SPNF_DROME
ID SPNF_DROME Reviewed; 364 AA.
AC Q9V9Y9;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Protein spindle-F {ECO:0000303|PubMed:16540510};
GN Name=spn-F {ECO:0000312|FlyBase:FBgn0086362};
GN ORFNames=CG12114 {ECO:0000312|FlyBase:FBgn0086362};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000312|EMBL:AAL28594.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28594.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAL28594.1};
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 [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH CTP, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16540510; DOI=10.1242/dev.02319;
RA Abdu U., Bar D., Schuepbach T.;
RT "spn-F encodes a novel protein that affects oocyte patterning and bristle
RT morphology in Drosophila.";
RL Development 133:1477-1484(2006).
RN [5] {ECO:0000305}
RP INTERACTION WITH IKKEPSILON, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=18796167; DOI=10.1186/1471-2121-9-51;
RA Dubin-Bar D., Bitan A., Bakhrat A., Kaiden-Hasson R., Etzion S.,
RA Shaanan B., Abdu U.;
RT "The Drosophila IKK-related kinase (Ik2) and Spindle-F proteins are part of
RT a complex that regulates cytoskeleton organization during oogenesis.";
RL BMC Cell Biol. 9:51-51(2008).
RN [6] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19917727; DOI=10.1128/mcb.00861-09;
RA Bitan A., Guild G.M., Bar-Dubin D., Abdu U.;
RT "Asymmetric microtubule function is an essential requirement for polarized
RT organization of the Drosophila bristle.";
RL Mol. Cell. Biol. 30:496-507(2010).
RN [7] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH JVL.
RX PubMed=24019068; DOI=10.1128/mcb.00713-13;
RA Amsalem S., Bakrhat A., Otani T., Hayashi S., Goldstein B., Abdu U.;
RT "Drosophila oocyte polarity and cytoskeleton organization require
RT regulation of Ik2 activity by Spn-F and Javelin-like.";
RL Mol. Cell. Biol. 33:4371-4380(2013).
RN [8] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN COMPLEX WITH CTP AND IKKEPSILON, TISSUE
RP SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26092846; DOI=10.1242/dev.121863;
RA Otani T., Oshima K., Kimpara A., Takeda M., Abdu U., Hayashi S.;
RT "A transport and retention mechanism for the sustained distal localization
RT of Spn-F-IKKepsilon during Drosophila bristle elongation.";
RL Development 142:2338-2351(2015).
RN [9]
RP ERRATUM OF PUBMED:26092846.
RX PubMed=26487782; DOI=10.1242/dev.130674;
RA Otani T., Oshima K., Kimpara A., Takeda M., Abdu U., Hayashi S.;
RL Development 142:3612-3612(2015).
RN [10] {ECO:0000305}
RP FUNCTION, SUBUNIT, IDENTIFICATION IN COMPLEX WITH CTP AND IKKEPSILON,
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, PHOSPHORYLATION AT SER-53;
RP SER-85; SER-172; SER-202; SER-264; SER-270; SER-325 AND SER-349, AND
RP MUTAGENESIS OF SER-53; SER-85; SER-172; SER-202; SER-264; SER-270; SER-325
RP AND SER-349.
RX PubMed=26540204; DOI=10.1371/journal.pgen.1005642;
RA Lin T., Pan P.Y., Lai Y.T., Chiang K.W., Hsieh H.L., Wu Y.P., Ke J.M.,
RA Lee M.C., Liao S.S., Shih H.T., Tang C.Y., Yang S.B., Cheng H.C., Wu J.T.,
RA Jan Y.N., Lee H.H.;
RT "Spindle-F is the central mediator of Ik2 kinase-dependent dendrite pruning
RT in Drosophila sensory neurons.";
RL PLoS Genet. 11:E1005642-E1005642(2015).
CC -!- FUNCTION: Plays a role in oocyte axis determination and microtubule
CC organization during oogenesis (PubMed:16540510, PubMed:24019068). Also
CC required for polarized organization of the bristle (PubMed:19917727).
CC Required, with jvl, for activation of the kinase IKKepsilon in the germ
CC line (PubMed:24019068). Also required for localization of IKKepsilon to
CC the distal tip of elongating bristles by acting as an adapter linking
CC IKKepsilon and cytoplasmic dynein (PubMed:26092846). Involved in
CC dendrite pruning in larval sensory neurons during metamorphosis
CC (PubMed:26540204). {ECO:0000269|PubMed:16540510,
CC ECO:0000269|PubMed:19917727, ECO:0000269|PubMed:24019068,
CC ECO:0000269|PubMed:26092846, ECO:0000269|PubMed:26540204}.
CC -!- SUBUNIT: Forms homooligomers (PubMed:26540204). Interacts with the
CC dynein light chain ctp (PubMed:16540510). Interacts (via C-terminus)
CC with IKKepsilon; this leads to phosphorylation of spn-F
CC (PubMed:18796167, PubMed:26092846). Forms ternary complexes with ctp
CC and IKKepsilon; this is required for spn-F redistribution from puncta
CC in larval neurons and for dendrite pruning (PubMed:26092846,
CC PubMed:26540204). Interacts with ctp and IKKepsilon through distinct
CC regions (PubMed:26092846). Interacts (via C-terminus) with jvl
CC (PubMed:24019068). {ECO:0000269|PubMed:16540510,
CC ECO:0000269|PubMed:18796167, ECO:0000269|PubMed:24019068,
CC ECO:0000269|PubMed:26092846, ECO:0000269|PubMed:26540204}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16540510}. Cytoplasm {ECO:0000269|PubMed:18796167}.
CC Cell projection, axon {ECO:0000269|PubMed:26540204}. Cell projection,
CC dendrite {ECO:0000269|PubMed:26540204}. Perikaryon
CC {ECO:0000269|PubMed:26540204}. Note=Localizes to the minus ends of
CC microtubules in oocytes (PubMed:16540510). Found in a punctate pattern
CC colocalized with IKKepsilon in nurse cells (PubMed:16540510,
CC PubMed:18796167). Displays a punctate pattern in the soma, dendrites
CC and axons of larval C4da neurons but becomes dispersed in pupal neurons
CC which is necessary for dendrite pruning (PubMed:26540204).
CC {ECO:0000269|PubMed:16540510, ECO:0000269|PubMed:18796167,
CC ECO:0000269|PubMed:26540204}.
CC -!- TISSUE SPECIFICITY: In pupal bristles, localizes to the bristle tip
CC throughout the elongation period (at protein level).
CC {ECO:0000269|PubMed:19917727, ECO:0000269|PubMed:26092846}.
CC -!- PTM: Phosphorylated by IKKepsilon (PubMed:18796167, PubMed:26540204).
CC Phosphorylation is required for spn-F neuronal distribution and
CC dendrite pruning and reduces spn-F homooligomerization
CC (PubMed:26540204). It does not lead to spn-F degradation
CC (PubMed:18796167). {ECO:0000269|PubMed:18796167,
CC ECO:0000269|PubMed:26540204}.
CC -!- DISRUPTION PHENOTYPE: Mutant females produce a ventralized eggshell. A
CC fraction of eggs are fertilized and the resulting embryos have a
CC variety of pattern abnormalities. In mutant ovaries, grk RNA is
CC mislocalized during mid-oogenesis and grk protein levels are reduced.
CC Defects in microtubule organization around the oocyte nucleus
CC (PubMed:16540510). Bristles are considerably shorter and thicker than
CC normal and have an altered morphology and growth direction
CC (PubMed:16540510, PubMed:19917727, PubMed:26092846). Actin bundles are
CC poorly oriented in mutant bristles (PubMed:19917727). Defective
CC dendrite pruning in C4da sensory neurons with primary dendrites
CC remaining connected to the cell body in contrast to wild-type neurons
CC where dendrites are pruned by 18 hours after puparium formation
CC (PubMed:26540204). {ECO:0000269|PubMed:16540510,
CC ECO:0000269|PubMed:19917727, ECO:0000269|PubMed:26092846,
CC ECO:0000269|PubMed:26540204}.
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DR EMBL; AE014297; AAF57139.1; -; Genomic_DNA.
DR EMBL; AY061046; AAL28594.1; -; mRNA.
DR RefSeq; NP_651858.1; NM_143601.3.
DR AlphaFoldDB; Q9V9Y9; -.
DR SMR; Q9V9Y9; -.
DR IntAct; Q9V9Y9; 10.
DR STRING; 7227.FBpp0085122; -.
DR iPTMnet; Q9V9Y9; -.
DR DNASU; 43700; -.
DR EnsemblMetazoa; FBtr0085760; FBpp0085122; FBgn0086362.
DR GeneID; 43700; -.
DR KEGG; dme:Dmel_CG12114; -.
DR UCSC; CG12114-RA; d. melanogaster.
DR CTD; 43700; -.
DR FlyBase; FBgn0086362; spn-F.
DR VEuPathDB; VectorBase:FBgn0086362; -.
DR eggNOG; ENOG502S41T; Eukaryota.
DR HOGENOM; CLU_728759_0_0_1; -.
DR InParanoid; Q9V9Y9; -.
DR OMA; AKRCMDG; -.
DR OrthoDB; 996459at2759; -.
DR PhylomeDB; Q9V9Y9; -.
DR SignaLink; Q9V9Y9; -.
DR BioGRID-ORCS; 43700; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43700; -.
DR PRO; PR:Q9V9Y9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0086362; Expressed in secondary oocyte and 24 other tissues.
DR ExpressionAtlas; Q9V9Y9; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:FlyBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0007314; P:oocyte anterior/posterior axis specification; IMP:FlyBase.
DR GO; GO:0007309; P:oocyte axis specification; IMP:FlyBase.
DR GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IDA:FlyBase.
DR GO; GO:0008103; P:oocyte microtubule cytoskeleton polarization; IMP:FlyBase.
DR GO; GO:1904801; P:positive regulation of neuron remodeling; IMP:FlyBase.
DR GO; GO:0008104; P:protein localization; IMP:UniProtKB.
DR GO; GO:0007317; P:regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1.
DR Pfam; PF18112; Zn-C2H2_12; 1.
DR PROSITE; PS51905; ZF_UBZ1; 1.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Differentiation;
KW Metal-binding; Neurogenesis; Oogenesis; Phosphoprotein; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..364
FT /note="Protein spindle-F"
FT /id="PRO_0000437139"
FT ZN_FING 310..336
FT /note="UBZ1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..114
FT /evidence="ECO:0000255"
FT COILED 210..243
FT /evidence="ECO:0000255"
FT COMPBIAS 9..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT BINDING 336
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26540204"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26540204"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26540204"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26540204"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26540204"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26540204"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26540204"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:26540204"
FT MUTAGEN 53
FT /note="S->A: Abolishes phosphorylation but does not affect
FT interaction with IKKepsilon; when associated with A-85; A-
FT 172; A-202; A-264; A-270; A-325 and A-349."
FT /evidence="ECO:0000269|PubMed:26540204"
FT MUTAGEN 85
FT /note="S->A: Abolishes phosphorylation but does not affect
FT interaction with IKKepsilon; when associated with A-53; A-
FT 172; A-202; A-264; A-270; A-325 and A-349."
FT /evidence="ECO:0000269|PubMed:26540204"
FT MUTAGEN 172
FT /note="S->A: Abolishes phosphorylation but does not affect
FT interaction with IKKepsilon; when associated with A-53; A-
FT 85; A-202; A-264; A-270; A-325 and A-349."
FT /evidence="ECO:0000269|PubMed:26540204"
FT MUTAGEN 202
FT /note="S->A: Abolishes phosphorylation but does not affect
FT interaction with IKKepsilon; when associated with A-53; A-
FT 85; A-172; A-264; A-270; A-325 and A-349."
FT /evidence="ECO:0000269|PubMed:26540204"
FT MUTAGEN 264
FT /note="S->A: Abolishes phosphorylation but does not affect
FT interaction with IKKepsilon; when associated with A-53; A-
FT 85; A-172; A-202; A-270; A-325 and A-349."
FT /evidence="ECO:0000269|PubMed:26540204"
FT MUTAGEN 270
FT /note="S->A: Abolishes phosphorylation but does not affect
FT interaction with IKKepsilon; when associated with A-53; A-
FT 85; A-172; A-202; A-264; A-325 and A-349."
FT /evidence="ECO:0000269|PubMed:26540204"
FT MUTAGEN 325
FT /note="S->A: Abolishes phosphorylation but does not affect
FT interaction with IKKepsilon; when associated with A-53; A-
FT 85; A-172; A-202; A-264; A-270 and A-349."
FT /evidence="ECO:0000269|PubMed:26540204"
FT MUTAGEN 349
FT /note="S->A: Abolishes phosphorylation but does not affect
FT interaction with IKKepsilon; when associated with A-53; A-
FT 85; A-172; A-202; A-264; A-270 and A-325."
FT /evidence="ECO:0000269|PubMed:26540204"
SQ SEQUENCE 364 AA; 40907 MW; 0054924096255480 CRC64;
MEASAAKITP MASSMSASGS TNSPSSEKMN YALQVALQTI KERCIQLQRR VASMEEENQQ
LREASSRSEG APRANEIGVT GDVLSLKAQV SELQRQKEQL EEHIGMVSNE NRRLWSRLSQ
ISKDQQLNAL PSSTDSRAQQ NQNLVRSKTF TQHSPNPHLR QKMLSDGIKD LSLEEIALDD
FGASSEELGY PYNLQKVEET TSEPDANVDA KRCLDGLQEL RREAMKQQQE LRSVMTLLEN
RIALKPCPEC AQKTIKKPEM ADKSLETDDS LTSELKNYES QHNGHNGTPP SQRINIIQEK
IKADAADAME KTCPMCGKQY SSQVSFNAFR EHVEMHFIDD ALELESENSI ERQFEFVSHA
VGDF
