NRT_DROME
ID NRT_DROME Reviewed; 846 AA.
AC P23654; A4V209; Q9V3F0;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Neurotactin;
GN Name=Nrt; ORFNames=CG9704;
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, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=2100266; DOI=10.1242/dev.110.4.1327;
RA Hortsch M., Patel N.P., Bieber A.J., Traquina Z.R., Goodman C.S.;
RT "Drosophila neurotactin, a surface glycoprotein with homology to serine
RT esterases, is dynamically expressed during embryogenesis.";
RL Development 110:1327-1340(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Oregon-R; TISSUE=Embryo;
RX PubMed=2120047;
RA de la Escalera S., Bockamp E.O., Moya F., Piovant M., Jimenez F.;
RT "Characterization and gene cloning of neurotactin, a Drosophila
RT transmembrane protein related to cholinesterases.";
RL EMBO J. 9:3593-3601(1990).
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=10731138; DOI=10.1126/science.287.5461.2222;
RA Rubin G.M., Hong L., Brokstein P., Evans-Holm M., Frise E., Stapleton M.,
RA Harvey D.A.;
RT "A Drosophila complementary DNA resource.";
RL Science 287:2222-2224(2000).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=2120048; DOI=10.1002/j.1460-2075.1990.tb07571.x;
RA Barthalay Y., Hipeau-Jacquotte R., de la Escalera S., Jimenez F.,
RA Piovant M.;
RT "Drosophila neurotactin mediates heterophilic cell adhesion.";
RL EMBO J. 9:3603-3609(1990).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42; SER-44; THR-47; SER-48;
RP SER-52; SER-77; SER-203; THR-206; SER-256; THR-259; SER-263 AND THR-269,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: May mediate or modulate cell adhesion between embryonic cells
CC during development. {ECO:0000269|PubMed:2100266,
CC ECO:0000269|PubMed:2120047, ECO:0000269|PubMed:2120048}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:2100266,
CC ECO:0000269|PubMed:2120047}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:2100266, ECO:0000269|PubMed:2120047}.
CC Note=Expressed in membranes during embryogenesis.
CC -!- TISSUE SPECIFICITY: Late in embryogenesis, expression is restricted to
CC cells of the peripheral and central nervous system undergoing
CC proliferation and differentiation. Also expressed in larval CNS,
CC mesoderm and imaginal disks. {ECO:0000269|PubMed:2100266,
CC ECO:0000269|PubMed:2120047, ECO:0000269|PubMed:2120048}.
CC -!- DEVELOPMENTAL STAGE: Expressed during embryogenesis and larvae.
CC {ECO:0000269|PubMed:2100266, ECO:0000269|PubMed:2120048}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the type-B
CC carboxylesterase/lipase family. {ECO:0000305}.
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DR EMBL; X54999; CAA38746.1; -; mRNA.
DR EMBL; X53837; CAA37831.1; -; mRNA.
DR EMBL; AE014296; AAF49416.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF49417.1; -; Genomic_DNA.
DR EMBL; AF132188; AAD34776.1; -; mRNA.
DR PIR; S12005; S12005.
DR PIR; S13795; S13795.
DR RefSeq; NP_001189121.1; NM_001202192.2.
DR RefSeq; NP_476798.1; NM_057450.5.
DR RefSeq; NP_730196.1; NM_168682.3.
DR AlphaFoldDB; P23654; -.
DR SMR; P23654; -.
DR BioGRID; 65172; 17.
DR IntAct; P23654; 1.
DR STRING; 7227.FBpp0075081; -.
DR ESTHER; drome-nrtac; Neurotactin.
DR GlyGen; P23654; 6 sites.
DR iPTMnet; P23654; -.
DR PaxDb; P23654; -.
DR PRIDE; P23654; -.
DR DNASU; 39873; -.
DR EnsemblMetazoa; FBtr0075322; FBpp0075081; FBgn0004108.
DR EnsemblMetazoa; FBtr0075323; FBpp0075082; FBgn0004108.
DR EnsemblMetazoa; FBtr0304018; FBpp0292987; FBgn0004108.
DR GeneID; 39873; -.
DR KEGG; dme:Dmel_CG9704; -.
DR CTD; 39873; -.
DR FlyBase; FBgn0004108; Nrt.
DR VEuPathDB; VectorBase:FBgn0004108; -.
DR eggNOG; KOG1516; Eukaryota.
DR HOGENOM; CLU_006586_6_0_1; -.
DR InParanoid; P23654; -.
DR OMA; WLHFPVD; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; P23654; -.
DR Reactome; R-DME-112311; Neurotransmitter clearance.
DR Reactome; R-DME-1483191; Synthesis of PC.
DR Reactome; R-DME-2022377; Metabolism of Angiotensinogen to Angiotensins.
DR Reactome; R-DME-211945; Phase I - Functionalization of compounds.
DR Reactome; R-DME-8964038; LDL clearance.
DR Reactome; R-DME-9749641; Aspirin ADME.
DR SignaLink; P23654; -.
DR BioGRID-ORCS; 39873; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39873; -.
DR PRO; PR:P23654; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0004108; Expressed in second segment of antenna (Drosophila) and 59 other tissues.
DR ExpressionAtlas; P23654; baseline and differential.
DR Genevisible; P23654; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0004895; F:cell adhesion receptor activity; IDA:FlyBase.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007413; P:axonal fasciculation; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0007417; P:central nervous system development; IGI:FlyBase.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IPI:FlyBase.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Disulfide bond; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..846
FT /note="Neurotactin"
FT /id="PRO_0000070297"
FT TOPO_DOM 1..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..346
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..846
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 28
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 42
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 75
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 103
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 169
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 186
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 206
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 269
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 417
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 422..437
FT /evidence="ECO:0000250"
FT DISULFID 600..605
FT /evidence="ECO:0000250"
FT DISULFID 738..830
FT /evidence="ECO:0000250"
FT CONFLICT 250
FT /note="G -> S (in Ref. 2; CAA37831)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="T -> S (in Ref. 1; CAA38746)"
FT /evidence="ECO:0000305"
FT CONFLICT 567
FT /note="Y -> F (in Ref. 1; CAA38746)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 846 AA; 92776 MW; DA7AA9CC058C8300 CRC64;
MGELEEKETP PTETTAAQQE ALEEPKETDK MLDKKEDAKE KTPSPQTSKP ASPNAGKKSS
PVAEKKIDDA ELAKSKSGNG EEIIDIPAEN GTKPDSADDK KISKEEREVK PKKIPIGGLK
LPGFFMKNKP KADGDGAEGE LLEKEKEEDK DKEANGDAAT GSGKDEQKSR PGLGERLRSF
FARKPSAEKE KKQLVNGDAD AKSEATAEAT PAEDASDAPP KRGLLNAIKL PIANMIPKKK
SNDDVELGLG KAGLASMETL DDSLKDQDTV DRAPVKTNGT EELKGELKDE KLAAEEKLAA
EEEEQNRPVS LLTRLRGYKC SVDDALIVFG ILLFVLLLGV IGYVLTHETL TSPPLREGRY
IMAVTGCGPV EGVKEDGAFA FRGIPYAKPP VDRLRWKPAE LIDDINMCWN DTLQTHNSSV
VCTQRLGNGT TVGDEDCLYL DVVTPHVRYN NPLPVVVLIG AESLAGPSPG ILRPSARYSR
SHDVIFVRPN FRLGVFGFLA LDALTKEAHP PTSGNYALTD IIAVLNWIKL NIVHFGGDPQ
SVTLLGHRAG ATLVTLLVNS QKVKGLYTRA WASSGSAILP GKPLSESGKQ NEQLMATLEC
ADIQCLREAS SERLWAATPD TWLHFPVDLP QPQEANASGS RHEWLVLDGD VVFEHPSDTW
KREQANDKPV LVMGATAHEA HTEKLRELHA NWTREEVRAY LENSQIGALG LTDEVIEKYN
ASSYASLVSI ISDIRSVCPL LTNARQQPSV PFYVVTQGEG PDQLATVDAD VQAILGRYEP
HTVEQRRFVS AMQQLFYYYV SHGTVQSFVQ NRRVINVGQD AQPEEDYLPC NYWISKDIVP
RYARVD
