Q9VMD9 · TIG_DROME
- ProteinTiggrin
- GeneTig
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2188 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a ligand for integrin alpha-PS2/beta-PS. Required in larvae for proper muscle structure and function. Involved in the regulation of cell adhesion during wing development.
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | basement membrane | |
Cellular Component | extracellular matrix | |
Cellular Component | extracellular region | |
Molecular Function | integrin binding | |
Biological Process | axon guidance | |
Biological Process | cell adhesion mediated by integrin | |
Biological Process | cell-substrate adhesion | |
Biological Process | photoreceptor cell axon guidance | |
Biological Process | regulation of cell adhesion mediated by integrin | |
Biological Process | substrate adhesion-dependent cell spreading |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTiggrin
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9VMD9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the basal surface of the dorsoventral cell layer interface during pupal wing development.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Pupal lethal with about 1% escapers. In mutant larvae, muscles 6 and 7 appear stringy and not anchored to other muscles or the epidermis, often these muscles are missing or unrecognizable. Sites where muscles 3, 4, 5, 8 and 16 come together are rarely recognizable and large gaps between muscles 9 and 10 can be observed. Muscle contraction waves that transverse the length of the larvae and are responsible for locomotion are much slower in mutant larvae. Mutant pupae are longer than wild type pupae. Mutant adult flies present elongated abdomen and wings with altered shapes and sizes.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 1989-1991 | Partially rescues muscle function and structure defects in the null mutant. Fails to interact with alpha-PS2/beta-PS. | ||||
Sequence: RGD → LGA |
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MRALGGITLLLAVAICQG | ||||||
Chain | PRO_5000144152 | 19-2188 | Tiggrin | |||
Sequence: YETYQRSSFRSSSSSSYGGGQTVPQLNSFASAHFNEVRELANQLKQKFNVLSQGSTNFAYTSPWSASILDLSGKSTLQLDQLSSEISRQLVQDMREGITNYHTIAQPNFFEAKAAELLERYSGAESASLQQTVGLGPYQPVDLSGFDEVKNYAYPAEVKVIDGKTYVVHRNCTEATKLSDYGSSGQLNSGFLGHQQTSLPLSSTTTTITRKKTIHDWVRENMEPSVVGYNSVVKLDGQLRNSALNQMVPLSPGSNVVIHRFNKTITTNPDGTSSVGGSEWQQRWQDGKLVYDHQQPFGQSTIPRDEQWKREERERLFWYLTTPQRLDDWQQQQEERLLGVVQRYQVSLPVLKEFHRRELARYEALLGQYQSRVQDTSSWQRQERGRLDWLIHQNGFTVQDIERWQNENARKLAEAARQHGISQNQLQQFQREELQRLYVHFNQVNESLAPQVPSVPQTTYNYQSSSSLTEDNTKEQQRLEELIRQHNATIAALQNSIKTDQQRLKNLSIKYQGDMQSQTQWLRGEVARIGDLIKEQNEQVSKITAWQSSERSRLENILLQHRGSVEEVQQRINMDRNYLQNLATKYQVSVEELEKWQKEELERLQVRGQQQLEEHIKDWQISVSSNLRDIATQNKLTIDEFQNYIINDRSHLEEMARLYKVKVEEIEQWIKSELKKFQSEGLLKGVEQELIQWQQKERERLQAIVQQNSLTVEQLEVRIKNDQDHFFKLADKYKINVEDIQDWLKKELLRLQSEGLVKAETLKEWQQQERAQISLLVQQNKYSLDEFERKMLADRARLQELSNTYNVKVSEIEQWIKSEGDRLQHEGQLRMESQLNNWQKIERQRLLDLINKNNLSIEEIESKISKDQTHLYSLAQQHQVRVEEIEQWIRQQIQKLQDQGLIEMQKLKNWQLEWRGNLTNMVQDRDFTVEEFHKWLLKDREQLQSLAMQHNVQIEEIEQFVKKEEQRFIGMGLLKPSEKLTNWQEVERLHLKNLAQQQYKSTEQLEARLRQDRELLERLARQYSVQVEEIESWMKQELARMRDEGQLQIDNLTSWQLAERERLEALIKQNKQWSAEELRAELEKDREHMQTMAFQYHTSVEEIEKWLQSEIERLKQQGKLNIEQLTAWQRTEQQRILSLLQQHSNITLEQFQAKVHNDRRFLMNLAEQHHVHIEEVDNYVKQVIEDLRKNGQFEIEQLQTWQRVERDYIKSLISEYKNSLSTAEYEEKLLADRAHLKHLADQYRINVEQIEEWMIAELKRLRGSTEETLKSLSAWQVSELERLQNLVKQQNHLTFVEFEMELNQERDRLQKLANQYSVNVVEIEEWLRQQLINLRTTGQAKVENLSKWQVEEQQRLIEMLLKKQQEMPYEQVERELTQDHARLQSLSQTHHVDIDHVDHWLREELRRLQSSGLVQIEQQTQWQQKISNGFNNWLEQQRNGASYQDFVDFLKRDKQRMDGIATDYHVTVEQVEKWVQKEAARLSLIGVIERPENNLKYEDISNIWVGDQTDSWKNELVTRLRSVTRQRPFTRQEFESYLIRNKPIFEQIARQYHVTIEDIHLWLDQSAKNEGLVTTEWQAKERLHIDNLINQQLRKQQRWTIEELELRLNNDQKHLQDAVAQYHVTVEELKVWYKDELNRLLEQRRIDRGSGISWQNIESQRIYLAIVNNPGISRQALENRLFRDVHVRASQYQITVEELRQFILSQLRRFSDMGLIVDNGRQANNWHDQERKRLREVVKGVVITEQELLDFISQDTSFQTQLAQSYQVGLEQLAPVQRIFIGNLAREQLLEQRRLNHLTTWQQRERDRLYEFIGNQNMTQTELKTWQIQDSKLLAEFAKRYEISVQQLSDWQKKELARINQLARYYGMSQSDLQQFREGELRQLAYINHRQLLSAAEAQKWEKRHQWTLSRLQSRYGKFGQELVAWRRTLYLLSQGLIDLPADSGSNGGYVVDAGSTNATAVYKPIFSKDRGDQPPHTYDESFVEGDEPGLEGETARPRPPNPAPIVSTPKPPLPYSRGGPSGGFEYRRQDYTFNVPVGSASASASGGPTGSSASASASLGKWNRASGDEPLQQEVDLGQQQQIEELGWNEKLEDLGQQTQVEDTDWNQQAEDLGQQQQVQVEDDLHFDQTQGHSSSSNSRSQPLQQATKVEVEATSEPSFWEKLKEKLG |
Post-translational modification
O-glycosylation by pgant3 is required for proper secretion and localization to the basal cell layer interface during wing development.
Proteomic databases
Expression
Tissue specificity
In embryos, expressed in the apodemes (muscle attachment sites) of the major longitudinal muscles 4, 6, 7, 12 and 13 and the wide dorsal oblique muscles 9 and 10, in hemocytes, in fat body cells, in basement membranes surrounding the gut and in the commissures of the ventral nerve cord. Expressed in larval imaginal wing disk and in pupal wing. In adult flies, expressed in the jump muscle (at protein level).
Developmental stage
Expressed throughout embryogenesis; first appears at 8-10 hours. Detected in larval and pupal stages (at protein level). Transcripts are first detected at 6-8 hours of development, expression peaks at 12-14 hours and then declines by the end of embryogenesis.
Gene expression databases
Structure
Family & Domains
Features
Showing features for coiled coil, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 570-635 | |||||
Sequence: SRLENILLQHRGSVEEVQQRINMDRNYLQNLATKYQVSVEELEKWQKEELERLQVRGQQQLEEHIK | ||||||
Coiled coil | 1009-1050 | |||||
Sequence: LKNLAQQQYKSTEQLEARLRQDRELLERLARQYSVQVEEIES | ||||||
Coiled coil | 1312-1343 | |||||
Sequence: TFVEFEMELNQERDRLQKLANQYSVNVVEIEE | ||||||
Coiled coil | 1613-1641 | |||||
Sequence: KQQRWTIEELELRLNNDQKHLQDAVAQYH | ||||||
Region | 1984-2188 | Disordered | ||||
Sequence: IFSKDRGDQPPHTYDESFVEGDEPGLEGETARPRPPNPAPIVSTPKPPLPYSRGGPSGGFEYRRQDYTFNVPVGSASASASGGPTGSSASASASLGKWNRASGDEPLQQEVDLGQQQQIEELGWNEKLEDLGQQTQVEDTDWNQQAEDLGQQQQVQVEDDLHFDQTQGHSSSSNSRSQPLQQATKVEVEATSEPSFWEKLKEKLG | ||||||
Compositional bias | 1988-2012 | Basic and acidic residues | ||||
Sequence: DRGDQPPHTYDESFVEGDEPGLEGE | ||||||
Motif | 1989-1991 | Cell attachment site | ||||
Sequence: RGD | ||||||
Compositional bias | 2014-2035 | Pro residues | ||||
Sequence: ARPRPPNPAPIVSTPKPPLPYS | ||||||
Compositional bias | 2053-2080 | Polar residues | ||||
Sequence: NVPVGSASASASGGPTGSSASASASLGK | ||||||
Compositional bias | 2112-2172 | Polar residues | ||||
Sequence: EDLGQQTQVEDTDWNQQAEDLGQQQQVQVEDDLHFDQTQGHSSSSNSRSQPLQQATKVEVE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length2,188
- Mass (Da)257,446
- Last updated2001-03-01 v2
- ChecksumFFD4715696C33E9E
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
X2JDD7 | X2JDD7_DROME | Tig | 2188 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 7 | in Ref. 1; AAA56998 | ||||
Sequence: I → V | ||||||
Sequence conflict | 77 | in Ref. 1; AAA56998 | ||||
Sequence: A → G | ||||||
Sequence conflict | 381 | in Ref. 1; AAA56998 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 869 | in Ref. 1; AAA56998 | ||||
Sequence: N → S | ||||||
Compositional bias | 1988-2012 | Basic and acidic residues | ||||
Sequence: DRGDQPPHTYDESFVEGDEPGLEGE | ||||||
Compositional bias | 2014-2035 | Pro residues | ||||
Sequence: ARPRPPNPAPIVSTPKPPLPYS | ||||||
Compositional bias | 2053-2080 | Polar residues | ||||
Sequence: NVPVGSASASASGGPTGSSASASASLGK | ||||||
Compositional bias | 2112-2172 | Polar residues | ||||
Sequence: EDLGQQTQVEDTDWNQQAEDLGQQQQVQVEDDLHFDQTQGHSSSSNSRSQPLQQATKVEVE | ||||||
Sequence conflict | 2157-2158 | in Ref. 1; AAA56998 | ||||
Sequence: Missing | ||||||
Sequence conflict | 2185 | in Ref. 1; AAA56998 | ||||
Sequence: E → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U09506 EMBL· GenBank· DDBJ | AAA56998.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014134 EMBL· GenBank· DDBJ | AAF52380.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT010260 EMBL· GenBank· DDBJ | AAQ23578.1 EMBL· GenBank· DDBJ | mRNA | Frameshift |