NUTC_DROME
ID NUTC_DROME Reviewed; 314 AA.
AC Q8SX86; Q9VZM8;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Protein nutcracker {ECO:0000312|EMBL:AAF47792.2};
GN Name=ntc {ECO:0000312|EMBL:AAF47792.2, ECO:0000312|FlyBase:FBgn0035461};
GN ORFNames=CG10855;
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] {ECO:0000312|EMBL:AAF47792.2}
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 [2] {ECO:0000312|EMBL:AAF47792.2}
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 [3] {ECO:0000312|EMBL:AAM11137.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM11137.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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, IDENTIFICATION IN A COMPLEX WITH SKPA AND CUL1, INTERACTION WITH
RP BRUCE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=20392747; DOI=10.1242/dev.050088;
RA Bader M., Arama E., Steller H.;
RT "A novel F-box protein is required for caspase activation during cellular
RT remodeling in Drosophila.";
RL Development 137:1679-1688(2010).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PROSALPHA7 AND PI31, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF VAL-188.
RX PubMed=21529711; DOI=10.1016/j.cell.2011.03.021;
RA Bader M., Benjamin S., Wapinski O.L., Smith D.M., Goldberg A.L.,
RA Steller H.;
RT "A conserved F box regulatory complex controls proteasome activity in
RT Drosophila.";
RL Cell 145:371-382(2011).
CC -!- FUNCTION: Functions together with PI31 to control non-apoptotic caspase
CC activation during sperm individualization. Positively regulates PI31
CC stability. {ECO:0000269|PubMed:20392747, ECO:0000269|PubMed:21529711}.
CC -!- SUBUNIT: Component of an SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-
CC protein ligase complex, at least composed of ntc, skpA and Cul1.
CC Interacts (via F-box domain) with skpA and Cul1. Interacts with
CC Prosalpha7 and PI31. Interacts with Bruce.
CC {ECO:0000269|PubMed:20392747, ECO:0000269|PubMed:21529711}.
CC -!- INTERACTION:
CC Q8SX86; Q9V637: PI31; NbExp=6; IntAct=EBI-137714, EBI-144377;
CC Q8SX86; O77430: SkpA; NbExp=3; IntAct=EBI-137714, EBI-180180;
CC Q8SX86; Q7KJ69: SkpB; NbExp=3; IntAct=EBI-137714, EBI-133084;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20392747,
CC ECO:0000269|PubMed:21529711}. Note=In the spermatid, colocalizes with
CC Cul1 at the actin-based individualization complex and the cystic bulge.
CC {ECO:0000269|PubMed:20392747, ECO:0000269|PubMed:21529711}.
CC -!- TISSUE SPECIFICITY: Expressed in testis (at protein level).
CC {ECO:0000269|PubMed:20392747, ECO:0000269|PubMed:21529711}.
CC -!- DISRUPTION PHENOTYPE: Male sterility. {ECO:0000269|PubMed:20392747}.
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DR EMBL; AE014296; AAF47792.2; -; Genomic_DNA.
DR EMBL; AY094784; AAM11137.1; -; mRNA.
DR RefSeq; NP_647829.1; NM_139572.3.
DR AlphaFoldDB; Q8SX86; -.
DR BioGRID; 63933; 8.
DR DIP; DIP-18929N; -.
DR IntAct; Q8SX86; 6.
DR STRING; 7227.FBpp0073041; -.
DR PaxDb; Q8SX86; -.
DR PRIDE; Q8SX86; -.
DR EnsemblMetazoa; FBtr0073185; FBpp0073041; FBgn0035461.
DR GeneID; 38443; -.
DR KEGG; dme:Dmel_CG10855; -.
DR UCSC; CG10855-RA; d. melanogaster.
DR CTD; 38443; -.
DR FlyBase; FBgn0035461; ntc.
DR VEuPathDB; VectorBase:FBgn0035461; -.
DR eggNOG; ENOG502T9P0; Eukaryota.
DR HOGENOM; CLU_076982_0_0_1; -.
DR InParanoid; Q8SX86; -.
DR OMA; YFEIFRY; -.
DR OrthoDB; 1056733at2759; -.
DR PhylomeDB; Q8SX86; -.
DR SignaLink; Q8SX86; -.
DR BioGRID-ORCS; 38443; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 38443; -.
DR PRO; PR:Q8SX86; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0035461; Expressed in testis and 24 other tissues.
DR Genevisible; Q8SX86; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:FlyBase.
DR GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IBA:GO_Central.
DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IMP:FlyBase.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISM:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR Pfam; PF00646; F-box; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome.
FT CHAIN 1..314
FT /note="Protein nutcracker"
FT /id="PRO_0000424890"
FT DOMAIN 264..309
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..314
FT /note="Required for interaction with skpA and Cul1, but not
FT with PI31"
FT /evidence="ECO:0000269|PubMed:20392747,
FT ECO:0000269|PubMed:21529711"
FT COMPBIAS 15..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 188
FT /note="V->E: Reduces interaction with PI31."
FT /evidence="ECO:0000269|PubMed:21529711"
SQ SEQUENCE 314 AA; 36487 MW; 5D0F06B57D952BF9 CRC64;
MSDTKSEIEG FIAIPTTSGE QQQQQPQQQQ NEQQVVGTKD IKAPDQVGKK QRPRLIQEKS
TQETNPLILE HATLEWVPQH MDKLLNQYQE CRKMPAAEWL HLLTYLVALE CGFVEEETFA
QKRHLIQPVP SFSSFHAQNV RILSEQPARY EVCFNDTVYI MRLRTLLDKH APEETSLVAA
LQCRLMAVSL GDQLMITLSP APPSKEPGYS VSLSIGRYVL NIQAKNKPIY HRFRKLDELS
YQLKQHLFQP MRSQQLMQME MKLQPSLLGL PDELYFEIFR YLDKSQLNVV ARVNRHLHFY
SKEVERKRLK GGRS
