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Q9VGW1 (CAD86_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length1943 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells By similarity.

Subcellular location

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

Tissue specificity

As cell intercalation proceeds, a row of stigmatophore cells surrounding the spiracular chamber show expression of Cad86C. Expression is regulated by the Abd-B cascade, requiring sal. Expressed in a broad region of the morphogenetic furrow and in clusters of cells posterior to the morphogenetic furrow. Weakly expressed in the epithelium of wing imaginal disks. In eye imaginal disk cells within the morphogenetic furrow, expression is localized to the apical region. Ref.1 Ref.5

Induction

By hedgehog (hh) and dpp signal transduction in the morphogenetic furrow. Ref.1

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 5 cadherin domains.

Sequence caution

The sequence AAM29379.1 differs from that shown. Reason: Erroneous termination at position 1331. Translated as Arg.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – ? Potential
Chain? – 1943Cadherin-86CPRO_0000004010

Regions

Topological domain1 – 934934Extracellular Potential
Transmembrane935 – 95521Helical; Potential
Topological domain956 – 1943988Cytoplasmic Potential
Domain238 – 366129Cadherin 1
Domain367 – 483117Cadherin 2
Domain484 – 600117Cadherin 3
Domain601 – 708108Cadherin 4
Domain709 – 832124Cadherin 5

Amino acid modifications

Glycosylation121N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Glycosylation4191N-linked (GlcNAc...) Potential
Glycosylation5311N-linked (GlcNAc...) Potential
Glycosylation5791N-linked (GlcNAc...) Potential
Glycosylation5851N-linked (GlcNAc...) Potential
Glycosylation6121N-linked (GlcNAc...) Potential
Glycosylation6451N-linked (GlcNAc...) Potential
Glycosylation9121N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict9261D → DTLTPLQ in AAM29379. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q9VGW1 [UniParc].

Last modified October 19, 2011. Version 3.
Checksum: 16ADFDBB8C0EED30

FASTA1,943220,408
        10         20         30         40         50         60 
MASTSSSQPE KNRSHVPLCR LGTEPVSRTG AAEEPSGQRE CYYYAPATSP HHHHHHHHQH 

        70         80         90        100        110        120 
HHHHRLKQHH RHHHHHHRLQ HHHHHHQQQH NHQNQQMQHH WPSRLGPIGP WLGAMTAYRL 

       130        140        150        160        170        180 
LTISLLIGIL CPHHVQGADP KFDPTTRMRL VLVPADAQVN SVIYRLRATD EEFDYPLTFE 

       190        200        210        220        230        240 
FVGDASASTV KVESLPCTKY NSVCQANIVL QRRLEPGRYY DFQVSVKDTK GGMTTQLCSI 

       250        260        270        280        290        300 
TATNFTTPHD LIFPHKPGII MIPEDAKRGT ELDYVIARKN PLFQKPVYLE LWGSPLFAIR 

       310        320        330        340        350        360 
QKIVSSETTE GTVFLLGPLD FEKQAMYHLT ILANDAYAEP GQDSRNIAGM EIVVIVQDVQ 

       370        380        390        400        410        420 
DQPPVFTSAP PVTKLPPGIL PGDKILQVHA EDGDKGNPRE VRYGLVSENN PFTSFFDINE 

       430        440        450        460        470        480 
TSGEIFLMRP LEDIAFITHV GDPVLLTVIA EEVKVGRDEP PALASTVQLA FFLPDRTNSP 

       490        500        510        520        530        540 
PYFENDHYVS RVDENAPQGT ALTFVDPYVP RVYDDDTGKN GVFSLTLLNN NGTFEISPNV 

       550        560        570        580        590        600 
AERSAGFLIR VRDNSMLDYE QQQSVQFQIL AQELGPATNL SALVNVTVYI NDVNDNAPVF 

       610        620        630        640        650        660 
EQPAYSVELP ENMTAGTKVV QVLATDPDSG LGGKVRYTAI LGYLNTSLNL DAETGLITVS 

       670        680        690        700        710        720 
TNKHGFDREV MPEYHLYVEA RDMDGEGNRA QVPLIIKLID VNDETPIFDK DLYEFILTHD 

       730        740        750        760        770        780 
LMGFTTTAVI HAEDKDATAP NNEVRYEIIN GNYDNQFVLD KVTGELTVRE KIHLRSKKNA 

       790        800        810        820        830        840 
KTRRRRQAGS DDEDTDIFIL TARAYDLGVP VRFSTTTIRV YPPESRKRSV KFVVPGHNPD 

       850        860        870        880        890        900 
KAKTEETLSA LSGGKVYIHN IRPLSPDEPG AKDIPAGNPG IKERSVVTAT VIYDSSSVVD 

       910        920        930        940        950        960 
ISEIQQRLSH HNNSYAIMPQ DTSSTDTQYK AENKVLFWLL ILLATLVALT ILILLLCCIC 

       970        980        990       1000       1010       1020 
SWCPLYGAAT KRIVNISRTE DDVHLVHREM ANGKQTKSVQ VAEWMGRRDA WSAEKPPDTR 

      1030       1040       1050       1060       1070       1080 
TKPTRWEFHD GREQLDEDVG RGQDIGEGDR RHIQSAEEQQ RRVRIKHNRT AKDDLHLNFH 

      1090       1100       1110       1120       1130       1140 
NSRTNLINDR DVYMEDVIEN RDLAGDREHI TRTRVNRQEY ARRKQYDSEV RHIDDDSMRR 

      1150       1160       1170       1180       1190       1200 
HEIDRGSDID FNTAHNSLKS KRELFIKDGN VEILQLMTRD KTRDGLNLDD DNIYVNVPLK 

      1210       1220       1230       1240       1250       1260 
PAGNLSHPQL LMVDNTGKEI LMRRFIEEQP DGKQIIREHY QIVPGATYIQ SMPNEVQQGS 

      1270       1280       1290       1300       1310       1320 
TLKGDTFPLG KSGPNSIVYS QLEPEVKVIH TQPVQAGEGV SLDQQMQPAV SNQSLTHELE 

      1330       1340       1350       1360       1370       1380 
HSLKQQNALL RQILMEKEKL ENAYTQHEVA LETQSLPGQS MAIGTQTDCD AGTQTEGFDG 

      1390       1400       1410       1420       1430       1440 
VLDPEISLAK PSRRRARSEN DESMSEDGYE YVRFNPPNSP EGVYWIKRRR TKKRPRQPRK 

      1450       1460       1470       1480       1490       1500 
RIVMVEEVKR KIRTPIKEEE EVQERKKRVP PKKPLRETKT SILRKQLSDE SRKDQSRNGE 

      1510       1520       1530       1540       1550       1560 
SQTGNRHRSE SDSHNRDMFM EITDSMDELA SPGSHSIRKI QVEKYYKHSD GDFDEDDTEY 

      1570       1580       1590       1600       1610       1620 
SIDSDGDEIV IRTNYPSRAQ ENERYRRQER TYAEPENPVD RKRPARKSSP TDSQPEAMPR 

      1630       1640       1650       1660       1670       1680 
LSRRDSSKRG SRKQTSSEPP HNRVSISKYE STVTENGRKL MSTSTEIVGS KRSLTDRSYQ 

      1690       1700       1710       1720       1730       1740 
SETELAGLEH EERNVPKYME WYYNKKKSSV SGRTSTESSK SQPSSKKKVG AAEKRVSKTR 

      1750       1760       1770       1780       1790       1800 
ITAQPKDVEE YDETGGRYKP EPAPRKSPPK GSRLLKEDRA LNKQHKPKIE TDTNHPLLQH 

      1810       1820       1830       1840       1850       1860 
SEHRFERENA LEVPAAPTKL PHYMYPETPP HAAAGGKESK SGRESKTSKE AKPKPSPIRE 

      1870       1880       1890       1900       1910       1920 
NEVKVSNSKI YVEHRGTGHP TQKQLNASTL EDDHDSGIAM NSLLNSLGRR NPIAEKKSVF 

      1930       1940 
SIAYDDVSRV KKINSGGESP QYS 

« Hide

References

« Hide 'large scale' references
[1]"Hedgehog and Dpp signaling induce cadherin Cad86C expression in the morphogenetic furrow during Drosophila eye development."
Schlichting K., Dahmann C.
Mech. Dev. 125:712-728(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
[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.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 726-1943.
Strain: Berkeley.
Tissue: Larva and Pupae.
[5]"Coordinated control of cell adhesion, polarity, and cytoskeleton underlies Hox-induced organogenesis in Drosophila."
Lovegrove B., Simoes S., Rivas M.L., Sotillos S., Johnson K., Knust E., Jacinto A., Hombria J.C.
Curr. Biol. 16:2206-2216(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EU707853 mRNA. Translation: ACD79974.1.
AE014297 Genomic DNA. Translation: AAF54562.5.
AY113374 mRNA. Translation: AAM29379.1. Sequence problems.
RefSeqNP_001247031.1. NM_001260102.1.
NP_788635.3. NM_176458.4.
UniGeneDm.1141.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid66446. 2 interactions.
IntActQ9VGW1. 1 interaction.
MINTMINT-892952.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID41302.
KEGGdme:Dmel_CG42601.

Organism-specific databases

CTD41302.
FlyBaseFBgn0261053. Cad86C.

Phylogenomic databases

eggNOGNOG260805.
InParanoidQ9VGW1.
OrthoDBEOG7CVPWS.

Gene expression databases

BgeeQ9VGW1.

Family and domain databases

Gene3D2.60.40.60. 6 hits.
InterProIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
[Graphical view]
PfamPF00028. Cadherin. 3 hits.
[Graphical view]
PRINTSPR00205. CADHERIN.
SMARTSM00112. CA. 5 hits.
[Graphical view]
SUPFAMSSF49313. SSF49313. 5 hits.
PROSITEPS00232. CADHERIN_1. 1 hit.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi41302.
NextBio823209.

Entry information

Entry nameCAD86_DROME
AccessionPrimary (citable) accession number: Q9VGW1
Secondary accession number(s): B3GN10, Q8MZ37
Entry history
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: October 19, 2011
Last modified: July 9, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

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