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Q94887

- NRX4_DROME

UniProt

Q94887 - NRX4_DROME

Protein

Neurexin-4

Gene

Nrx-IV

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (05 Dec 2001)
      Previous versions | rss
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    Functioni

    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.1 Publication

    GO - Biological processi

    1. axon ensheathment Source: FlyBase
    2. cell adhesion involved in heart morphogenesis Source: FlyBase
    3. cell-cell junction organization Source: FlyBase
    4. dorsal closure Source: FlyBase
    5. establishment of glial blood-brain barrier Source: FlyBase
    6. establishment or maintenance of cell polarity Source: FlyBase
    7. heart process Source: FlyBase
    8. nerve maturation Source: FlyBase
    9. presynaptic membrane assembly Source: BHF-UCL
    10. protein localization Source: FlyBase
    11. regulation of tube size, open tracheal system Source: FlyBase
    12. septate junction assembly Source: FlyBase
    13. synaptic target recognition Source: FlyBase
    14. synaptic vesicle docking involved in exocytosis Source: FlyBase
    15. synaptic vesicle targeting Source: FlyBase
    16. terminal button organization Source: BHF-UCL

    Keywords - Biological processi

    Cell adhesion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Neurexin-4
    Alternative name(s):
    Neurexin IV
    Gene namesi
    Name:Nrx-IV
    Synonyms:Nrx
    ORF Names:CG6827
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0013997. Nrx-IV.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: FlyBase
    2. plasma membrane Source: FlyBase
    3. pleated septate junction Source: FlyBase
    4. presynaptic active zone Source: BHF-UCL
    5. septate junction Source: FlyBase

    Keywords - Cellular componenti

    Cell junction, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535Sequence AnalysisAdd
    BLAST
    Chaini36 – 12841249Neurexin-4PRO_0000019512Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi47 ↔ 185By similarity
    Glycosylationi195 – 1951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi333 ↔ 369By similarity
    Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi507 ↔ 540By similarity
    Disulfide bondi546 ↔ 557By similarity
    Disulfide bondi551 ↔ 566By similarity
    Disulfide bondi568 ↔ 578By similarity
    Glycosylationi668 – 6681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi934 ↔ 962By similarity
    Disulfide bondi966 ↔ 977By similarity
    Disulfide bondi971 ↔ 986By similarity
    Glycosylationi974 – 9741N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi988 ↔ 998By similarity
    Glycosylationi1047 – 10471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1137 – 11371N-linked (GlcNAc...)1 Publication
    Disulfide bondi1147 ↔ 1183By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ94887.
    PRIDEiQ94887.

    Expressioni

    Tissue specificityi

    Found in septate junctions of epithelial and glial cells.1 Publication

    Gene expression databases

    BgeeiQ94887.

    Interactioni

    Subunit structurei

    The C-terminal region interacts with coracle. Interacts with Patj in cis form. Forms a complex with Nrg and Cont.3 Publications

    Protein-protein interaction databases

    BioGridi64741. 5 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ94887.
    SMRiQ94887. Positions 61-586, 724-751, 775-1154.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini36 – 12171182ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1239 – 128446CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1218 – 123821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini47 – 185139F5/8 type CPROSITE-ProRule annotationAdd
    BLAST
    Domaini220 – 369150Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini403 – 540138Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini542 – 57938EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini824 – 962139Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini962 – 99938EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1032 – 1183152Laminin G-like 4PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the neurexin family.Curated
    Contains 2 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 F5/8 type C domain.PROSITE-ProRule annotation
    Contains 4 laminin G-like domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG291100.
    GeneTreeiENSGT00750000117263.
    InParanoidiQ94887.
    OMAiIDRCMPN.
    OrthoDBiEOG7GXP9N.
    PhylomeDBiQ94887.

    Family and domain databases

    Gene3Di2.60.120.200. 4 hits.
    2.60.120.260. 1 hit.
    InterProiIPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR008979. Galactose-bd-like.
    IPR001791. Laminin_G.
    IPR003585. Neurexin-like.
    [Graphical view]
    PfamiPF00754. F5_F8_type_C. 1 hit.
    PF02210. Laminin_G_2. 4 hits.
    [Graphical view]
    SMARTiSM00294. 4.1m. 1 hit.
    SM00181. EGF. 2 hits.
    SM00231. FA58C. 1 hit.
    SM00282. LamG. 4 hits.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 5 hits.
    PROSITEiPS50026. EGF_3. 2 hits.
    PS01285. FA58C_1. 1 hit.
    PS01286. FA58C_2. 1 hit.
    PS50022. FA58C_3. 1 hit.
    PS50025. LAM_G_DOMAIN. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q94887-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRPPRSNTKA AFSSLQFGLL CLLLLVNNGI KSVQADAFTD YFSDYDCNQP     50
    LMERAVLTAT SSLTERGPDK ARLNGNAAWT PVENTYNHFL TLDLGDPRMV 100
    RKIATMGRMH TDEFVTEYIV QYSDDGEFWR SYVNPTSEPQ MFKGNSDGNS 150
    IHYNVFEVPI IAQWVRINPT RWHDRISMRV ELYGCDYISE NLYFNGTGLV 200
    RYDLRREPIT STKESIRFRF KTAFANGVMM YSRGTQGDYY ALQLKDNKMV 250
    LNLDLGSRVM TSLSVGSLLD DNVWHDVVIS RNQRDIIFSV DRVIVRGRIQ 300
    GEFTRLNLNR ELYLGGVPNV QEGLIVQQNF SGCLENIYFN STNFIRVMKD 350
    STELGEGYLF TRVNTIYACP SPPIYPVTFT TRSSFVRLKG YENSQRLNVS 400
    FYFRTYEETG VMLHHDFYSG GYLKVFLEFG KVKIDLKVKD KARIILDNYD 450
    DQFNDGKWHS FVISIEKNRL ILNIDQRPMT TTKSMQVATG AQYYIAGGKD 500
    KNGFVGCMRL ISVDGNYKLP QDWVKGEEVC CGDDVVVDAC QMIDRCNPNP 550
    CQHKGLCHQN SREFFCDCGH TGYAGAVCHT SNNPLSCLAL KNVQHVQQRV 600
    NLNLDVDGSG PLEPFPVTCE FYSDGRVITT LSHSQEHTTT VDGFQEPGSF 650
    EQSIMYDANQ LQIEALLNRS HSCWQRLSYS CRSSRLFNSP SEAGNFRPFS 700
    WWISRHNQPM DYWAGALPGS RKCECGILGK CHDPTKWCNC DSNSLEWMED 750
    GGDIREKEYL PVRAVKFGDT GTPLDEKMGR YTLGPLRCEG DDLFSNVVTF 800
    RIADASINLP PFDMGHSGDI YLEFRTTQEN SVIFHATGPT DYIKLSLNGG 850
    NKLQFQYQAG SGPLGVNVGT SYHLNDNNWH TVSVERNRKE ARLVVDGSIK 900
    AEVREPPGPV RALHLTSDLV IGATTEYRDG YVGCIRALLL NGKMVDLKEY 950
    SKRGLYGIST GCVGRCESNP CLNNGTCIER YDGYSCDCRW SAFKGPICAD 1000
    EIGVNLRSSS IIRYEFEGSF RSTIAENIRV GFTTTIPKGF LLGFSSNLTG 1050
    EYLTIQISNS GHLRCVFDFG FERQEIIFPK KHFGLGQYHD MHFMRKNGGS 1100
    TVVLKVDNYE PVEYNFDIKA SADAQFNNIQ YMYIGKNESM TDGFVGCVSR 1150
    VQFDDIYPLK LMFQQNPPKN VKSLGTQLTE DFCGVEPVTH PPIEIETRPP 1200
    PLVDEEKLRK AYNEVDSVLL ACLLVILFLL LILMFFLIGR YLHRHKGDYL 1250
    THEDQGADGA DDPDDAVLHS TTGHQVRKRT EIFI 1284
    Length:1,284
    Mass (Da):145,468
    Last modified:December 5, 2001 - v2
    Checksum:i9372C71AC70E3D56
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 44MRPP → MSA(PubMed:8978610)Curated
    Sequence conflicti926 – 9261E → D in CAA60383. (PubMed:8978610)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X86685 mRNA. Translation: CAA60383.1.
    AE014296 Genomic DNA. Translation: AAF49951.1.
    PIRiT13799.
    RefSeqiNP_524034.2. NM_079310.3.
    UniGeneiDm.1843.

    Genome annotation databases

    EnsemblMetazoaiFBtr0075998; FBpp0075730; FBgn0013997.
    GeneIDi39387.
    KEGGidme:Dmel_CG6827.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X86685 mRNA. Translation: CAA60383.1 .
    AE014296 Genomic DNA. Translation: AAF49951.1 .
    PIRi T13799.
    RefSeqi NP_524034.2. NM_079310.3.
    UniGenei Dm.1843.

    3D structure databases

    ProteinModelPortali Q94887.
    SMRi Q94887. Positions 61-586, 724-751, 775-1154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 64741. 5 interactions.

    Proteomic databases

    PaxDbi Q94887.
    PRIDEi Q94887.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0075998 ; FBpp0075730 ; FBgn0013997 .
    GeneIDi 39387.
    KEGGi dme:Dmel_CG6827.

    Organism-specific databases

    CTDi 39387.
    FlyBasei FBgn0013997. Nrx-IV.

    Phylogenomic databases

    eggNOGi NOG291100.
    GeneTreei ENSGT00750000117263.
    InParanoidi Q94887.
    OMAi IDRCMPN.
    OrthoDBi EOG7GXP9N.
    PhylomeDBi Q94887.

    Miscellaneous databases

    GenomeRNAii 39387.
    NextBioi 813387.
    PROi Q94887.

    Gene expression databases

    Bgeei Q94887.

    Family and domain databases

    Gene3Di 2.60.120.200. 4 hits.
    2.60.120.260. 1 hit.
    InterProi IPR000421. Coagulation_fac_5/8-C_type_dom.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR000742. EG-like_dom.
    IPR008979. Galactose-bd-like.
    IPR001791. Laminin_G.
    IPR003585. Neurexin-like.
    [Graphical view ]
    Pfami PF00754. F5_F8_type_C. 1 hit.
    PF02210. Laminin_G_2. 4 hits.
    [Graphical view ]
    SMARTi SM00294. 4.1m. 1 hit.
    SM00181. EGF. 2 hits.
    SM00231. FA58C. 1 hit.
    SM00282. LamG. 4 hits.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 5 hits.
    PROSITEi PS50026. EGF_3. 2 hits.
    PS01285. FA58C_1. 1 hit.
    PS01286. FA58C_2. 1 hit.
    PS50022. FA58C_3. 1 hit.
    PS50025. LAM_G_DOMAIN. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A Drosophila neurexin is required for septate junction and blood-nerve barrier formation and function."
      Baumgartner S.W., Littleton J.T., Broadie K., Bhat M.A., Harbecke R., Lengyel J.A., Chiquet-Ehrismann R., Prokop A., Bellen H.J.
      Cell 87:1059-1068(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Strain: Canton-S.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. "A conserved functional domain of Drosophila coracle is required for localization at the septate junction and has membrane-organizing activity."
      Ward R.E. IV, Lamb R.S., Fehon R.G.
      J. Cell Biol. 140:1463-1473(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CORACLE.
    5. "Discs Lost, a novel multi-PDZ domain protein, establishes and maintains epithelial polarity."
      Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.
      Cell 96:833-845(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PATJ.
    6. Erratum
      Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.
      Cell 115:765-766(2003)
    7. "Drosophila contactin, a homolog of vertebrate contactin, is required for septate junction organization and paracellular barrier function."
      Faivre-Sarrailh C., Banerjee S., Li J., Hortsch M., Laval M., Bhat M.A.
      Development 131:4931-4942(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH NRX AND CONT.
    8. "Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster."
      Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V.
      Glycobiology 17:1388-1403(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1137, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Oregon-R.
      Tissue: Head.

    Entry informationi

    Entry nameiNRX4_DROME
    AccessioniPrimary (citable) accession number: Q94887
    Secondary accession number(s): Q9VTU5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 5, 2001
    Last sequence update: December 5, 2001
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3