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NPLP1_DROME
ID   NPLP1_DROME             Reviewed;         309 AA.
AC   Q9W0W6; Q95T41;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Neuropeptide-like 1;
DE   Contains:
DE     RecName: Full=MTYamide peptide;
DE   Contains:
DE     RecName: Full=IPNamide peptide;
DE   Contains:
DE     RecName: Full=NAP peptide;
DE   Contains:
DE     RecName: Full=NPLP1-1;
DE   Contains:
DE     RecName: Full=NPLP1-2;
DE   Contains:
DE     RecName: Full=NPLP1-3;
DE   Contains:
DE     RecName: Full=NPLP1-4;
DE   Contains:
DE     RecName: Full=NPLP1-5;
DE   Contains:
DE     RecName: Full=NPLP1-6;
DE   Flags: Precursor;
GN   Name=Nplp1; ORFNames=CG3441;
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 [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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Ovary;
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   [4]
RP   PROTEIN SEQUENCE OF 102-115; 151-164 AND 168-182, AND AMIDATION AT TYR-164
RP   AND ASN-182.
RC   TISSUE=Larva;
RX   PubMed=12171930; DOI=10.1074/jbc.m206257200;
RA   Baggerman G., Cerstiaens A., De Loof A., Schoofs L.;
RT   "Peptidomics of the larval Drosophila melanogaster central nervous
RT   system.";
RL   J. Biol. Chem. 277:40368-40374(2002).
RN   [5]
RP   PROTEIN SEQUENCE OF 102-115; 151-164 AND 168-182, AND TISSUE SPECIFICITY.
RC   TISSUE=CNS;
RX   PubMed=14690519; DOI=10.1046/j.1471-4159.2003.02161.x;
RA   Verleyen P., Baggerman G., Wiehart U., Schoeters E., Van Lommel A.,
RA   De Loof A., Schoofs L.;
RT   "Expression of a novel neuropeptide, NVGTLARDFQLPIPNamide, in the larval
RT   and adult brain of Drosophila melanogaster.";
RL   J. Neurochem. 88:311-319(2004).
RN   [6]
RP   FUNCTION (NPLP1-4 PEPTIDE).
RX   PubMed=21893139; DOI=10.1016/j.peptides.2011.08.019;
RA   Overend G., Cabrero P., Guo A.X., Sebastian S., Cundall M., Armstrong H.,
RA   Mertens I., Schoofs L., Dow J.A., Davies S.A.;
RT   "The receptor guanylate cyclase Gyc76C and a peptide ligand, NPLP1-VQQ,
RT   modulate the innate immune IMD pathway in response to salt stress.";
RL   Peptides 34:209-218(2012).
RN   [7]
RP   FUNCTION (NPLP1-4 PEPTIDE), AND DISRUPTION PHENOTYPE (NPLP1-4 PEPTIDE).
RX   PubMed=26440503; DOI=10.1371/journal.pgen.1005576;
RA   Schleede J., Blair S.S.;
RT   "The Gyc76C receptor guanylyl cyclase and the foraging cGMP-dependent
RT   kinase regulate extracellular matrix organization and BMP signaling in the
RT   developing wing of Drosophila melanogaster.";
RL   PLoS Genet. 11:E1005576-E1005576(2015).
CC   -!- FUNCTION: [NPLP1-4]: Acts as a ligand for the receptor-type guanylate
CC       cyclase Gyc76C (PubMed:21893139). Stimulates Gyc76c-dependent cGMP
CC       production and modulates the IMD innate immune pathway in response to
CC       salt stress by inducing nuclear translocation of NF-kappa-B protein Rel
CC       which leads to increased expression of the antimicrobial peptide
CC       diptericin (PubMed:21893139). Does not appear to play a role in Gyc76C-
CC       mediated wing development (PubMed:26440503).
CC       {ECO:0000269|PubMed:21893139, ECO:0000269|PubMed:26440503}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: MTYamide peptide: Expressed in the larval CNS (at
CC       protein level). NAP peptide: Expressed in the larval CNS (at protein
CC       level). IPNamide peptide: Expressed in the ventral ganglion of the
CC       third larval instar and adult brain (at protein level).
CC       {ECO:0000269|PubMed:14690519}.
CC   -!- DISRUPTION PHENOTYPE: [NPLP1-4]: Occasional ectopic branching from the
CC       posterior crossvein. {ECO:0000269|PubMed:26440503}.
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DR   EMBL; AE013599; AAF47313.2; -; Genomic_DNA.
DR   EMBL; AY060340; AAL25379.1; -; mRNA.
DR   RefSeq; NP_611993.1; NM_138149.3.
DR   AlphaFoldDB; Q9W0W6; -.
DR   SMR; Q9W0W6; -.
DR   BioGRID; 63571; 4.
DR   DIP; DIP-17872N; -.
DR   IntAct; Q9W0W6; 1.
DR   STRING; 7227.FBpp0288531; -.
DR   PaxDb; Q9W0W6; -.
DR   PRIDE; Q9W0W6; -.
DR   DNASU; 38003; -.
DR   EnsemblMetazoa; FBtr0072443; FBpp0072348; FBgn0035092.
DR   GeneID; 38003; -.
DR   KEGG; dme:Dmel_CG3441; -.
DR   CTD; 100529111; -.
DR   FlyBase; FBgn0035092; Nplp1.
DR   VEuPathDB; VectorBase:FBgn0035092; -.
DR   eggNOG; ENOG502S8KI; Eukaryota.
DR   InParanoid; Q9W0W6; -.
DR   BioGRID-ORCS; 38003; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 38003; -.
DR   PRO; PR:Q9W0W6; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0035092; Expressed in brain and 13 other tissues.
DR   ExpressionAtlas; Q9W0W6; baseline and differential.
DR   Genevisible; Q9W0W6; DM.
DR   GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IC:FlyBase.
DR   GO; GO:0005184; F:neuropeptide hormone activity; IDA:FlyBase.
DR   GO; GO:0048018; F:receptor ligand activity; IPI:FlyBase.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; NAS:UniProtKB.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IDA:FlyBase.
PE   1: Evidence at protein level;
KW   Amidation; Cleavage on pair of basic residues; Direct protein sequencing;
KW   Neuropeptide; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   PROPEP          29..99
FT                   /id="PRO_0000021832"
FT   PEPTIDE         102..115
FT                   /note="NAP peptide"
FT                   /id="PRO_0000021833"
FT   PEPTIDE         118..148
FT                   /note="NPLP1-1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000021834"
FT   PEPTIDE         151..164
FT                   /note="MTYamide peptide"
FT                   /id="PRO_0000021835"
FT   PEPTIDE         168..182
FT                   /note="IPNamide peptide"
FT                   /id="PRO_0000021836"
FT   PEPTIDE         186..203
FT                   /note="NPLP1-2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000021837"
FT   PEPTIDE         206..226
FT                   /note="NPLP1-3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000021838"
FT   PEPTIDE         229..243
FT                   /note="NPLP1-4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000021839"
FT   PEPTIDE         246..287
FT                   /note="NPLP1-5"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000021840"
FT   PEPTIDE         290..309
FT                   /note="NPLP1-6"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000021841"
FT   REGION          126..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         164
FT                   /note="Tyrosine amide"
FT                   /evidence="ECO:0000269|PubMed:12171930"
FT   MOD_RES         182
FT                   /note="Asparagine amide"
FT                   /evidence="ECO:0000269|PubMed:12171930"
SQ   SEQUENCE   309 AA;  34198 MW;  620BB8A464BEF487 CRC64;
     MQAVLQSAHS SRRLMLLLSM LLNAAIQPRS IIVSATDDVA NVSPCEMESL INQLMSPSPE
     YQLHASALRN QLKNLLRERQ LAVGEEQPLG EYPDYLEEDK RSVAALAAQG LLNAPKRSLA
     TLAKNGQLPT AEPGEDYGDA DSGEPSEQKR YIGSLARAGG LMTYGKRNVG TLARDFQLPI
     PNGKRNIATM ARLQSAPSTH RDPKRNVAAV ARYNSQHGHI QRAGAEKRNL GALKSSPVHG
     VQQKREDEEM LLPAAAPDYA DPMQSYWWYP SYAGYADLDW NDYRRAEKRF LGRVLPPTRA
     TASTHRSRL
 
 
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