Q9NB04 · PATJ_DROME
- ProteinPatj homolog
- GenePatj
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids871 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in cell polarity establishment. Probably participates in the assembly, positioning and maintenance of adherens junctions via its interaction with the SAC complex.
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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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePatj homolog
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9NB04
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Membrane-associated. Localizes to the subapical domain of cells. Sdt is required for its localization. At mitotic cycles 13 and 14, during cellularization, it localizes at the leading edge of the invaginating membranes. It is then exclusively localized to the basal area of columnal epithelial cells. In the germline, it localizes at the membrane of the nurse cells during early and mid oogenesis. Later, it is found in the nuclear membrane in close association with actin filaments that connect the nuclei of the nurse cells with the plasma membrane.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000094591 | 1-871 | Patj homolog | |||
Sequence: MHLSADISSALQQIEAVKKGIDESDDPKLQMQTAESLSTILGILQDPVFRTIVHVQDSLSELNAQLAQHPSMLPNDFDIDVAGNLVLSLNGGEVMYDFDEQRSSSHSHSAPGSPDKSGGVGEEPRPQSQNSKGAGVADLYATDYAQIQAIELVNDGTGLGFGIIGARNSGVIVKTILPGGVADKDGRLRSGDHILQIGDVNLHEMVSEQVAAVLRQSGTHVRLVVARPVEQSVPTPQYALEPGTAVVPTRVLVDPAELERYLISTGYPEIFGESSTASTPQTTTEDDRFVYRGETSMLIDPNIDLEELLALPETEKLQVELKKDANGLGITIAGYVCEKEELSGIFVKSVSPGSAADLSGRIRVNDRIIEVDGQSLQGYSNHQAVELLKKSGQVVNLRLERYLRGPKFEQLQQAIAANDKLPSSAPGTPSRAPMPTPVATTSSATTTPSRSITRELEEEALPAPEAFMTTPPSVTTMTTTTLSSFGAGKQLVAVRDSLDGSTKIIPTEVVPLADKTEAKNSGVITRHKYYTDPELSDDAETEIIRKWQKIVGSDVEVIVAQIKKFAVGGLGISLEGTVDVEGGREVRPHHYIRSILPDGPVGVNGVLRSGDELLEVNGERLLGMNHLEVVAILKELPLDVRMVCGRNRNSSLLPFSDDTLKKLSNNFENLLPATDRLVKAKSDGSLATAGSVADGDSVAAAAASFSKLKSRSLEPLTGLAMWSSQPQIIELVKGDRGLGFSILDYQDPLDPNDTLIVIRSLVPGGVAQLDGRLIPGDRLLFVNSINLENASLDQAVQALKGASKGVVRIGVAKPLPMTDNSLKACSNASTTSEETLDAQPSPPALPTVAPPAMPPSASMGAEPDLIPDWRN | ||||||
Modified residue | 682 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in primary and some secondary epithelial cells such as ectodermal cells, salivary glands, foregut, hindgut and invaginating tracheal cells. Also expressed in specific cells of the peripheral nervous system. Expressed in the germline.
Developmental stage
Expressed both maternally and zygotically. Appears in mitotic cycle 11 when the furrows made by the imprint of the embryonic nuclei become apparent.
Gene expression databases
Interaction
Subunit
Component of the SAC complex, a complex composed of crb, Patj and sdt. Interacts directly with nrx via its third and fourth PDZ domains. Interacts directly with par-6, possibly mediating a link between the SAC complex and the par-6 complex, which is composed of par-6, baz and aPKC.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NB04 | aPKC A1Z9X0 | 2 | EBI-442573, EBI-160861 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-67 | L27 | ||||
Sequence: LSADISSALQQIEAVKKGIDESDDPKLQMQTAESLSTILGILQDPVFRTIVHVQDSLSELNAQLA | ||||||
Region | 100-134 | Disordered | ||||
Sequence: EQRSSSHSHSAPGSPDKSGGVGEEPRPQSQNSKGA | ||||||
Domain | 149-229 | PDZ 1 | ||||
Sequence: AIELVNDGTGLGFGIIGARNSGVIVKTILPGGVADKDGRLRSGDHILQIGDVNLHEMVSEQVAAVLRQSGTHVRLVVARPV | ||||||
Domain | 318-403 | PDZ 2 | ||||
Sequence: QVELKKDANGLGITIAGYVCEKEELSGIFVKSVSPGSAADLSGRIRVNDRIIEVDGQSLQGYSNHQAVELLKKSGQVVNLRLERYL | ||||||
Region | 420-453 | Disordered | ||||
Sequence: KLPSSAPGTPSRAPMPTPVATTSSATTTPSRSIT | ||||||
Compositional bias | 434-451 | Polar residues | ||||
Sequence: MPTPVATTSSATTTPSRS | ||||||
Domain | 559-648 | PDZ 3 | ||||
Sequence: VAQIKKFAVGGLGISLEGTVDVEGGREVRPHHYIRSILPDGPVGVNGVLRSGDELLEVNGERLLGMNHLEVVAILKELPLDVRMVCGRNR | ||||||
Domain | 728-814 | PDZ 4 | ||||
Sequence: IIELVKGDRGLGFSILDYQDPLDPNDTLIVIRSLVPGGVAQLDGRLIPGDRLLFVNSINLENASLDQAVQALKGASKGVVRIGVAKP | ||||||
Compositional bias | 822-838 | Polar residues | ||||
Sequence: LKACSNASTTSEETLDA | ||||||
Region | 822-871 | Disordered | ||||
Sequence: LKACSNASTTSEETLDAQPSPPALPTVAPPAMPPSASMGAEPDLIPDWRN | ||||||
Compositional bias | 843-857 | Pro residues | ||||
Sequence: PALPTVAPPAMPPSA |
Sequence similarities
Belongs to the Patj family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length871
- Mass (Da)92,852
- Last updated2004-02-16 v2
- ChecksumCE41E80AA2925B4D
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A4V1B2 | A4V1B2_DROME | Patj | 871 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 349 | in Ref. 3; AAF81829 | ||||
Sequence: S → N | ||||||
Sequence conflict | 359 | in Ref. 3; AAF81829 | ||||
Sequence: S → N | ||||||
Compositional bias | 434-451 | Polar residues | ||||
Sequence: MPTPVATTSSATTTPSRS | ||||||
Compositional bias | 822-838 | Polar residues | ||||
Sequence: LKACSNASTTSEETLDA | ||||||
Compositional bias | 843-857 | Pro residues | ||||
Sequence: PALPTVAPPAMPPSA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF103942 EMBL· GenBank· DDBJ | AAD43031.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AF274350 EMBL· GenBank· DDBJ | AAF81829.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014296 EMBL· GenBank· DDBJ | AAN11498.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF132193 EMBL· GenBank· DDBJ | AAD34781.1 EMBL· GenBank· DDBJ | mRNA |