LASP1_DROME
ID LASP1_DROME Reviewed; 657 AA.
AC Q8I7C3; Q59E31; Q9VV91;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=LIM and SH3 domain protein Lasp;
GN Name=Lasp {ECO:0000312|FlyBase:FBgn0063485}; ORFNames=CG3849;
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:0000305, ECO:0000312|EMBL:CAC82378.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC TISSUE=Ovary {ECO:0000312|EMBL:CAC82378.1};
RA Jenny A.P., van Berkel W., Filardo P., Ephrussi A.;
RT "Lasp interacts with Osk.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAF49426.3}
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF49426.3}
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, ECO:0000312|EMBL:CAC82378.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-530, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530, AND IDENTIFICATION BY
RP 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 -!- SUBUNIT: Interacts with osk.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000269|Ref.1};
CC IsoId=Q8I7C3-1; Sequence=Displayed;
CC Name=B {ECO:0000303|PubMed:10731132};
CC IsoId=Q8I7C3-2; Sequence=VSP_051636, VSP_051637;
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DR EMBL; AJ294538; CAC82378.1; -; mRNA.
DR EMBL; AE014296; AAF49426.3; -; Genomic_DNA.
DR EMBL; AE014296; AAN11739.2; -; Genomic_DNA.
DR EMBL; BT003801; AAO41484.1; -; mRNA.
DR RefSeq; NP_648912.2; NM_140655.3. [Q8I7C3-2]
DR RefSeq; NP_730192.2; NM_168681.4. [Q8I7C3-1]
DR AlphaFoldDB; Q8I7C3; -.
DR SMR; Q8I7C3; -.
DR BioGRID; 65163; 17.
DR IntAct; Q8I7C3; 43.
DR STRING; 7227.FBpp0099495; -.
DR iPTMnet; Q8I7C3; -.
DR PaxDb; Q8I7C3; -.
DR PRIDE; Q8I7C3; -.
DR DNASU; 39864; -.
DR EnsemblMetazoa; FBtr0075350; FBpp0075109; FBgn0063485. [Q8I7C3-2]
DR EnsemblMetazoa; FBtr0100145; FBpp0099495; FBgn0063485. [Q8I7C3-1]
DR GeneID; 39864; -.
DR KEGG; dme:Dmel_CG3849; -.
DR CTD; 39864; -.
DR FlyBase; FBgn0063485; Lasp.
DR VEuPathDB; VectorBase:FBgn0063485; -.
DR eggNOG; KOG1702; Eukaryota.
DR GeneTree; ENSGT00940000154775; -.
DR InParanoid; Q8I7C3; -.
DR PhylomeDB; Q8I7C3; -.
DR SignaLink; Q8I7C3; -.
DR BioGRID-ORCS; 39864; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Lasp; fly.
DR GenomeRNAi; 39864; -.
DR PRO; PR:Q8I7C3; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0063485; Expressed in testis and 11 other tissues.
DR Genevisible; Q8I7C3; DM.
DR GO; GO:0031672; C:A band; IDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005925; C:focal adhesion; IDA:FlyBase.
DR GO; GO:0070864; C:sperm individualization complex; IDA:FlyBase.
DR GO; GO:0030018; C:Z disc; IDA:FlyBase.
DR GO; GO:0003779; F:actin binding; IDA:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071689; P:muscle thin filament assembly; IMP:FlyBase.
DR GO; GO:0007279; P:pole cell formation; IMP:FlyBase.
DR GO; GO:0045856; P:positive regulation of pole plasm oskar mRNA localization; IMP:FlyBase.
DR GO; GO:0014881; P:regulation of myofibril size; IMP:FlyBase.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR InterPro; IPR000900; Nebulin_repeat.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 1.
DR Pfam; PF00880; Nebulin; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00132; LIM; 1.
DR SMART; SM00227; NEBU; 2.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR PROSITE; PS50023; LIM_DOMAIN_2; 1.
DR PROSITE; PS51216; NEBULIN; 2.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; LIM domain; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Zinc.
FT CHAIN 1..657
FT /note="LIM and SH3 domain protein Lasp"
FT /id="PRO_0000075766"
FT DOMAIN 3..63
FT /note="LIM zinc-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REPEAT 64..95
FT /note="Nebulin 1"
FT REPEAT 96..130
FT /note="Nebulin 2"
FT DOMAIN 596..657
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 130..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT VAR_SEQ 145
FT /note="N -> T (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10731132, ECO:0000303|Ref.4"
FT /id="VSP_051636"
FT VAR_SEQ 146..298
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10731132, ECO:0000303|Ref.4"
FT /id="VSP_051637"
FT CONFLICT 190
FT /note="Q -> QQQQ (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 657 AA; 74247 MW; 9383E1DEFBF6B529 CRC64;
MNKTCARCQK VVYPIEELKC LDKTWHKTCF KCTECGMTLN MKTYKGYNKM PYCEAHIPKA
KATAIADTPE LKRIAENTKI QSNVKYHADF EKAKGKFTQV ADDPETLRIK QNTKHISNVA
YHGDLEKKAA MEKQRGSAEV SDSSNESEYF SEQLAAEQFS QYAPTASPIP PAATTLHQQQ
QQLQHQQQQQ YQQHQQQLQQ QQHQHQHYLQ QQQQTLPPPP IQHQQYNTAA ITPTYQQLQQ
QQQQQQQQRA QQQQLHDPYA HYQQPQALRQ QQQQQQQQQQ QLLQQQAIKQ ASHLYPTATS
QQQQMPPPQS PANPQQQALN SYNEMRSAIL QNSHHPSGNS VDQYDQPQQQ QHQPQQQSTN
PTLVAAQQQQ SHHSLLNNNA SNGGISHSHH SNINNNGHGS QNQMLPPQMR RSAASVVAYD
GNSKQQVAAG PGAAQNHLQQ LYASPNYAAV TPSENSINVK QHASNGHMPN QQQQHVAGGS
NIGKIADYDP LTDGPRVVPN AGRSSTTLVY SSEPRGNQGG NSVYPKRIGS VSDIDPANGI
YGSLTAAEQA HQQQKHQQYY QQVQMMQQQE HPPQQQQMRQ QPSYSSLQEK QSRQSTAMRV
YRAIYDYEAQ DVDEVSFREG DVIFEVESID SGWMTGRVER TGKTGMLPAN YVEQAVI
