ASP_DROME
ID ASP_DROME Reviewed; 1954 AA.
AC Q9VC45; O01401; Q8SX66;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Protein abnormal spindle;
GN Name=asp {ECO:0000312|EMBL:AAF56330.3}; ORFNames=CG6875;
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:AAF56330.3}
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAF56330.3}
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAB51540.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 94-1954, FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Oregon-R {ECO:0000312|EMBL:AAB51540.1};
RX PubMed=9151690; DOI=10.1083/jcb.137.4.881;
RA Saunders R.D.C., do Carmo Avides M., Howard T.I.A., Gonzalez C.,
RA Glover D.M.;
RT "The Drosophila gene abnormal spindle encodes a novel microtubule-
RT associated protein that associates with the polar regions of the mitotic
RT spindle.";
RL J. Cell Biol. 137:881-890(1997).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAM11178.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 700-1954.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM11178.1};
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 [5] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10073938; DOI=10.1126/science.283.5408.1733;
RA do Carmo Avides M., Glover D.M.;
RT "Abnormal spindle protein, Asp, and the integrity of mitotic centrosomal
RT microtubule organizing centers.";
RL Science 283:1733-1735(1999).
RN [6]
RP FUNCTION.
RX PubMed=15242765; DOI=10.1016/j.yexcr.2004.03.054;
RA Riparbelli M.G., Massarelli C., Robbins L.G., Callaini G.;
RT "The abnormal spindle protein is required for germ cell mitosis and oocyte
RT differentiation during Drosophila oogenesis.";
RL Exp. Cell Res. 298:96-106(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-360; THR-364;
RP SER-388; SER-390; SER-395; SER-398; SER-491; SER-495; SER-497; SER-501;
RP SER-504 AND SER-514, AND IDENTIFICATION BY 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: Required to maintain the structure of the centrosomal
CC microtubule organizing center (MTOC) during mitosis. May have a
CC preferential role in regulating neurogenesis. Required for germ cell
CC mitosis and oocyte differentiation. {ECO:0000269|PubMed:10073938,
CC ECO:0000269|PubMed:15242765, ECO:0000269|PubMed:9151690}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton,
CC spindle. Note=During interphase in syncytial embryos distribution is
CC cytoplasmic. On entering mitosis, moves to polar regions of the spindle
CC immediately surrounding the centrosome. At telophase, migrates to
CC microtubules on the spindle side of both daughter nuclei. The nuclear-
CC cytoplasmic distribution could be regulated by the availability of
CC calmodulin.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
CC embryos. {ECO:0000269|PubMed:9151690}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM11178.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AE014297; AAF56330.3; -; Genomic_DNA.
DR EMBL; U95171; AAB51540.1; -; mRNA.
DR EMBL; AY094825; AAM11178.1; ALT_SEQ; mRNA.
DR PIR; T13845; T13845.
DR RefSeq; NP_524488.3; NM_079764.3.
DR AlphaFoldDB; Q9VC45; -.
DR SMR; Q9VC45; -.
DR BioGRID; 67871; 18.
DR IntAct; Q9VC45; 7.
DR MINT; Q9VC45; -.
DR STRING; 7227.FBpp0084071; -.
DR iPTMnet; Q9VC45; -.
DR PaxDb; Q9VC45; -.
DR PRIDE; Q9VC45; -.
DR EnsemblMetazoa; FBtr0084692; FBpp0084071; FBgn0000140.
DR GeneID; 42946; -.
DR KEGG; dme:Dmel_CG6875; -.
DR CTD; 42946; -.
DR FlyBase; FBgn0000140; asp.
DR VEuPathDB; VectorBase:FBgn0000140; -.
DR eggNOG; KOG0165; Eukaryota.
DR GeneTree; ENSGT00560000077332; -.
DR HOGENOM; CLU_231302_0_0_1; -.
DR InParanoid; Q9VC45; -.
DR OMA; TFCYGIM; -.
DR OrthoDB; 482623at2759; -.
DR PhylomeDB; Q9VC45; -.
DR SignaLink; Q9VC45; -.
DR BioGRID-ORCS; 42946; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42946; -.
DR PRO; PR:Q9VC45; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0000140; Expressed in egg chamber and 25 other tissues.
DR ExpressionAtlas; Q9VC45; baseline and differential.
DR Genevisible; Q9VC45; DM.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; IDA:FlyBase.
DR GO; GO:0005815; C:microtubule organizing center; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000922; C:spindle pole; IDA:FlyBase.
DR GO; GO:0005516; F:calmodulin binding; IDA:FlyBase.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0032027; F:myosin light chain binding; IPI:FlyBase.
DR GO; GO:0030037; P:actin filament reorganization involved in cell cycle; IMP:FlyBase.
DR GO; GO:0030954; P:astral microtubule nucleation; IMP:FlyBase.
DR GO; GO:0048854; P:brain morphogenesis; IMP:FlyBase.
DR GO; GO:0051298; P:centrosome duplication; IMP:FlyBase.
DR GO; GO:0051642; P:centrosome localization; IMP:FlyBase.
DR GO; GO:0007282; P:cystoblast division; IMP:FlyBase.
DR GO; GO:0051295; P:establishment of meiotic spindle localization; IMP:FlyBase.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:FlyBase.
DR GO; GO:0048132; P:female germ-line stem cell asymmetric division; IMP:FlyBase.
DR GO; GO:0030706; P:germarium-derived oocyte differentiation; IMP:FlyBase.
DR GO; GO:0051383; P:kinetochore organization; IMP:FlyBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:0007097; P:nuclear migration; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IMP:FlyBase.
DR GO; GO:0030723; P:ovarian fusome organization; IMP:FlyBase.
DR GO; GO:0007051; P:spindle organization; IMP:FlyBase.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR InterPro; IPR031549; ASH.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR Pfam; PF15780; ASH; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00612; IQ; 7.
DR SMART; SM00033; CH; 1.
DR SMART; SM00015; IQ; 16.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS50096; IQ; 5.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Developmental protein; Differentiation; Microtubule; Mitosis;
KW Nucleus; Oogenesis; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1954
FT /note="Protein abnormal spindle"
FT /id="PRO_0000191342"
FT DOMAIN 836..968
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1004..1033
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1386..1415
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1467..1496
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1656..1687
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1690..1721
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 134..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 476..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1614..1641
FT /evidence="ECO:0000255"
FT COMPBIAS 529..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 364
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 497
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 504
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 811
FT /note="L -> P (in Ref. 3; AAB51540)"
FT /evidence="ECO:0000305"
FT CONFLICT 898
FT /note="M -> V (in Ref. 3; AAB51540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1129
FT /note="S -> T (in Ref. 3; AAB51540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1138..1139
FT /note="QQ -> HE (in Ref. 3; AAB51540)"
FT /evidence="ECO:0000305"
FT CONFLICT 1761
FT /note="R -> Q (in Ref. 3; AAB51540)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1954 AA; 230180 MW; 4912B4E20CA9E659 CRC64;
MSAFEITVTP SRLKQKKRAE GREPAVVVMA PFSAKAIVQF EDVPITKTAR RQVRVLNPSD
DDIEVKVMKA IREEHNLSLE WMEHTVPARD EVSMELVWSP VLEVACKETL QLIDNRNFRK
EVMIILKSKS NQPVKNPRKF PTVGKTLQLK SPTGAGKTMK SVVSAAVQQK KRMSAAAAPP
SKQTWRVTAP SRPAAWAHPP PQAPLVEKNV YKTPQEEPVY ISPQPRSLKE NLSPMTPGNL
LDVIDNLRFT PLTETRGKGQ ATIFPDNLAA WPTPTLKGNV KSCANDMRPR RITPDDLEDQ
PATNKTFDVK HSETINISLD TLDCSRIDGQ PHTPLNKTTT IVHATHTRAL ACIHEEEGPS
PPRTPTKSAI HDLKRDIKLV GSPLRKYSES MKDLSLLSPQ TKYAIQGSMP NLNEMKIRSI
EQNRYYQEQQ IQIKAKDLNS SSSSEASLAG QQEFLFNHSE ILAQSSRFNL HEVGRKSVKG
SPVKNPHKRR SHELSFSDAP SNESLYRNET VAISPPKKQR VEDTTLPRSA APANASARSS
SAHAWPHAQS KKFKLAQTMS LMKKPATPRK VRDTSIQPSV KLYDSELYMQ TCINPDPFAA
TTTIDPFLAS TMYLDEQAVD RHQADFKKWL NALVSIPADL DADLNNKIDV GKLFNEVRNK
ELVVAPTKEE QSMNYLTKYR LETLRKAAVE LFFSEQMRLP CSKVAVYVNK QALRIRSDRN
LHLDVVMQRT ILELLLCFNP LWLRLGLEVV FGEKIQMQSN RDIVGLSTFI LNRLFRNKCE
EQRYSKAYTL TEEYAETIKK HSLQKILFLL LFLDQAKQKR IVKHNPCLFV KKSPHKETKD
ILLRFSSELL ANIGDITREL RRLGYVLQHR QTFLDEFDYA FNNLAVDLRD GVRLTRVMEV
ILLRDDLTRQ LRVPAISRLQ RIFNVKLALG ALGEANFQLG GDIAAQDIVD GHREKTLSLL
WQLIYKFRSP KFHAAATVLQ KWWRRHWLHV VIQRRIRHKE LMRRHRAATV IQAVFRGHQM
RKYVKLFKTE RTQAAIILQK FTRRYLAQKQ LYQSYHSIIT IQRWWRAQQL GRQHRQRFVE
LREAAIFLQR IWRRRLFAKK LLAAAETARL QRSQKQQAAA SYIQMQWRSY QLGRIQRQQF
LRQRDLIMFV QRRMRSKWSM LEQRKEFQQL KRAAINIQQR WRAKLSMRKC NADYLALRSS
VLKVQAYRKA TIQMRIDRNH YYSLRKNVIC LQQRLRAIMK MREQRENYLR LRNASILVQK
RYRMRQQMIQ DRNAYLRTRK CIINVQRRWR ATLQMRRERK NYLHLQTTTK RIQIKFRAKR
EMKKQRAEFL QLKKVTLVVQ KRRRALLQMR KERQEYLHLR EVTIKLQRRF HAQKSMRFMR
AKYRGTQAAV SCLQMHWRNH LLRKRERNSF LQLRQAAITL QRRYRARLNM IKQLKSYAQL
KQAAITIQTR YRAKKAMQKQ VVLYQKQREA IIKVQRRYRG NLEMRKQIEV YQKQRQAVIR
LQKWWRSIRD MRLCKAGYRR IRLSSLSIQR KWRATVQARR QREIFLSTIR KVRLMQAFIR
ATLLMRQQRR EFEMKRRAAV VIQRRFRARC AMLKARQDYQ LIQSSVILVQ RKFRANRSMK
QARQEFVQLR TIAVHLQQKF RGKRLMIEQR NCFQLLRCSM PGFQARARGF MARKRFQALM
TPEMMDLIRQ KRAAKVIQRY WRGYLIRRRQ KHQGLLDIRK RIAQLRQEAK AVNSVRCKVQ
EAVRFLRGRF IASDALAVLS RLDRLSRTVP HLLMWCSEFM STFCYGIMAQ AIRSEVDKQL
IERCSRIILN LARYNSTTVN TFQEGGLVTI AQMLLRWCDK DSEIFNTLCT LIWVFAHCPK
KRKIIHDYMT NPEAIYMVRE TKKLVARKEK MKQNARKPPP MTSGRYKSQK INFTPCSLPS
LEPDFGIIRY SPYTFISSVY AFDTILCKLQ IDMF
