Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q94887 (NRX4_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurexin-4
Alternative name(s):
Neurexin IV
Gene names
Name:Nrx-IV
Synonyms:Nrx
ORF Names:CG6827
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length1284 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1

Subunit structure

The C-terminal region interacts with coracle. Interacts with Patj in cis form. Forms a complex with Nrg and Cont. Ref.4 Ref.5 Ref.7

Subcellular location

Membrane; Single-pass type I membrane protein Potential. Cell junctionseptate junction.

Tissue specificity

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

Sequence similarities

Belongs to the neurexin family.

Contains 2 EGF-like domains.

Contains 1 F5/8 type C domain.

Contains 4 laminin G-like domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Membrane
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon ensheathment

Inferred from mutant phenotype PubMed 16554482. Source: FlyBase

cell adhesion involved in heart morphogenesis

Inferred from mutant phenotype PubMed 19000835. Source: FlyBase

cell-cell junction organization

Traceable author statement PubMed 12147138. Source: FlyBase

dorsal closure

Inferred from mutant phenotype PubMed 12782681. Source: FlyBase

establishment of glial blood-brain barrier

Inferred from mutant phenotype PubMed 16213218PubMed 18199760. Source: FlyBase

establishment or maintenance of cell polarity

Non-traceable author statement PubMed 12766944. Source: FlyBase

heart process

Inferred from mutant phenotype PubMed 19000835. Source: FlyBase

nerve maturation

Inferred from mutant phenotype PubMed 16554482. Source: FlyBase

presynaptic membrane assembly

Inferred from mutant phenotype PubMed 19896112. Source: BHF-UCL

protein localization

Traceable author statement PubMed 10449347PubMed 12565697. Source: FlyBase

regulation of tube size, open tracheal system

Inferred from mutant phenotype PubMed 12930776. Source: FlyBase

septate junction assembly

Inferred from mutant phenotype PubMed 16554482. Source: FlyBase

synaptic target recognition

Inferred from mutant phenotype PubMed 18817735. Source: FlyBase

synaptic vesicle docking involved in exocytosis

Non-traceable author statement PubMed 10798391. Source: FlyBase

synaptic vesicle targeting

Non-traceable author statement PubMed 10798391. Source: FlyBase

terminal button organization

Inferred from mutant phenotype PubMed 19896112. Source: BHF-UCL

   Cellular_componentintegral component of plasma membrane

Non-traceable author statement PubMed 12147138. Source: FlyBase

plasma membrane

Inferred from direct assay PubMed 19000835PubMed 20462449. Source: FlyBase

pleated septate junction

Inferred from direct assay Ref.7. Source: FlyBase

presynaptic active zone

Inferred from direct assay PubMed 19896112. Source: BHF-UCL

septate junction

Non-traceable author statement PubMed 11700298PubMed 12147138. Source: FlyBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Potential
Chain36 – 12841249Neurexin-4
PRO_0000019512

Regions

Topological domain36 – 12171182Extracellular Potential
Transmembrane1218 – 123821Helical; Potential
Topological domain1239 – 128446Cytoplasmic Potential
Domain47 – 185139F5/8 type C
Domain220 – 369150Laminin G-like 1
Domain403 – 540138Laminin G-like 2
Domain542 – 57938EGF-like 1
Domain824 – 962139Laminin G-like 3
Domain962 – 99938EGF-like 2
Domain1032 – 1183152Laminin G-like 4

Amino acid modifications

Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation3291N-linked (GlcNAc...) Potential
Glycosylation3401N-linked (GlcNAc...) Potential
Glycosylation3981N-linked (GlcNAc...) Potential
Glycosylation6681N-linked (GlcNAc...) Potential
Glycosylation9741N-linked (GlcNAc...) Potential
Glycosylation10471N-linked (GlcNAc...) Potential
Glycosylation11371N-linked (GlcNAc...) Ref.8
Disulfide bond47 ↔ 185 By similarity
Disulfide bond333 ↔ 369 By similarity
Disulfide bond507 ↔ 540 By similarity
Disulfide bond546 ↔ 557 By similarity
Disulfide bond551 ↔ 566 By similarity
Disulfide bond568 ↔ 578 By similarity
Disulfide bond934 ↔ 962 By similarity
Disulfide bond966 ↔ 977 By similarity
Disulfide bond971 ↔ 986 By similarity
Disulfide bond988 ↔ 998 By similarity
Disulfide bond1147 ↔ 1183 By similarity

Experimental info

Sequence conflict1 – 44MRPP → MSA Ref.1
Sequence conflict9261E → D in CAA60383. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q94887 [UniParc].

Last modified December 5, 2001. Version 2.
Checksum: 9372C71AC70E3D56

FASTA1,284145,468
        10         20         30         40         50         60 
MRPPRSNTKA AFSSLQFGLL CLLLLVNNGI KSVQADAFTD YFSDYDCNQP LMERAVLTAT 

        70         80         90        100        110        120 
SSLTERGPDK ARLNGNAAWT PVENTYNHFL TLDLGDPRMV RKIATMGRMH TDEFVTEYIV 

       130        140        150        160        170        180 
QYSDDGEFWR SYVNPTSEPQ MFKGNSDGNS IHYNVFEVPI IAQWVRINPT RWHDRISMRV 

       190        200        210        220        230        240 
ELYGCDYISE NLYFNGTGLV RYDLRREPIT STKESIRFRF KTAFANGVMM YSRGTQGDYY 

       250        260        270        280        290        300 
ALQLKDNKMV LNLDLGSRVM TSLSVGSLLD DNVWHDVVIS RNQRDIIFSV DRVIVRGRIQ 

       310        320        330        340        350        360 
GEFTRLNLNR ELYLGGVPNV QEGLIVQQNF SGCLENIYFN STNFIRVMKD STELGEGYLF 

       370        380        390        400        410        420 
TRVNTIYACP SPPIYPVTFT TRSSFVRLKG YENSQRLNVS FYFRTYEETG VMLHHDFYSG 

       430        440        450        460        470        480 
GYLKVFLEFG KVKIDLKVKD KARIILDNYD DQFNDGKWHS FVISIEKNRL ILNIDQRPMT 

       490        500        510        520        530        540 
TTKSMQVATG AQYYIAGGKD KNGFVGCMRL ISVDGNYKLP QDWVKGEEVC CGDDVVVDAC 

       550        560        570        580        590        600 
QMIDRCNPNP CQHKGLCHQN SREFFCDCGH TGYAGAVCHT SNNPLSCLAL KNVQHVQQRV 

       610        620        630        640        650        660 
NLNLDVDGSG PLEPFPVTCE FYSDGRVITT LSHSQEHTTT VDGFQEPGSF EQSIMYDANQ 

       670        680        690        700        710        720 
LQIEALLNRS HSCWQRLSYS CRSSRLFNSP SEAGNFRPFS WWISRHNQPM DYWAGALPGS 

       730        740        750        760        770        780 
RKCECGILGK CHDPTKWCNC DSNSLEWMED GGDIREKEYL PVRAVKFGDT GTPLDEKMGR 

       790        800        810        820        830        840 
YTLGPLRCEG DDLFSNVVTF RIADASINLP PFDMGHSGDI YLEFRTTQEN SVIFHATGPT 

       850        860        870        880        890        900 
DYIKLSLNGG NKLQFQYQAG SGPLGVNVGT SYHLNDNNWH TVSVERNRKE ARLVVDGSIK 

       910        920        930        940        950        960 
AEVREPPGPV RALHLTSDLV IGATTEYRDG YVGCIRALLL NGKMVDLKEY SKRGLYGIST 

       970        980        990       1000       1010       1020 
GCVGRCESNP CLNNGTCIER YDGYSCDCRW SAFKGPICAD EIGVNLRSSS IIRYEFEGSF 

      1030       1040       1050       1060       1070       1080 
RSTIAENIRV GFTTTIPKGF LLGFSSNLTG EYLTIQISNS GHLRCVFDFG FERQEIIFPK 

      1090       1100       1110       1120       1130       1140 
KHFGLGQYHD MHFMRKNGGS TVVLKVDNYE PVEYNFDIKA SADAQFNNIQ YMYIGKNESM 

      1150       1160       1170       1180       1190       1200 
TDGFVGCVSR VQFDDIYPLK LMFQQNPPKN VKSLGTQLTE DFCGVEPVTH PPIEIETRPP 

      1210       1220       1230       1240       1250       1260 
PLVDEEKLRK AYNEVDSVLL ACLLVILFLL LILMFFLIGR YLHRHKGDYL THEDQGADGA 

      1270       1280 
DDPDDAVLHS TTGHQVRKRT EIFI 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X86685 mRNA. Translation: CAA60383.1.
AE014296 Genomic DNA. Translation: AAF49951.1.
PIRT13799.
RefSeqNP_524034.2. NM_079310.3.
UniGeneDm.1843.

3D structure databases

ProteinModelPortalQ94887.
SMRQ94887. Positions 61-586, 792-1169.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid64741. 5 interactions.

Proteomic databases

PaxDbQ94887.
PRIDEQ94887.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0075998; FBpp0075730; FBgn0013997.
GeneID39387.
KEGGdme:Dmel_CG6827.

Organism-specific databases

CTD39387.
FlyBaseFBgn0013997. Nrx-IV.

Phylogenomic databases

eggNOGNOG291100.
GeneTreeENSGT00750000117263.
InParanoidQ94887.
OMAQKCDEPL.
OrthoDBEOG7GXP9N.
PhylomeDBQ94887.

Gene expression databases

BgeeQ94887.

Family and domain databases

Gene3D2.60.120.200. 4 hits.
2.60.120.260. 1 hit.
InterProIPR000421. 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]
PfamPF00754. F5_F8_type_C. 1 hit.
PF02210. Laminin_G_2. 4 hits.
[Graphical view]
SMARTSM00294. 4.1m. 1 hit.
SM00181. EGF. 2 hits.
SM00231. FA58C. 1 hit.
SM00282. LamG. 4 hits.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 5 hits.
PROSITEPS50026. 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]
ProtoNetSearch...

Other

GenomeRNAi39387.
NextBio813387.
PROQ94887.

Entry information

Entry nameNRX4_DROME
AccessionPrimary (citable) accession number: Q94887
Secondary accession number(s): Q9VTU5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: December 5, 2001
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase