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Protein

Protein peanut

Gene

pnut

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

Functioni

Involved in cytokinesis and possibly cellularization. Also acts as an enhancer of the sina gene, thus having a role in photoreceptor development.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei183 – 1831GTPBy similarity
Binding sitei209 – 2091GTP; via amide nitrogenBy similarity
Binding sitei345 – 3451GTP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei360 – 3601GTPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi149 – 1568GTPBy similarity
Nucleotide bindingi288 – 2969GTPBy similarity

GO - Molecular functioni

  • actin binding Source: FlyBase
  • GTPase activity Source: FlyBase
  • GTP binding Source: FlyBase
  • microtubule binding Source: FlyBase
  • protein homodimerization activity Source: FlyBase
  • ubiquitin protein ligase binding Source: FlyBase

GO - Biological processi

  • actomyosin contractile ring assembly Source: FlyBase
  • apoptotic process Source: FlyBase
  • cellularization Source: FlyBase
  • mitotic cytokinesis Source: FlyBase
  • positive regulation of apoptotic process Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein peanut
Gene namesi
Name:pnut
ORF Names:CG8705
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0013726. pnut.

Subcellular locationi

  • Apical cell membrane 1 Publication; Peripheral membrane protein 1 Publication
  • Cleavage furrow 1 Publication

  • Note: Localized to the cleavage furrow of dividing cells during cytokinesis and to the intercellular bridge connecting postmitotic daughter cells. Equally found on the cell surfaces of the embryonic central nervous system and on the apical membranes of developing photoreceptor cells in the eye imaginal disk.

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB-SubCell
  • cleavage furrow Source: FlyBase
  • contractile ring Source: FlyBase
  • germline ring canal Source: FlyBase
  • intercellular bridge Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • mitochondrion Source: FlyBase
  • plasma membrane Source: FlyBase
  • septin complex Source: FlyBase
  • septin ring Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 539539Protein peanutPRO_0000173510Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei13 – 131Phosphoserine1 Publication
Modified residuei517 – 5171Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP40797.
PRIDEiP40797.

PTM databases

iPTMnetiP40797.

Expressioni

Developmental stagei

Maternal gene products found in the early embryo prior to zygotic transcription.1 Publication

Gene expression databases

BgeeiP40797.
GenevisibleiP40797. DM.

Interactioni

Subunit structurei

May well assemble into a multicomponent structure.

GO - Molecular functioni

  • actin binding Source: FlyBase
  • microtubule binding Source: FlyBase
  • protein homodimerization activity Source: FlyBase
  • ubiquitin protein ligase binding Source: FlyBase

Protein-protein interaction databases

BioGridi61655. 10 interactions.
DIPiDIP-60735N.
IntActiP40797. 2 interactions.
MINTiMINT-291495.
STRINGi7227.FBpp0087869.

Structurei

3D structure databases

ProteinModelPortaliP40797.
SMRiP40797. Positions 141-410.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini139 – 411273Septin-type GAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili420 – 51697Sequence analysisAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00760000118899.
InParanoidiP40797.
KOiK16944.
OMAiSDNVDGK.
OrthoDBiEOG79KPF0.
PhylomeDBiP40797.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40797-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSPRSNAVN GGSGGAISAL PSTLAQLALR DKQQAASASA SSATNGSSGS
60 70 80 90 100
ESLVGVGGRP PNQPPSVPVA ASGKLDTSGG GASNGDSNKL THDLQEKEHQ
110 120 130 140 150
QAQKPQKPPL PVRQKPMEIA GYVGFANLPN QVYRKAVKRG FEFTLMVVGA
160 170 180 190 200
SGLGKSTLIN SMFLSDIYNA EQYPGPSLRK KKTVAVEATK VMLKENGVNL
210 220 230 240 250
TLTVVDTPGF GDAVDNSNCW VPILEYVDSK YEEYLTAESR VYRKTISDSR
260 270 280 290 300
VHCCLYFIAP SGHGLLPLDI ACMQSLSDKV NLVPVIAKAD TMTPDEVHLF
310 320 330 340 350
KKQILNEIAQ HKIKIYDFPA TLEDAAEEAK TTQNLRSRVP FAVVGANTII
360 370 380 390 400
EQDGKKVRGR RYPWGLVEVE NLTHCDFIAL RNMVIRTHLQ DLKDVTNNVH
410 420 430 440 450
YENYRCRKLS ELGLVDGKAR LSNKNPLTQM EEEKREHEQK MKKMEAEMEQ
460 470 480 490 500
VFDMKVKEKM QKLRDSELEL ARRHEERKKA LELQIRELEE KRREFEREKK
510 520 530
EWEDVNHVTL EELKRRSLGA NSSTDNVDGK KEKKKKGLF
Length:539
Mass (Da):60,143
Last modified:November 8, 2005 - v2
Checksum:iA8009F7E6F331A32
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti79 – 791G → S in AAA19603 (PubMed:8181057).Curated
Sequence conflicti249 – 2491S → N in AAA19603 (PubMed:8181057).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08103 mRNA. Translation: AAA19603.1.
AE013599 Genomic DNA. Translation: AAM68857.1.
AY058663 mRNA. Translation: AAL13892.1.
PIRiA54294.
RefSeqiNP_477064.1. NM_057716.4.
NP_724659.1. NM_165597.2.
UniGeneiDm.4132.

Genome annotation databases

EnsemblMetazoaiFBtr0088792; FBpp0087869; FBgn0013726.
FBtr0088793; FBpp0087870; FBgn0013726.
GeneIDi35801.
KEGGidme:Dmel_CG8705.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08103 mRNA. Translation: AAA19603.1.
AE013599 Genomic DNA. Translation: AAM68857.1.
AY058663 mRNA. Translation: AAL13892.1.
PIRiA54294.
RefSeqiNP_477064.1. NM_057716.4.
NP_724659.1. NM_165597.2.
UniGeneiDm.4132.

3D structure databases

ProteinModelPortaliP40797.
SMRiP40797. Positions 141-410.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61655. 10 interactions.
DIPiDIP-60735N.
IntActiP40797. 2 interactions.
MINTiMINT-291495.
STRINGi7227.FBpp0087869.

PTM databases

iPTMnetiP40797.

Proteomic databases

PaxDbiP40797.
PRIDEiP40797.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0088792; FBpp0087869; FBgn0013726.
FBtr0088793; FBpp0087870; FBgn0013726.
GeneIDi35801.
KEGGidme:Dmel_CG8705.

Organism-specific databases

CTDi35801.
FlyBaseiFBgn0013726. pnut.

Phylogenomic databases

eggNOGiKOG2655. Eukaryota.
COG5019. LUCA.
GeneTreeiENSGT00760000118899.
InParanoidiP40797.
KOiK16944.
OMAiSDNVDGK.
OrthoDBiEOG79KPF0.
PhylomeDBiP40797.

Miscellaneous databases

ChiTaRSipnt. fly.
GenomeRNAii35801.
NextBioi795276.
PROiP40797.

Gene expression databases

BgeeiP40797.
GenevisibleiP40797. DM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR030379. G_SEPTIN_dom.
IPR027417. P-loop_NTPase.
IPR016491. Septin.
[Graphical view]
PANTHERiPTHR18884. PTHR18884. 1 hit.
PfamiPF00735. Septin. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51719. G_SEPTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The Drosophila peanut gene is required for cytokinesis and encodes a protein similar to yeast putative bud neck filament proteins."
    Neufeld T.P., Rubin G.M.
    Cell 77:371-379(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, 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: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "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-6 AND SER-13, IDENTIFICATION BY MASS SPECTROMETRY.
  6. "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 SER-517, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiPNUT_DROME
AccessioniPrimary (citable) accession number: P40797
Secondary accession number(s): Q0E9F5, Q9V385
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 8, 2005
Last modified: May 11, 2016
This is version 128 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.