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LSP1G_DROME
ID   LSP1G_DROME             Reviewed;         772 AA.
AC   P11997; O16162; Q9W0V6;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2001, sequence version 2.
DT   03-AUG-2022, entry version 173.
DE   RecName: Full=Larval serum protein 1 gamma chain;
DE   AltName: Full=Hexamerin-1-gamma;
DE   Flags: Precursor;
GN   Name=Lsp1gamma; Synonyms=Lsp1-g; ORFNames=CG6821;
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=Larva, and Pupae;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-711.
RX   PubMed=9402735; DOI=10.1093/oxfordjournals.molbev.a025734;
RA   Bauer V.L., Aquadro C.F.;
RT   "Rates of DNA sequence evolution are not sex-biased in Drosophila
RT   melanogaster and D. simulans.";
RL   Mol. Biol. Evol. 14:1252-1257(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-105, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=3097321; DOI=10.1016/0022-2836(86)90376-1;
RA   Delaney S.J., Smith D.F., McClelland A., Sunkel C., Glover D.M.;
RT   "Sequence conservation around the 5' ends of the larval serum protein 1
RT   genes of Drosophila melanogaster.";
RL   J. Mol. Biol. 189:1-11(1986).
CC   -!- FUNCTION: Larval storage protein (LSP) which may serve as a store of
CC       amino acids for synthesis of adult proteins. {ECO:0000250}.
CC   -!- SUBUNIT: Heterohexamer, composed of three subunits, alpha, beta and
CC       gamma.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:3097321}.
CC   -!- TISSUE SPECIFICITY: Larval hemolymph. {ECO:0000269|PubMed:3097321}.
CC   -!- SIMILARITY: Belongs to the hemocyanin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA27508.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AE014296; AAF47324.1; -; Genomic_DNA.
DR   EMBL; AY069748; AAL39893.1; -; mRNA.
DR   EMBL; AF016033; AAB71666.1; -; Genomic_DNA.
DR   EMBL; X03874; CAA27508.1; ALT_FRAME; Genomic_DNA.
DR   PIR; C27144; C27144.
DR   RefSeq; NP_523868.1; NM_079144.5.
DR   AlphaFoldDB; P11997; -.
DR   SMR; P11997; -.
DR   BioGRID; 63580; 2.
DR   STRING; 7227.FBpp0072365; -.
DR   GlyGen; P11997; 1 site.
DR   PaxDb; P11997; -.
DR   PRIDE; P11997; -.
DR   DNASU; 38015; -.
DR   EnsemblMetazoa; FBtr0072463; FBpp0072365; FBgn0002564.
DR   GeneID; 38015; -.
DR   KEGG; dme:Dmel_CG6821; -.
DR   CTD; 38015; -.
DR   FlyBase; FBgn0002564; Lsp1gamma.
DR   VEuPathDB; VectorBase:FBgn0002564; -.
DR   eggNOG; ENOG502QR98; Eukaryota.
DR   GeneTree; ENSGT00940000165243; -.
DR   HOGENOM; CLU_012213_1_0_1; -.
DR   InParanoid; P11997; -.
DR   OMA; EYGRVIP; -.
DR   OrthoDB; 244455at2759; -.
DR   PhylomeDB; P11997; -.
DR   BioGRID-ORCS; 38015; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; Lsp1gamma; fly.
DR   GenomeRNAi; 38015; -.
DR   PRO; PR:P11997; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0002564; Expressed in arthropod fat body and 13 other tissues.
DR   ExpressionAtlas; P11997; baseline and differential.
DR   Genevisible; P11997; DM.
DR   GO; GO:0005616; C:larval serum protein complex; IDA:FlyBase.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1280.10; -; 1.
DR   Gene3D; 1.20.1370.10; -; 1.
DR   Gene3D; 2.60.40.1520; -; 1.
DR   InterPro; IPR008922; Di-copper_centre_dom_sf.
DR   InterPro; IPR013788; Hemocyanin/hexamerin.
DR   InterPro; IPR000896; Hemocyanin/hexamerin_mid_dom.
DR   InterPro; IPR005203; Hemocyanin_C.
DR   InterPro; IPR037020; Hemocyanin_C_sf.
DR   InterPro; IPR005204; Hemocyanin_N.
DR   InterPro; IPR036697; Hemocyanin_N_sf.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR11511; PTHR11511; 1.
DR   Pfam; PF03723; Hemocyanin_C; 1.
DR   Pfam; PF00372; Hemocyanin_M; 1.
DR   Pfam; PF03722; Hemocyanin_N; 1.
DR   PRINTS; PR00187; HAEMOCYANIN.
DR   SUPFAM; SSF48050; SSF48050; 1.
DR   SUPFAM; SSF48056; SSF48056; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   PROSITE; PS00210; HEMOCYANIN_2; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Reference proteome; Secreted; Signal; Storage protein.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..772
FT                   /note="Larval serum protein 1 gamma chain"
FT                   /id="PRO_0000013335"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        326..328
FT                   /note="QQI -> SRS (in Ref. 4; AAB71666)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        624
FT                   /note="S -> T (in Ref. 4; AAB71666)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   772 AA;  93408 MW;  FC2BC0A7336F636D CRC64;
     MKLTLVILAL VACVTAFSVP TQKVKIADKN FLEKQKFLFE IVHRIDEPLM FEEWIKMGQK
     LITDKAQYET FDFYMEKLWE SYKLGALLPK GEFFGALVKT HHKQAYGLFN FFYYAKDWET
     FVRNVAWARI HVNEGMFVYA LTLAVIHKPE FEGLILPQIY EIFPQYFFNS KFVYAAEKFD
     YEVFSKLTMY EKEYKDILYK DYSEFTGNFY FYTKDWKTWQ WYKMMGLDQE WYVEDKYFLR
     ENLSQFVNDP KYVDVVKGLK KFYMPVDYTR DIDFFNDETK MTYFTEDLGW NAYWYYLNMD
     YAFFLNGKQF GLDKDRRGEY WIYNVQQILA RYYQERLANG FGEIPEFFWY KQIEYGYDPQ
     LIYYNGIGYS YRKNYYDFYT YGKFEMYSQI QNFFSRVYKV LETGFYKTAD GQVFDLHKPE
     AIKIVGNYLQ GNADTFDKYF FNYYYLLAHM YFADVDYNDM EVFPNVFLNF ETMLRDPFFY
     TFYKKFTDVF YTFKYYLKPY TQKDLFYEGI TIKDVSVSKL VTYYDIVDFD VTNLLNDKMT
     FVDGQYIWDK ALLARQARLN HKPFNFEFTI DSDKVQKGVV RVFLGPKFDE YGRVIPLDYN
     RKNFVQIDSF VYPFIAGTNT IKRSSKEFSW TAEDRITYTE LYKYVMLASE GKYDFPLDIS
     EPHNAFPDRL VLPKGWEQGM PMQFYFFVSP FAETYEQFSN FDYTYSSGVG SGTRFVDTKP
     FGYPFDRQID ESDFFVPNGF FKDVKVYYVD TFAKYFEKKY TQFGTFDYSI EY
 
 
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