Q09103 · DGK2_DROME

Function

function

Required for the maintenance of phospholipid turnover within the photoreceptor.

Catalytic activity

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmembrane
Molecular FunctionATP binding
Molecular FunctionATP-dependent diacylglycerol kinase activity
Molecular Functionmetal ion binding
Biological Processdiacylglycerol metabolic process
Biological ProcessG protein-coupled opsin signaling pathway
Biological Processintracellular signal transduction
Biological Processlipid phosphorylation
Biological Processnegative regulation of opsin-mediated signaling pathway
Biological Processphosphatidic acid biosynthetic process
Biological Processphosphatidylinositol biosynthetic process
Biological Processphotoreceptor cell maintenance
Biological Processphototransduction
Biological Processprotein kinase C-activating G protein-coupled receptor signaling pathway
Biological Processsensory perception of smell
Biological Processsensory perception of sound
Biological Processthermotaxis
Biological Processvisual perception

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Eye-specific diacylglycerol kinase
  • EC number
  • Short names
    DAG kinase 2; DGK 2; Diglyceride kinase 2
  • Alternative names
    • Retinal degeneration A protein

Gene names

    • Name
      rdgA
    • Synonyms
      DGK2
    • ORF names
      CG34344

Organism names

  • Taxonomic identifier
  • Strains
    • Canton-S
    • Berkeley
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora

Accessions

  • Primary accession
    Q09103
  • Secondary accessions
    • A8JV38
    • A8JV40
    • Q0KHU7
    • Q7YU71
    • Q8SY47
    • Q9W3A4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Flies exhibit photoreceptor cells that degenerate within a week after eclosion.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002184741-1457Eye-specific diacylglycerol kinase

Proteomic databases

Expression

Tissue specificity

Expressed specifically in adult eye.

Gene expression databases

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, zinc finger, domain, repeat.

TypeIDPosition(s)Description
Compositional bias1-120Polar residues
Region1-123Disordered
Compositional bias136-151Polar residues
Region136-177Disordered
Region207-339Disordered
Compositional bias213-257Acidic residues
Compositional bias258-275Basic and acidic residues
Compositional bias301-339Polar residues
Zinc finger591-641Phorbol-ester/DAG-type 1
Zinc finger661-724Phorbol-ester/DAG-type 2
Region758-799Disordered
Domain808-944DAGKc
Compositional bias1264-1292Polar residues
Region1264-1302Disordered
Repeat1320-1349ANK 1
Repeat1353-1382ANK 2
Repeat1389-1418ANK 3
Repeat1422-1451ANK 4

Sequence similarities

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q09103-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    1,457
  • Mass (Da)
    160,142
  • Last updated
    2005-06-21 v2
  • Checksum
    8F4E33E9C1B665D1
MQQQQQPSIDQLPEPTASTSNSATTKPTIATATTSTTTTSGNNFHQQLQATTAATMQRLRTTFTRSRTPTGAEMKMQNSLEVPKQVRSASFDEMQLESQRASSSLLKQQSSSSASADERSSEAGFLQVPLAAHQQRSHSFDSATASAGSDDSGTFLEVPRRLKARRSSSTKTPPPCIHCHYLEEYERRMTAEQRYFIDHRELTALSYSNTSSEASEDEDEVEGHNAEEEEEGSAAIEDAEEETTEAATEEADEDPRTEVESEHDHDPDDDAALEMDIRIGNMSQGSSIEESRARLPRQMRRHTIGSSSVTSASEDEGLEGSDNGSPHFGNTLLPPQPTTPCGITFTLSPTNGDYPSPPHLPLDPGSPPISPCSSNSGRLPALAPIISTPCSSADADDAGAAMGLPVRARRRSISRQEAIFVEPTGNSLENVSHEEVDNSNTKSSVDTADSLDEASTMATCGSPGAAGGSGASSSHHNAFVVRDIYLMVPDLKRDRAASVDSCFSKLSSNAKTEELQPSADGCFLTVPNINATRSRSVDIVLPTDEQARYKALSMTGSTVTYADGRTASASNSRRPIRIVPDWTENAVQGEHYWKPTSASGDLCCLNEECIKSGQRMKCSACQLVAHHNCIPFVNEKSTLACKPTYRDVGIRQYREQTTTHHHWVHRKLEKGKCKQCGKFFPMKQAVQSKLFGSKEIVALACAWCHEIYHNKEACFNQAKIGEECRLGNYAPIIVPPSWIVKLPTKGNFKSSIRVSNKNNAASGSGGGGAGGGAGGGGGKSKKQTQRRQKGKEEKKEPRAFIVKPIPSPEVIPVIVFINPKSGGNQGHKLLGKFQHLLNPRQVFDLTQGGPKMGLDMFRKAPNLRVLACGGDGTVGWVLSVLDQIQPPLQPAPAVGVLPLGTGNDLARALGWGGGYTDEPIGKILREIGMSQCVLMDRWRVKVTPNDDVTDDHVDRSKPNVPLNVINNYFSFGVDAHIALEFHEAREAHPERFNSRLRNKMYYGQMGGKDLILRQYRNLSQWVTLECDGQDFTGKLRDAGCHAVLFLNIPSYGGGTHPWNDSFGASKPSIDDGLMEVVGLTTYQLPMLQAGMHGTCICQCRKARIITKRTIPMQVDGEACRVKPSVIEIELLNKALMLSKRKHGRGDVQVNPLEKMQLHILRVTMQQYEQYHYDKEMLRKLANKLGQIEIESQCDLEHVRNMLNTKFEESISYPKVSQDWCFIDSCTAEHYFRIDRAQEHLHYICDIAIDELYILDHEAATMPQTPDQERSFAAFSQRQAQNERRQMDQAQGRGPGSTDEDLQIGSKPIKVMKWKSPILEQTSDAILLAAQSGDLNMLRALHEQGYSLQSVNKNGQTALHFACKYNHRDIVKYIIASATRRLINMADKELGQTALHIAAEQNRRDICVMLVAAGAHLDTLDSGGNTPMMVAFNKNANEIATYLESKQGTQPVDGWLDD

Q09103-3

  • Name
    B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-116: MQQQQQPSIDQLPEPTASTSNSATTKPTIATATTSTTTTSGNNFHQQLQATTAATMQRLRTTFTRSRTPTGAEMKMQNSLEVPKQVRSASFDEMQLESQRASSSLLKQQSSSSASA → MPERSISQRDLDEIEIESDEEEEELEQGVGLSTRSRRNRRGASDSPAASRARNATNGIQNRGRERERERERERSRERFGGTNAADEARFYDDEEQRMEDDGEEDSDEDIEMLDYDT
    • 117-564: Missing
    • 1315-1315: S → SNKDRLFSFNEDVFGCGFS
    • 1445-1457: KQGTQPVDGWLDD → QERFMHLEKQTRI

Q09103-2

  • Name
    C
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-132: MQQQQQPSIDQLPEPTASTSNSATTKPTIATATTSTTTTSGNNFHQQLQATTAATMQRLRTTFTRSRTPTGAEMKMQNSLEVPKQVRSASFDEMQLESQRASSSLLKQQSSSSASADERSSEAGFLQVPLAA → MERLLHAVREEFQTEDEYETEVDDEGNVLHRSSISSCSSSSSSSNTSSSSDGSNSTASQPLSPSLPQPRRRLQRSDSFGSVGGGVAGGVAGSGATGAGGVRRFRRSSIGMQRKSAFRQRKLDSLGAWRRKRR
    • 133-565: Missing

Computationally mapped potential isoform sequences

There are 8 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A6H2EFG8A0A6H2EFG8_DROMErdgA1365
M9PH20M9PH20_DROMErdgA1460
M9PHG3M9PHG3_DROMErdgA1462
X2JE67X2JE67_DROMErdgA1307
M9MSN3M9MSN3_DROMErdgA1009
M9MS31M9MS31_DROMErdgA1452
X2JEJ9X2JEJ9_DROMErdgA1314
A0A023GPM5A0A023GPM5_DROMErdgA991

Sequence caution

The sequence AAQ22428.1 differs from that shown. Reason: Miscellaneous discrepancy Intron retention.

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0302641-116in isoform B
Compositional bias1-120Polar residues
Alternative sequenceVSP_0302651-132in isoform C
Sequence conflict32in Ref. 1; BAA04135
Alternative sequenceVSP_030266117-564in isoform B
Alternative sequenceVSP_030267133-565in isoform C
Compositional bias136-151Polar residues
Sequence conflict208in Ref. 1; BAA04135
Compositional bias213-257Acidic residues
Compositional bias258-275Basic and acidic residues
Compositional bias301-339Polar residues
Sequence conflict438in Ref. 1; BAA04135
Sequence conflict565in Ref. 1; BAA04135
Sequence conflict667in Ref. 1; BAA04135
Sequence conflict679-684in Ref. 1; BAA04135
Sequence conflict778in Ref. 1; BAA04135
Sequence conflict924in Ref. 5; AAQ22428
Sequence conflict983in Ref. 5; AAQ22428
Sequence conflict1128in Ref. 5; AAQ22428
Compositional bias1264-1292Polar residues
Alternative sequenceVSP_0287321315in isoform B
Alternative sequenceVSP_0287331445-1457in isoform B

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D17315
EMBL· GenBank· DDBJ
BAA04135.1
EMBL· GenBank· DDBJ
mRNA
AE014298
EMBL· GenBank· DDBJ
AAF46430.2
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
ABW09364.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014298
EMBL· GenBank· DDBJ
ABW09365.1
EMBL· GenBank· DDBJ
Genomic DNA
AY075349
EMBL· GenBank· DDBJ
AAL68208.1
EMBL· GenBank· DDBJ
mRNA
BT009959
EMBL· GenBank· DDBJ
AAQ22428.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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