Q94887 · NRX4_DROME
- ProteinNeurexin-4
- GeneNrx-IV
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1284 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Seems to play a role in the formation and function of septate junctions. Septate junctions, which are the equivalent of vertebrates tight junctions, are characterized by regular arrays of transverse structures that span the intermembrane space and form a physical barrier to diffusion. Required for the blood-brain barrier formation.
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 | plasma membrane | |
Cellular Component | pleated septate junction | |
Cellular Component | presynaptic active zone | |
Cellular Component | synapse | |
Biological Process | axon ensheathment | |
Biological Process | cell adhesion involved in heart morphogenesis | |
Biological Process | cell-cell junction organization | |
Biological Process | dorsal closure | |
Biological Process | establishment of glial blood-brain barrier | |
Biological Process | heart process | |
Biological Process | nerve maturation | |
Biological Process | presynaptic membrane assembly | |
Biological Process | protein localization | |
Biological Process | regulation of tube size, open tracheal system | |
Biological Process | septate junction assembly | |
Biological Process | synaptic target recognition | |
Biological Process | terminal button organization |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameNeurexin-4
- 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 accessionQ94887
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 36-1217 | Extracellular | ||||
Sequence: DAFTDYFSDYDCNQPLMERAVLTATSSLTERGPDKARLNGNAAWTPVENTYNHFLTLDLGDPRMVRKIATMGRMHTDEFVTEYIVQYSDDGEFWRSYVNPTSEPQMFKGNSDGNSIHYNVFEVPIIAQWVRINPTRWHDRISMRVELYGCDYISENLYFNGTGLVRYDLRREPITSTKESIRFRFKTAFANGVMMYSRGTQGDYYALQLKDNKMVLNLDLGSRVMTSLSVGSLLDDNVWHDVVISRNQRDIIFSVDRVIVRGRIQGEFTRLNLNRELYLGGVPNVQEGLIVQQNFSGCLENIYFNSTNFIRVMKDSTELGEGYLFTRVNTIYACPSPPIYPVTFTTRSSFVRLKGYENSQRLNVSFYFRTYEETGVMLHHDFYSGGYLKVFLEFGKVKIDLKVKDKARIILDNYDDQFNDGKWHSFVISIEKNRLILNIDQRPMTTTKSMQVATGAQYYIAGGKDKNGFVGCMRLISVDGNYKLPQDWVKGEEVCCGDDVVVDACQMIDRCNPNPCQHKGLCHQNSREFFCDCGHTGYAGAVCHTSNNPLSCLALKNVQHVQQRVNLNLDVDGSGPLEPFPVTCEFYSDGRVITTLSHSQEHTTTVDGFQEPGSFEQSIMYDANQLQIEALLNRSHSCWQRLSYSCRSSRLFNSPSEAGNFRPFSWWISRHNQPMDYWAGALPGSRKCECGILGKCHDPTKWCNCDSNSLEWMEDGGDIREKEYLPVRAVKFGDTGTPLDEKMGRYTLGPLRCEGDDLFSNVVTFRIADASINLPPFDMGHSGDIYLEFRTTQENSVIFHATGPTDYIKLSLNGGNKLQFQYQAGSGPLGVNVGTSYHLNDNNWHTVSVERNRKEARLVVDGSIKAEVREPPGPVRALHLTSDLVIGATTEYRDGYVGCIRALLLNGKMVDLKEYSKRGLYGISTGCVGRCESNPCLNNGTCIERYDGYSCDCRWSAFKGPICADEIGVNLRSSSIIRYEFEGSFRSTIAENIRVGFTTTIPKGFLLGFSSNLTGEYLTIQISNSGHLRCVFDFGFERQEIIFPKKHFGLGQYHDMHFMRKNGGSTVVLKVDNYEPVEYNFDIKASADAQFNNIQYMYIGKNESMTDGFVGCVSRVQFDDIYPLKLMFQQNPPKNVKSLGTQLTEDFCGVEPVTHPPIEIETRPPPLVDEEKLRKAYNEVDS | ||||||
Transmembrane | 1218-1238 | Helical | ||||
Sequence: VLLACLLVILFLLLILMFFLI | ||||||
Topological domain | 1239-1284 | Cytoplasmic | ||||
Sequence: GRYLHRHKGDYLTHEDQGADGADDPDDAVLHSTTGHQVRKRTEIFI |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-35 | |||||
Sequence: MRPPRSNTKAAFSSLQFGLLCLLLLVNNGIKSVQA | ||||||
Chain | PRO_0000019512 | 36-1284 | Neurexin-4 | |||
Sequence: DAFTDYFSDYDCNQPLMERAVLTATSSLTERGPDKARLNGNAAWTPVENTYNHFLTLDLGDPRMVRKIATMGRMHTDEFVTEYIVQYSDDGEFWRSYVNPTSEPQMFKGNSDGNSIHYNVFEVPIIAQWVRINPTRWHDRISMRVELYGCDYISENLYFNGTGLVRYDLRREPITSTKESIRFRFKTAFANGVMMYSRGTQGDYYALQLKDNKMVLNLDLGSRVMTSLSVGSLLDDNVWHDVVISRNQRDIIFSVDRVIVRGRIQGEFTRLNLNRELYLGGVPNVQEGLIVQQNFSGCLENIYFNSTNFIRVMKDSTELGEGYLFTRVNTIYACPSPPIYPVTFTTRSSFVRLKGYENSQRLNVSFYFRTYEETGVMLHHDFYSGGYLKVFLEFGKVKIDLKVKDKARIILDNYDDQFNDGKWHSFVISIEKNRLILNIDQRPMTTTKSMQVATGAQYYIAGGKDKNGFVGCMRLISVDGNYKLPQDWVKGEEVCCGDDVVVDACQMIDRCNPNPCQHKGLCHQNSREFFCDCGHTGYAGAVCHTSNNPLSCLALKNVQHVQQRVNLNLDVDGSGPLEPFPVTCEFYSDGRVITTLSHSQEHTTTVDGFQEPGSFEQSIMYDANQLQIEALLNRSHSCWQRLSYSCRSSRLFNSPSEAGNFRPFSWWISRHNQPMDYWAGALPGSRKCECGILGKCHDPTKWCNCDSNSLEWMEDGGDIREKEYLPVRAVKFGDTGTPLDEKMGRYTLGPLRCEGDDLFSNVVTFRIADASINLPPFDMGHSGDIYLEFRTTQENSVIFHATGPTDYIKLSLNGGNKLQFQYQAGSGPLGVNVGTSYHLNDNNWHTVSVERNRKEARLVVDGSIKAEVREPPGPVRALHLTSDLVIGATTEYRDGYVGCIRALLLNGKMVDLKEYSKRGLYGISTGCVGRCESNPCLNNGTCIERYDGYSCDCRWSAFKGPICADEIGVNLRSSSIIRYEFEGSFRSTIAENIRVGFTTTIPKGFLLGFSSNLTGEYLTIQISNSGHLRCVFDFGFERQEIIFPKKHFGLGQYHDMHFMRKNGGSTVVLKVDNYEPVEYNFDIKASADAQFNNIQYMYIGKNESMTDGFVGCVSRVQFDDIYPLKLMFQQNPPKNVKSLGTQLTEDFCGVEPVTHPPIEIETRPPPLVDEEKLRKAYNEVDSVLLACLLVILFLLLILMFFLIGRYLHRHKGDYLTHEDQGADGADDPDDAVLHSTTGHQVRKRTEIFI | ||||||
Disulfide bond | 47↔185 | |||||
Sequence: CNQPLMERAVLTATSSLTERGPDKARLNGNAAWTPVENTYNHFLTLDLGDPRMVRKIATMGRMHTDEFVTEYIVQYSDDGEFWRSYVNPTSEPQMFKGNSDGNSIHYNVFEVPIIAQWVRINPTRWHDRISMRVELYGC | ||||||
Glycosylation | 195 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 329 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 333↔369 | |||||
Sequence: CLENIYFNSTNFIRVMKDSTELGEGYLFTRVNTIYAC | ||||||
Glycosylation | 340 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 398 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 507↔540 | |||||
Sequence: CMRLISVDGNYKLPQDWVKGEEVCCGDDVVVDAC | ||||||
Disulfide bond | 546↔557 | |||||
Sequence: CNPNPCQHKGLC | ||||||
Disulfide bond | 551↔566 | |||||
Sequence: CQHKGLCHQNSREFFC | ||||||
Disulfide bond | 568↔578 | |||||
Sequence: CGHTGYAGAVC | ||||||
Glycosylation | 668 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 934↔962 | |||||
Sequence: CIRALLLNGKMVDLKEYSKRGLYGISTGC | ||||||
Disulfide bond | 966↔977 | |||||
Sequence: CESNPCLNNGTC | ||||||
Disulfide bond | 971↔986 | |||||
Sequence: CLNNGTCIERYDGYSC | ||||||
Glycosylation | 974 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 988↔998 | |||||
Sequence: CRWSAFKGPIC | ||||||
Glycosylation | 1047 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1137 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1147↔1183 | |||||
Sequence: CVSRVQFDDIYPLKLMFQQNPPKNVKSLGTQLTEDFC |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Found in septate junctions of epithelial and glial cells.
Developmental stage
In embryos, expressed in trachea and hindgut (at protein level).
Gene expression databases
Interaction
Subunit
Forms a complex with Nrg and Cont (PubMed:15459097).
Forms a complex composed of septa junction proteins Nrx-IV/Nrx, Tsf2/MTf, Cont and Nrg during late embryogenesis (PubMed:20935638).
The C-terminal region interacts with coracle (PubMed:9508778).
Interacts with Patj in cis form (PubMed:10102271).
Forms a complex composed of septa junction proteins Nrx-IV/Nrx, Tsf2/MTf, Cont and Nrg during late embryogenesis (PubMed:20935638).
The C-terminal region interacts with coracle (PubMed:9508778).
Interacts with Patj in cis form (PubMed:10102271).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 47-185 | F5/8 type C | ||||
Sequence: CNQPLMERAVLTATSSLTERGPDKARLNGNAAWTPVENTYNHFLTLDLGDPRMVRKIATMGRMHTDEFVTEYIVQYSDDGEFWRSYVNPTSEPQMFKGNSDGNSIHYNVFEVPIIAQWVRINPTRWHDRISMRVELYGC | ||||||
Domain | 220-369 | Laminin G-like 1 | ||||
Sequence: FKTAFANGVMMYSRGTQGDYYALQLKDNKMVLNLDLGSRVMTSLSVGSLLDDNVWHDVVISRNQRDIIFSVDRVIVRGRIQGEFTRLNLNRELYLGGVPNVQEGLIVQQNFSGCLENIYFNSTNFIRVMKDSTELGEGYLFTRVNTIYAC | ||||||
Domain | 403-540 | Laminin G-like 2 | ||||
Sequence: FRTYEETGVMLHHDFYSGGYLKVFLEFGKVKIDLKVKDKARIILDNYDDQFNDGKWHSFVISIEKNRLILNIDQRPMTTTKSMQVATGAQYYIAGGKDKNGFVGCMRLISVDGNYKLPQDWVKGEEVCCGDDVVVDAC | ||||||
Domain | 542-579 | EGF-like 1 | ||||
Sequence: MIDRCNPNPCQHKGLCHQNSREFFCDCGHTGYAGAVCH | ||||||
Domain | 824-962 | Laminin G-like 3 | ||||
Sequence: FRTTQENSVIFHATGPTDYIKLSLNGGNKLQFQYQAGSGPLGVNVGTSYHLNDNNWHTVSVERNRKEARLVVDGSIKAEVREPPGPVRALHLTSDLVIGATTEYRDGYVGCIRALLLNGKMVDLKEYSKRGLYGISTGC | ||||||
Domain | 962-999 | EGF-like 2 | ||||
Sequence: CVGRCESNPCLNNGTCIERYDGYSCDCRWSAFKGPICA | ||||||
Domain | 1032-1183 | Laminin G-like 4 | ||||
Sequence: FTTTIPKGFLLGFSSNLTGEYLTIQISNSGHLRCVFDFGFERQEIIFPKKHFGLGQYHDMHFMRKNGGSTVVLKVDNYEPVEYNFDIKASADAQFNNIQYMYIGKNESMTDGFVGCVSRVQFDDIYPLKLMFQQNPPKNVKSLGTQLTEDFC |
Sequence similarities
Belongs to the neurexin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,284
- Mass (Da)145,468
- Last updated2001-12-05 v2
- Checksum9372C71AC70E3D56
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q8IQH0 | Q8IQH0_DROME | Nrx-IV | 1284 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1-4 | in Ref. 1 | ||||
Sequence: MRPP → MSA | ||||||
Sequence conflict | 926 | in Ref. 1; CAA60383 | ||||
Sequence: E → D |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X86685 EMBL· GenBank· DDBJ | CAA60383.1 EMBL· GenBank· DDBJ | mRNA | ||
AE014296 EMBL· GenBank· DDBJ | AAF49951.1 EMBL· GenBank· DDBJ | Genomic DNA |