SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9VGW1

- CAD86_DROME

UniProt

Q9VGW1 - CAD86_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Cadherin-86C
Gene
Cad86C, CG4509
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

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

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. calcium-dependent cell-cell adhesion Source: FlyBase
  2. homophilic cell adhesion Source: InterPro
  3. regulation of cell shape Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-86C
Gene namesi
Name:Cad86C
ORF Names:CG4509
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0261053. Cad86C.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 934934Extracellular Reviewed prediction
Add
BLAST
Transmembranei935 – 95521Helical; Reviewed prediction
Add
BLAST
Topological domaini956 – 1943988Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: FlyBase
  2. subapical complex Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 1943Cadherin-86CPRO_0000004010
Signal peptidei1 – ? Reviewed prediction

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi12 – 121N-linked (GlcNAc...) Reviewed prediction
Glycosylationi244 – 2441N-linked (GlcNAc...) Reviewed prediction
Glycosylationi419 – 4191N-linked (GlcNAc...) Reviewed prediction
Glycosylationi531 – 5311N-linked (GlcNAc...) Reviewed prediction
Glycosylationi579 – 5791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi585 – 5851N-linked (GlcNAc...) Reviewed prediction
Glycosylationi612 – 6121N-linked (GlcNAc...) Reviewed prediction
Glycosylationi645 – 6451N-linked (GlcNAc...) Reviewed prediction
Glycosylationi912 – 9121N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

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

Gene expression databases

BgeeiQ9VGW1.

Interactioni

Protein-protein interaction databases

BioGridi66446. 2 interactions.
IntActiQ9VGW1. 1 interaction.
MINTiMINT-892952.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini238 – 366129Cadherin 1
Add
BLAST
Domaini367 – 483117Cadherin 2
Add
BLAST
Domaini484 – 600117Cadherin 3
Add
BLAST
Domaini601 – 708108Cadherin 4
Add
BLAST
Domaini709 – 832124Cadherin 5
Add
BLAST

Domaini

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 similaritiesi

Contains 5 cadherin domains.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG260805.
InParanoidiQ9VGW1.
OrthoDBiEOG7CVPWS.

Family and domain databases

Gene3Di2.60.40.60. 6 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
[Graphical view]
PfamiPF00028. Cadherin. 3 hits.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 5 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 5 hits.
PROSITEiPS00232. CADHERIN_1. 1 hit.
PS50268. CADHERIN_2. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9VGW1-1 [UniParc]FASTAAdd to Basket

« Hide

MASTSSSQPE KNRSHVPLCR LGTEPVSRTG AAEEPSGQRE CYYYAPATSP     50
HHHHHHHHQH HHHHRLKQHH RHHHHHHRLQ HHHHHHQQQH NHQNQQMQHH 100
WPSRLGPIGP WLGAMTAYRL LTISLLIGIL CPHHVQGADP KFDPTTRMRL 150
VLVPADAQVN SVIYRLRATD EEFDYPLTFE FVGDASASTV KVESLPCTKY 200
NSVCQANIVL QRRLEPGRYY DFQVSVKDTK GGMTTQLCSI TATNFTTPHD 250
LIFPHKPGII MIPEDAKRGT ELDYVIARKN PLFQKPVYLE LWGSPLFAIR 300
QKIVSSETTE GTVFLLGPLD FEKQAMYHLT ILANDAYAEP GQDSRNIAGM 350
EIVVIVQDVQ DQPPVFTSAP PVTKLPPGIL PGDKILQVHA EDGDKGNPRE 400
VRYGLVSENN PFTSFFDINE TSGEIFLMRP LEDIAFITHV GDPVLLTVIA 450
EEVKVGRDEP PALASTVQLA FFLPDRTNSP PYFENDHYVS RVDENAPQGT 500
ALTFVDPYVP RVYDDDTGKN GVFSLTLLNN NGTFEISPNV AERSAGFLIR 550
VRDNSMLDYE QQQSVQFQIL AQELGPATNL SALVNVTVYI NDVNDNAPVF 600
EQPAYSVELP ENMTAGTKVV QVLATDPDSG LGGKVRYTAI LGYLNTSLNL 650
DAETGLITVS TNKHGFDREV MPEYHLYVEA RDMDGEGNRA QVPLIIKLID 700
VNDETPIFDK DLYEFILTHD LMGFTTTAVI HAEDKDATAP NNEVRYEIIN 750
GNYDNQFVLD KVTGELTVRE KIHLRSKKNA KTRRRRQAGS DDEDTDIFIL 800
TARAYDLGVP VRFSTTTIRV YPPESRKRSV KFVVPGHNPD KAKTEETLSA 850
LSGGKVYIHN IRPLSPDEPG AKDIPAGNPG IKERSVVTAT VIYDSSSVVD 900
ISEIQQRLSH HNNSYAIMPQ DTSSTDTQYK AENKVLFWLL ILLATLVALT 950
ILILLLCCIC SWCPLYGAAT KRIVNISRTE DDVHLVHREM ANGKQTKSVQ 1000
VAEWMGRRDA WSAEKPPDTR TKPTRWEFHD GREQLDEDVG RGQDIGEGDR 1050
RHIQSAEEQQ RRVRIKHNRT AKDDLHLNFH NSRTNLINDR DVYMEDVIEN 1100
RDLAGDREHI TRTRVNRQEY ARRKQYDSEV RHIDDDSMRR HEIDRGSDID 1150
FNTAHNSLKS KRELFIKDGN VEILQLMTRD KTRDGLNLDD DNIYVNVPLK 1200
PAGNLSHPQL LMVDNTGKEI LMRRFIEEQP DGKQIIREHY QIVPGATYIQ 1250
SMPNEVQQGS TLKGDTFPLG KSGPNSIVYS QLEPEVKVIH TQPVQAGEGV 1300
SLDQQMQPAV SNQSLTHELE HSLKQQNALL RQILMEKEKL ENAYTQHEVA 1350
LETQSLPGQS MAIGTQTDCD AGTQTEGFDG VLDPEISLAK PSRRRARSEN 1400
DESMSEDGYE YVRFNPPNSP EGVYWIKRRR TKKRPRQPRK RIVMVEEVKR 1450
KIRTPIKEEE EVQERKKRVP PKKPLRETKT SILRKQLSDE SRKDQSRNGE 1500
SQTGNRHRSE SDSHNRDMFM EITDSMDELA SPGSHSIRKI QVEKYYKHSD 1550
GDFDEDDTEY SIDSDGDEIV IRTNYPSRAQ ENERYRRQER TYAEPENPVD 1600
RKRPARKSSP TDSQPEAMPR LSRRDSSKRG SRKQTSSEPP HNRVSISKYE 1650
STVTENGRKL MSTSTEIVGS KRSLTDRSYQ SETELAGLEH EERNVPKYME 1700
WYYNKKKSSV SGRTSTESSK SQPSSKKKVG AAEKRVSKTR ITAQPKDVEE 1750
YDETGGRYKP EPAPRKSPPK GSRLLKEDRA LNKQHKPKIE TDTNHPLLQH 1800
SEHRFERENA LEVPAAPTKL PHYMYPETPP HAAAGGKESK SGRESKTSKE 1850
AKPKPSPIRE NEVKVSNSKI YVEHRGTGHP TQKQLNASTL EDDHDSGIAM 1900
NSLLNSLGRR NPIAEKKSVF SIAYDDVSRV KKINSGGESP QYS 1943
Length:1,943
Mass (Da):220,408
Last modified:October 19, 2011 - v3
Checksum:i16ADFDBB8C0EED30
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti926 – 9261D → DTLTPLQ in AAM29379. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EU707853 mRNA. Translation: ACD79974.1.
AE014297 Genomic DNA. Translation: AAF54562.5.
AY113374 mRNA. Translation: AAM29379.1. Sequence problems.
RefSeqiNP_001247031.1. NM_001260102.1.
NP_788635.3. NM_176458.4.
UniGeneiDm.1141.

Genome annotation databases

GeneIDi41302.
KEGGidme:Dmel_CG42601.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
EU707853 mRNA. Translation: ACD79974.1 .
AE014297 Genomic DNA. Translation: AAF54562.5 .
AY113374 mRNA. Translation: AAM29379.1 . Sequence problems.
RefSeqi NP_001247031.1. NM_001260102.1.
NP_788635.3. NM_176458.4.
UniGenei Dm.1141.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 66446. 2 interactions.
IntActi Q9VGW1. 1 interaction.
MINTi MINT-892952.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 41302.
KEGGi dme:Dmel_CG42601.

Organism-specific databases

CTDi 41302.
FlyBasei FBgn0261053. Cad86C.

Phylogenomic databases

eggNOGi NOG260805.
InParanoidi Q9VGW1.
OrthoDBi EOG7CVPWS.

Miscellaneous databases

GenomeRNAii 41302.
NextBioi 823209.

Gene expression databases

Bgeei Q9VGW1.

Family and domain databases

Gene3Di 2.60.40.60. 6 hits.
InterProi IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
[Graphical view ]
Pfami PF00028. Cadherin. 3 hits.
[Graphical view ]
PRINTSi PR00205. CADHERIN.
SMARTi SM00112. CA. 5 hits.
[Graphical view ]
SUPFAMi SSF49313. SSF49313. 5 hits.
PROSITEi PS00232. CADHERIN_1. 1 hit.
PS50268. CADHERIN_2. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    Strain: Berkeley.
  4. 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.

Entry informationi

Entry nameiCAD86_DROME
AccessioniPrimary (citable) accession number: Q9VGW1
Secondary accession number(s): B3GN10, Q8MZ37
Entry historyi
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 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

External Data

Dasty 3

Similar proteinsi