ID NETA_DROME Reviewed; 726 AA.
AC Q24567; Q7JXY0; Q94528; Q9VY25;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 27-MAR-2024, entry version 188.
DE RecName: Full=Netrin-A;
DE Flags: Precursor;
GN Name=NetA; ORFNames=CG18657;
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 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], FUNCTION, AND TISSUE SPECIFICITY.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Netrins control guidance of CNS commissural axons at the
CC midline and peripheral motor axons to their target muscles.
CC {ECO:0000269|PubMed:8780645, ECO:0000269|PubMed:8780646}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- TISSUE SPECIFICITY: At the midline of developing CNS at the time of
CC commissure formation and in different subsets of neurons, muscles, and
CC epidermal patches. {ECO:0000269|PubMed:8780645,
CC ECO:0000269|PubMed:8780646}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL90318.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U60316; AAB17533.1; -; mRNA.
DR EMBL; U63736; AAB17547.1; -; mRNA.
DR EMBL; AE014298; AAF48380.3; -; Genomic_DNA.
DR EMBL; AY089580; AAL90318.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001245667.1; NM_001258738.2.
DR RefSeq; NP_001285243.1; NM_001298314.1.
DR RefSeq; NP_511154.3; NM_078599.5.
DR AlphaFoldDB; Q24567; -.
DR SMR; Q24567; -.
DR BioGRID; 58759; 8.
DR IntAct; Q24567; 42.
DR STRING; 7227.FBpp0311922; -.
DR GlyCosmos; Q24567; 6 sites, No reported glycans.
DR GlyGen; Q24567; 6 sites.
DR PaxDb; 7227-FBpp0073759; -.
DR DNASU; 32398; -.
DR EnsemblMetazoa; FBtr0073942; FBpp0073759; FBgn0015773.
DR EnsemblMetazoa; FBtr0346088; FBpp0311922; FBgn0015773.
DR GeneID; 32398; -.
DR KEGG; dme:Dmel_CG18657; -.
DR AGR; FB:FBgn0015773; -.
DR CTD; 32398; -.
DR FlyBase; FBgn0015773; NetA.
DR VEuPathDB; VectorBase:FBgn0015773; -.
DR eggNOG; KOG3512; Eukaryota.
DR HOGENOM; CLU_018213_2_0_1; -.
DR InParanoid; Q24567; -.
DR OMA; AADCESY; -.
DR OrthoDB; 2916807at2759; -.
DR PhylomeDB; Q24567; -.
DR SignaLink; Q24567; -.
DR BioGRID-ORCS; 32398; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32398; -.
DR PRO; PR:Q24567; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0015773; Expressed in midline glial cell (Drosophila) and 55 other cell types or tissues.
DR ExpressionAtlas; Q24567; baseline and differential.
DR Genevisible; Q24567; DM.
DR GO; GO:0044295; C:axonal growth cone; IMP:UniProtKB.
DR GO; GO:0005604; C:basement membrane; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0031012; C:extracellular matrix; ISS:FlyBase.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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:0009888; P:tissue development; IBA:GO_Central.
DR CDD; cd00055; EGF_Lam; 3.
DR CDD; cd03579; NTR_netrin-1_like; 1.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
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 PANTHER; PTHR10574:SF444; -; 1.
DR PANTHER; PTHR10574; NETRIN/LAMININ-RELATED; 1.
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; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF50242; TIMP-like; 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 2: Evidence at transcript level;
KW Developmental protein; Differentiation; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Laminin EGF-like domain; Neurogenesis;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..726
FT /note="Netrin-A"
FT /id="PRO_0000017088"
FT DOMAIN 46..312
FT /note="Laminin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00466"
FT DOMAIN 313..368
FT /note="Laminin EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 369..431
FT /note="Laminin EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 432..481
FT /note="Laminin EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00460"
FT DOMAIN 533..725
FT /note="NTR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT REGION 490..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 652
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 679
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 313..322
FT /evidence="ECO:0000250"
FT DISULFID 315..332
FT /evidence="ECO:0000250"
FT DISULFID 334..343
FT /evidence="ECO:0000250"
FT DISULFID 346..366
FT /evidence="ECO:0000250"
FT DISULFID 369..378
FT /evidence="ECO:0000250"
FT DISULFID 371..396
FT /evidence="ECO:0000250"
FT DISULFID 399..408
FT /evidence="ECO:0000250"
FT DISULFID 411..429
FT /evidence="ECO:0000250"
FT DISULFID 432..444
FT /evidence="ECO:0000250"
FT DISULFID 434..451
FT /evidence="ECO:0000250"
FT DISULFID 453..462
FT /evidence="ECO:0000250"
FT DISULFID 465..479
FT /evidence="ECO:0000250"
FT DISULFID 533..671
FT /evidence="ECO:0000250"
FT DISULFID 549..725
FT /evidence="ECO:0000250"
FT CONFLICT 22
FT /note="S -> F (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="E -> A (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 514..516
FT /note="GAA -> APP (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 517..532
FT /note="GMAAQSQYYRTEGGRE -> EWPPSLSTIAPRAAGVK (in Ref. 1 and
FT 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="S -> T (in Ref. 1; AAB17533)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 726 AA; 80366 MW; FCDB6372B19E30E5 CRC64;
MIRGILLLLL GTTRFSPIQC ISNDVYFKMF SQQAPPEDPC YNKAHEPRAC IPDFVNAAYD
APVVASSTCG SSGAQRYCEY QDHERSCHTC DMTDPLRSFP ARSLTDLNNS NNVTCWRSEP
VTGSGDNVTL TLSLGKKFEL TYVILQLCPH APRPDSMVIY KSTDHGLSWQ PFQFFSSQCR
RLFGRPARQS TGRHNEHEAR CSDVTRPLVS RIAFSTLEGR PSSRDLDSSP VLQDWVTATD
IRVVFHRLQR PDPQALLSLE AGGATDLASG KYSVPLANGP AGNNIEANLG GDVATSGSGL
HYAISDFSVG GRCKCNGHAS KCSTDASGQL NCECSHNTAG RDCERCKPFH FDRPWARATA
KEANECKECN CNKHARQCRF NMEIFRLSQG VSGGVCQNCR HSTTGRNCHQ CKEGFYRDAT
KPLTHRKVCK ACDCHPIGSS GKICNSTSGQ CPCKDGVTGL TCNRCARGYQ QSRSHIAPCI
KQPPRMINML DTQNTAPEPD EPESSPGSGG DRNGAAGMAA QSQYYRTEGG RECGKCRVST
KRLNLNKFCK RDYAIMAKVI GRDTSSEAVS REVQRRAMDP DVADYEMDQV QPGSARSPIT
GVYEFQAADY PNPNPNPRGS EMERFDLQIQ AVFKRSRPGE SSGAGNVYGM PNTTLKRGPM
TWIIPTKDLE CRCPRIRVNR SYLILGRDSE APPGYLGIGP HSIVIEWKED WYRRMKRFQR
RARTCA
//
