PNUT_DROME
ID PNUT_DROME Reviewed; 539 AA.
AC P40797; Q0E9F5; Q9V385;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Protein peanut;
GN Name=pnut; ORFNames=CG8705;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=8181057; DOI=10.1016/0092-8674(94)90152-x;
RA Neufeld T.P., Rubin G.M.;
RT "The Drosophila peanut gene is required for cytokinesis and encodes a
RT protein similar to yeast putative bud neck filament proteins.";
RL Cell 77:371-379(1994).
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=Embryo;
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 INTERACTION WITH SEP1, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=8590810; DOI=10.1091/mbc.6.12.1843;
RA Fares H., Peifer M., Pringle J.R.;
RT "Localization and possible functions of Drosophila septins.";
RL Mol. Biol. Cell 6:1843-1859(1995).
RN [6]
RP INTERACTION WITH HIL, AND SUBCELLULAR LOCATION.
RX PubMed=15818553; DOI=10.1002/neu.20131;
RA Ji Y., Rath U., Girton J., Johansen K.M., Johansen J.;
RT "D-Hillarin, a novel W180-domain protein, affects cytokinesis through
RT interaction with the septin family member Pnut.";
RL J. Neurobiol. 64:157-169(2005).
RN [7]
RP FUNCTION, INTERACTION WITH PARK, AND UBIQUITINATION.
RX PubMed=17456438; DOI=10.1016/j.ibmb.2007.01.007;
RA Bae Y.J., Kang S.J., Park K.S.;
RT "Drosophila melanogaster Parkin ubiquitinates peanut and septin1 as an E3
RT ubiquitin-protein ligase.";
RL Insect Biochem. Mol. Biol. 37:430-439(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-13, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Involved in cytokinesis and possibly cellularization
CC (PubMed:8181057). Also acts as an enhancer of the sina gene, thus
CC having a role in photoreceptor development (PubMed:8181057). May be
CC involved in p53-dependent apoptosis (PubMed:17456438).
CC {ECO:0000269|PubMed:17456438, ECO:0000269|PubMed:8181057}.
CC -!- SUBUNIT: Likely part of a multicomponent septin complex that includes
CC Sep1 (PubMed:8590810). Interacts with Sep1 (PubMed:8590810). Interacts
CC with hil (PubMed:15818553). Interacts with park (PubMed:17456438).
CC {ECO:0000269|PubMed:15818553, ECO:0000269|PubMed:17456438,
CC ECO:0000269|PubMed:8590810}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:8181057}; Peripheral membrane protein
CC {ECO:0000269|PubMed:8181057}. Cleavage furrow
CC {ECO:0000269|PubMed:8181057}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:15818553}. Note=Localized to the cleavage furrow of
CC dividing cells during cytokinesis and to the intercellular bridge
CC connecting postmitotic daughter cells. Equally found on the cell
CC surfaces of the embryonic central nervous system and on the apical
CC membranes of developing photoreceptor cells in the eye imaginal disk
CC (PubMed:8181057). Colocalizes with hil at the cell cortex
CC (PubMed:15818553). {ECO:0000269|PubMed:15818553,
CC ECO:0000269|PubMed:8181057}.
CC -!- TISSUE SPECIFICITY: Accumulates at the leading edge of the cleavage
CC furrow in dividing cells and cellularizing embryos (at protein level).
CC {ECO:0000269|PubMed:8590810}.
CC -!- DEVELOPMENTAL STAGE: Maternal gene products found in the early embryo
CC prior to zygotic transcription. {ECO:0000269|PubMed:8181057}.
CC -!- PTM: Ubiquitinated by park, leading to its degradation by the
CC proteasome. {ECO:0000269|PubMed:17456438}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01056}.
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DR EMBL; U08103; AAA19603.1; -; mRNA.
DR EMBL; AE013599; AAM68857.1; -; Genomic_DNA.
DR EMBL; AY058663; AAL13892.1; -; mRNA.
DR PIR; A54294; A54294.
DR RefSeq; NP_477064.1; NM_057716.4.
DR RefSeq; NP_724659.1; NM_165597.2.
DR AlphaFoldDB; P40797; -.
DR SMR; P40797; -.
DR BioGRID; 61655; 31.
DR DIP; DIP-60735N; -.
DR IntAct; P40797; 4.
DR STRING; 7227.FBpp0087869; -.
DR iPTMnet; P40797; -.
DR PaxDb; P40797; -.
DR PRIDE; P40797; -.
DR DNASU; 35801; -.
DR EnsemblMetazoa; FBtr0088792; FBpp0087869; FBgn0013726.
DR EnsemblMetazoa; FBtr0088793; FBpp0087870; FBgn0013726.
DR GeneID; 35801; -.
DR KEGG; dme:Dmel_CG8705; -.
DR CTD; 35801; -.
DR FlyBase; FBgn0013726; pnut.
DR VEuPathDB; VectorBase:FBgn0013726; -.
DR eggNOG; KOG2655; Eukaryota.
DR GeneTree; ENSGT00940000154222; -.
DR HOGENOM; CLU_017718_8_1_1; -.
DR InParanoid; P40797; -.
DR OMA; HTNNFLY; -.
DR OrthoDB; 845354at2759; -.
DR PhylomeDB; P40797; -.
DR BioGRID-ORCS; 35801; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35801; -.
DR PRO; PR:P40797; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0013726; Expressed in wing disc and 25 other tissues.
DR Genevisible; P40797; DM.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032153; C:cell division site; IBA:GO_Central.
DR GO; GO:0032154; C:cleavage furrow; IDA:FlyBase.
DR GO; GO:0070938; C:contractile ring; IDA:FlyBase.
DR GO; GO:0045171; C:intercellular bridge; IDA:FlyBase.
DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0031105; C:septin complex; IDA:FlyBase.
DR GO; GO:0005940; C:septin ring; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:FlyBase.
DR GO; GO:0005525; F:GTP binding; IDA:FlyBase.
DR GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:FlyBase.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
DR GO; GO:0006915; P:apoptotic process; IGI:FlyBase.
DR GO; GO:0007349; P:cellularization; TAS:FlyBase.
DR GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
DR GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; IBA:GO_Central.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:FlyBase.
DR GO; GO:0045572; P:positive regulation of imaginal disc growth; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR CDD; cd01850; CDC_Septin; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016491; Septin.
DR Pfam; PF00735; Septin; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Coiled coil; Cytoplasm;
KW GTP-binding; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..539
FT /note="Protein peanut"
FT /id="PRO_0000173510"
FT DOMAIN 139..411
FT /note="Septin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 29..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..156
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 206..209
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 287..290
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01056"
FT REGION 513..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 420..516
FT /evidence="ECO:0000255"
FT COMPBIAS 29..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 183
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 288..296
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 360
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 79
FT /note="G -> S (in Ref. 1; AAA19603)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="S -> N (in Ref. 1; AAA19603)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 60143 MW; A8009F7E6F331A32 CRC64;
MNSPRSNAVN GGSGGAISAL PSTLAQLALR DKQQAASASA SSATNGSSGS ESLVGVGGRP
PNQPPSVPVA ASGKLDTSGG GASNGDSNKL THDLQEKEHQ QAQKPQKPPL PVRQKPMEIA
GYVGFANLPN QVYRKAVKRG FEFTLMVVGA SGLGKSTLIN SMFLSDIYNA EQYPGPSLRK
KKTVAVEATK VMLKENGVNL TLTVVDTPGF GDAVDNSNCW VPILEYVDSK YEEYLTAESR
VYRKTISDSR VHCCLYFIAP SGHGLLPLDI ACMQSLSDKV NLVPVIAKAD TMTPDEVHLF
KKQILNEIAQ HKIKIYDFPA TLEDAAEEAK TTQNLRSRVP FAVVGANTII EQDGKKVRGR
RYPWGLVEVE NLTHCDFIAL RNMVIRTHLQ DLKDVTNNVH YENYRCRKLS ELGLVDGKAR
LSNKNPLTQM EEEKREHEQK MKKMEAEMEQ VFDMKVKEKM QKLRDSELEL ARRHEERKKA
LELQIRELEE KRREFEREKK EWEDVNHVTL EELKRRSLGA NSSTDNVDGK KEKKKKGLF
