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Protein

Cadherin-89D

Gene

Cad89D

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-89D
Gene namesi
Name:Cad89D
ORF Names:CG14900
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0038439. Cad89D.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini? – 1883ExtracellularSequence analysis
Transmembranei1884 – 190421HelicalSequence analysisAdd
BLAST
Topological domaini1905 – 2240336CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 2240Cadherin-89DPRO_0000004008
Signal peptidei1 – ?Sequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence analysis
Glycosylationi191 – 1911N-linked (GlcNAc...)Sequence analysis
Glycosylationi278 – 2781N-linked (GlcNAc...)Sequence analysis
Glycosylationi334 – 3341N-linked (GlcNAc...)Sequence analysis
Glycosylationi417 – 4171N-linked (GlcNAc...)Sequence analysis
Glycosylationi585 – 5851N-linked (GlcNAc...)Sequence analysis
Glycosylationi720 – 7201N-linked (GlcNAc...)Sequence analysis
Glycosylationi752 – 7521N-linked (GlcNAc...)Sequence analysis
Glycosylationi822 – 8221N-linked (GlcNAc...)Sequence analysis
Glycosylationi833 – 8331N-linked (GlcNAc...)Sequence analysis
Glycosylationi983 – 9831N-linked (GlcNAc...)Sequence analysis
Glycosylationi989 – 9891N-linked (GlcNAc...)Sequence analysis
Glycosylationi1006 – 10061N-linked (GlcNAc...)Sequence analysis
Glycosylationi1255 – 12551N-linked (GlcNAc...)Sequence analysis
Glycosylationi1318 – 13181N-linked (GlcNAc...)Sequence analysis
Glycosylationi1486 – 14861N-linked (GlcNAc...)Sequence analysis
Glycosylationi1529 – 15291N-linked (GlcNAc...)Sequence analysis
Glycosylationi1556 – 15561N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9VEU1.
PRIDEiQ9VEU1.

Expressioni

Gene expression databases

BgeeiQ9VEU1.
GenevisibleiQ9VEU1. DM.

Interactioni

Protein-protein interaction databases

BioGridi67051. 2 interactions.
DIPiDIP-18418N.
IntActiQ9VEU1. 5 interactions.
MINTiMINT-341752.
STRINGi7227.FBpp0290916.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 179110Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini180 – 295116Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini296 – 411116Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini412 – 528117Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini529 – 643115Cadherin 5PROSITE-ProRule annotationAdd
BLAST
Domaini824 – 927104Cadherin 6PROSITE-ProRule annotationAdd
BLAST
Domaini928 – 1087160Cadherin 7PROSITE-ProRule annotationAdd
BLAST
Domaini1171 – 1284114Cadherin 8PROSITE-ProRule annotationAdd
BLAST
Domaini1285 – 1389105Cadherin 9PROSITE-ProRule annotationAdd
BLAST
Domaini1411 – 1520110Cadherin 10PROSITE-ProRule annotationAdd
BLAST
Domaini1534 – 1660127Cadherin 11PROSITE-ProRule annotationAdd
BLAST
Domaini1661 – 1774114Cadherin 12PROSITE-ProRule annotationAdd
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 12 cadherin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00840000129706.
InParanoidiQ9VEU1.
OMAiARENMAG.
OrthoDBiEOG73V6JB.

Family and domain databases

Gene3Di2.60.40.60. 13 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
[Graphical view]
PfamiPF00028. Cadherin. 6 hits.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 12 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 12 hits.
PROSITEiPS00232. CADHERIN_1. 7 hits.
PS50268. CADHERIN_2. 12 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9VEU1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSEAYPMKS SVKISQKKKA SQDMAVICVW VMPLAVFGLI AIGQAAKTGQ
60 70 80 90 100
VQASSGSCAF HTLDGVAAES EGVRFIRLRE DAQVGKEILR LQAYPRSTAA
110 120 130 140 150
LKGADASGDH KYFNLTEHNA TTLVVSLARS LERLVDRDVP RNLLKFRILC
160 170 180 190 200
AGKQEKLEEG SYLSITVYIE DVNDNAPEFL NVPYVVDVDE NTSIESIIFE
210 220 230 240 250
GVQAFDRDKP NTPNSEVHFS MSTVPEQLSA DGSPYFALKS PHRPLLILKR
260 270 280 290 300
ELDFDNGIRQ FKLPIFAWDR GTPANQANTT ITINVRDVDD LPPKFTEGVY
310 320 330 340 350
RTRINEFYPM TGVPIRIPLY FAPPIMAFDQ DSLNASLVYD IISGNERQLF
360 370 380 390 400
RVNPHNGVMY LQKEIDLEEE SLPGNTFVLQ LEARQKDNPL KKALARIEVE
410 420 430 440 450
VLDLNDNVPE FEADYYNISI VENLPTGFSV LQVNAVDRDQ GENSEFLYNL
460 470 480 490 500
VETKDAAGAF RIDSRTGWIT VRDDRLLDRE QRRSIQLNVE ALERNPSYLD
510 520 530 540 550
DKHLKKPGPS KVQVEITLLD TNDNTPKFEH GNLYEFKVPI NAPTGYVIGQ
560 570 580 590 600
VVAHDPDEGP NGHLLYELQR PKGSGYIPFR LDNKNGTIYV GGPLRRGRIA
610 620 630 640 650
VFVEATDQPT NPSERRFSLA VITIEVYATI DDQAIDFVGA PYEFWVGANT
660 670 680 690 700
PLGTSVGQVR TTLIYEGGDE IMYDLLHTYS EGVPFAIEER SGIITVIREL
710 720 730 740 750
SEFKRKVYQF EAVANYLFAN SSQSLVMSRS SSPLTTIASP AELSDEGVLI
760 770 780 790 800
TNLTIHIVNK PEQKVPLRPV IEEINMNVIH FHVEENVVGG IIGQLLYKNG
810 820 830 840 850
INLVNNELGT YREMPSEPTS RNITMGSRFR SRNRSRSSKS KRRLPRRLVG
860 870 880 890 900
DANIKLRYII ANQQEVVNKI SITEDGTLLT LTGLDREQQP SYELTVIVEY
910 920 930 940 950
STGLVSGAGI YQVNIKVDDV NDNAPKFNAL TYVGLINENC VVGTELSMNH
960 970 980 990 1000
AILIQDADEG PNAEFRVQLQ GDYSDEFSIE YVNGTSSENS THHKMPSTTG
1010 1020 1030 1040 1050
AFNIFNLTDQ WNDEFKYQEL HTTFMQTNFK LSSGPYFRIS YTGKRGLDRE
1060 1070 1080 1090 1100
KQQLYNLKII AADTGGLSGY AHLTVLVADV NDNAPMFERI SVFKDSRLEI
1110 1120 1130 1140 1150
REYTTDMEIY FVESSSGMTA PQATAAMMLA PPPYHIPGSP RFNVDRERSV
1160 1170 1180 1190 1200
GAGLGVVARA KSRRRMVRAL TTKCPLFAIY EDTPVGTKVL QLSASDEDFG
1210 1220 1230 1240 1250
KNALLHYELQ GEQVERTPGM PMLRVHGVKY FAIDKLSGEL SVNYPLSANI
1260 1270 1280 1290 1300
EIMLNLTVTD IDGLKDSTCL RFTVMDVNNH APTFKKSWYS FDTPEGEYKD
1310 1320 1330 1340 1350
SVLGQLTAID MDFGENANIT YTLSDSHLPF TIKPASGVLK IGGQLDRELK
1360 1370 1380 1390 1400
DKYSFQVIAT DNAPVMQRMS SSVDVEVNVL DINDNRPEFI GYDDQTKAVK
1410 1420 1430 1440 1450
FIPSVADRTL MLPVYKAYLD RSTQPGTFVR QLTAIDKDNV GNGNGLVLYS
1460 1470 1480 1490 1500
IRHQEMQAPL FQIDSRDGTI STISRINGYN DYEHLNVSVI ASDVGSPALS
1510 1520 1530 1540 1550
ATAIVIVNLQ GQAVTDPPKS TPKPEPPANV TVFQHAYYEV KLTENNEAPI
1560 1570 1580 1590 1600
EVMRLNLSAG LNPENYRWSL WLEEGLDETD AHPPFEYDAK NMLLYALKPF
1610 1620 1630 1640 1650
DREHISRYQL RIRADRLSRE ARNYARVSYP VVDERIEGLS LNECRILVHI
1660 1670 1680 1690 1700
ADENDNAPKF RGNGQPIVAV LPQSASFGYP VTRVEANDLD EGLNAEIRYR
1710 1720 1730 1740 1750
LLNEPARLFG IDELSGNIRL LGELSRTEHI YGFDVKATDR MGADDGRSGI
1760 1770 1780 1790 1800
VNVFVYIINE AKQVRLVVAG MPVEVERRIE GLMEALSDAI GKDVRVRLLE
1810 1820 1830 1840 1850
PYSGGLEPAT NAYIYAVDPH TNSIMEMEQL QDALAGLQLD ALQLQQQKLD
1860 1870 1880 1890 1900
GGKPMPRILE LAEFGQLARP AHASASSFMG GLEFVTVVLL ALISLGALIA
1910 1920 1930 1940 1950
ACCYVCMRQK RRLWSQRDFS ASDAGLTYTI AGIGSPRGQK QRRQRQQRHT
1960 1970 1980 1990 2000
QRCSKGSTGS QRPTSAFMPE SVCSSAQTQS TATATEKLEQ QLHHHHQQQA
2010 2020 2030 2040 2050
MATQQQHHQY LNEQQRQQKR EYIDVPLPKS IAKAAAVTSG GDGAVGVGST
2060 2070 2080 2090 2100
PFVLKYNACQ PVNNLNNYET SLFSLHSTGQ DSGVEFLSSR ELYETSPDSF
2110 2120 2130 2140 2150
QHGGSKRGNN TEVLCPRHAK AHLELRQPNT DSSDTYEDSL KTDEPLVAHN
2160 2170 2180 2190 2200
CRSANCEHRQ HQQHPSHHPH YQNTRFEKRS CVRHSFSGVK DDLMQQSPQI
2210 2220 2230 2240
SLRPRGHALR NSMNDLEQRL HNLEQSFRRP LEFSKSNSLF
Length:2,240
Mass (Da):250,636
Last modified:October 19, 2011 - v3
Checksum:i7D8001742A8AD826
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81M → R in BAB20634 (Ref. 1) Curated
Sequence conflicti208 – 2081D → E in BAB20634 (Ref. 1) Curated
Sequence conflicti305 – 3051N → Y in BAB20634 (Ref. 1) Curated
Sequence conflicti310 – 3101M → I in BAB20634 (Ref. 1) Curated
Sequence conflicti311 – 3111T → S in AAQ23544 (Ref. 4) Curated
Sequence conflicti456 – 4561A → G in AAQ23544 (Ref. 4) Curated
Sequence conflicti702 – 7021E → D in BAB20634 (Ref. 1) Curated
Sequence conflicti823 – 8231I → L in BAB20634 (Ref. 1) Curated
Sequence conflicti945 – 9451E → G in AAQ23544 (Ref. 4) Curated
Sequence conflicti997 – 9971S → P in BAB20634 (Ref. 1) Curated
Sequence conflicti1187 – 11871T → A in BAB20634 (Ref. 1) Curated
Sequence conflicti1258 – 12581V → G in BAB20634 (Ref. 1) Curated
Sequence conflicti1319 – 13191I → M in BAB20634 (Ref. 1) Curated
Sequence conflicti1330 – 13301F → S in BAB20634 (Ref. 1) Curated
Sequence conflicti1342 – 13421G → S in BAB20634 (Ref. 1) Curated
Sequence conflicti1497 – 14971P → A in BAB20634 (Ref. 1) Curated
Sequence conflicti1504 – 15041I → V in BAB20634 (Ref. 1) Curated
Sequence conflicti1606 – 16061S → C in BAB20634 (Ref. 1) Curated
Sequence conflicti1618 – 16181S → N in AAQ23544 (Ref. 4) Curated
Sequence conflicti1633 – 16331D → G in BAB20634 (Ref. 1) Curated
Sequence conflicti1660 – 16601F → Y in BAB20634 (Ref. 1) Curated
Sequence conflicti1745 – 17451D → V in BAB20634 (Ref. 1) Curated
Sequence conflicti1801 – 18011P → R in BAB20634 (Ref. 1) Curated
Sequence conflicti1892 – 18921L → R in BAB20634 (Ref. 1) Curated
Sequence conflicti2095 – 20951T → A in AAQ23544 (Ref. 4) Curated
Sequence conflicti2138 – 21381D → G in AAQ23544 (Ref. 4) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB053260 mRNA. Translation: BAB20634.1.
AE014297 Genomic DNA. Translation: AAF55327.3.
BT010226 mRNA. Translation: AAQ23544.1.
RefSeqiNP_650554.3. NM_142297.4.
UniGeneiDm.6421.

Genome annotation databases

EnsemblMetazoaiFBtr0301702; FBpp0290916; FBgn0038439.
GeneIDi42006.
KEGGidme:Dmel_CG14900.
UCSCiCG14900-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB053260 mRNA. Translation: BAB20634.1.
AE014297 Genomic DNA. Translation: AAF55327.3.
BT010226 mRNA. Translation: AAQ23544.1.
RefSeqiNP_650554.3. NM_142297.4.
UniGeneiDm.6421.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi67051. 2 interactions.
DIPiDIP-18418N.
IntActiQ9VEU1. 5 interactions.
MINTiMINT-341752.
STRINGi7227.FBpp0290916.

Proteomic databases

PaxDbiQ9VEU1.
PRIDEiQ9VEU1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0301702; FBpp0290916; FBgn0038439.
GeneIDi42006.
KEGGidme:Dmel_CG14900.
UCSCiCG14900-RA. d. melanogaster.

Organism-specific databases

CTDi42006.
FlyBaseiFBgn0038439. Cad89D.

Phylogenomic databases

eggNOGiKOG3594. Eukaryota.
ENOG410XQHI. LUCA.
GeneTreeiENSGT00840000129706.
InParanoidiQ9VEU1.
OMAiARENMAG.
OrthoDBiEOG73V6JB.

Miscellaneous databases

GenomeRNAii42006.
NextBioi826702.
PROiQ9VEU1.

Gene expression databases

BgeeiQ9VEU1.
GenevisibleiQ9VEU1. DM.

Family and domain databases

Gene3Di2.60.40.60. 13 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
[Graphical view]
PfamiPF00028. Cadherin. 6 hits.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 12 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 12 hits.
PROSITEiPS00232. CADHERIN_1. 7 hits.
PS50268. CADHERIN_2. 12 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel member of the Drosophila cadherin superfamily, Cad89D."
    Hirano S., Kimura H., Takeichi M., Uemura T.
    Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Strain: Berkeley.
    Tissue: Embryo.

Entry informationi

Entry nameiCAD89_DROME
AccessioniPrimary (citable) accession number: Q9VEU1
Secondary accession number(s): Q6NR53, Q9GR86
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 27, 2003
Last sequence update: October 19, 2011
Last modified: May 11, 2016
This is version 117 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.