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Protein

Protein lingerer

Gene

lig

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

Functioni

Acts in the nervous system to mediate the control of copulatory organs during courtship.1 Publication

GO - Biological processi

  • copulation Source: FlyBase
  • dorsal/ventral axis specification, ovarian follicular epithelium Source: FlyBase
  • male mating behavior Source: FlyBase
  • negative regulation of imaginal disc growth Source: FlyBase
  • negative regulation of JAK-STAT cascade Source: FlyBase
  • positive regulation of transcription, DNA-templated Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Behavior

Names & Taxonomyi

Protein namesi
Recommended name:
Protein lingerer
Gene namesi
Name:ligImported
ORF Names:CG8715
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0020279. lig.

Subcellular locationi

  • Cytoplasm 1 Publication

  • Note: Found in the cytoplasm of many neuronal and glial cells in the brain and ventral ganglion, and in imaginal disks.1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Male flies exhibit abnormal copulation. They fail to successfully withdraw their genitalia upon termination of copulation so end up 'stuck' to the female, tugging to separate. There is also a "non-copulating" behavioral phenotype. There are no morphological defects in the male genitalia. Females can mate successfully but have reduced fertility. Complete loss of lig function results in lethality during early pupal stages.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13751375Protein lingererPRO_0000314621Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei321 – 3211Phosphotyrosine1 Publication
Modified residuei324 – 3241Phosphoserine1 Publication
Modified residuei672 – 6721Phosphoserine1 Publication
Modified residuei673 – 6731Phosphothreonine1 Publication
Modified residuei674 – 6741Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ86S05.
PRIDEiQ86S05.

PTM databases

iPTMnetiQ86S05.

Expressioni

Tissue specificityi

At stage 11, expression is restricted to the neuroblasts, predominant in the central nervous system (CNS), including the brain and ventral nerve cord, and in the PNS. Later embryonic expression is seen in the gonads. Late third instar larvae show expression in the CNS, imaginal disks (including genital, eye-antennal, leg, wing and haltere disks), and gonads. In the larval brain, it is expressed in all of the glial cells and in clusters of neurons that projected contralaterally. In the larval ventral ganglion, it is expressed in subperineurial glia, peripheral exit glia, and a number of interneurons, but not in motor neurons. Isoform B is abundantly expressed in males and females. Isoform D is male specific and expressed at low levels.2 Publications

Developmental stagei

Expressed both maternally and zygotically throughout development. Zygotic expression levels rise after embryonic stage 9.1 Publication

Gene expression databases

BgeeiQ86S05.
ExpressionAtlasiQ86S05. differential.

Interactioni

Protein-protein interaction databases

BioGridi61631. 13 interactions.
IntActiQ86S05. 2 interactions.
STRINGi7227.FBpp0303481.

Structurei

3D structure databases

ProteinModelPortaliQ86S05.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini84 – 12441UBASequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi226 – 28257Gly-richSequence analysisAdd
BLAST
Compositional biasi629 – 67850Gln-richSequence analysisAdd
BLAST
Compositional biasi881 – 1038158Gly-richSequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 UBA domain.Sequence analysis

Phylogenomic databases

eggNOGiENOG410IGWX. Eukaryota.
ENOG4110RI8. LUCA.
GeneTreeiENSGT00390000003453.
InParanoidiQ86S05.
OMAiDYTEPAQ.
OrthoDBiEOG761BTB.
PhylomeDBiQ86S05.

Family and domain databases

InterProiIPR022166. DUF3697_Uba2.
IPR009060. UBA-like.
[Graphical view]
PfamiPF12478. DUF3697. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform D1 Publication (identifier: Q86S05-1) [UniParc]FASTAAdd to basket

Also known as: Lig-B1 Publication

, type21 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSTQTRSGGG GGGGHARNQK KSNASNSGGG GTGHHDGVSH AAAAGKKGGQ
60 70 80 90 100
DASKTDKPEK AQPKATTEQL RIAQITNSTT EDPQINEKVL LLLTMTQRSE
110 120 130 140 150
EEVCCALNEC DYDLEAAANF LIEELPQGAF AKYEKKRKNK AANNTADGAA
160 170 180 190 200
GDGDWADGNG NADRREKSRN RSSNRGGTRG SSDSRGWRGR ETRENERNQR
210 220 230 240 250
ESREPWSGQN AGQDRGDDRA NDNYRGQRNG GGRSGPGGGG RGGGFVSRSG
260 270 280 290 300
RGGGRMGGRT GGPRGDRGSG GPGGAYGSGR GGNANEDHHE VELWDNTIAQ
310 320 330 340 350
NAEKQQQAHD DAWGDWNNEE YEGSLKDSKV FTTSNLATQS AANVVSGTGA
360 370 380 390 400
SVTAVPAAAG TEISAPPGLE HQLVQQGSHL EESSSSGPAA VTPPATLSGS
410 420 430 440 450
ATTPLLQYSA AVSNPPPQLQ SQGTQSGAGT GASAAAGGGA GSTPSSFVSA
460 470 480 490 500
SPDTFSSAAS AAATLVHQAQ KQQQLQQQTT PIKPSATLSV EQSQYFNSLA
510 520 530 540 550
SQGVSPGSVP VQSAPAGYAQ NPVAAYSQTS TSVGVSQYPN TYANVFASGT
560 570 580 590 600
AAGAGTAEQS QQQPQIRRAR VKLPPPSKIP ASAVEMPGDN ALNNIGYLDV
610 620 630 640 650
QFGALDFGTD DGFEPLPEKV GSGFSIDGQQ QQQQPDDYQS KSQQQQQVTL
660 670 680 690 700
AAGLQSSQIS DALNAAGYTS RSTSQQQQGV SSAVNATIDQ LTKSDPYGQT
710 720 730 740 750
GGSGNAYQNA YQSSGASKTA SGFPTTAPGG YSSSTYANVQ SSVANSYQQQ
760 770 780 790 800
GYGSYQPSSY QQQAGSGAQS GTGAVSGGGG TATQNIPVGG SSSQNSTSGN
810 820 830 840 850
ASSAYLTSGY STPQSAYQSS QSVYGNTGLS NSSGFSGSAS NASSQYANFS
860 870 880 890 900
ASAKLKDATT ASSAAHYDSV STSSGVSSNS GSTGNGGVVS GQTGANQAAV
910 920 930 940 950
SNNNSVSGSS SVSNVTAGVA SGNVAGVGGG VSQSGVSSGV GVPGGSASSV
960 970 980 990 1000
GVNVNNNSSS ASSVGAATVA QTATGTTAAV LASLTNKNTS SSNSSGSGGS
1010 1020 1030 1040 1050
AATTTGNASG QGAGASTGGV GSSSGAGGAG SGGGSGSGLV PTNIQMVSQY
1060 1070 1080 1090 1100
IQTGLPYYQQ PVYSYEELQM MQQRVPHVQG YYDLNYPPAS LGAGRDNLGS
1110 1120 1130 1140 1150
VTYSAMNDGR FARTDNNSSP VGNVSSTMSQ QAGSSAPMLN VPYAYFYGGN
1160 1170 1180 1190 1200
VMPGSFQYGT PAIYPQIPAA NTASGQQFPK PSYSAGYGST SYDTLSQTTQ
1210 1220 1230 1240 1250
DYSKGGYSSS VNQQSKTQTV SNQSQAGTGS DLTSSMYGKG HVALNKVNSY
1260 1270 1280 1290 1300
EKQSFHSGTP PPFNMPNTQT AGGTSAQPYG MYLPMPAAGH HNMIHQPIHQ
1310 1320 1330 1340 1350
VHSELPLQVV VGGGTESHVL IHGNVNGPQV TYHRIWQTEP VQCQNQLVAA
1360 1370
HCNNFEPNID CCVHDNNNDL SFFAD
Length:1,375
Mass (Da):139,491
Last modified:June 1, 2003 - v1
Checksum:i5FE3204D18FDE70A
GO
Isoform A1 Publication (identifier: Q86S05-2) [UniParc]FASTAAdd to basket

Also known as: C1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1301-1375: VHSELPLQVV...NNNDLSFFAD → MDGRIHSSSR...YSPSYWAGQN

Note: No experimental confirmation available.Curated
Show »
Length:1,343
Mass (Da):135,845
Checksum:i63CF1A76DE780CFA
GO
Isoform B1 Publication (identifier: Q86S05-3) [UniParc]FASTAAdd to basket

Also known as: Lig-A1 Publication

, type11 Publication, type31 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1301-1375: VHSELPLQVV...NNNDLSFFAD → DSNSAGQRQQSTSQSKSAGKQGYSPSYWAGQN

Show »
Length:1,332
Mass (Da):134,561
Checksum:iF1E59F730B014024
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti185 – 1851R → C in AAO23022 (PubMed:12524348).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1301 – 137575VHSEL…SFFAD → MDGRIHSSSRRDSNSAGQRQ QSTSQSKSAGKQGYSPSYWA GQN in isoform A. 1 PublicationVSP_052633Add
BLAST
Alternative sequencei1301 – 137575VHSEL…SFFAD → DSNSAGQRQQSTSQSKSAGK QGYSPSYWAGQN in isoform B. 2 PublicationsVSP_052634Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF276963 mRNA. Translation: AAO23022.1.
AF276964 mRNA. Translation: AAO23023.1.
AE013599 Genomic DNA. Translation: AAF59144.3.
AE013599 Genomic DNA. Translation: AAM68848.2.
AE013599 Genomic DNA. Translation: AAS64895.2.
AE013599 Genomic DNA. Translation: AAX52724.1.
AY069682 mRNA. Translation: AAL39827.1.
RefSeqiNP_001014503.1. NM_001014503.2. [Q86S05-1]
NP_001163081.1. NM_001169610.2. [Q86S05-3]
NP_001163082.1. NM_001169611.1. [Q86S05-3]
NP_001163083.1. NM_001169612.2. [Q86S05-3]
NP_610348.3. NM_136504.5. [Q86S05-2]
NP_724643.2. NM_165586.5. [Q86S05-3]
NP_995778.2. NM_206056.5. [Q86S05-2]
UniGeneiDm.517.

Genome annotation databases

EnsemblMetazoaiFBtr0100575; FBpp0100030; FBgn0020279. [Q86S05-1]
GeneIDi35771.
KEGGidme:Dmel_CG8715.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF276963 mRNA. Translation: AAO23022.1.
AF276964 mRNA. Translation: AAO23023.1.
AE013599 Genomic DNA. Translation: AAF59144.3.
AE013599 Genomic DNA. Translation: AAM68848.2.
AE013599 Genomic DNA. Translation: AAS64895.2.
AE013599 Genomic DNA. Translation: AAX52724.1.
AY069682 mRNA. Translation: AAL39827.1.
RefSeqiNP_001014503.1. NM_001014503.2. [Q86S05-1]
NP_001163081.1. NM_001169610.2. [Q86S05-3]
NP_001163082.1. NM_001169611.1. [Q86S05-3]
NP_001163083.1. NM_001169612.2. [Q86S05-3]
NP_610348.3. NM_136504.5. [Q86S05-2]
NP_724643.2. NM_165586.5. [Q86S05-3]
NP_995778.2. NM_206056.5. [Q86S05-2]
UniGeneiDm.517.

3D structure databases

ProteinModelPortaliQ86S05.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61631. 13 interactions.
IntActiQ86S05. 2 interactions.
STRINGi7227.FBpp0303481.

PTM databases

iPTMnetiQ86S05.

Proteomic databases

PaxDbiQ86S05.
PRIDEiQ86S05.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0100575; FBpp0100030; FBgn0020279. [Q86S05-1]
GeneIDi35771.
KEGGidme:Dmel_CG8715.

Organism-specific databases

CTDi35771.
FlyBaseiFBgn0020279. lig.

Phylogenomic databases

eggNOGiENOG410IGWX. Eukaryota.
ENOG4110RI8. LUCA.
GeneTreeiENSGT00390000003453.
InParanoidiQ86S05.
OMAiDYTEPAQ.
OrthoDBiEOG761BTB.
PhylomeDBiQ86S05.

Miscellaneous databases

ChiTaRSilig. fly.
GenomeRNAii35771.
PROiQ86S05.

Gene expression databases

BgeeiQ86S05.
ExpressionAtlasiQ86S05. differential.

Family and domain databases

InterProiIPR022166. DUF3697_Uba2.
IPR009060. UBA-like.
[Graphical view]
PfamiPF12478. DUF3697. 1 hit.
[Graphical view]
SUPFAMiSSF46934. SSF46934. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Lingerer, a Drosophila gene involved in initiation and termination of copulation, encodes a set of novel cytoplasmic proteins."
    Kuniyoshi H., Baba K., Ueda R., Kondo S., Awano W., Juni N., Yamamoto D.
    Genetics 162:1775-1789(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND D), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
  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: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    Strain: BerkeleyImported.
    Tissue: Embryo1 Publication.
  5. "Expression analysis of the lingerer gene in the larval central nervous system of Drosophila melanogaster."
    Kuniyoshi H., Usui-Aoki K., Juni N., Yamamoto D.
    J. Neurogenet. 17:117-137(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
    Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
    Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; THR-673 AND SER-674, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-321 AND SER-324, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiLIG_DROME
AccessioniPrimary (citable) accession number: Q86S05
Secondary accession number(s): A1Z794, Q86S06, Q8SZZ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: June 8, 2016
This is version 96 of the entry and version 1 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.