NRX4_DROME
ID NRX4_DROME Reviewed; 1284 AA.
AC Q94887; Q9VTU5;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Neurexin-4;
DE AltName: Full=Neurexin IV;
DE Flags: Precursor;
GN Name=Nrx-IV; Synonyms=Nrx; ORFNames=CG6827;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Canton-S;
RX PubMed=8978610; DOI=10.1016/s0092-8674(00)81800-0;
RA Baumgartner S.W., Littleton J.T., Broadie K., Bhat M.A., Harbecke R.,
RA Lengyel J.A., Chiquet-Ehrismann R., Prokop A., Bellen H.J.;
RT "A Drosophila neurexin is required for septate junction and blood-nerve
RT barrier formation and function.";
RL Cell 87:1059-1068(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP INTERACTION WITH CORACLE.
RX PubMed=9508778; DOI=10.1083/jcb.140.6.1463;
RA Ward R.E. IV, Lamb R.S., Fehon R.G.;
RT "A conserved functional domain of Drosophila coracle is required for
RT localization at the septate junction and has membrane-organizing
RT activity.";
RL J. Cell Biol. 140:1463-1473(1998).
RN [5]
RP INTERACTION WITH PATJ.
RX PubMed=10102271; DOI=10.1016/s0092-8674(00)80593-0;
RA Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.;
RT "Discs Lost, a novel multi-PDZ domain protein, establishes and maintains
RT epithelial polarity.";
RL Cell 96:833-845(1999).
RN [6]
RP ERRATUM OF PUBMED:10102271.
RA Bhat M.A., Izaddoost S., Lu Y., Cho K.-O., Choi K.-W., Bellen H.J.;
RL Cell 115:765-766(2003).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH NRX AND CONT.
RX PubMed=15459097; DOI=10.1242/dev.01372;
RA Faivre-Sarrailh C., Banerjee S., Li J., Hortsch M., Laval M., Bhat M.A.;
RT "Drosophila contactin, a homolog of vertebrate contactin, is required for
RT septate junction organization and paracellular barrier function.";
RL Development 131:4931-4942(2004).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1137, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
CC -!- FUNCTION: Seems to play a role in the formation and function of septate
CC junctions. Septate junctions, which are the equivalent of vertebrates
CC tight junctions, are characterized by regular arrays of transverse
CC structures that span the intermembrane space and form a physical
CC barrier to diffusion. Required for the blood-brain barrier formation.
CC {ECO:0000269|PubMed:8978610}.
CC -!- SUBUNIT: The C-terminal region interacts with coracle. Interacts with
CC Patj in cis form. Forms a complex with Nrg and Cont.
CC {ECO:0000269|PubMed:10102271, ECO:0000269|PubMed:15459097,
CC ECO:0000269|PubMed:9508778}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Cell junction, septate junction.
CC -!- TISSUE SPECIFICITY: Found in septate junctions of epithelial and glial
CC cells. {ECO:0000269|PubMed:8978610}.
CC -!- SIMILARITY: Belongs to the neurexin family. {ECO:0000305}.
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DR EMBL; X86685; CAA60383.1; -; mRNA.
DR EMBL; AE014296; AAF49951.1; -; Genomic_DNA.
DR PIR; T13799; T13799.
DR RefSeq; NP_524034.2; NM_079310.3.
DR AlphaFoldDB; Q94887; -.
DR SMR; Q94887; -.
DR BioGRID; 64741; 15.
DR IntAct; Q94887; 30.
DR STRING; 7227.FBpp0075730; -.
DR GlyGen; Q94887; 8 sites.
DR iPTMnet; Q94887; -.
DR PaxDb; Q94887; -.
DR PRIDE; Q94887; -.
DR EnsemblMetazoa; FBtr0075998; FBpp0075730; FBgn0013997.
DR GeneID; 39387; -.
DR KEGG; dme:Dmel_CG6827; -.
DR CTD; 39387; -.
DR FlyBase; FBgn0013997; Nrx-IV.
DR VEuPathDB; VectorBase:FBgn0013997; -.
DR eggNOG; KOG3516; Eukaryota.
DR GeneTree; ENSGT00940000170887; -.
DR InParanoid; Q94887; -.
DR OMA; GVEPITH; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; Q94887; -.
DR BioGRID-ORCS; 39387; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39387; -.
DR PRO; PR:Q94887; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0013997; Expressed in wing disc and 29 other tissues.
DR ExpressionAtlas; Q94887; baseline and differential.
DR Genevisible; Q94887; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0005919; C:pleated septate junction; IDA:FlyBase.
DR GO; GO:0048786; C:presynaptic active zone; IDA:BHF-UCL.
DR GO; GO:0045202; C:synapse; IDA:FlyBase.
DR GO; GO:0008366; P:axon ensheathment; IMP:FlyBase.
DR GO; GO:0061343; P:cell adhesion involved in heart morphogenesis; IMP:FlyBase.
DR GO; GO:0045216; P:cell-cell junction organization; TAS:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:FlyBase.
DR GO; GO:0003015; P:heart process; IMP:FlyBase.
DR GO; GO:0021682; P:nerve maturation; IMP:FlyBase.
DR GO; GO:0097105; P:presynaptic membrane assembly; IMP:BHF-UCL.
DR GO; GO:0008104; P:protein localization; TAS:FlyBase.
DR GO; GO:0035151; P:regulation of tube size, open tracheal system; IMP:FlyBase.
DR GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
DR GO; GO:0008039; P:synaptic target recognition; IMP:FlyBase.
DR GO; GO:0072553; P:terminal button organization; IMP:BHF-UCL.
DR CDD; cd00057; FA58C; 1.
DR CDD; cd00110; LamG; 4.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR003585; Neurexin-like.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF02210; Laminin_G_2; 4.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00231; FA58C; 1.
DR SMART; SM00282; LamG; 4.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49899; SSF49899; 4.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01285; FA58C_1; 1.
DR PROSITE; PS01286; FA58C_2; 1.
DR PROSITE; PS50022; FA58C_3; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..35
FT /evidence="ECO:0000255"
FT CHAIN 36..1284
FT /note="Neurexin-4"
FT /id="PRO_0000019512"
FT TOPO_DOM 36..1217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1218..1238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1239..1284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..185
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 220..369
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 403..540
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 542..579
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 824..962
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 962..999
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1032..1183
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 340
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 974
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1047
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT DISULFID 47..185
FT /evidence="ECO:0000250"
FT DISULFID 333..369
FT /evidence="ECO:0000250"
FT DISULFID 507..540
FT /evidence="ECO:0000250"
FT DISULFID 546..557
FT /evidence="ECO:0000250"
FT DISULFID 551..566
FT /evidence="ECO:0000250"
FT DISULFID 568..578
FT /evidence="ECO:0000250"
FT DISULFID 934..962
FT /evidence="ECO:0000250"
FT DISULFID 966..977
FT /evidence="ECO:0000250"
FT DISULFID 971..986
FT /evidence="ECO:0000250"
FT DISULFID 988..998
FT /evidence="ECO:0000250"
FT DISULFID 1147..1183
FT /evidence="ECO:0000250"
FT CONFLICT 1..4
FT /note="MRPP -> MSA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 926
FT /note="E -> D (in Ref. 1; CAA60383)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1284 AA; 145468 MW; 9372C71AC70E3D56 CRC64;
MRPPRSNTKA AFSSLQFGLL CLLLLVNNGI KSVQADAFTD YFSDYDCNQP LMERAVLTAT
SSLTERGPDK ARLNGNAAWT PVENTYNHFL TLDLGDPRMV RKIATMGRMH TDEFVTEYIV
QYSDDGEFWR SYVNPTSEPQ MFKGNSDGNS IHYNVFEVPI IAQWVRINPT RWHDRISMRV
ELYGCDYISE NLYFNGTGLV RYDLRREPIT STKESIRFRF KTAFANGVMM YSRGTQGDYY
ALQLKDNKMV LNLDLGSRVM TSLSVGSLLD DNVWHDVVIS RNQRDIIFSV DRVIVRGRIQ
GEFTRLNLNR ELYLGGVPNV QEGLIVQQNF SGCLENIYFN STNFIRVMKD STELGEGYLF
TRVNTIYACP SPPIYPVTFT TRSSFVRLKG YENSQRLNVS FYFRTYEETG VMLHHDFYSG
GYLKVFLEFG KVKIDLKVKD KARIILDNYD DQFNDGKWHS FVISIEKNRL ILNIDQRPMT
TTKSMQVATG AQYYIAGGKD KNGFVGCMRL ISVDGNYKLP QDWVKGEEVC CGDDVVVDAC
QMIDRCNPNP CQHKGLCHQN SREFFCDCGH TGYAGAVCHT SNNPLSCLAL KNVQHVQQRV
NLNLDVDGSG PLEPFPVTCE FYSDGRVITT LSHSQEHTTT VDGFQEPGSF EQSIMYDANQ
LQIEALLNRS HSCWQRLSYS CRSSRLFNSP SEAGNFRPFS WWISRHNQPM DYWAGALPGS
RKCECGILGK CHDPTKWCNC DSNSLEWMED GGDIREKEYL PVRAVKFGDT GTPLDEKMGR
YTLGPLRCEG DDLFSNVVTF RIADASINLP PFDMGHSGDI YLEFRTTQEN SVIFHATGPT
DYIKLSLNGG NKLQFQYQAG SGPLGVNVGT SYHLNDNNWH TVSVERNRKE ARLVVDGSIK
AEVREPPGPV RALHLTSDLV IGATTEYRDG YVGCIRALLL NGKMVDLKEY SKRGLYGIST
GCVGRCESNP CLNNGTCIER YDGYSCDCRW SAFKGPICAD EIGVNLRSSS IIRYEFEGSF
RSTIAENIRV GFTTTIPKGF LLGFSSNLTG EYLTIQISNS GHLRCVFDFG FERQEIIFPK
KHFGLGQYHD MHFMRKNGGS TVVLKVDNYE PVEYNFDIKA SADAQFNNIQ YMYIGKNESM
TDGFVGCVSR VQFDDIYPLK LMFQQNPPKN VKSLGTQLTE DFCGVEPVTH PPIEIETRPP
PLVDEEKLRK AYNEVDSVLL ACLLVILFLL LILMFFLIGR YLHRHKGDYL THEDQGADGA
DDPDDAVLHS TTGHQVRKRT EIFI
