NAAT1_DROME
ID NAAT1_DROME Reviewed; 641 AA.
AC Q9W4C5; Q1AK15; Q8MRC8;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sodium-dependent nutrient amino acid transporter 1;
DE Short=DmNAT1;
GN Name=NAAT1; ORFNames=CG3252;
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 {ECO:0000312|EMBL:AAF46031.2};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=W118; TISSUE=Gastrointestinal tract;
RX PubMed=18718864; DOI=10.1016/j.ibmb.2008.07.005;
RA Miller M.M., Popova L.B., Meleshkevitch E.A., Tran P.V., Boudko D.Y.;
RT "The invertebrate B(0) system transporter, D. melanogaster NAT1, has unique
RT d-amino acid affinity and mediates gut and brain functions.";
RL Insect Biochem. Mol. Biol. 38:923-931(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAF46031.2};
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] {ECO:0000305}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAF46031.2};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM51989.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM51989.1};
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).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-190, AND IDENTIFICATION BY MASS
RP 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: Unusual broad substrate spectrum amino acid:sodium
CC cotransporter that promotes absorption of the D isomers of essential
CC amino acids. Neutral amino acids are the preferred substrates,
CC especially methionine and phenylalanine. {ECO:0000269|PubMed:18718864}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In larvae, weak specific expression in the anterior
CC midgut just proximal to the gastric caeca reproductive rudiments,
CC common ureters of the Malpighian tubules, and distal swollen portion of
CC the anterior pair of Malpighian tubules. Expression is also seen in the
CC imaginal disks of the head; brain hemispheres and the ventral ganglion.
CC Stronger expression in the posterior midgut.
CC {ECO:0000269|PubMed:18718864}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. {ECO:0000305}.
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DR EMBL; DQ073009; AAY56384.1; -; mRNA.
DR EMBL; AE014298; AAF46031.2; -; Genomic_DNA.
DR EMBL; AY121662; AAM51989.1; -; mRNA.
DR RefSeq; NP_572219.1; NM_131991.3.
DR AlphaFoldDB; Q9W4C5; -.
DR SMR; Q9W4C5; -.
DR BioGRID; 57964; 1.
DR STRING; 7227.FBpp0070763; -.
DR TCDB; 2.A.22.2.13; the neurotransmitter:sodium symporter (nss) family.
DR GlyGen; Q9W4C5; 2 sites.
DR iPTMnet; Q9W4C5; -.
DR SwissPalm; Q9W4C5; -.
DR PaxDb; Q9W4C5; -.
DR DNASU; 31457; -.
DR EnsemblMetazoa; FBtr0070797; FBpp0070763; FBgn0029762.
DR GeneID; 31457; -.
DR KEGG; dme:Dmel_CG3252; -.
DR UCSC; CG3252-RA; d. melanogaster.
DR CTD; 31457; -.
DR FlyBase; FBgn0029762; NAAT1.
DR VEuPathDB; VectorBase:FBgn0029762; -.
DR eggNOG; KOG3660; Eukaryota.
DR GeneTree; ENSGT00940000167578; -.
DR HOGENOM; CLU_006855_9_5_1; -.
DR InParanoid; Q9W4C5; -.
DR OMA; WIYGLQN; -.
DR OrthoDB; 250396at2759; -.
DR PhylomeDB; Q9W4C5; -.
DR Reactome; R-DME-442660; Na+/Cl- dependent neurotransmitter transporters.
DR Reactome; R-DME-71288; Creatine metabolism.
DR BioGRID-ORCS; 31457; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31457; -.
DR PRO; PR:Q9W4C5; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0029762; Expressed in seminal fluid secreting gland and 29 other tissues.
DR ExpressionAtlas; Q9W4C5; baseline and differential.
DR Genevisible; Q9W4C5; DM.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005416; F:amino acid:cation symporter activity; ISM:FlyBase.
DR GO; GO:0005283; F:amino acid:sodium symporter activity; IMP:UniProtKB.
DR GO; GO:0042943; F:D-amino acid transmembrane transporter activity; IDA:FlyBase.
DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IDA:FlyBase.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; ISS:FlyBase.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IDA:FlyBase.
DR GO; GO:0003333; P:amino acid transmembrane transport; ISM:FlyBase.
DR GO; GO:0042940; P:D-amino acid transport; IDA:FlyBase.
DR GO; GO:0015807; P:L-amino acid transport; IDA:FlyBase.
DR GO; GO:0006836; P:neurotransmitter transport; ISS:FlyBase.
DR GO; GO:0015804; P:neutral amino acid transport; IDA:FlyBase.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IMP:UniProtKB.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Glycoprotein; Ion transport; Membrane;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..641
FT /note="Sodium-dependent nutrient amino acid transporter 1"
FT /id="PRO_0000214817"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CONFLICT 622
FT /note="D -> G (in Ref. 4; AAM51989)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="F -> L (in Ref. 1; AAY56384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 71762 MW; FE62F64EE090BD69 CRC64;
MELKGVQPSN GSSNGSGNGA TNAASTEKTD AEKPTAERTN WGNGLEFLMS CISVSVGLGN
VWRFPFTAYE NGGGAFLIPY IIVLFLIGKP MYYLEMIMGQ FTSQGTVKIW SVVPGFVGVG
YGQAFGTICI ISYYSSLLAL TLYYLFVSFQ SELPWSYCRD EWTNCVNSRP QEYVDNLLTG
VSLANESARN LSGIVANDET EKLQSSSELY FLNVVIKEKL DISDGVGDPD WKLTLALFVA
WVVIFLVIMR GVKSSGKAAY FLALFPYVVL FVLLIRAVTL EGARDGILFF LEPQWGELLN
PTVWKEAVVQ CFFSLAVGSG PIIMFASYNR FDHGIYRDAM IVTTLDTLTS LLGGITIFAI
LGNLAHNLQI ENIRDVVRSG TGLAFISYPD AISKFQAVPQ LFSVLFFFML FVLGIGSIVA
LQSTIVTIIC DQFKGWKYWK VALTTSVCGF LMGLVYVTPG GQWILTLVDF YGGTYVVFIL
AIFELAGIVW VYGLQNFCDD IEFMCNRRVS LYWRVCWSFF TPVMMIIIFI YSMVTIEPIK
YSELYFPEAA NIAGWLLFAI GAAQFPLWGL WYISRHPQGT YWKSLKASLK PSDRWGPANP
EIRREWVIFK NQKAAQRATQ KDTSKLGFFW RKVANFCGSN K
