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Protein

Inactivation-no-after-potential D protein

Gene

inaD

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the negative feedback regulation of the light-activated signaling cascade in photoreceptors through a calcium-mediated process. Interacts with tetrapeptide ligand located in C-terminal sequence of 3 key components of the visual cascade, tethering them and forming a macromolecular signaling phototransduction complex.2 Publications

GO - Molecular functioni

  • calmodulin binding Source: FlyBase
  • myosin binding Source: FlyBase
  • myosin III binding Source: FlyBase
  • photoreceptor activity Source: FlyBase
  • receptor signaling complex scaffold activity Source: FlyBase
  • structural molecule activity Source: FlyBase

GO - Biological processi

  • cellular response to light stimulus Source: FlyBase
  • deactivation of rhodopsin mediated signaling Source: FlyBase
  • detection of light stimulus involved in sensory perception Source: FlyBase
  • phototransduction Source: FlyBase
  • protein localization Source: FlyBase
  • sensory perception of sound Source: FlyBase
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

SignaLinkiQ24008.

Names & Taxonomyi

Protein namesi
Recommended name:
Inactivation-no-after-potential D protein
Gene namesi
Name:inaD
ORF Names:CG3504
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0001263. inaD.

Subcellular locationi

  • Cell membrane 1 Publication; Peripheral membrane protein 1 Publication

GO - Cellular componenti

  • inaD signaling complex Source: FlyBase
  • plasma membrane Source: FlyBase
  • rhabdomere Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi282P → L: Nearly 2-fold increase in interaction with inaC. 1 Publication1
Mutagenesisi308 – 310RCH → GCL: 75% reduced interaction with inaC. 1 Publication3
Mutagenesisi310H → L: 100% increased interaction with inaC. 1 Publication1
Mutagenesisi310H → R: 50% reduced interaction with inaC. 1 Publication1
Mutagenesisi319N → S: Over 3-fold increase in interaction with inaC. 1 Publication1
Mutagenesisi333K → Q: Slight reduction in interaction with inaC. 1 Publication1
Mutagenesisi442M → K in allele inaD-P215; slow recovery of light-induced responses and altered light sensitivity. Abolishes interaction with trp. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000841941 – 674Inactivation-no-after-potential D proteinAdd BLAST674

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei598Phosphoserine1 Publication1
Modified residuei600Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated by inaC.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ24008.
PRIDEiQ24008.

PTM databases

iPTMnetiQ24008.

Expressioni

Tissue specificityi

Expressed in rhabdomeres of the compound eyes and ocelli.1 Publication

Gene expression databases

BgeeiFBgn0001263.
ExpressionAtlasiQ24008. baseline.
GenevisibleiQ24008. DM.

Interactioni

Subunit structurei

Interacts with the C-terminus of trp, and with norpA and inaC to form the inaD signaling complex. Interacts with FKBP59, which together with trpl, rhodopsin and calmodulin may also be part of the inaD complex.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
inaCP136772EBI-195326,EBI-130595
KonA3RLX33EBI-195326,EBI-4306640
norpAP132173EBI-195326,EBI-101510
PRKCAP172522EBI-195326,EBI-1383528From a different organism.
trpP193345EBI-195326,EBI-165136
X11LbetaQ9W2S52EBI-195326,EBI-121784

GO - Molecular functioni

  • calmodulin binding Source: FlyBase
  • myosin binding Source: FlyBase
  • myosin III binding Source: FlyBase
  • receptor signaling complex scaffold activity Source: FlyBase

Protein-protein interaction databases

BioGridi63241. 13 interactors.
DIPiDIP-18621N.
IntActiQ24008. 9 interactors.
MINTiMINT-851851.
STRINGi7227.FBpp0293662.

Structurei

Secondary structure

1674
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 21Combined sources8
Beta strandi25 – 27Combined sources3
Beta strandi30 – 37Combined sources8
Beta strandi40 – 42Combined sources3
Beta strandi45 – 53Combined sources9
Helixi58 – 62Combined sources5
Beta strandi70 – 74Combined sources5
Helixi84 – 93Combined sources10
Beta strandi96 – 104Combined sources9
Turni353 – 356Combined sources4
Helixi357 – 360Combined sources4
Beta strandi365 – 370Combined sources6
Beta strandi376 – 384Combined sources9
Turni385 – 387Combined sources3
Beta strandi388 – 397Combined sources10
Helixi401 – 404Combined sources4
Beta strandi412 – 416Combined sources5
Helixi426 – 435Combined sources10
Beta strandi438 – 445Combined sources8
Turni477 – 479Combined sources3
Beta strandi488 – 493Combined sources6
Beta strandi501 – 504Combined sources4
Beta strandi507 – 510Combined sources4
Beta strandi515 – 520Combined sources6
Helixi525 – 529Combined sources5
Beta strandi537 – 541Combined sources5
Helixi548 – 550Combined sources3
Helixi553 – 561Combined sources9
Beta strandi565 – 573Combined sources9
Beta strandi583 – 588Combined sources6
Beta strandi590 – 593Combined sources4
Beta strandi597 – 601Combined sources5
Beta strandi603 – 611Combined sources9
Helixi617 – 622Combined sources6
Beta strandi628 – 632Combined sources5
Beta strandi638 – 640Combined sources3
Helixi642 – 650Combined sources9
Beta strandi653 – 661Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IHJX-ray1.80A/B11-107[»]
2LA8NMR-A580-665[»]
2QKTX-ray2.05A/B580-665[»]
2QKUX-ray2.20A/B/C580-665[»]
2QKVX-ray1.55A/B580-665[»]
3R0HX-ray2.60A/B/C/D/E/F/G/H473-674[»]
5F67X-ray1.76A/B345-448[»]
ProteinModelPortaliQ24008.
SMRiQ24008.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ24008.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 106PDZ 1PROSITE-ProRule annotationCuratedAdd BLAST90
Domaini249 – 332PDZ 2PROSITE-ProRule annotationCuratedAdd BLAST84
Domaini364 – 448PDZ 3PROSITE-ProRule annotationCuratedAdd BLAST85
Domaini489 – 577PDZ 4PROSITE-ProRule annotationCuratedAdd BLAST89
Domaini584 – 664PDZ 5PROSITE-ProRule annotationCuratedAdd BLAST81

Domaini

Second PDZ domain is a type I PDZ domain that tethers type I PDZ ligand inaC by interaction with its C-terminus.1 Publication

Sequence similaritiesi

Contains 5 PDZ (DHR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410ITA0. Eukaryota.
ENOG41101DI. LUCA.
GeneTreeiENSGT00760000119017.
InParanoidiQ24008.
KOiK13804.
OrthoDBiEOG091G039O.
PhylomeDBiQ24008.

Family and domain databases

Gene3Di2.30.42.10. 5 hits.
InterProiIPR001478. PDZ.
[Graphical view]
PfamiPF00595. PDZ. 3 hits.
[Graphical view]
SMARTiSM00228. PDZ. 5 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 5 hits.
PROSITEiPS50106. PDZ. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q24008-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQFLGKQGT AGELIHMVTL DKTGKKSFGI CIVRGEVKDS PNTKTTGIFI
60 70 80 90 100
KGIVPDSPAH LCGRLKVGDR ILSLNGKDVR NSTEQAVIDL IKEADFKIEL
110 120 130 140 150
EIQTFDKSDE QQAKSDPRSN GYMQAKNKFN QEQTTNNNAS GGQGMGQGQG
160 170 180 190 200
QGQGMAGMNR QQSMQKRNTT FTASMRQKHS NYADEDDEDT RDMTGRIRTE
210 220 230 240 250
AGYEIDRASA GNCKLNKQEK DRDKEQEDEF GYTMAKINKR YNMMKDLRRI
260 270 280 290 300
EVQRDASKPL GLALAGHKDR QKMACFVAGV DPNGALGSVD IKPGDEIVEV
310 320 330 340 350
NGNVLKNRCH LNASAVFKNV DGDKLVMITS RRKPNDEGMC VKPIKKFPTA
360 370 380 390 400
SDETKFIFDQ FPKARTVQVR KEGFLGIMVI YGKHAEVGSG IFISDLREGS
410 420 430 440 450
NAELAGVKVG DMLLAVNQDV TLESNYDDAT GLLKRAEGVV TMILLTLKSE
460 470 480 490 500
EAIKAEKAAE EKKKEEAKKE EEKPQEPATA EIKPNKKILI ELKVEKKPMG
510 520 530 540 550
VIVCGGKNNH VTTGCVITHV YPEGQVAADK RLKIFDHICD INGTPIHVGS
560 570 580 590 600
MTTLKVHQLF HTTYEKAVTL TVFRADPPEL EKFNVDLMKK AGKELGLSLS
610 620 630 640 650
PNEIGCTIAD LIQGQYPEID SKLQRGDIIT KFNGDALEGL PFQVCYALFK
660 670
GANGKVSMEV TRPKPTLRTE APKA
Length:674
Mass (Da):74,332
Last modified:November 1, 1998 - v2
Checksum:iD4C24091D99EA7F3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti319N → S in AAF81203 (PubMed:11342563).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15803 mRNA. Translation: AAC36490.1.
AF245280 Genomic DNA. Translation: AAF81203.1.
AE013599 Genomic DNA. Translation: AAF46915.1.
BT004473 mRNA. Translation: AAO42637.1.
RefSeqiNP_726260.1. NM_166566.1.
UniGeneiDm.2964.

Genome annotation databases

EnsemblMetazoaiFBtr0071909; FBpp0071820; FBgn0001263.
GeneIDi37629.
KEGGidme:Dmel_CG3504.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U15803 mRNA. Translation: AAC36490.1.
AF245280 Genomic DNA. Translation: AAF81203.1.
AE013599 Genomic DNA. Translation: AAF46915.1.
BT004473 mRNA. Translation: AAO42637.1.
RefSeqiNP_726260.1. NM_166566.1.
UniGeneiDm.2964.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IHJX-ray1.80A/B11-107[»]
2LA8NMR-A580-665[»]
2QKTX-ray2.05A/B580-665[»]
2QKUX-ray2.20A/B/C580-665[»]
2QKVX-ray1.55A/B580-665[»]
3R0HX-ray2.60A/B/C/D/E/F/G/H473-674[»]
5F67X-ray1.76A/B345-448[»]
ProteinModelPortaliQ24008.
SMRiQ24008.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63241. 13 interactors.
DIPiDIP-18621N.
IntActiQ24008. 9 interactors.
MINTiMINT-851851.
STRINGi7227.FBpp0293662.

PTM databases

iPTMnetiQ24008.

Proteomic databases

PaxDbiQ24008.
PRIDEiQ24008.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071909; FBpp0071820; FBgn0001263.
GeneIDi37629.
KEGGidme:Dmel_CG3504.

Organism-specific databases

CTDi37629.
FlyBaseiFBgn0001263. inaD.

Phylogenomic databases

eggNOGiENOG410ITA0. Eukaryota.
ENOG41101DI. LUCA.
GeneTreeiENSGT00760000119017.
InParanoidiQ24008.
KOiK13804.
OrthoDBiEOG091G039O.
PhylomeDBiQ24008.

Enzyme and pathway databases

SignaLinkiQ24008.

Miscellaneous databases

ChiTaRSiinaD. fly.
EvolutionaryTraceiQ24008.
GenomeRNAii37629.
PROiQ24008.

Gene expression databases

BgeeiFBgn0001263.
ExpressionAtlasiQ24008. baseline.
GenevisibleiQ24008. DM.

Family and domain databases

Gene3Di2.30.42.10. 5 hits.
InterProiIPR001478. PDZ.
[Graphical view]
PfamiPF00595. PDZ. 3 hits.
[Graphical view]
SMARTiSM00228. PDZ. 5 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 5 hits.
PROSITEiPS50106. PDZ. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiINAD_DROME
AccessioniPrimary (citable) accession number: Q24008
Secondary accession number(s): Q9NBV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: November 1, 1998
Last modified: November 30, 2016
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.