ID LSP1B_DROME Reviewed; 789 AA.
AC P11996; Q29R17; Q9VPV2;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 3.
DT 24-JAN-2024, entry version 175.
DE RecName: Full=Larval serum protein 1 beta chain;
DE AltName: Full=Hexamerin-1-beta;
DE Flags: Precursor;
GN Name=Lsp1beta; Synonyms=Lsp1-b; ORFNames=CG4178;
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 [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=9128742; DOI=10.1111/j.1432-1033.1997.00199.x;
RA Massey H.C. Jr., Kejzlarova-Lepesant J., Willis R.L., Castleberry A.B.,
RA Benes H.;
RT "The Drosophila Lsp-1 beta gene. A structural and phylogenetic analysis.";
RL Eur. J. Biochem. 245:199-207(1997).
RN [2]
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]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Larva, and Pupae;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100.
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 -!- TISSUE SPECIFICITY: Larval hemolymph.
CC -!- SIMILARITY: Belongs to the hemocyanin family. {ECO:0000305}.
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DR EMBL; U63556; AAB58821.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF51434.1; -; Genomic_DNA.
DR EMBL; AY069163; AAL39308.1; -; mRNA.
DR EMBL; BT024223; ABC86285.1; -; mRNA.
DR EMBL; X03873; CAA27507.1; -; Genomic_DNA.
DR PIR; B27144; B27144.
DR RefSeq; NP_001285556.1; NM_001298627.1.
DR RefSeq; NP_476624.1; NM_057276.4.
DR AlphaFoldDB; P11996; -.
DR SMR; P11996; -.
DR BioGRID; 59528; 2.
DR ComplexPortal; CPX-2224; Larval serum protein complex.
DR IntAct; P11996; 1.
DR STRING; 7227.FBpp0311765; -.
DR PaxDb; 7227-FBpp0077690; -.
DR DNASU; 33274; -.
DR EnsemblMetazoa; FBtr0078025; FBpp0077690; FBgn0002563.
DR EnsemblMetazoa; FBtr0345738; FBpp0311765; FBgn0002563.
DR GeneID; 33274; -.
DR KEGG; dme:Dmel_CG4178; -.
DR AGR; FB:FBgn0002563; -.
DR CTD; 33274; -.
DR FlyBase; FBgn0002563; Lsp1beta.
DR VEuPathDB; VectorBase:FBgn0002563; -.
DR eggNOG; ENOG502QR98; Eukaryota.
DR HOGENOM; CLU_012213_1_0_1; -.
DR InParanoid; P11996; -.
DR OMA; ADGHMID; -.
DR OrthoDB; 5406463at2759; -.
DR PhylomeDB; P11996; -.
DR BioGRID-ORCS; 33274; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Lsp1beta; fly.
DR GenomeRNAi; 33274; -.
DR PRO; PR:P11996; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0002563; Expressed in arthropod fat body and 18 other cell types or tissues.
DR ExpressionAtlas; P11996; baseline and differential.
DR Genevisible; P11996; 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; Di-copper center containing domain from catechol oxidase; 1.
DR Gene3D; 2.60.40.1520; Hemocyanin, C-terminal domain; 1.
DR Gene3D; 1.20.1370.10; Hemocyanin, N-terminal domain; 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:SF5; FAT-BODY PROTEIN 1-RELATED; 1.
DR PANTHER; PTHR11511; LARVAL STORAGE PROTEIN/PHENOLOXIDASE; 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; SSF48056; Di-copper centre-containing domain; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF48050; Hemocyanin, N-terminal domain; 1.
DR PROSITE; PS00210; HEMOCYANIN_2; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Secreted; Signal; Storage protein.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..789
FT /note="Larval serum protein 1 beta chain"
FT /id="PRO_0000013334"
FT CONFLICT 275
FT /note="T -> N (in Ref. 1; AAB58821)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="S -> R (in Ref. 1; AAB58821)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 789 AA; 95914 MW; AE12594515806A5B CRC64;
MKIAIALLAC LGLAAAASFH QTHEVKIADK AFLMKQKFLF EIVYRVEDPL MFEDHIKQGE
KFYFEESYYT HYDMYMKKFF EAYKAHALLP KGEFFGALVM SHAKQARGLF NFFYYAKDWE
TFAANVAWAR MHVNEGMFVY ALTMAVIHRN DFHGLMLPSI YEIFPQFFFN SKFVFEAEKF
DYEMWMKMTM YEKEYMDVYY KTNGYDYSTM YRSSDYTYMK DFKTWQWWKL MGLGEHWYTE
DKFILRENIY EFNQETKWLS MMKDVKKFYM PVDYTRDLNL YNKESKLSYF TEDLGWNAYW
YYLNMDYSFF LDGNTFDLKN DRRGEWWLYN VHQLLSRYYM ERLSHGFGEI PEFSWYQQIE
MGYDPQLIYY NGIGYSFRKN YYEMETYANY DMLDKITGFL KRIHNIVEMG YYKTADGHTI
DLRKPEAIEF IGNMLQGNVD AMDKMFYQFW YMLAHMYFAD ADYYQMDVYP NVMLNFETMM
RDPMYYMFYK SIAQVYFQFM HYLPKYTKEQ LLMPGVTMKN VEVSDLTTYF DLVDFDVTNM
LNDKMIFQDG KFVWDMSLFA RQMRLNHKPF TYTYTIESEK VEKVVIRAFL GPKFDEFGKV
ISLAENRMNF MEIDEFYYEL KAGTNKITRK SSEFYWTVKD RTTYTELYYY TMMAFDGKYD
FPLDISEPHC GFPDRLVLPM GWQKGMPMQM FFMVVPYVAP AHEQFSTFDY TYSCGIGSGA
RYVDSLPFGY PFDRAIDEYE FFVPNMYFKD VSIYHADTME PYYKYKSYSN YGHFDYTFFN
DYYTKYFKF
//
