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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)DescriptionActionsGraphical viewLength
Topological domaini? – 1883ExtracellularSequence analysis
Transmembranei1884 – 1904HelicalSequence analysisAdd BLAST21
Topological domaini1905 – 2240CytoplasmicSequence analysisAdd BLAST336

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)DescriptionActionsGraphical viewLength
ChainiPRO_0000004008? – 2240Cadherin-89D
Signal peptidei1 – ?Sequence analysis

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi114N-linked (GlcNAc...)Sequence analysis1
Glycosylationi119N-linked (GlcNAc...)Sequence analysis1
Glycosylationi191N-linked (GlcNAc...)Sequence analysis1
Glycosylationi278N-linked (GlcNAc...)Sequence analysis1
Glycosylationi334N-linked (GlcNAc...)Sequence analysis1
Glycosylationi417N-linked (GlcNAc...)Sequence analysis1
Glycosylationi585N-linked (GlcNAc...)Sequence analysis1
Glycosylationi720N-linked (GlcNAc...)Sequence analysis1
Glycosylationi752N-linked (GlcNAc...)Sequence analysis1
Glycosylationi822N-linked (GlcNAc...)Sequence analysis1
Glycosylationi833N-linked (GlcNAc...)Sequence analysis1
Glycosylationi983N-linked (GlcNAc...)Sequence analysis1
Glycosylationi989N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1006N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1255N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1318N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1486N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1529N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1556N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9VEU1.
PRIDEiQ9VEU1.

Expressioni

Gene expression databases

BgeeiFBgn0038439.
GenevisibleiQ9VEU1. DM.

Interactioni

Protein-protein interaction databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini70 – 179Cadherin 1PROSITE-ProRule annotationAdd BLAST110
Domaini180 – 295Cadherin 2PROSITE-ProRule annotationAdd BLAST116
Domaini296 – 411Cadherin 3PROSITE-ProRule annotationAdd BLAST116
Domaini412 – 528Cadherin 4PROSITE-ProRule annotationAdd BLAST117
Domaini529 – 643Cadherin 5PROSITE-ProRule annotationAdd BLAST115
Domaini824 – 927Cadherin 6PROSITE-ProRule annotationAdd BLAST104
Domaini928 – 1087Cadherin 7PROSITE-ProRule annotationAdd BLAST160
Domaini1171 – 1284Cadherin 8PROSITE-ProRule annotationAdd BLAST114
Domaini1285 – 1389Cadherin 9PROSITE-ProRule annotationAdd BLAST105
Domaini1411 – 1520Cadherin 10PROSITE-ProRule annotationAdd BLAST110
Domaini1534 – 1660Cadherin 11PROSITE-ProRule annotationAdd BLAST127
Domaini1661 – 1774Cadherin 12PROSITE-ProRule annotationAdd BLAST114

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.
GeneTreeiENSGT00850000132356.
InParanoidiQ9VEU1.
OMAiARENMAG.
OrthoDBiEOG091G00EI.

Family and domain databases

Gene3Di2.60.40.60. 14 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)DescriptionActionsGraphical viewLength
Sequence conflicti8M → R in BAB20634 (Ref. 1) Curated1
Sequence conflicti208D → E in BAB20634 (Ref. 1) Curated1
Sequence conflicti305N → Y in BAB20634 (Ref. 1) Curated1
Sequence conflicti310M → I in BAB20634 (Ref. 1) Curated1
Sequence conflicti311T → S in AAQ23544 (Ref. 4) Curated1
Sequence conflicti456A → G in AAQ23544 (Ref. 4) Curated1
Sequence conflicti702E → D in BAB20634 (Ref. 1) Curated1
Sequence conflicti823I → L in BAB20634 (Ref. 1) Curated1
Sequence conflicti945E → G in AAQ23544 (Ref. 4) Curated1
Sequence conflicti997S → P in BAB20634 (Ref. 1) Curated1
Sequence conflicti1187T → A in BAB20634 (Ref. 1) Curated1
Sequence conflicti1258V → G in BAB20634 (Ref. 1) Curated1
Sequence conflicti1319I → M in BAB20634 (Ref. 1) Curated1
Sequence conflicti1330F → S in BAB20634 (Ref. 1) Curated1
Sequence conflicti1342G → S in BAB20634 (Ref. 1) Curated1
Sequence conflicti1497P → A in BAB20634 (Ref. 1) Curated1
Sequence conflicti1504I → V in BAB20634 (Ref. 1) Curated1
Sequence conflicti1606S → C in BAB20634 (Ref. 1) Curated1
Sequence conflicti1618S → N in AAQ23544 (Ref. 4) Curated1
Sequence conflicti1633D → G in BAB20634 (Ref. 1) Curated1
Sequence conflicti1660F → Y in BAB20634 (Ref. 1) Curated1
Sequence conflicti1745D → V in BAB20634 (Ref. 1) Curated1
Sequence conflicti1801P → R in BAB20634 (Ref. 1) Curated1
Sequence conflicti1892L → R in BAB20634 (Ref. 1) Curated1
Sequence conflicti2095T → A in AAQ23544 (Ref. 4) Curated1
Sequence conflicti2138D → G in AAQ23544 (Ref. 4) Curated1

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 interactors.
DIPiDIP-18418N.
IntActiQ9VEU1. 5 interactors.
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.
GeneTreeiENSGT00850000132356.
InParanoidiQ9VEU1.
OMAiARENMAG.
OrthoDBiEOG091G00EI.

Miscellaneous databases

GenomeRNAii42006.
PROiQ9VEU1.

Gene expression databases

BgeeiFBgn0038439.
GenevisibleiQ9VEU1. DM.

Family and domain databases

Gene3Di2.60.40.60. 14 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...

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: November 30, 2016
This is version 121 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.