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SPZ3_DROME
ID   SPZ3_DROME              Reviewed;         611 AA.
AC   Q9VLV7; Q8WTE9;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 160.
DE   RecName: Full=Protein spaetzle 3 {ECO:0000303|PubMed:11536362};
DE   AltName: Full=Protein spatzle 3 {ECO:0000312|FlyBase:FBgn0031959};
DE   Flags: Precursor;
GN   Name=spz3 {ECO:0000312|FlyBase:FBgn0031959};
GN   ORFNames=CG7104 {ECO:0000312|FlyBase:FBgn0031959};
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|Proteomes:UP000000803};
RN   [1] {ECO:0000312|EMBL:AAL33883.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION.
RX   PubMed=11536362; DOI=10.1002/prot.1125;
RA   Parker J.S., Mizuguchi K., Gay N.J.;
RT   "A family of proteins related to Spaetzle, the toll receptor ligand, are
RT   encoded in the Drosophila genome.";
RL   Proteins 45:71-80(2001).
RN   [2] {ECO:0000312|Proteomes:UP000000803}
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   [3] {ECO:0000312|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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:0000312|EMBL:AAM52001.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000312|EMBL:AAM52001.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAM52001.1};
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000305}
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=24662564; DOI=10.1083/jcb.201308115;
RA   Ballard S.L., Miller D.L., Ganetzky B.;
RT   "Retrograde neurotrophin signaling through Tollo regulates synaptic growth
RT   in Drosophila.";
RL   J. Cell Biol. 204:1157-1172(2014).
CC   -!- FUNCTION: Neurotrophin which may function as a ligand to the Toll-
CC       related receptor Tollo. Involved in a Tollo and JNK signaling pathway
CC       that positively regulates neuromuscular junction (NMJ) growth in
CC       presynaptic motorneurons. May function by activating Tollo to promote
CC       the phosphorylation of JNK. {ECO:0000269|PubMed:24662564}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250|UniProtKB:P48607}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in larval muscles.
CC       {ECO:0000269|PubMed:24662564}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown has no effect on
CC       neuromuscular junction (NMJ) growth. However, conditional knockdown in
CC       the muscles results in a decrease in bouton number at the NMJs.
CC       {ECO:0000269|PubMed:24662564}.
CC   -!- MISCELLANEOUS: 'Spaetzle' means 'noodles' in German. {ECO:0000305}.
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DR   EMBL; AF296285; AAL33883.1; -; mRNA.
DR   EMBL; AE014134; AAF52574.2; -; Genomic_DNA.
DR   EMBL; AY121674; AAM52001.1; -; mRNA.
DR   RefSeq; NP_609160.2; NM_135316.3.
DR   AlphaFoldDB; Q9VLV7; -.
DR   IntAct; Q9VLV7; 2.
DR   STRING; 7227.FBpp0079183; -.
DR   GlyGen; Q9VLV7; 4 sites.
DR   PaxDb; Q9VLV7; -.
DR   DNASU; 34077; -.
DR   EnsemblMetazoa; FBtr0079561; FBpp0079183; FBgn0031959.
DR   GeneID; 34077; -.
DR   KEGG; dme:Dmel_CG7104; -.
DR   UCSC; CG7104-RA; d. melanogaster.
DR   CTD; 34077; -.
DR   FlyBase; FBgn0031959; spz3.
DR   VEuPathDB; VectorBase:FBgn0031959; -.
DR   eggNOG; ENOG502QWM3; Eukaryota.
DR   HOGENOM; CLU_035541_1_0_1; -.
DR   InParanoid; Q9VLV7; -.
DR   OMA; KNNPYGP; -.
DR   OrthoDB; 844699at2759; -.
DR   PhylomeDB; Q9VLV7; -.
DR   BioGRID-ORCS; 34077; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 34077; -.
DR   PRO; PR:Q9VLV7; -.
DR   Proteomes; UP000000803; Chromosome 2L.
DR   Bgee; FBgn0031959; Expressed in wing disc and 11 other tissues.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IDA:FlyBase.
DR   GO; GO:0008083; F:growth factor activity; IBA:GO_Central.
DR   GO; GO:0005121; F:Toll binding; IBA:GO_Central.
DR   GO; GO:0021556; P:central nervous system formation; IBA:GO_Central.
DR   GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR   GO; GO:0008592; P:regulation of Toll signaling pathway; IBA:GO_Central.
DR   Gene3D; 2.10.90.10; -; 1.
DR   InterPro; IPR029034; Cystine-knot_cytokine.
DR   InterPro; IPR032104; Spaetzle.
DR   Pfam; PF16077; Spaetzle; 1.
DR   SUPFAM; SSF57501; SSF57501; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Reference proteome; Signal.
FT   SIGNAL          1..14
FT                   /evidence="ECO:0000255"
FT   CHAIN           15..611
FT                   /note="Protein spaetzle 3"
FT                   /evidence="ECO:0000303|PubMed:11536362"
FT                   /id="PRO_0000437665"
FT   DOMAIN          521..609
FT                   /note="Spaetzle"
FT                   /evidence="ECO:0000255"
FT   REGION          57..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        218..243
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..307
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..518
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        511
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        522..573
FT                   /evidence="ECO:0000250|UniProtKB:P48607"
FT   DISULFID        559..605
FT                   /evidence="ECO:0000250|UniProtKB:P48607"
FT   DISULFID        567..607
FT                   /evidence="ECO:0000250|UniProtKB:P48607"
FT   DISULFID        604
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P48607"
SQ   SEQUENCE   611 AA;  67126 MW;  67B6C56AC3E47E8A CRC64;
     MALTNFSLPF GALGQPWGVT IAPLHPIHQL ASNTNNLLYS PADHQQQTPA EAAADPEYFK
     NNPYAPPQSG GYQYQNTAGR RKQSNAYLPP TAPNAVRNSV YHIQQVQQTQ QQQTQQQHQQ
     QDQHENSVSF QSSSSRSSSS STTGQSSIQL TQTHASGRGP AEGSYSRYPG QQAQPPQQQQ
     PQQKQYFNAH GSASATFTKN SGSFSITSFG SRQQQQQPPQ PQQPPPSQQQ QPPPAPPPQR
     SRQAKPEAQP AQTYGVAPPE NYPERAPGFT RVQAGQGSRT QVHAVLDYDV EEGEEDEEED
     GEEEGQFYEG QENDKSNNNQ MPTVTPIQGP IYLKNGTVPV VPLFSYPKLN NGSFLQIPIW
     WTALSVALGL DVRGDVIKGV PCIKRYHQLF CPTAGNSYPI DKIERFIDDN KALMRRMYGD
     FEMNMEGPGG GGGRQQGKVR KRRFIDEPDI FIPPGAFAAN AGETVEAGDS YFGQLRKKRQ
     AAAGGSRNRG GSAGGSGNGN TNANRQPGNK NGSSGTGRLD ACESKIEIVT PYWASNSAGK
     IRAIVNTQHF EQAIHQEVCS NTQTPRCEGE CGCEQKYKWH RLLAYDPDND CKGIFMDWFL
     FPSCCVCRCN P
 
 
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