Q9VJE5 · CL190_DROME
- ProteinRestin homolog
- GeneCLIP-190
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1690 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | axon | |
Cellular Component | axonal growth cone | |
Cellular Component | fusome | |
Cellular Component | Golgi apparatus | |
Cellular Component | kinetochore | |
Cellular Component | microtubule associated complex | |
Cellular Component | microtubule organizing center | |
Cellular Component | microtubule plus-end | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | spindle microtubule | |
Molecular Function | actin binding | |
Molecular Function | microtubule binding | |
Molecular Function | microtubule plus-end binding | |
Molecular Function | myosin VI heavy chain binding | |
Biological Process | cellularization |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRestin homolog
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9VJE5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000083514 | 1-1690 | Restin homolog | |||
Sequence: MSDDTSASGGTSAPFPSPVTADPEPGATASKLPGPIRSNIPTPATSGTGIPQPSKMKAPSSFGSTGSVSKIGRPCCNHTTPKSGPPPREATSMSRESDDNLSSINSAYTDNSSAVLTANTEQFIIGQRVWLGGTRPGQIAFIGDTHFAAGEWAGVVLDEPNGKNDGCVSGKRYFQCEPKRGIFSRLTRLTTYPLAGAQTPTSPLAKSSPDRSRTVSPTASIRSSMLRSPGIGGKNGMAVGDRVIVSSGFGSRPGILRYLGETQFAPGNWCGVELDEPSGKNDGTVDDIRYFECKPKYGVFVPIAKVSLSPSSKKTRLSRTGSRESLTSIGTMNSIATTATSRMRMNAQQRKSSTPVKPILATPKSQFSMQDLLREKQQHVEKLMVERDLDREDAQNQALQLQKNINELKARIVELESALDNERKKTEELQCSIDEAQFCGDELNAQSQVYKEKIHDLESKITKLVSATPSLQSILPPDLPSDDGALQEEIAKLQEKMTIQQKEVESRIAEQLEEEQRLRENVKYLNEQIATLQSELVSKDEALEKFSLSECGIENLRRELELLKEENEKQAQEAQAEFTRKLAEKSVEVLRLSSELQNLKATSDSLESERVNKTDECEILQTEVRMRDEQIRELNQQLDEVTTQLNVQKADSSALDDMLRLQKEGTEEKSTLLEKTEKELVQSKEQAAKTLNDKEQLEKQISDLKQLAEQEKLVREMTENAINQIQLEKESIEQQLALKQNELEDFQKKQSESEVHLQEIKAQNTQKDFELVESGESLKKLQQQLEQKTLGHEKLQAALEELKKEKETIIKEKEQELQQLQSKSAESESALKVVQVQLEQLQQQAAASGEEGSKTVAKLHDEISQLKSQAEETQSELKSTQSNLEAKSKQLEAANGSLEEEAKKSGHLLEQITKLKSEVGETQAALSSCHTDVESKTKQLEAANAALEKVNKEYAESRAEASDLQDKVKEITDTLHAELQAERSSSSALHTKLSKFSDEIATGHKELTSKADAWSQEMLQKEKELQELRQQLQDSQDSQTKLKAEGERKEKSFEESIKNLQEEVTKAKTENLELSTGTQTTIKDLQERLEITNAELQHKEKMASEDAQKIADLKTLVEAIQVANANISATNAELSTVLEVLQAEKSETNHIFELFEMEADMNSERLIEKVTGIKEELKETHLQLDERQKKFEELEEKLKQAQQSEQKLQQESQTSKEKLTEIQQSLQELQDSVKQKEELVQNLEEKVRESSSIIEAQNTKLNESNVQLENKTSCLKETQDQLLESQKKEKQLQEEAAKLSGELQQVQEANGDIKDSLVKVEELVKVLEEKLQAATSQLDAQQATNKELQELLVKSQENEGNLQGESLAVTEKLQQLEQANGELKEALCQKENGLKELQGKLDESNTVLESQKKSHNEIQDKLEQAQQKERTLQEETSKLAEQLSQLKQANEELQKSLQQKQLLLEKGNEFDTQLAEYQKVIDEMDDAASVKSALLEQLQNRVAELETALRQANDAQKTAYLETKELRRQLESLELEKSREVLSLKAQMNGASSRSGKGDEVESLDIETSLAKINFLNSIIADMQQKNDALKAKVQTLETLPMDFTKPHAFDALTKRKPAPRLFCDICDEFDQHDTEDCPIQGSEDQDYSTPSSESNNNEKERKLPAPRKYCDSCEVFGHDTSECADDETY | ||||||
Modified residue | 64 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 67 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 216 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 309 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 322 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 325 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 327 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 328 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 362 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1681 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1682 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
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
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MSDDTSASGGTSAPF | ||||||
Region | 1-105 | Disordered | ||||
Sequence: MSDDTSASGGTSAPFPSPVTADPEPGATASKLPGPIRSNIPTPATSGTGIPQPSKMKAPSSFGSTGSVSKIGRPCCNHTTPKSGPPPREATSMSRESDDNLSSIN | ||||||
Compositional bias | 39-76 | Polar residues | ||||
Sequence: NIPTPATSGTGIPQPSKMKAPSSFGSTGSVSKIGRPCC | ||||||
Domain | 143-185 | CAP-Gly 1 | ||||
Sequence: GDTHFAAGEWAGVVLDEPNGKNDGCVSGKRYFQCEPKRGIFSR | ||||||
Compositional bias | 195-225 | Polar residues | ||||
Sequence: AGAQTPTSPLAKSSPDRSRTVSPTASIRSSM | ||||||
Region | 195-227 | Disordered | ||||
Sequence: AGAQTPTSPLAKSSPDRSRTVSPTASIRSSMLR | ||||||
Domain | 260-302 | CAP-Gly 2 | ||||
Sequence: GETQFAPGNWCGVELDEPSGKNDGTVDDIRYFECKPKYGVFVP | ||||||
Coiled coil | 378-468 | |||||
Sequence: QHVEKLMVERDLDREDAQNQALQLQKNINELKARIVELESALDNERKKTEELQCSIDEAQFCGDELNAQSQVYKEKIHDLESKITKLVSAT | ||||||
Coiled coil | 484-660 | |||||
Sequence: GALQEEIAKLQEKMTIQQKEVESRIAEQLEEEQRLRENVKYLNEQIATLQSELVSKDEALEKFSLSECGIENLRRELELLKEENEKQAQEAQAEFTRKLAEKSVEVLRLSSELQNLKATSDSLESERVNKTDECEILQTEVRMRDEQIRELNQQLDEVTTQLNVQKADSSALDDMLR | ||||||
Coiled coil | 667-916 | |||||
Sequence: EEKSTLLEKTEKELVQSKEQAAKTLNDKEQLEKQISDLKQLAEQEKLVREMTENAINQIQLEKESIEQQLALKQNELEDFQKKQSESEVHLQEIKAQNTQKDFELVESGESLKKLQQQLEQKTLGHEKLQAALEELKKEKETIIKEKEQELQQLQSKSAESESALKVVQVQLEQLQQQAAASGEEGSKTVAKLHDEISQLKSQAEETQSELKSTQSNLEAKSKQLEAANGSLEEEAKKSGHLLEQITKLK | ||||||
Region | 843-905 | Disordered | ||||
Sequence: QQAAASGEEGSKTVAKLHDEISQLKSQAEETQSELKSTQSNLEAKSKQLEAANGSLEEEAKKS | ||||||
Compositional bias | 868-890 | Polar residues | ||||
Sequence: SQAEETQSELKSTQSNLEAKSKQ | ||||||
Coiled coil | 926-981 | |||||
Sequence: LSSCHTDVESKTKQLEAANAALEKVNKEYAESRAEASDLQDKVKEITDTLHAELQA | ||||||
Coiled coil | 1001-1121 | |||||
Sequence: ATGHKELTSKADAWSQEMLQKEKELQELRQQLQDSQDSQTKLKAEGERKEKSFEESIKNLQEEVTKAKTENLELSTGTQTTIKDLQERLEITNAELQHKEKMASEDAQKIADLKTLVEAIQ | ||||||
Region | 1031-1052 | Disordered | ||||
Sequence: QLQDSQDSQTKLKAEGERKEKS | ||||||
Coiled coil | 1158-1549 | |||||
Sequence: EADMNSERLIEKVTGIKEELKETHLQLDERQKKFEELEEKLKQAQQSEQKLQQESQTSKEKLTEIQQSLQELQDSVKQKEELVQNLEEKVRESSSIIEAQNTKLNESNVQLENKTSCLKETQDQLLESQKKEKQLQEEAAKLSGELQQVQEANGDIKDSLVKVEELVKVLEEKLQAATSQLDAQQATNKELQELLVKSQENEGNLQGESLAVTEKLQQLEQANGELKEALCQKENGLKELQGKLDESNTVLESQKKSHNEIQDKLEQAQQKERTLQEETSKLAEQLSQLKQANEELQKSLQQKQLLLEKGNEFDTQLAEYQKVIDEMDDAASVKSALLEQLQNRVAELETALRQANDAQKTAYLETKELRRQLESLELEKSREVLSLKAQMN | ||||||
Region | 1400-1419 | Disordered | ||||
Sequence: KLDESNTVLESQKKSHNEIQ | ||||||
Coiled coil | 1565-1600 | |||||
Sequence: DIETSLAKINFLNSIIADMQQKNDALKAKVQTLETL | ||||||
Region | 1635-1665 | Disordered | ||||
Sequence: TEDCPIQGSEDQDYSTPSSESNNNEKERKLP |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- NameA
- Length1,690
- Mass (Da)189,065
- Last updated2000-05-01 v1
- ChecksumD6F7916A9C532F16
Q9VJE5-2
- NameB
- Differences from canonical
- 348-348: Missing
Q9VJE5-3
- NameC
- Differences from canonical
- 1-109: MSDDTSASGGTSAPFPSPVTADPEPGATASKLPGPIRSNIPTPATSGTGIPQPSKMKAPSSFGSTGSVSKIGRPCCNHTTPKSGPPPREATSMSRESDDNLSSINSAYT → MSRESDDNLSSINSAYTDLYQETVRRFTRSSLSPTPDWDRFSPARRSLKSEAGSRASYDYYLEATGRRRSS
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B7YZW7 | B7YZW7_DROME | CLIP-190 | 456 | ||
B7YZW8 | B7YZW8_DROME | CLIP-190 | 1653 | ||
A0A6F7UQK0 | A0A6F7UQK0_DROME | CLIP-190 | 1795 | ||
M9PBC9 | M9PBC9_DROME | CLIP-190 | 306 | ||
M9PDB4 | M9PDB4_DROME | CLIP-190 | 311 | ||
M9PG37 | M9PG37_DROME | CLIP-190 | 1601 | ||
Q0E8Q0 | Q0E8Q0_DROME | CLIP-190 | 328 | ||
Q0E8Q1 | Q0E8Q1_DROME | CLIP-190 | 365 | ||
E1JHK0 | E1JHK0_DROME | CLIP-190 | 1598 | ||
E1JHJ9 | E1JHJ9_DROME | CLIP-190 | 1668 | ||
X2JAQ4 | X2JAQ4_DROME | CLIP-190 | 327 | ||
Q7KT48 | Q7KT48_DROME | CLIP-190 | 1623 |
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Polar residues | ||||
Sequence: MSDDTSASGGTSAPF | ||||||
Alternative sequence | VSP_050480 | 1-109 | in isoform C | |||
Sequence: MSDDTSASGGTSAPFPSPVTADPEPGATASKLPGPIRSNIPTPATSGTGIPQPSKMKAPSSFGSTGSVSKIGRPCCNHTTPKSGPPPREATSMSRESDDNLSSINSAYT → MSRESDDNLSSINSAYTDLYQETVRRFTRSSLSPTPDWDRFSPARRSLKSEAGSRASYDYYLEATGRRRSS | ||||||
Compositional bias | 39-76 | Polar residues | ||||
Sequence: NIPTPATSGTGIPQPSKMKAPSSFGSTGSVSKIGRPCC | ||||||
Sequence conflict | 109 | in Ref. 5; AAR82803 | ||||
Sequence: T → I | ||||||
Compositional bias | 195-225 | Polar residues | ||||
Sequence: AGAQTPTSPLAKSSPDRSRTVSPTASIRSSM | ||||||
Sequence conflict | 207 | in Ref. 1; AAB96783 | ||||
Sequence: S → N | ||||||
Alternative sequence | VSP_050479 | 348 | in isoform B | |||
Sequence: Missing | ||||||
Sequence conflict | 420 | in Ref. 1; AAB96783 and 5; AAR82803 | ||||
Sequence: D → G | ||||||
Sequence conflict | 492 | in Ref. 1; AAB96783 and 5; AAR82803 | ||||
Sequence: K → Q | ||||||
Sequence conflict | 561 | in Ref. 1; AAB96783 | ||||
Sequence: E → A | ||||||
Sequence conflict | 614 | in Ref. 1; AAB96783 | ||||
Sequence: T → S | ||||||
Sequence conflict | 683 | in Ref. 1; AAB96783 and 5; AAR82803 | ||||
Sequence: S → I | ||||||
Sequence conflict | 692 | in Ref. 1; AAB96783 and 5; AAR82803 | ||||
Sequence: N → Q | ||||||
Sequence conflict | 717 | in Ref. 1; AAB96783 and 5; AAR82803 | ||||
Sequence: M → K | ||||||
Sequence conflict | 728 | in Ref. 5; AAR82803 | ||||
Sequence: E → D | ||||||
Sequence conflict | 745 | in Ref. 5; AAR82803 | ||||
Sequence: D → V | ||||||
Sequence conflict | 769 | in Ref. 1; AAB96783 and 5; AAR82803 | ||||
Sequence: F → L | ||||||
Sequence conflict | 787 | in Ref. 1; AAB96783 and 5; AAR82803 | ||||
Sequence: Q → E | ||||||
Sequence conflict | 805-807 | in Ref. 5; AAR82803 | ||||
Sequence: EKE → KKK | ||||||
Compositional bias | 868-890 | Polar residues | ||||
Sequence: SQAEETQSELKSTQSNLEAKSKQ | ||||||
Sequence conflict | 881 | in Ref. 1; AAB96783 | ||||
Sequence: Q → E | ||||||
Sequence conflict | 907-909 | in Ref. 1; AAB96783 | ||||
Sequence: HLL → QLQ | ||||||
Sequence conflict | 920 | in Ref. 1; AAB96783 | ||||
Sequence: G → E | ||||||
Sequence conflict | 929 | in Ref. 1; AAB96783 | ||||
Sequence: C → Y |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |