SKEL2_DROME
ID SKEL2_DROME Reviewed; 1503 AA.
AC Q9GPJ1; Q8T0R5;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Protein Skeletor, isoforms D/E;
DE Flags: Precursor;
GN Name=Skeletor; ORFNames=CG43161;
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|EMBL:AAG46059.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S {ECO:0000269|PubMed:11134070};
RC TISSUE=Embryo {ECO:0000269|PubMed:11134070};
RX PubMed=11134070; DOI=10.1083/jcb.151.7.1401;
RA Walker D.L., Wang D., Jin Y., Rath U., Wang Y., Johansen J., Johansen K.M.;
RT "Skeletor, a novel chromosomal protein that redistributes during mitosis
RT provides evidence for the formation of a spindle matrix.";
RL J. Cell Biol. 151:1401-1411(2000).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305}
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Head {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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15367580; DOI=10.1242/jcs.01334;
RA Wilson P.G., Simmons R., Saighal S.;
RT "Novel nuclear defects in KLP61F-deficient mutants in Drosophila are
RT partially suppressed by loss of Ncd function.";
RL J. Cell Sci. 117:4921-4933(2004).
RN [6]
RP INTERACTION WITH CHRO, AND SUBCELLULAR LOCATION.
RX PubMed=15389869; DOI=10.1002/jcb.20243;
RA Rath U., Wang D., Ding Y., Xu Y.Z., Qi H., Blacketer M.J., Girton J.,
RA Johansen J., Johansen K.M.;
RT "Chromator, a novel and essential chromodomain protein interacts directly
RT with the putative spindle matrix protein skeletor.";
RL J. Cell. Biochem. 93:1033-1047(2004).
RN [7]
RP INTERACTION WITH MTOR, AND SUBCELLULAR LOCATION.
RX PubMed=15356261; DOI=10.1091/mbc.e04-07-0579;
RA Qi H., Rath U., Wang D., Xu Y.Z., Ding Y., Zhang W., Blacketer M.J.,
RA Paddy M.R., Girton J., Johansen J., Johansen K.M.;
RT "Megator, an essential coiled-coil protein that localizes to the putative
RT spindle matrix during mitosis in Drosophila.";
RL Mol. Biol. Cell 15:4854-4865(2004).
CC -!- FUNCTION: Provides structural support to stabilize and organize the
CC microtubule spindle during mitosis (within embryonic somatic cells) and
CC meiosis (within spermatocytes). The role in mitosis regulation depends
CC on the Ran pathway. {ECO:0000269|PubMed:11134070,
CC ECO:0000269|PubMed:15367580}.
CC -!- SUBUNIT: Interacts with Chro and Mtor as part of a macromolecular
CC complex forming the spindle matrix. Chro colocalizes with Skeletor on
CC the chromosomes at interphase and on spindle during metaphase.
CC {ECO:0000269|PubMed:15356261, ECO:0000269|PubMed:15389869}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Nucleus,
CC nucleolus. Chromosome. Note=Part of a macromolecular complex forming
CC the spindle matrix. During mitosis, associated with chromatin at
CC interphase, redistributes to the spindle structure at prophase
CC (preceding the formation of the microtubule spindle) through to
CC anaphase. Extends from one end of the spindle to the other during
CC metaphase and anaphase, coaligns with the microtubule spindle.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=E;
CC IsoId=Q9GPJ1-1; Sequence=Displayed;
CC Name=D; Synonyms=ORF2;
CC IsoId=Q9GPJ1-2; Sequence=VSP_041898;
CC Name=B; Synonyms=ORF1a;
CC IsoId=Q9VGY6-2; Sequence=External;
CC Name=C; Synonyms=ORF1b;
CC IsoId=Q9VGY6-1; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: Isoform D is expressed during embryonic
CC development. {ECO:0000269|PubMed:11134070}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG46059.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAL39254.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAO41539.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF321289; AAG46059.1; ALT_SEQ; mRNA.
DR EMBL; AE014297; AAO41539.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY069109; AAL39254.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001027173.2; NM_001032002.2. [Q9GPJ1-2]
DR RefSeq; NP_001247027.1; NM_001260098.1. [Q9GPJ1-1]
DR AlphaFoldDB; Q9GPJ1; -.
DR SMR; Q9GPJ1; -.
DR BioGRID; 534156; 1.
DR STRING; 7227.FBpp0296946; -.
DR PaxDb; Q9GPJ1; -.
DR DNASU; 3772559; -.
DR EnsemblMetazoa; FBtr0305665; FBpp0296945; FBgn0262717. [Q9GPJ1-2]
DR EnsemblMetazoa; FBtr0305666; FBpp0296946; FBgn0262717. [Q9GPJ1-1]
DR GeneID; 3772559; -.
DR UCSC; CG33676-RA; d. melanogaster. [Q9GPJ1-1]
DR CTD; 3772559; -.
DR FlyBase; FBgn0262717; Skeletor.
DR VEuPathDB; VectorBase:FBgn0262717; -.
DR eggNOG; KOG4731; Eukaryota.
DR HOGENOM; CLU_004063_0_0_1; -.
DR InParanoid; Q9GPJ1; -.
DR PhylomeDB; Q9GPJ1; -.
DR BioGRID-ORCS; 3772559; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 3772559; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0262717; Expressed in capitellum (Drosophila) and 9 other tissues.
DR ExpressionAtlas; Q9GPJ1; baseline and differential.
DR Genevisible; Q9GPJ1; DM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006997; P:nucleus organization; NAS:FlyBase.
DR GO; GO:0051225; P:spindle assembly; IDA:FlyBase.
DR CDD; cd09631; DOMON_DOH; 1.
DR InterPro; IPR019545; DM13_domain.
DR InterPro; IPR045266; DOH_DOMON.
DR InterPro; IPR005018; DOMON_domain.
DR Pfam; PF10517; DM13; 2.
DR SMART; SM00686; DM13; 2.
DR SMART; SM00664; DoH; 1.
DR PROSITE; PS51549; DM13; 2.
DR PROSITE; PS50836; DOMON; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW Cytoskeleton; Meiosis; Microtubule; Mitosis; Nucleus; Reference proteome;
KW Repeat; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..1503
FT /note="Protein Skeletor, isoforms D/E"
FT /id="PRO_0000097778"
FT DOMAIN 34..143
FT /note="DM13 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00882"
FT DOMAIN 151..258
FT /note="DM13 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00882"
FT DOMAIN 287..419
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT REGION 451..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1426..1503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..791
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:11134070,
FT ECO:0000303|PubMed:12537569"
FT /id="VSP_041898"
SQ SEQUENCE 1503 AA; 165043 MW; B5321298E35819E5 CRC64;
MLAMKDKPWL LLFGLLAALS CLASFGDAAY PYYGTKIGAL TRLHHGVSGD VYAVDSRTIF
IKKFNYDGEA PAAYFYVGNT ARPSNEGAAR LRDERGGTAS LTRRYRNKDV TLSLPEGKTL
RDIKWFSVWC DEFAVNFGDV SIPPNLDFPR PQKISALRGV HGVSSDNIVI VDAQTLLVPN
FSYDGEAPDA KFWVGRGQRP TSDGLRIPDE NGKENPLRRY ERKTIVLTLP EDLTIFDIGH
FGVWCEAFTV DFGHVRLPEG LNVPPSLKML GISPQSKLNC EVLYDDLAFE VRWAVAGESI
VVQLVAKLEP NHYMSFGISP NKNISQMIGA DAVVAWVDPQ TGNGFATDYF LEGKAQCSGG
RGACPDTKIS EKTNSIRLLN AAMVNGYSIV TYQRSLAATD RLDLPISITG AESVVWAIGP
LNDYQEVSFH TFYNKHLHQI EFGRQPKWNC PLPEGARGNS NSSEQEDSAP AAQSSTGGAG
YPPAGRPNVE PDEEFYENRA EALHRQPPQR RQETAIITQR RPVPTPKPVN SNGAWDIPAI
QCHEPEDGVF YAQMGPTGGK HGYPAITGHV GWGISWYING LLIPEIHVVR GKTYTFVVEG
GNNPDIPAKY HPFYISDDPV GGYEHKREEE KKAVRIYAGV HRSRSGQVTP TGVGRLCNWT
PDVEGPPADD YQSFGAYQRT LTLKCDAGEP GVITWKPDRN TPDTVYYHCF THRYLGWKIH
VHDSCDSEAG GLKGAASERH EIRLPAKATV AEPAPVHEDY AGEASVRHET KVSANDNFLL
KHQTDLIKNH NMNGTPPKLS FEITKSSEIT KLISDGIRAA EALEESLLRN PNLNPNHPNQ
NPIPNPHQKP NVTPTEISSR PEILLGETHA HTLNASPSAS AYPSPSATLP SANLKLPILA
AGPHLIHHPP HLHRLHHQPQ HAPHPHVHLH HHNLTANLPA LAQKTIGLSE FLRPPQNAPL
FHPVKLPGRR PFPAPIKKVP ASRPILPQQH PHLHPHPQQH PVLLQQQPSL IVSHYRKPIP
GLLKPFVKEK PFPLQPLAAS VLLLGQPTEL GGLNNKGERL KIKGKPKIPV PYVDLEPQGS
LQNTAIFNQP GGKGKGDQKP KASSVSISTT PIPLVKRPTV KEPSQEEIAS MRPAVNQGFK
PDTVIVESGF KPIVRTDGTG VQLPKEIIDQ VAHRREDPGT EIDEVMETDT LFLAAQQGGS
ETQSFEPMFI PSPLDSTNAT KVLRVNVKEV SPTASALRLP SAALEHALPS ASELIKPTLD
ELFAEDLNEE ELEMEPMPVA DDVESLEETT KKDAVTTTIN IPRNTTKKPD PDLLEDLFGP
DEEELYADEL ELDMDDRVAA AAERIDTYYL PPDNRKIPDT RVPSGALYTF DGKSVVDSSL
VLPPKLDAPD NANVHQRHAQ YGLTPLEQLV RTTPQFGVYR GELPQEFRGT EPQPVSEYSH
PAPFSRTTPV FSSSSGSTIY PYSSSTGAST STVSSSASSP LSSSSLRPIS TKLQLLKPEG
RRA
