SKEL1_DROME
ID SKEL1_DROME Reviewed; 784 AA.
AC Q9VGY6; B9EQQ8; Q7YU64; Q9VGY7;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Protein Skeletor, isoforms B/C;
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:AAF54536.2};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND C), FUNCTION, SUBCELLULAR
RP LOCATION, AND 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 C).
RC STRAIN=Berkeley {ECO:0000305}; TISSUE=Embryo {ECO:0000305};
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Booth B.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.E.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 -!- 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=C; Synonyms=ORF1b {ECO:0000269|PubMed:11134070};
CC IsoId=Q9VGY6-1; Sequence=Displayed;
CC Name=B; Synonyms=ORF1a {ECO:0000269|PubMed:11134070};
CC IsoId=Q9VGY6-2; Sequence=VSP_050746, VSP_050747;
CC Name=D; Synonyms=ORF2;
CC IsoId=Q9GPJ1-2; Sequence=External;
CC Name=E;
CC IsoId=Q9GPJ1-1; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: Isoform B is expressed during embryonic
CC development. {ECO:0000269|PubMed:11134070}.
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DR EMBL; AF321290; AAG46060.1; -; mRNA.
DR EMBL; AE014297; AAF54535.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF54536.2; -; Genomic_DNA.
DR EMBL; BT009971; AAQ22440.1; -; mRNA.
DR EMBL; BT057983; ACM16693.1; -; mRNA.
DR RefSeq; NP_001027171.1; NM_001032000.2. [Q9VGY6-1]
DR RefSeq; NP_001027172.1; NM_001032001.2. [Q9VGY6-2]
DR AlphaFoldDB; Q9VGY6; -.
DR SMR; Q9VGY6; -.
DR BioGRID; 534156; 1.
DR IntAct; Q9VGY6; 1.
DR DNASU; 3772559; -.
DR EnsemblMetazoa; FBtr0305663; FBpp0296943; FBgn0262717. [Q9VGY6-2]
DR EnsemblMetazoa; FBtr0305664; FBpp0296944; FBgn0262717. [Q9VGY6-1]
DR GeneID; 3772559; -.
DR KEGG; dme:Dmel_CG43161; -.
DR UCSC; CG14681-RA; d. melanogaster. [Q9VGY6-1]
DR CTD; 3772559; -.
DR FlyBase; FBgn0262717; Skeletor.
DR VEuPathDB; VectorBase:FBgn0262717; -.
DR HOGENOM; CLU_007940_0_0_1; -.
DR OMA; RHETKMA; -.
DR PhylomeDB; Q9VGY6; -.
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; Q9VGY6; baseline and differential.
DR Genevisible; Q9VGY6; 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: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..784
FT /note="Protein Skeletor, isoforms B/C"
FT /id="PRO_0000021113"
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 ECO:0000305"
FT REGION 451..491
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 VAR_SEQ 276..289
FT /note="SKLNCEVLYDDLAF -> VKKNASQILSELQR (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11134070"
FT /id="VSP_050746"
FT VAR_SEQ 290..784
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11134070"
FT /id="VSP_050747"
FT CONFLICT 138
FT /note="G -> S (in Ref. 4; AAQ22440)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 784 AA; 86562 MW; 5757CD4475B5A3B2 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 KMASALLRLS
RRAY
