Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Neuroglian

Gene

Nrg

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The long isoform may play a role in neural and glial cell adhesion in the developing embryo. The short isoform may be a more general cell adhesion molecule involved in other tissues and imaginal disk morphogenesis. Vital for embryonic development. Essential for 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 - Molecular functioni

  • calcium ion binding Source: FlyBase

GO - Biological processi

  • axon ensheathment Source: FlyBase
  • axon extension Source: FlyBase
  • axonogenesis Source: FlyBase
  • cell adhesion involved in heart morphogenesis Source: FlyBase
  • central complex development Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • epidermal growth factor receptor signaling pathway Source: FlyBase
  • establishment of glial blood-brain barrier Source: FlyBase
  • female courtship behavior Source: FlyBase
  • imaginal disc morphogenesis Source: UniProtKB
  • male courtship behavior Source: FlyBase
  • melanotic encapsulation of foreign target Source: FlyBase
  • motor neuron axon guidance Source: FlyBase
  • mushroom body development Source: FlyBase
  • nerve maturation Source: FlyBase
  • neuron cell-cell adhesion Source: UniProtKB
  • neuron projection morphogenesis Source: FlyBase
  • photoreceptor cell axon guidance Source: FlyBase
  • regulation of female receptivity Source: FlyBase
  • regulation of tube size, open tracheal system Source: FlyBase
  • septate junction assembly Source: FlyBase
  • synapse organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-DME-210991. Basigin interactions.
R-DME-373760. L1CAM interactions.
R-DME-437239. Recycling pathway of L1.
R-DME-445095. Interaction between L1 and Ankyrins.
R-DME-445144. Signal transduction by L1.
R-DME-447043. Neurofascin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroglian
Gene namesi
Name:Nrg
ORF Names:CG1634
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0264975. Nrg.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 11381115ExtracellularSequence analysisAdd
BLAST
Transmembranei1139 – 115416HelicalSequence analysisAdd
BLAST
Topological domaini1155 – 1302148CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • bicellular tight junction Source: UniProtKB-SubCell
  • filopodium Source: FlyBase
  • integral component of membrane Source: UniProtKB-KW
  • lateral plasma membrane Source: FlyBase
  • plasma membrane Source: UniProtKB
  • pleated septate junction Source: FlyBase
  • septate junction Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Tight junction

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 13021279NeuroglianPRO_0000015055Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi59 ↔ 111PROSITE-ProRule annotation
Disulfide bondi155 ↔ 212By similarity
Glycosylationi182 – 1821N-linked (GlcNAc...)Sequence analysis
Glycosylationi198 – 1981N-linked (GlcNAc...)1 Publication
Disulfide bondi268 ↔ 317By similarity
Disulfide bondi360 ↔ 410By similarity
Glycosylationi411 – 4111N-linked (GlcNAc...)2 Publications
Glycosylationi414 – 4141N-linked (GlcNAc...); atypical1 Publication
Glycosylationi448 – 4481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi625 ↔ 706PROSITE-ProRule annotation1 Publication
Glycosylationi652 – 6521N-linked (GlcNAc...)1 Publication
Glycosylationi683 – 6831N-linked (GlcNAc...)1 Publication
Glycosylationi821 – 8211N-linked (GlcNAc...)Sequence analysis
Glycosylationi1125 – 11251N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP20241.

PTM databases

iPTMnetiP20241.

Expressioni

Tissue specificityi

Long isoform is restricted to surface of neurons and glia in the developing nervous system and the short isoform to other non-neuronal tissues.1 Publication

Gene expression databases

BgeeiP20241.
ExpressionAtlasiP20241. differential.
GenevisibleiP20241. DM.

Interactioni

Subunit structurei

Forms a complex with Nrx and Cont.1 Publication

Protein-protein interaction databases

BioGridi58251. 6 interactions.
DIPiDIP-22412N.
IntActiP20241. 79 interactions.
MINTiMINT-1694518.
STRINGi7227.FBpp0297081.

Structurei

Secondary structure

1
1302
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi619 – 6257Combined sources
Beta strandi627 – 6359Combined sources
Beta strandi646 – 65611Combined sources
Beta strandi661 – 6688Combined sources
Beta strandi672 – 6776Combined sources
Beta strandi680 – 69213Combined sources
Beta strandi706 – 7083Combined sources
Beta strandi721 – 7233Combined sources
Beta strandi730 – 7334Combined sources
Helixi739 – 7413Combined sources
Beta strandi744 – 7463Combined sources
Beta strandi748 – 75710Combined sources
Beta strandi763 – 7675Combined sources
Beta strandi774 – 7774Combined sources
Beta strandi785 – 79410Combined sources
Beta strandi806 – 8127Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CFBX-ray2.00A610-814[»]
ProteinModelPortaliP20241.
SMRiP20241. Positions 16-1005, 1037-1114.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP20241.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 133105Ig-like C2-type 1Add
BLAST
Domaini134 – 22592Ig-like C2-type 2Add
BLAST
Domaini245 – 33086Ig-like C2-type 3Add
BLAST
Domaini339 – 42688Ig-like C2-type 4Add
BLAST
Domaini432 – 52493Ig-like C2-type 5Add
BLAST
Domaini521 – 61090Ig-like C2-type 6Add
BLAST
Domaini614 – 71198Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini716 – 81398Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini818 – 91598Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini916 – 1017102Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini1021 – 111999Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 5 fibronectin type-III domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3513. Eukaryota.
ENOG410XSVG. LUCA.
GeneTreeiENSGT00760000118840.
InParanoidiP20241.
PhylomeDBiP20241.

Family and domain databases

Gene3Di2.60.40.10. 11 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR026966. Neurofascin/L1/NrCAM_C.
[Graphical view]
PfamiPF13882. Bravo_FIGEY. 1 hit.
PF00041. fn3. 3 hits.
PF07679. I-set. 2 hits.
PF00047. ig. 2 hits.
[Graphical view]
SMARTiSM00060. FN3. 5 hits.
SM00409. IG. 6 hits.
SM00408. IGc2. 6 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 6 hits.
SSF49265. SSF49265. 3 hits.
PROSITEiPS50853. FN3. 5 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B (identifier: P20241-1) [UniParc]FASTAAdd to basket

Also known as: 180 kDa form

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MWRQSTILAA LLVALLCAGS AESKGNRPPR ITKQPAPGEL LFKVAQQNKE
60 70 80 90 100
SDNPFIIECE ADGQPEPEYS WIKNGKKFDW QAYDNRMLRQ PGRGTLVITI
110 120 130 140 150
PKDEDRGHYQ CFASNEFGTA TSNSVYVRKA ELNAFKDEAA KTLEAVEGEP
160 170 180 190 200
FMLKCAAPDG FPSPTVNWMI QESIDGSIKS INNSRMTLDP EGNLWFSNVT
210 220 230 240 250
REDASSDFYY ACSATSVFRS EYKIGNKVLL DVKQMGVSAS QNKHPPVRQY
260 270 280 290 300
VSRRQSLALR GKRMELFCIY GGTPLPQTVW SKDGQRIQWS DRITQGHYGK
310 320 330 340 350
SLVIRQTNFD DAGTYTCDVS NGVGNAQSFS IILNVNSVPY FTKEPEIATA
360 370 380 390 400
AEDEEVVFEC RAAGVPEPKI SWIHNGKPIE QSTPNPRRTV TDNTIRIINL
410 420 430 440 450
VKGDTGNYGC NATNSLGYVY KDVYLNVQAE PPTISEAPAA VSTVDGRNVT
460 470 480 490 500
IKCRVNGSPK PLVKWLRASN WLTGGRYNVQ ANGDLEIQDV TFSDAGKYTC
510 520 530 540 550
YAQNKFGEIQ ADGSLVVKEH TRITQEPQNY EVAAGQSATF RCNEAHDDTL
560 570 580 590 600
EIEIDWWKDG QSIDFEAQPR FVKTNDNSLT IAKTMELDSG EYTCVARTRL
610 620 630 640 650
DEATARANLI VQDVPNAPKL TGITCQADKA EIHWEQQGDN RSPILHYTIQ
660 670 680 690 700
FNTSFTPASW DAAYEKVPNT DSSFVVQMSP WANYTFRVIA FNKIGASPPS
710 720 730 740 750
AHSDSCTTQP DVPFKNPDNV VGQGTEPNNL VISWTPMPEI EHNAPNFHYY
760 770 780 790 800
VSWKRDIPAA AWENNNIFDW RQNNIVIADQ PTFVKYLIKV VAINDRGESN
810 820 830 840 850
VAAEEVVGYS GEDRPLDAPT NFTMRQITSS TSGYMAWTPV SEESVRGHFK
860 870 880 890 900
GYKIQTWTEN EGEEGLREIH VKGDTHNALV TQFKPDSKNY ARILAYNGRF
910 920 930 940 950
NGPPSAVIDF DTPEGVPSPV QGLDAYPLGS SAFMLHWKKP LYPNGKLTGY
960 970 980 990 1000
KIYYEEVKES YVGERREYDP HITDPRVTRM KMAGLKPNSK YRISITATTK
1010 1020 1030 1040 1050
MGEGSEHYIE KTTLKDAVNV APATPSFSWE QLPSDNGLAK FRINWLPSTE
1060 1070 1080 1090 1100
GHPGTHFFTM HRIKGETQWI RENEEKNSDY QEVGGLDPET AYEFRVVSVD
1110 1120 1130 1140 1150
GHFNTESATQ EIDTNTVEGP IMVANETVAN AGWFIGMMLA LAFIIILFII
1160 1170 1180 1190 1200
ICIIRRNRGG KYDVHDRELA NGRRDYPEEG GFHEYSQPLD NKSAGRQSVS
1210 1220 1230 1240 1250
SANKPGVESD TDSMAEYGDG DTGQFTEDGS FIGQYVPGKL QPPVSPQPLN
1260 1270 1280 1290 1300
NSAAAHQAAP TAGGSGAAGS AAAAGASGGA SSAGGAAASN GGAAAGAVAT

YV
Length:1,302
Mass (Da):143,618
Last modified:June 1, 2001 - v2
Checksum:i59BD9DF286756F1A
GO
Isoform A (identifier: P20241-2) [UniParc]FASTAAdd to basket

Also known as: C, 167 kDa form

The sequence of this isoform differs from the canonical sequence as follows:
     1224-1239: QFTEDGSFIGQYVPGK → MNEDGSFIGQYGRKGL
     1240-1302: Missing.

Show »
Length:1,239
Mass (Da):138,362
Checksum:i49E12282D0D7F27D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 862NR → KP in AAC28613 (PubMed:9666073).Curated
Sequence conflicti85 – 862NR → KP in AAC28614 (PubMed:9666073).Curated
Sequence conflicti1232 – 12321Missing in ABE01201 (Ref. 7) Curated
Sequence conflicti1282 – 12821Missing in CAA53823 (PubMed:1693086).Curated
Sequence conflicti1299 – 12991A → V in ABE01201 (Ref. 7) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1224 – 123916QFTED…YVPGK → MNEDGSFIGQYGRKGL in isoform A. 3 PublicationsVSP_002601Add
BLAST
Alternative sequencei1240 – 130263Missing in isoform A. 3 PublicationsVSP_002602Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28231 mRNA. Translation: AAA28728.2.
AF050085, AF050084 Genomic DNA. Translation: AAC28613.2.
AF050085, AF050084 Genomic DNA. Translation: AAC28614.2.
AE014298 Genomic DNA. Translation: AAF46387.1.
AE014298 Genomic DNA. Translation: AAN09236.1.
AE014298 Genomic DNA. Translation: AAS65287.1.
AY058284 mRNA. Translation: AAL13513.1.
BT024971 mRNA. Translation: ABE01201.1.
X76243 mRNA. Translation: CAA53822.1.
X76244 mRNA. Translation: CAA53823.1.
PIRiA32579.
RefSeqiNP_001162704.1. NM_001169233.2. [P20241-2]
NP_001162705.1. NM_001169234.3. [P20241-1]
NP_001162706.1. NM_001169235.1. [P20241-2]
NP_001259336.1. NM_001272407.2. [P20241-2]
NP_001259337.1. NM_001272408.1. [P20241-1]
NP_511090.1. NM_078535.3. [P20241-2]
NP_727274.1. NM_167160.2. [P20241-1]
NP_996380.1. NM_206657.4. [P20241-2]
UniGeneiDm.3700.

Genome annotation databases

EnsemblMetazoaiFBtr0071208; FBpp0071155; FBgn0264975. [P20241-1]
FBtr0301763; FBpp0290977; FBgn0264975. [P20241-1]
FBtr0333523; FBpp0305703; FBgn0264975. [P20241-1]
GeneIDi31792.
KEGGidme:Dmel_CG1634.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28231 mRNA. Translation: AAA28728.2.
AF050085, AF050084 Genomic DNA. Translation: AAC28613.2.
AF050085, AF050084 Genomic DNA. Translation: AAC28614.2.
AE014298 Genomic DNA. Translation: AAF46387.1.
AE014298 Genomic DNA. Translation: AAN09236.1.
AE014298 Genomic DNA. Translation: AAS65287.1.
AY058284 mRNA. Translation: AAL13513.1.
BT024971 mRNA. Translation: ABE01201.1.
X76243 mRNA. Translation: CAA53822.1.
X76244 mRNA. Translation: CAA53823.1.
PIRiA32579.
RefSeqiNP_001162704.1. NM_001169233.2. [P20241-2]
NP_001162705.1. NM_001169234.3. [P20241-1]
NP_001162706.1. NM_001169235.1. [P20241-2]
NP_001259336.1. NM_001272407.2. [P20241-2]
NP_001259337.1. NM_001272408.1. [P20241-1]
NP_511090.1. NM_078535.3. [P20241-2]
NP_727274.1. NM_167160.2. [P20241-1]
NP_996380.1. NM_206657.4. [P20241-2]
UniGeneiDm.3700.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CFBX-ray2.00A610-814[»]
ProteinModelPortaliP20241.
SMRiP20241. Positions 16-1005, 1037-1114.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58251. 6 interactions.
DIPiDIP-22412N.
IntActiP20241. 79 interactions.
MINTiMINT-1694518.
STRINGi7227.FBpp0297081.

PTM databases

iPTMnetiP20241.

Proteomic databases

PaxDbiP20241.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0071208; FBpp0071155; FBgn0264975. [P20241-1]
FBtr0301763; FBpp0290977; FBgn0264975. [P20241-1]
FBtr0333523; FBpp0305703; FBgn0264975. [P20241-1]
GeneIDi31792.
KEGGidme:Dmel_CG1634.

Organism-specific databases

CTDi31792.
FlyBaseiFBgn0264975. Nrg.

Phylogenomic databases

eggNOGiKOG3513. Eukaryota.
ENOG410XSVG. LUCA.
GeneTreeiENSGT00760000118840.
InParanoidiP20241.
PhylomeDBiP20241.

Enzyme and pathway databases

ReactomeiR-DME-210991. Basigin interactions.
R-DME-373760. L1CAM interactions.
R-DME-437239. Recycling pathway of L1.
R-DME-445095. Interaction between L1 and Ankyrins.
R-DME-445144. Signal transduction by L1.
R-DME-447043. Neurofascin interactions.

Miscellaneous databases

ChiTaRSiNrg. fly.
EvolutionaryTraceiP20241.
GenomeRNAii31792.
PROiP20241.

Gene expression databases

BgeeiP20241.
ExpressionAtlasiP20241. differential.
GenevisibleiP20241. DM.

Family and domain databases

Gene3Di2.60.40.10. 11 hits.
InterProiIPR003961. FN3_dom.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR026966. Neurofascin/L1/NrCAM_C.
[Graphical view]
PfamiPF13882. Bravo_FIGEY. 1 hit.
PF00041. fn3. 3 hits.
PF07679. I-set. 2 hits.
PF00047. ig. 2 hits.
[Graphical view]
SMARTiSM00060. FN3. 5 hits.
SM00409. IG. 6 hits.
SM00408. IGc2. 6 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 6 hits.
SSF49265. SSF49265. 3 hits.
PROSITEiPS50853. FN3. 5 hits.
PS50835. IG_LIKE. 6 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drosophila neuroglian: a member of the immunoglobulin superfamily with extensive homology to the vertebrate neural adhesion molecule L1."
    Bieber A.J., Snow P.M., Hortsch M., Patel N.H., Jacobs J.R., Traquina Z.R., Schilling J., Goodman C.S.
    Cell 59:447-460(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 24-41 AND 737-751.
  2. "The analysis of genomic structures in the L1 family of cell adhesion molecules provides no evidence for exon shuffling events after the separation of arthropod and chordate lineages."
    Zhao G., Hortsch M.
    Gene 215:47-55(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS A AND B).
  3. Hortsch M.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. "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.
  5. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Head.
  7. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1088-1302.
    Strain: Berkeley.
  8. "Differential splicing generates a nervous system-specific form of Drosophila neuroglian."
    Hortsch M., Bieber A.J., Patel N.H., Goodman C.S.
    Neuron 4:697-709(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1182-1302 (ISOFORMS A AND B), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Embryo.
  9. "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 NRG AND CONT.
  10. "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-198 AND ASN-411, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Oregon-R.
    Tissue: Head.
  11. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-411 AND ASN-414, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "Crystal structure of tandem type III fibronectin domains from Drosophila neuroglian at 2.0 A."
    Huber A.H., Wang Y.-M.E., Bieber A.J., Bjorkman P.J.
    Neuron 12:717-731(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 610-814, DISULFIDE BONDS, GLYCOSYLATION AT ASN-652 AND ASN-683.

Entry informationi

Entry nameiNRG_DROME
AccessioniPrimary (citable) accession number: P20241
Secondary accession number(s): A4V452
, O61541, O61542, Q1WWD5, Q24414, Q24415, Q95U64, Q9V3X0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 184 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.