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Protein

Larval serum protein 2

Gene

Lsp2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Larval storage protein (LSP) which may serve as a store of amino acids for synthesis of adult proteins.By similarity

GO - Molecular functioni

GO - Biological processi

  • motor neuron axon guidance Source: FlyBase
  • synaptic target inhibition Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Storage protein

Names & Taxonomyi

Protein namesi
Recommended name:
Larval serum protein 2
Short name:
LSP-2
Alternative name(s):
Hexamerin-2
Gene namesi
Name:Lsp2
ORF Names:CG6806
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0002565. Lsp2.

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: FlyBase
  • larval serum protein complex Source: FlyBase
  • lipid particle Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence analysisAdd
BLAST
Chaini22 – 701680Larval serum protein 2PRO_0000013336Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi204 – 2041N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ24388.

Expressioni

Gene expression databases

BgeeiQ24388.
ExpressionAtlasiQ24388. differential.
GenevisibleiQ24388. DM.

Interactioni

Subunit structurei

Homohexamer.

Binary interactionsi

WithEntry#Exp.IntActNotes
Dpit47Q9V9C51EBI-172558,EBI-117913

Protein-protein interaction databases

BioGridi69593. 29 interactions.
IntActiQ24388. 1 interaction.
MINTiMINT-1763088.
STRINGi7227.FBpp0088363.

Structurei

3D structure databases

ProteinModelPortaliQ24388.
SMRiQ24388. Positions 24-696.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the hemocyanin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410II6Z. Eukaryota.
ENOG410XR2D. LUCA.
InParanoidiQ24388.
OMAiHIKRASG.
OrthoDBiEOG7RNJZH.
PhylomeDBiQ24388.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProiIPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERiPTHR11511. PTHR11511. 1 hit.
PfamiPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSiPR00187. HAEMOCYANIN.
SUPFAMiSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00210. HEMOCYANIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q24388-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSFTVIALA AVALLATLGQ AKHLDSKVAD KDFLMKQKFM YQILQHIYQD
60 70 80 90 100
DVFTTPFGGS YVEYKPWEHV ADYVHPEMLE HFFELWQHQP FTDDMVWSVM
110 120 130 140 150
YDKHEEYVVG LVRLFYFAKN WETFQHVVYW ARQHVNKQLF VYAVTIASLF
160 170 180 190 200
RDDMQGVVLP AHYEIHPWSY FDSQALEWAE HYKMHGFHHV KQMDNIYNVV
210 220 230 240 250
IRTNYSNVHG SLNYDHDLAY YLEDVGFNAF YYYFNLDYPF WTKGGEEHVL
260 270 280 290 300
NKDRRGELYL YVHWQLLARW YLERLSHDLG EVPAFNMYVP TESGYASNLR
310 320 330 340 350
TYYGVPQWHR ENHHSFYHEH NYEHIEHVEM YTQRVMDWIH KNEKFDVETI
360 370 380 390 400
NVLGNIIQGN ADSVDKKFYG SLDKLYRFIV NEGHHYGHGD ESFPGLFMHY
410 420 430 440 450
DTSMRDPIFY EVYKTIVSHY WHLMETYPEY HKKDYAFEGV HIDAVHMPES
460 470 480 490 500
LTTYFEHFDS DISNAVNVEP AVEGSADPLY TFGRNSHYKG SSYVIKARQQ
510 520 530 540 550
RLNHKPFEFT LDVTSDKAQD AVVKVFIGPK YDEHGHEIPL EHNYQNFFEL
560 570 580 590 600
EHFKVHLEAG VNHIKRASGD FSFWVNDRTT YLELYQKLMD ATNSDYKFKL
610 620 630 640 650
DQSEAHCGVP NRMMLPRGKK GGQVFQFFYM VYPYHQPEVA QFTGYDPVVS
660 670 680 690 700
CGVGHGSRYV DALPFGFPFN RPVKHDYYFD VHNFKFVDVK IFHRDEHTNV

V
Length:701
Mass (Da):83,349
Last modified:June 21, 2005 - v2
Checksum:i4CC348AC7C05138D
GO

Sequence cautioni

The sequence CAA66371.1 differs from that shown. Reason: Frameshift at position 700. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711Y → H in CAA66371 (PubMed:9128741).Curated
Sequence conflicti335 – 3351V → L in CAA66371 (PubMed:9128741).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97770 Genomic DNA. Translation: CAA66371.1. Frameshift.
AE014296 Genomic DNA. Translation: AAF49958.1.
AY119005 mRNA. Translation: AAM50865.1.
RefSeqiNP_001287042.1. NM_001300113.1.
NP_524816.1. NM_080077.2.
UniGeneiDm.19654.

Genome annotation databases

EnsemblMetazoaiFBtr0089324; FBpp0088363; FBgn0002565.
FBtr0345352; FBpp0311507; FBgn0002565.
GeneIDi45326.
KEGGidme:Dmel_CG6806.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97770 Genomic DNA. Translation: CAA66371.1. Frameshift.
AE014296 Genomic DNA. Translation: AAF49958.1.
AY119005 mRNA. Translation: AAM50865.1.
RefSeqiNP_001287042.1. NM_001300113.1.
NP_524816.1. NM_080077.2.
UniGeneiDm.19654.

3D structure databases

ProteinModelPortaliQ24388.
SMRiQ24388. Positions 24-696.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi69593. 29 interactions.
IntActiQ24388. 1 interaction.
MINTiMINT-1763088.
STRINGi7227.FBpp0088363.

Proteomic databases

PaxDbiQ24388.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089324; FBpp0088363; FBgn0002565.
FBtr0345352; FBpp0311507; FBgn0002565.
GeneIDi45326.
KEGGidme:Dmel_CG6806.

Organism-specific databases

CTDi45326.
FlyBaseiFBgn0002565. Lsp2.

Phylogenomic databases

eggNOGiENOG410II6Z. Eukaryota.
ENOG410XR2D. LUCA.
InParanoidiQ24388.
OMAiHIKRASG.
OrthoDBiEOG7RNJZH.
PhylomeDBiQ24388.

Miscellaneous databases

ChiTaRSiLsp2. fly.
GenomeRNAii45326.
NextBioi838026.
PROiQ24388.

Gene expression databases

BgeeiQ24388.
ExpressionAtlasiQ24388. differential.
GenevisibleiQ24388. DM.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
1.20.1370.10. 1 hit.
2.60.40.1520. 1 hit.
InterProiIPR013788. Hemocyanin/hexamerin.
IPR000896. Hemocyanin/hexamerin_mid_dom.
IPR005203. Hemocyanin_C.
IPR005204. Hemocyanin_N.
IPR014756. Ig_E-set.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PANTHERiPTHR11511. PTHR11511. 1 hit.
PfamiPF03723. Hemocyanin_C. 1 hit.
PF00372. Hemocyanin_M. 1 hit.
PF03722. Hemocyanin_N. 1 hit.
[Graphical view]
PRINTSiPR00187. HAEMOCYANIN.
SUPFAMiSSF48050. SSF48050. 1 hit.
SSF48056. SSF48056. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS00210. HEMOCYANIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence, structure and evolution of the ecdysone-inducible Lsp-2 gene of Drosophila melanogaster."
    Mousseron-Grall S., Kejzlarova-Lepesant J., Burmester T., Chihara C., Barray M., Delain E., Pictet R., Lepesant J.-A.
    Eur. J. Biochem. 245:191-198(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Canton-S.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Larva and Pupae.

Entry informationi

Entry nameiLSP2_DROME
AccessioniPrimary (citable) accession number: Q24388
Secondary accession number(s): Q9VTT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 21, 2005
Last modified: May 11, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.