Q9VJE5 · CL190_DROME

Function

function

Together CLIP-190 and jar may coordinate the interaction between the actin and microtubule cytoskeleton. May link endocytic vesicles to microtubules. May play a role in formation of furrows during cellularization.

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 Componentaxon
Cellular Componentaxonal growth cone
Cellular Componentfusome
Cellular ComponentGolgi apparatus
Cellular Componentkinetochore
Cellular Componentmicrotubule associated complex
Cellular Componentmicrotubule organizing center
Cellular Componentmicrotubule plus-end
Cellular Componentperinuclear region of cytoplasm
Cellular Componentspindle microtubule
Molecular Functionactin binding
Molecular Functionmicrotubule binding
Molecular Functionmicrotubule plus-end binding
Molecular Functionmyosin VI heavy chain binding
Biological Processcellularization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Restin homolog
  • Alternative names
    • Cytoplasmic linker protein 190
    • Microtubule-binding protein 190
    • d-CLIP-190

Gene names

    • Name
      CLIP-190
    • ORF names
      CG5020

Organism names

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

Accessions

  • Primary accession
    Q9VJE5
  • Secondary accessions
    • O44929
    • Q8INY8
    • Q8MSD0

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Golgi apparatus
Note: Microtubule-associated (PubMed:9472041).
Lva-CLIP-190 complexes are found at the Golgi (PubMed:11076973).
In the fat body, localizes to a perinuclear non-centrosomal microtubule-organizing centers (ncMTOCs) (PubMed:32066907).

Keywords

Phenotypes & Variants

Disruption phenotype

RNAi-mediated knockdown has no effect on nuclear positioning in fat body cells.

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000835141-1690Restin homolog
Modified residue64Phosphoserine
Modified residue67Phosphoserine
Modified residue216Phosphoserine
Modified residue309Phosphoserine
Modified residue322Phosphoserine
Modified residue325Phosphoserine
Modified residue327Phosphothreonine
Modified residue328Phosphoserine
Modified residue362Phosphothreonine
Modified residue1681Phosphothreonine
Modified residue1682Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Specifically expressed at the tip of the furrow in cellularizing blastoderms. CLIP-190 and jar are coexpressed at several times in development and in a number of tissues, including embryonic axonal neuron processes and posterior pole.

Gene expression databases

Interaction

Subunit

Interacts with Lva.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain, coiled coil.

TypeIDPosition(s)Description
Compositional bias1-15Polar residues
Region1-105Disordered
Compositional bias39-76Polar residues
Domain143-185CAP-Gly 1
Compositional bias195-225Polar residues
Region195-227Disordered
Domain260-302CAP-Gly 2
Coiled coil378-468
Coiled coil484-660
Coiled coil667-916
Region843-905Disordered
Compositional bias868-890Polar residues
Coiled coil926-981
Coiled coil1001-1121
Region1031-1052Disordered
Coiled coil1158-1549
Region1400-1419Disordered
Coiled coil1565-1600
Region1635-1665Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q9VJE5-1

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
    1,690
  • Mass (Da)
    189,065
  • Last updated
    2000-05-01 v1
  • Checksum
    D6F7916A9C532F16
MSDDTSASGGTSAPFPSPVTADPEPGATASKLPGPIRSNIPTPATSGTGIPQPSKMKAPSSFGSTGSVSKIGRPCCNHTTPKSGPPPREATSMSRESDDNLSSINSAYTDNSSAVLTANTEQFIIGQRVWLGGTRPGQIAFIGDTHFAAGEWAGVVLDEPNGKNDGCVSGKRYFQCEPKRGIFSRLTRLTTYPLAGAQTPTSPLAKSSPDRSRTVSPTASIRSSMLRSPGIGGKNGMAVGDRVIVSSGFGSRPGILRYLGETQFAPGNWCGVELDEPSGKNDGTVDDIRYFECKPKYGVFVPIAKVSLSPSSKKTRLSRTGSRESLTSIGTMNSIATTATSRMRMNAQQRKSSTPVKPILATPKSQFSMQDLLREKQQHVEKLMVERDLDREDAQNQALQLQKNINELKARIVELESALDNERKKTEELQCSIDEAQFCGDELNAQSQVYKEKIHDLESKITKLVSATPSLQSILPPDLPSDDGALQEEIAKLQEKMTIQQKEVESRIAEQLEEEQRLRENVKYLNEQIATLQSELVSKDEALEKFSLSECGIENLRRELELLKEENEKQAQEAQAEFTRKLAEKSVEVLRLSSELQNLKATSDSLESERVNKTDECEILQTEVRMRDEQIRELNQQLDEVTTQLNVQKADSSALDDMLRLQKEGTEEKSTLLEKTEKELVQSKEQAAKTLNDKEQLEKQISDLKQLAEQEKLVREMTENAINQIQLEKESIEQQLALKQNELEDFQKKQSESEVHLQEIKAQNTQKDFELVESGESLKKLQQQLEQKTLGHEKLQAALEELKKEKETIIKEKEQELQQLQSKSAESESALKVVQVQLEQLQQQAAASGEEGSKTVAKLHDEISQLKSQAEETQSELKSTQSNLEAKSKQLEAANGSLEEEAKKSGHLLEQITKLKSEVGETQAALSSCHTDVESKTKQLEAANAALEKVNKEYAESRAEASDLQDKVKEITDTLHAELQAERSSSSALHTKLSKFSDEIATGHKELTSKADAWSQEMLQKEKELQELRQQLQDSQDSQTKLKAEGERKEKSFEESIKNLQEEVTKAKTENLELSTGTQTTIKDLQERLEITNAELQHKEKMASEDAQKIADLKTLVEAIQVANANISATNAELSTVLEVLQAEKSETNHIFELFEMEADMNSERLIEKVTGIKEELKETHLQLDERQKKFEELEEKLKQAQQSEQKLQQESQTSKEKLTEIQQSLQELQDSVKQKEELVQNLEEKVRESSSIIEAQNTKLNESNVQLENKTSCLKETQDQLLESQKKEKQLQEEAAKLSGELQQVQEANGDIKDSLVKVEELVKVLEEKLQAATSQLDAQQATNKELQELLVKSQENEGNLQGESLAVTEKLQQLEQANGELKEALCQKENGLKELQGKLDESNTVLESQKKSHNEIQDKLEQAQQKERTLQEETSKLAEQLSQLKQANEELQKSLQQKQLLLEKGNEFDTQLAEYQKVIDEMDDAASVKSALLEQLQNRVAELETALRQANDAQKTAYLETKELRRQLESLELEKSREVLSLKAQMNGASSRSGKGDEVESLDIETSLAKINFLNSIIADMQQKNDALKAKVQTLETLPMDFTKPHAFDALTKRKPAPRLFCDICDEFDQHDTEDCPIQGSEDQDYSTPSSESNNNEKERKLPAPRKYCDSCEVFGHDTSECADDETY

Q9VJE5-2

  • Name
    B
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q9VJE5-3

  • Name
    C
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-109: MSDDTSASGGTSAPFPSPVTADPEPGATASKLPGPIRSNIPTPATSGTGIPQPSKMKAPSSFGSTGSVSKIGRPCCNHTTPKSGPPPREATSMSRESDDNLSSINSAYT → MSRESDDNLSSINSAYTDLYQETVRRFTRSSLSPTPDWDRFSPARRSLKSEAGSRASYDYYLEATGRRRSS

Computationally mapped potential isoform sequences

There are 12 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
B7YZW7B7YZW7_DROMECLIP-190456
B7YZW8B7YZW8_DROMECLIP-1901653
A0A6F7UQK0A0A6F7UQK0_DROMECLIP-1901795
M9PBC9M9PBC9_DROMECLIP-190306
M9PDB4M9PDB4_DROMECLIP-190311
M9PG37M9PG37_DROMECLIP-1901601
Q0E8Q0Q0E8Q0_DROMECLIP-190328
Q0E8Q1Q0E8Q1_DROMECLIP-190365
E1JHK0E1JHK0_DROMECLIP-1901598
E1JHJ9E1JHJ9_DROMECLIP-1901668
X2JAQ4X2JAQ4_DROMECLIP-190327
Q7KT48Q7KT48_DROMECLIP-1901623

Features

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

TypeIDPosition(s)Description
Compositional bias1-15Polar residues
Alternative sequenceVSP_0504801-109in isoform C
Compositional bias39-76Polar residues
Sequence conflict109in Ref. 5; AAR82803
Compositional bias195-225Polar residues
Sequence conflict207in Ref. 1; AAB96783
Alternative sequenceVSP_050479348in isoform B
Sequence conflict420in Ref. 1; AAB96783 and 5; AAR82803
Sequence conflict492in Ref. 1; AAB96783 and 5; AAR82803
Sequence conflict561in Ref. 1; AAB96783
Sequence conflict614in Ref. 1; AAB96783
Sequence conflict683in Ref. 1; AAB96783 and 5; AAR82803
Sequence conflict692in Ref. 1; AAB96783 and 5; AAR82803
Sequence conflict717in Ref. 1; AAB96783 and 5; AAR82803
Sequence conflict728in Ref. 5; AAR82803
Sequence conflict745in Ref. 5; AAR82803
Sequence conflict769in Ref. 1; AAB96783 and 5; AAR82803
Sequence conflict787in Ref. 1; AAB96783 and 5; AAR82803
Sequence conflict805-807in Ref. 5; AAR82803
Compositional bias868-890Polar residues
Sequence conflict881in Ref. 1; AAB96783
Sequence conflict907-909in Ref. 1; AAB96783
Sequence conflict920in Ref. 1; AAB96783
Sequence conflict929in Ref. 1; AAB96783

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF041382
EMBL· GenBank· DDBJ
AAB96783.1
EMBL· GenBank· DDBJ
mRNA
AE014134
EMBL· GenBank· DDBJ
AAF53604.1
EMBL· GenBank· DDBJ
Genomic DNA
AE014134
EMBL· GenBank· DDBJ
AAF53605.2
EMBL· GenBank· DDBJ
Genomic DNA
AE014134
EMBL· GenBank· DDBJ
AAN10987.1
EMBL· GenBank· DDBJ
Genomic DNA
AY118896
EMBL· GenBank· DDBJ
AAM50756.1
EMBL· GenBank· DDBJ
mRNA
BT011136
EMBL· GenBank· DDBJ
AAR82803.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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