NETB_DROME
ID NETB_DROME Reviewed; 793 AA.
AC Q24568; Q9VY23;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Netrin-B;
DE Flags: Precursor;
GN Name=NetB; ORFNames=CG10521;
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].
RC TISSUE=Embryo;
RX PubMed=8780645; DOI=10.1016/s0896-6273(00)80153-1;
RA Mitchell K.J., Doyle J.L., Serafini T., Kennedy T., Tessier-Lavigne M.,
RA Goodman C.S., Dickson B.J.;
RT "Genetic analysis of netrin genes in Drosophila: netrins guide CNS
RT commissural axons and peripheral motor axons.";
RL Neuron 17:203-215(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8780646; DOI=10.1016/s0896-6273(00)80154-3;
RA Harris R., Moore-Sabatelli L., Seeger M.;
RT "Guidance cues at the Drosophila CNS midline: identification and
RT characterization of two Drosophila Netrin/UNC-6 homologs.";
RL Neuron 17:217-228(1996).
RN [3]
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 [4]
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 [5]
RP INTERACTION WITH FRA AND UNC-5.
RX PubMed=11719202; DOI=10.1016/s0896-6273(01)00505-0;
RA Keleman K., Dickson B.J.;
RT "Short- and long-range repulsion by the Drosophila Unc5 netrin receptor.";
RL Neuron 32:605-617(2001).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29513217; DOI=10.7554/elife.33962;
RA Peng J., Santiago I.J., Ahn C., Gur B., Tsui C.K., Su Z., Xu C.,
RA Karakhanyan A., Silies M., Pecot M.Y.;
RT "Fezf coordinates laminar-specific connectivity through cell-intrinsic and
RT cell-extrinsic mechanisms.";
RL Elife 7:0-0(2018).
CC -!- FUNCTION: Netrins control guidance of CNS commissural axons and
CC peripheral motor axons (PubMed:8780645, PubMed:8780646,
CC PubMed:11719202). Its association with either fra or unc-5 receptors
CC will lead to axon attraction or repulsion, respectively
CC (PubMed:11719202). While short-range repulsion requires both fra and
CC unc-5 receptors, long-range repulsion only requires unc-5
CC (PubMed:11719202). {ECO:0000269|PubMed:11719202,
CC ECO:0000269|PubMed:8780645, ECO:0000269|PubMed:8780646}.
CC -!- SUBUNIT: Binds to unc-5 and fra receptors.
CC {ECO:0000269|PubMed:11719202}.
CC -!- INTERACTION:
CC Q24568; Q94538: fra; NbExp=2; IntAct=EBI-3406532, EBI-6895101;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000305}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:29513217}. Note=Expressed in the perinuclear region
CC of the oldest most anterior lamina neurons at 24 hours after puparium
CC formation. {ECO:0000269|PubMed:29513217}.
CC -!- TISSUE SPECIFICITY: At 24 hr after puparium formation (APF), detected
CC in the most anterior (oldest) L3, L4 and L5 lamina neurons (at protein
CC level) (PubMed:29513217). At 48 hr APF, expressed in all L3, L4 and L5
CC neurons with slightly higher expression in the L3 neurons (at protein
CC level) (PubMed:29513217). At the midline of developing CNS and in
CC different subsets of neurons, muscles, and epidermal patches
CC (PubMed:8780645, PubMed:8780646). {ECO:0000269|PubMed:29513217,
CC ECO:0000269|PubMed:8780645, ECO:0000269|PubMed:8780646}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
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DR EMBL; U60317; AAB17534.1; -; mRNA.
DR EMBL; U63737; AAB17548.1; -; mRNA.
DR EMBL; AE014298; AAF48382.1; -; Genomic_DNA.
DR RefSeq; NP_001162753.1; NM_001169282.1.
DR RefSeq; NP_001162754.1; NM_001169283.2.
DR RefSeq; NP_001162755.1; NM_001169284.2.
DR RefSeq; NP_001245668.1; NM_001258739.2.
DR RefSeq; NP_001245669.1; NM_001258740.2.
DR RefSeq; NP_511155.1; NM_078600.4.
DR AlphaFoldDB; Q24568; -.
DR SMR; Q24568; -.
DR BioGRID; 58761; 6.
DR IntAct; Q24568; 890.
DR STRING; 7227.FBpp0291228; -.
DR GlyGen; Q24568; 4 sites.
DR PaxDb; Q24568; -.
DR PRIDE; Q24568; -.
DR EnsemblMetazoa; FBtr0073940; FBpp0073757; FBgn0015774.
DR EnsemblMetazoa; FBtr0302016; FBpp0291226; FBgn0015774.
DR EnsemblMetazoa; FBtr0302017; FBpp0291227; FBgn0015774.
DR EnsemblMetazoa; FBtr0302018; FBpp0291228; FBgn0015774.
DR EnsemblMetazoa; FBtr0304874; FBpp0293414; FBgn0015774.
DR EnsemblMetazoa; FBtr0304875; FBpp0293415; FBgn0015774.
DR GeneID; 32400; -.
DR KEGG; dme:Dmel_CG10521; -.
DR CTD; 32400; -.
DR FlyBase; FBgn0015774; NetB.
DR VEuPathDB; VectorBase:FBgn0015774; -.
DR eggNOG; KOG3512; Eukaryota.
DR GeneTree; ENSGT00940000153882; -.
DR InParanoid; Q24568; -.
DR OMA; YFSQFSM; -.
DR OrthoDB; 858946at2759; -.
DR PhylomeDB; Q24568; -.
DR SignaLink; Q24568; -.
DR BioGRID-ORCS; 32400; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32400; -.
DR PRO; PR:Q24568; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0015774; Expressed in brain and 51 other tissues.
DR ExpressionAtlas; Q24568; baseline and differential.
DR Genevisible; Q24568; DM.
DR GO; GO:0044295; C:axonal growth cone; IMP:UniProtKB.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0031012; C:extracellular matrix; ISS:FlyBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IGI:FlyBase.
DR GO; GO:0048749; P:compound eye development; IMP:UniProtKB.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0070983; P:dendrite guidance; IGI:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:2000289; P:regulation of photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:0007432; P:salivary gland boundary specification; IMP:FlyBase.
DR GO; GO:0016200; P:synaptic target attraction; TAS:FlyBase.
DR GO; GO:0008039; P:synaptic target recognition; IMP:FlyBase.
DR GO; GO:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 3.
DR Gene3D; 2.40.50.120; -; 1.
DR InterPro; IPR008211; Laminin_N.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR Pfam; PF00053; Laminin_EGF; 3.
DR Pfam; PF00055; Laminin_N; 1.
DR Pfam; PF01759; NTR; 1.
DR SMART; SM00643; C345C; 1.
DR SMART; SM00180; EGF_Lam; 3.
DR SMART; SM00136; LamNT; 1.
DR SUPFAM; SSF50242; SSF50242; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01248; EGF_LAM_1; 3.
DR PROSITE; PS50027; EGF_LAM_2; 3.
DR PROSITE; PS51117; LAMININ_NTER; 1.
DR PROSITE; PS50189; NTR; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Disulfide bond; Extracellular matrix; Glycoprotein;
KW Laminin EGF-like domain; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..793
FT /note="Netrin-B"
FT /id="PRO_0000017089"
FT DOMAIN 39..303
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 405..497
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 498..560
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 561..610
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 649..792
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 332..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..347
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 746
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 405..414
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 407..461
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 463..472
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 475..495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 498..507
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 500..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 528..537
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 540..558
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 561..573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 563..580
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 582..591
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 594..608
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DISULFID 649..738
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 652..740
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT DISULFID 665..792
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
SQ SEQUENCE 793 AA; 87134 MW; 7F6CEAD3B09B79F4 CRC64;
MVRATGTRMG LLLPIILALA IGSSAAGISS NDPCYFEGKP RKCLPSFVNA AYGNPVQASS
VCGAQQPERY CELLRDGNAG ECRSCEQQRY GPAALTDLNN PSNVTCWRSG AVNVPHDPDS
APPDNVTLTL SLGKKYELTY ISLSFCPRSP RPDSLAIFKS SDFGQTWQPF QFYSSQCQKF
YGRPDRAKIS KFNEQEARCI NSQHDTGGAA QRFAFNTLEG RPSANDLDSS LVLQDWVTAT
DIRVVFHRLE LPPQLLKVKN ANAFSDEMGG SREEDEDDDA DLELDGEQDE YDYNLQDNDS
ADAGYDEYEE PKKHLELDDD HLHLDYASDG ESVVKRQGKH KGSAYEKHYQ SKLAATTPPQ
QPPKVTPPGK VTPPSTAAPS AAASAVTLPI SQHYAVSDFA VGGRCKCNGH ASECVATVSS
GSGTALSDQD DGQDEDTPSA PSLANHFGRS TQMSAKLTMT CACKHNTAGP ECERCKPFYF
DRPWGRATDN DANECKMCQC NGHARRCRFN LELYKLSGRV SGGVCYNCQH DTTGRYCHYC
REGYYRDATK PPNHRKVCKR CDCHPVGSTG KTCNHLSGQC PCKEGVTGLT CNRCARGYQQ
TRSHVAPCIK VPTNANMIQA ESAGGGGGGG TGDYKDGGGS QVEEMKKYCG KCKASPKKLN
LNKFCMEDYA ILAKVIGHDR ASQDISTEKF SIERQNEIYK YEINIQTIFK RNPMSGTTSS
LLGRGNMMLL VPRKSIECQC PKIKLNKSYL ILGRDSEAAP GYLAIGPSSV VLEWKDEWSL
RMKRFQRRAR KCS
