement PubMed 10218152. Source: FlyBase

calcium-dependent cell-cell adhesion

Inferred from physical interaction Ref.1. Source: FlyBase

cell-cell adhesion mediated by cadherin

Inferred from direct assay PubMed 17320070. Source: FlyBase

homophilic cell adhesion

Inferred from direct assay PubMed 17320070Ref.1. Source: FlyBase

negative regulation of dendrite morphogenesis

Inferred from mutant phenotype PubMed 15066265. Source: FlyBase

ommatidial rotation

Inferred from mutant phenotype PubMed 16887833. Source: FlyBase

regulation of axon extension involved in axon guidance

Inferred from mutant phenotype PubMed 19766621. Source: FlyBase

regulation of dendrite morphogenesis

Inferred from mutant phenotype PubMed 21303851. Source: FlyBase

retinal ganglion cell axon guidance

Inferred from mutant phenotype PubMed 16864799. Source: FlyBase

   Cellular_componentaxon

Inferred from direct assay PubMed 19343204. Source: FlyBase

cell-cell junction

Inferred from direct assay Ref.1. Source: FlyBase

dendrite

Inferred from direct assay PubMed 19343204. Source: FlyBase

integral component of membrane

Inferred from sequence or structural similarity Ref.1. Source: FlyBase

integral component of plasma membrane

Inferred from sequence or structural similarity PubMed 10908592. Source: FlyBase

plasma membrane

Inferred from direct assay PubMed 20462449PubMed 21283588PubMed 22595515. Source: FlyBase

   Molecular_functionbeta-catenin binding

Non-traceable author statement PubMed 11253370. Source: FlyBase

cadherin binding

Inferred from physical interaction PubMed 22171007. Source: FlyBase

calcium ion binding

Inferred from direct assay PubMed 22171007. Source: FlyBase

cell adhesion molecule binding

Inferred from sequence or structural similarity PubMed 10908592. Source: FlyBase

protein homodimerization activity

Inferred from physical interaction PubMed 22171007. Source: FlyBase

receptor activity

Inferred from sequence or structural similarity PubMed 10908592. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform D (identifier: O15943-1)

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.
Isoform A (identifier: O15943-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1147-1206: ETYKLEAMAQ...MPVGGKVVSI → DRYRLRVSAS...VTVGTVVTSV
     1486-1536: RLAASDNLKE...DDRNLPKRVL → KLVASDSLNE...GMTNTPFTIM
Isoform B (identifier: O15943-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1486-1536: RLAASDNLKE...DDRNLPKRVL → KLVASDSLNE...GMTNTPFTIM
Isoform C (identifier: O15943-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1147-1206: ETYKLEAMAQ...MPVGGKVVSI → DRYRLRVSAS...VTVGTVVTSV
     1486-1536: RLAASDNLKE...DDRNLPKRVL → KLVASDSLNE...GMTNTPFTIM
     2851-2930: GEGRIMSPDS...ILVCLLIILI → PAGYKSSGST...LALCLGTLIL
Isoform E (identifier: O15943-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1147-1206: ETYKLEAMAQ...MPVGGKVVSI → DRYRLRVSAS...VTVGTVVTSV
Isoform F (identifier: O15943-6)

The sequence of this isoform differs from the canonical sequence as follows:
     2851-2930: GEGRIMSPDS...ILVCLLIILI → PAGYKSSGST...LALCLGTLIL
Isoform G (identifier: O15943-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1147-1206: ETYKLEAMAQ...MPVGGKVVSI → DRYRLRVSAS...VTVGTVVTSV
     2851-2930: GEGRIMSPDS...ILVCLLIILI → PAGYKSSGST...LALCLGTLIL
Isoform H (identifier: O15943-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1486-1536: RLAASDNLKE...DDRNLPKRVL → KLVASDSLNE...GMTNTPFTIM
     2851-2930: GEGRIMSPDS...ILVCLLIILI → PAGYKSSGST...LALCLGTLIL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3636 Potential
Propeptide37 – ?PRO_0000003881
Chain? – 3097Neural-cadherinPRO_0000003882

Regions

Topological domain? – 2916Extracellular Potential
Transmembrane2917 – 293721Helical; Potential
Topological domain2938 – 3097160Cytoplasmic Potential
Domain181 – 305125Cadherin 1
Domain430 – 543114Cadherin 2
Domain554 – 65198Cadherin 3
Domain660 – 75697Cadherin 4
Domain766 – 85893Cadherin 5
Domain867 – 968102Cadherin 6
Domain978 – 1078101Cadherin 7
Domain1087 – 118397Cadherin 8
Domain1193 – 1299107Cadherin 9
Domain1307 – 1414108Cadherin 10
Domain1423 – 151492Cadherin 11
Domain1523 – 1630108Cadherin 12
Domain1639 – 1742104Cadherin 13
Domain1749 – 1861113Cadherin 14
Domain1870 – 196697Cadherin 15
Domain1974 – 2085112Cadherin 16
Domain2346 – 237732EGF-like 1
Domain2379 – 2585207Laminin G-like 1
Domain2592 – 262736EGF-like 2
Domain2631 – 2822192Laminin G-like 2
Domain2869 – 290234EGF-like 3

Amino acid modifications

Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation1501N-linked (GlcNAc...) Potential
Glycosylation3251N-linked (GlcNAc...) Potential
Glycosylation4261N-linked (GlcNAc...) Potential
Glycosylation9301N-linked (GlcNAc...) Potential
Glycosylation12661N-linked (GlcNAc...) Potential
Disulfide bond2346 ↔ 2357 Potential
Disulfide bond2351 ↔ 2366 Potential
Disulfide bond2368 ↔ 2377 Potential
Disulfide bond2559 ↔ 2585 By similarity
Disulfide bond2592 ↔ 2607 Potential
Disulfide bond2601 ↔ 2616 Potential
Disulfide bond2618 ↔ 2627 Potential
Disulfide bond2787 ↔ 2822 By similarity
Disulfide bond2869 ↔ 2880 Potential
Disulfide bond2874 ↔ 2891 Potential
Disulfide bond2893 ↔ 2902 Potential

Natural variations

Alternative sequence1147 – 120660ETYKL…KVVSI → DRYRLRVSASDKGTPASAAD VDVELDVVDRNNKPPIWDKS IYGPIHIRENVTVGTVVTSV in isoform A, isoform C, isoform E and isoform G.
VSP_000667
Alternative sequence1486 – 153651RLAAS…PKRVL → KLVASDSLNENQTTIVINVR DVNDLPPQFPQTSYERTLDE GMTNTPFTIM in isoform A, isoform B, isoform C and isoform H.
VSP_000668
Alternative sequence2851 – 293080GEGRI…LIILI → PAGYKSSGSTCVNDNECLLF PCRNGGRCRDHHPPKKYECH CPMGFTGMHCELELLASGVL TPSRDFIVALALCLGTLIL in isoform C, isoform F, isoform G and isoform H.
VSP_000669
Natural variant14251E → K in allele CADN-M12; muscle defects.

Experimental info

Sequence conflict13421P → A in BAA22151. Ref.1
Sequence conflict27861S → T in BAA22151. Ref.1

Secondary structure

............................................................................. 3097
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform D [UniParc].

Last modified June 1, 2000. Version 2.
Checksum: 082242F28D9B5CC3

FASTA3,097347,204
        10         20         30         40         50         60 
MAARRCLNQL RQRYITNRFN ICTCAIFLIS LPFILAIEET TFAGLSAENA ARMLAGSPGD 

        70         80         90        100        110        120 
VEKSSLSHHS EMSLVLPHDT YPGFSIKKFK THPVKINGSS HSGAAAYHML DTDYSKYFTV 

       130        140        150        160        170        180 
LEDGVVMTTA DISPLVNRPV QLVVVEQTPN ATNTHNLQLF VMHRNDMLRF SGSLLDASGE 

       190        200        210        220        230        240 
VRENQPAGTR VRGVPLMQAF SGSILDEELA TPKKVRYTII DGNVDDAFAL QERKANKNIQ 

       250        260        270        280        290        300 
ISAKSLVING DDESGVWLVT NRPLDREERA HYDLSVEASD VDGLDRTVSK IQITVLDEND 

       310        320        330        340        350        360 
NRPIFKSLDY KFAIAGQKSA SMESNSSVTY QRFAIMGKVE ATDADGDKIA YRLKSPSNVV 

       370        380        390        400        410        420 
IIVPQTGEIM LAGEPTSNEL LIEVIAHDLR YPSLVSAKPA KVLLEFLAAE PVSFIMQHLE 

       430        440        450        460        470        480 
HDDINNHSHH REKRRVTRAV RPTKRIEFTE ADGDTEGKSV FQLEKETDKE TFKIRDDNPW 

       490        500        510        520        530        540 
VTVETNGAVR VKKKWDYEEL GPEKTIDFWV IITNMGHNAG IKYTDNQRVI ILVKDVNDEP 

       550        560        570        580        590        600 
PYFINRPLPM QAVVQLNAPP NTPVFTLQAR DPDTDHNIHY FIVRDRTGGR FEVDERSGVV 

       610        620        630        640        650        660 
RTRGTDLFQL DMEYVLYVKA EDQNGKVDDR RFQSTPEERL SIVGGKRAPQ FYMPSYEAEI 

       670        680        690        700        710        720 
PENQKKDSDI ISIKAKSFAD REIRYTLKAQ GQGAGTFNIG PTSGIVKLAK ELDFEDLRQP 

       730        740        750        760        770        780 
HVYSLIVTAT EDSGGFSTSV DLTIRVTDVN DNAPKFELPD YQAHNVDEDI PLGTSILRVK 

       790        800        810        820        830        840 
AMDSDSGSNA EIEYLVSDDH FAVDSNGIIV NNKQLDADNN NAYYEFIVTA KDKGEPPKSG 

       850        860        870        880        890        900 
VATVRVYTKN KNDEEPKFSQ QVYTPNVDEN AGPNTLVTTV VASDKDGDNV RFGFVGGGTS 

       910        920        930        940        950        960 
SGQFVIEDIT GVIRLHNKAI SLDKDKYELN VTAMDDGSCC VNGDQTIHTS TAVVVVFITD 

       970        980        990       1000       1010       1020 
VNDNKPVFKD CSTYYPKVEE GAPNGSPVIK VVATDEDKGV NGQVKYSIVQ QPNQKGTKFT 

      1030       1040       1050       1060       1070       1080 
VDEETGEVST NKVFDREGDD GKFVSVTVKA TDQGDPSLEG VCSFTVEITD VNDNPPLFDR 

      1090       1100       1110       1120       1130       1140 
QKYVENVKQD ASIGTNILRV SASDEDADNN GAIVYSLTAP FNPNDLEYFE IQAESGWIVL 

      1150       1160       1170       1180       1190       1200 
KKPLDRETYK LEAMAQDKGY PPLSRTVEVQ IDVVDRANNP PVWDHTVYGP IYVKENMPVG 

      1210       1220       1230       1240       1250       1260 
GKVVSIKASS GIEGNPTVFY RLMPGSTAQT NKFHTFYLQQ RPDNGDTWAD IKVNHPLDYE 

      1270       1280       1290       1300       1310       1320 
SIKEYNLTIR VENNGAQQLA SEATVYIMLE DVNDEIPLFT EREQETVLEG EPIGTKVTQV 

      1330       1340       1350       1360       1370       1380 
NAIDKDGTFP NNQVYYYIVD SPRNEGKEFF EINLQSGEIF TKTVFDREKK GAYALEVEAR 

      1390       1400       1410       1420       1430       1440 
DGAPSARPNS NGPNSVTKFI RIGIADKNDN PPYFDKSLYE AEVDENEDIQ HTVLTVTAKD 

      1450       1460       1470       1480       1490       1500 
HDESSRIRYE ITSGNIGGAF AVKNMTGAIY VAGALDYETR RRYELRLAAS DNLKENYTTV 

      1510       1520       1530       1540       1550       1560 
IIHVKDVNDN PPVFERPTYR TQITEEDDRN LPKRVLQVTA TDGDKDRPQN IVYFLTGQGI 

      1570       1580       1590       1600       1610       1620 
DPDNPANSKF DINRTTGEIF VLKPLDRDQP NGRPQWRFTV FAQDEGGEGL VGYADVQVNL 

      1630       1640       1650       1660       1670       1680 
KDINDNAPIF PQGVYFGNVT ENGTAGMVVM TMTAVDYDDP NEGSNARLVY SIEKNVIEEE 

      1690       1700       1710       1720       1730       1740 
TGSPIFEIEP DTGVIKTAVC CLDRERTPDY SIQVVAMDGG GLKGTGTASI RVKDINDMPP 

      1750       1760       1770       1780       1790       1800 
QFTKDEWFTE VDETDGTALP EMPILTVTVH DEDETNKFQY KVIDNSGYGA DKFTMVRNND 

      1810       1820       1830       1840       1850       1860 
GTGSLKIVQP LDYEDQLQSN GFRFRIQVND KGEDNDNDKY HVAYSWVVVK LRDINDNKPH 

      1870       1880       1890       1900       1910       1920 
FERANVEVSV FEDTKVGTEL EKFKATDPDQ GGKSKVSYSI DRSSDRQRQF AINQNGSVTI 

      1930       1940       1950       1960       1970       1980 
QRSLDREVVP RHQVKILAID DGSPPKTATA TLTVIVQDIN DNAPKFLKDY RPVLPEHVPP 

      1990       2000       2010       2020       2030       2040 
RKVVEILATD DDDRSKSNGP PFQFRLDPSA DDIIRASFKV EQDQKGANGD GMAVISSLRS 

      2050       2060       2070       2080       2090       2100 
FDREQQKEYM IPIVIKDHGS PAMTGTSTLT VIIGDVNDNK MQPGSKDIFV YNYQGQSPDT 

      2110       2120       2130       2140       2150       2160 
PIGRVYVYDL DDWDLPDKKF YWEAMEHPRF KLDEDSGMVT MRAGTREGRY HLRFKVYDRK 

      2170       2180       2190       2200       2210       2220 
HTQTDIPANV TVTVREIPHE AVVNSGSVRL SGISDEDFIR VWNYRTQSMS RSKMDRFRDK 

      2230       2240       2250       2260       2270       2280 
LADLLNTERE NVDIFSVQLK RKHPPLTDVR FSAHGSPYYK PVRLNGIVLM HREEIEKDVG 

      2290       2300       2310       2320       2330       2340 
INITMVGIDE CLYENQMCEG SCTNSLEISP LPYMVNANKT ALVGVRVDTI ADCTCGARNF 

      2350       2360       2370       2380       2390       2400 
TKPESCRTTP CHNGGRCVDT RFGPHCSCPV GYTGPRCQQT TRSFRGNGWA WYPPLEMCDE 

      2410       2420       2430       2440       2450       2460 
SHLSLEFITR KPDGLIIYNG PIVPPERDET LISDFIALEL ERGYPRLLID FGSGTLELRV 

      2470       2480       2490       2500       2510       2520 
KTKKTLDDGE WHRIDLFWDT ESIRMVVDFC KSAEIAEMED GTPPEFDDMS CQARGQIPPF 

      2530       2540       2550       2560       2570       2580 
NEYLNVNAPL QVGGLYREQF DQSLYFWHYM PTAKGFDGCI RNLVHNSKLY DLAHPGLSRN 

      2590       2600       2610       2620       2630       2640 
SVAGCPQTEE VCAQTETTAR CWEHGNCVGS LSEARCHCRP GWTGPACNIP TIPTTFKAQS 

      2650       2660       2670       2680       2690       2700 
YVKYALSFEP DRFSTQVQLR FRTREEYGEL FRVSDQHNRE YGILEIKDGH LHFRYNLNSL 

      2710       2720       2730       2740       2750       2760 
RTEEKDLWLN AIVVNDGQWH VVKVNRYGSA ATLELDGGEG RRYNETFEFV GHQWLLVDKQ 

      2770       2780       2790       2800       2810       2820 
EGVYAGGKAE YTGVRTFEVY ADYQKSCLDD IRLEGKHLPL PPAMNGTQWG QATMARNLEK 

      2830       2840       2850       2860       2870       2880 
GCPSNKPCSN VICPDPFECV DLWNVYECTC GEGRIMSPDS KGCMDRNECL DMPCMNGATC 

      2890       2900       2910       2920       2930       2940 
INLEPRLRYR CICPDGFWGE NCELVQEGQT LKLSMGALAA ILVCLLIILI LVLVFVVYNR 

      2950       2960       2970       2980       2990       3000 
RREAHIKYPG PDDDVRENII NYDDEGGGED DMTAFDITPL QIPIGGPMPP ELAPMKMPIM 

      3010       3020       3030       3040       3050       3060 
YPVMTLMPGQ EPNVGMFIEE HKKRADGDPN APPFDDLRNY AYEGGGSTAG SLSSLASGTD 

      3070       3080       3090 
DEQQEYDYLG AWGPRFDKLA NMYGPEAPNP HNTELEL 

« Hide

Isoform A [UniParc].

Checksum: 37E1B66D6CA30974
Show »

FASTA3,096346,741
Isoform B [UniParc].

Checksum: 5A7B35628893589D
Show »

FASTA3,096346,863
Isoform C [UniParc].

Checksum: CB4EBB76A3574D75
Show »

FASTA3,095346,500
Isoform E [UniParc].

Checksum: 867FD871827F6C92
Show »

FASTA3,097347,082
Isoform F [UniParc].

Checksum: 98BA24979B02FA5A
Show »

FASTA3,096346,962
Isoform G [UniParc].

Checksum: F520A7987F32ABB3
Show »

FASTA3,096346,840
Isoform H [UniParc].

Checksum: E1CDB4929306A434
Show »

FASTA3,095346,622

References

« Hide 'large scale' references
[1]"Axon patterning requires DN-cadherin, a novel neuronal adhesion receptor, in the Drosophila embryonic CNS."
Iwai Y., Usui T., Hirano S., Steward R., Takeichi M., Uemura T.
Neuron 19:77-89(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D).
Tissue: Embryo and Head.
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
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. expand/collapse author list , 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.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]"Roles of Armadillo, a Drosophila catenin, during central nervous system development."
Loureiro J., Peifer M.
Curr. Biol. 8:622-632(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002397 mRNA. Translation: BAA22151.1.
AE014134 Genomic DNA. Translation: AAF53635.1.
AE014134 Genomic DNA. Translation: AAN10992.1.
AE014134 Genomic DNA. Translation: AAN10993.1.
AE014134 Genomic DNA. Translation: AAN10994.1.
AE014134 Genomic DNA. Translation: AAN10995.1.
AE014134 Genomic DNA. Translation: AAN10996.1.
AE014134 Genomic DNA. Translation: AAN10997.1.
AE014134 Genomic DNA. Translation: AAN10998.1.
PIRT00021.
RefSeqNP_724068.1. NM_165224.2.
NP_724069.1. NM_165225.2.
NP_724070.1. NM_165226.2.
NP_724071.1. NM_165227.3.
NP_724072.1. NM_165228.2.
NP_724073.1. NM_165229.2.
NP_724074.1. NM_165230.2.
NP_724075.1. NM_165231.3.
UniGeneDm.5768.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UBFX-ray2.50A439-753[»]
3UBGX-ray2.50A/B439-753[»]
3UBHX-ray2.70A434-851[»]
ProteinModelPortalO15943.
SMRO15943. Positions 180-404, 438-2180, 2330-2904, 2991-3084.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid61066. 5 interactions.
IntActO15943. 1 interaction.
MINTMINT-1327969.

Proteomic databases

PaxDbO15943.
PRIDEO15943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0081015; FBpp0080568; FBgn0015609. [O15943-1]
GeneID35070.
KEGGdme:Dmel_CG7100.

Organism-specific databases

CTD35070.
FlyBaseFBgn0015609. CadN.

Phylogenomic databases

eggNOGNOG298859.
GeneTreeENSGT00750000117611.
InParanoidO15943.
OrthoDBEOG718KB7.
PhylomeDBO15943.

Gene expression databases

BgeeO15943.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
2.60.40.60. 17 hits.
4.10.900.10. 1 hit.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR000233. Cadherin_cytoplasmic-dom.
IPR027397. Catenin_binding_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamPF00028. Cadherin. 12 hits.
PF01049. Cadherin_C. 1 hit.
PF00008. EGF. 2 hits.
PF02210. Laminin_G_2. 2 hits.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 16 hits.
SM00181. EGF. 3 hits.
SM00179. EGF_CA. 1 hit.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMSSF49313. SSF49313. 18 hits.
SSF49899. SSF49899. 2 hits.
SSF57184. SSF57184. 2 hits.
PROSITEPS00232. CADHERIN_1. 9 hits.
PS50268. CADHERIN_2. 16 hits.
PS00022. EGF_1. 3 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 3 hits.
PS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi35070.
NextBio791671.

Entry information

Entry nameCADN_DROME
AccessionPrimary (citable) accession number: O15943
Secondary accession number(s): Q9VJB7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 1, 2000
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

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