HOW_DROME
ID HOW_DROME Reviewed; 405 AA.
AC O01367; O02392; P91680; Q4AB28; Q8IN11; Q8T999; Q94539;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein held out wings;
DE AltName: Full=KH domain protein KH93F;
DE AltName: Full=Protein muscle-specific;
DE AltName: Full=Protein struthio;
DE AltName: Full=Protein wings held out;
DE AltName: Full=Putative RNA-binding protein;
DE AltName: Full=Quaking-related 93F;
GN Name=how; Synonyms=KH93F, qkr93F, stru, who; ORFNames=CG10293;
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:AAN13901.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZYGOTIC), FUNCTION, INDUCTION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF ARG-185.
RX PubMed=9118803; DOI=10.1242/dev.124.7.1323;
RA Baehrecke E.H.;
RT "who encodes a KH RNA binding protein that functions in muscle
RT development.";
RL Development 124:1323-1332(1997).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZYGOTIC), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=Oregon-R {ECO:0000269|PubMed:9169854};
RX PubMed=9169854; DOI=10.1242/dev.124.10.2087;
RA Zaffran S., Astier M., Gratecos D., Semeriva M.;
RT "The held out wings (how) Drosophila gene encodes a putative RNA-binding
RT protein involved in the control of muscular and cardiac activity.";
RL Development 124:2087-2098(1997).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZYGOTIC), PARTIAL NUCLEOTIDE SEQUENCE
RP [MRNA] (ISOFORM MATERNAL), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RC TISSUE=Embryo {ECO:0000269|PubMed:9344542};
RX PubMed=9344542; DOI=10.1006/dbio.1997.8699;
RA Lo P.C.H., Frasch M.;
RT "A novel KH-domain protein mediates cell adhesion processes in
RT Drosophila.";
RL Dev. Biol. 190:241-256(1997).
RN [4] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZYGOTIC), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S; TISSUE=Embryo {ECO:0000269|PubMed:9332381};
RX PubMed=9332381; DOI=10.1016/s0378-1119(97)00278-3;
RA Fyrberg C., Becker J., Barthmaier P., Mahaffey J., Fyrberg E.;
RT "A Drosophila muscle-specific gene related to the mouse quaking locus.";
RL Gene 197:315-323(1997).
RN [5] {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 [6] {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 [7] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ZYGOTIC).
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
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).
CC -!- FUNCTION: Required for integrin-mediated cell-adhesion in wing blade.
CC Vital role in steroid regulation of muscle development and to control
CC heart rate. Required during embryogenesis, in late stages of somatic
CC muscle development, for myotube migration and during metamorphosis for
CC muscle reorganization. {ECO:0000269|PubMed:9118803,
CC ECO:0000269|PubMed:9169854, ECO:0000269|PubMed:9344542}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9169854}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Zygotic {ECO:0000269|PubMed:9344542}; Synonyms=A
CC {ECO:0000303|PubMed:10731132};
CC IsoId=O01367-1; Sequence=Displayed;
CC Name=Maternal {ECO:0000269|PubMed:9344542}; Synonyms=B
CC {ECO:0000303|PubMed:10731132};
CC IsoId=O01367-2; Sequence=VSP_050197;
CC Name=C;
CC IsoId=O01367-3; Sequence=VSP_018594;
CC -!- TISSUE SPECIFICITY: During embryogenesis, expression is seen in
CC mesodermal precursors of somatic, visceral and pharyngeal muscle. Later
CC in embryogenesis, expression is restricted to heart and muscle
CC attachment sites of the epidermis. During onset of metamorphosis,
CC expression is seen in muscle and muscle attachment cells.
CC {ECO:0000269|PubMed:9118803, ECO:0000269|PubMed:9332381,
CC ECO:0000269|PubMed:9344542}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically during
CC embryonic, larval and pupal development. {ECO:0000269|PubMed:9332381,
CC ECO:0000269|PubMed:9344542}.
CC -!- INDUCTION: By 20-hydroxyecdysone at the onset of metamorphosis.
CC {ECO:0000269|PubMed:9118803}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit wing blisters and flight
CC impairment. {ECO:0000269|PubMed:9344542}.
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DR EMBL; U85651; AAB51251.1; -; mRNA.
DR EMBL; U72331; AAB17350.1; -; mRNA.
DR EMBL; AF003106; AAB60946.1; -; mRNA.
DR EMBL; AF003107; AAB60947.1; -; mRNA.
DR EMBL; U87150; AAB47553.1; -; mRNA.
DR EMBL; AE014297; AAF55952.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN13901.1; -; Genomic_DNA.
DR EMBL; AE014297; AAZ52538.1; -; Genomic_DNA.
DR EMBL; AY069862; AAL40007.1; -; mRNA.
DR RefSeq; NP_001027203.1; NM_001032032.3. [O01367-3]
DR RefSeq; NP_001163683.1; NM_001170212.2. [O01367-1]
DR RefSeq; NP_001163684.1; NM_001170213.2.
DR RefSeq; NP_524447.2; NM_079723.4. [O01367-1]
DR RefSeq; NP_732695.1; NM_169992.3. [O01367-2]
DR AlphaFoldDB; O01367; -.
DR SMR; O01367; -.
DR BioGRID; 67557; 29.
DR IntAct; O01367; 1.
DR STRING; 7227.FBpp0083575; -.
DR PaxDb; O01367; -.
DR DNASU; 42596; -.
DR EnsemblMetazoa; FBtr0084177; FBpp0083575; FBgn0264491. [O01367-1]
DR EnsemblMetazoa; FBtr0084178; FBpp0083576; FBgn0264491. [O01367-2]
DR EnsemblMetazoa; FBtr0100514; FBpp0099954; FBgn0264491. [O01367-3]
DR EnsemblMetazoa; FBtr0301401; FBpp0290615; FBgn0264491. [O01367-1]
DR GeneID; 42596; -.
DR KEGG; dme:Dmel_CG10293; -.
DR CTD; 42596; -.
DR FlyBase; FBgn0264491; how.
DR VEuPathDB; VectorBase:FBgn0264491; -.
DR eggNOG; KOG1588; Eukaryota.
DR GeneTree; ENSGT00940000167937; -.
DR InParanoid; O01367; -.
DR OMA; VCDEDWR; -.
DR PhylomeDB; O01367; -.
DR BioGRID-ORCS; 42596; 1 hit in 1 CRISPR screen.
DR ChiTaRS; how; fly.
DR GenomeRNAi; 42596; -.
DR PRO; PR:O01367; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0264491; Expressed in musculature of body and 59 other tissues.
DR ExpressionAtlas; O01367; baseline and differential.
DR Genevisible; O01367; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:FlyBase.
DR GO; GO:0003729; F:mRNA binding; IDA:FlyBase.
DR GO; GO:0003727; F:single-stranded RNA binding; IEA:InterPro.
DR GO; GO:0007475; P:apposition of dorsal and ventral imaginal disc-derived wing surfaces; IMP:FlyBase.
DR GO; GO:0008366; P:axon ensheathment; IMP:FlyBase.
DR GO; GO:0007155; P:cell adhesion; IMP:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; TAS:FlyBase.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0030718; P:germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
DR GO; GO:0007498; P:mesoderm development; IEP:FlyBase.
DR GO; GO:0008078; P:mesodermal cell migration; IMP:FlyBase.
DR GO; GO:0016203; P:muscle attachment; IMP:UniProtKB.
DR GO; GO:0007521; P:muscle cell fate determination; IDA:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
DR GO; GO:0007438; P:oenocyte development; IMP:FlyBase.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IMP:FlyBase.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:FlyBase.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006417; P:regulation of translation; IEA:InterPro.
DR GO; GO:0045214; P:sarcomere organization; IMP:FlyBase.
DR GO; GO:0007525; P:somatic muscle development; IMP:FlyBase.
DR GO; GO:0007284; P:spermatogonial cell division; IMP:FlyBase.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR045071; BBP-like.
DR InterPro; IPR031119; GLD1-like.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR032377; STAR_dimer.
DR PANTHER; PTHR11208; PTHR11208; 1.
DR PANTHER; PTHR11208:SF125; PTHR11208:SF125; 1.
DR Pfam; PF00013; KH_1; 1.
DR Pfam; PF16544; STAR_dimer; 1.
DR SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..405
FT /note="Protein held out wings"
FT /id="PRO_0000050113"
FT DOMAIN 142..210
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117,
FT ECO:0000305"
FT VAR_SEQ 370..405
FT /note="VGAIKQQRRLATNREHPYQRATVGVPAKPAGFIEIQ -> GGLFAR (in
FT isoform Maternal)"
FT /evidence="ECO:0000303|PubMed:9344542"
FT /id="VSP_050197"
FT VAR_SEQ 372..405
FT /note="AIKQQRRLATNREHPYQRATVGVPAKPAGFIEIQ -> RYMHAGSVF (in
FT isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_018594"
FT MUTAGEN 185
FT /note="R->C: In allele how-E44; embryonic lethal."
FT /evidence="ECO:0000269|PubMed:9118803"
FT CONFLICT 46
FT /note="Q -> QAQ (in Ref. 3 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="P -> S (in Ref. 7; AAL40007)"
FT /evidence="ECO:0000305"
FT CONFLICT 338..339
FT /note="QT -> RA (in Ref. 4; AAB47553)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="Missing (in Ref. 2, 4 and 7)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="E -> A (in Ref. 4; AAB47553)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 44325 MW; DCA3A29A12D1A55E CRC64;
MSVCESKAVV QQQLQQHLQQ QAAAAVVAVA QQQQAQAQAQ AQAQAQQQQQ APQVVVPMTP
QHLTPQQQQQ STQSIADYLA QLLKDRKQLA AFPNVFTHVE RLLDEEIARV RASLFQINGV
KKEPLTLPEP EGSVVTMNEK VYVPVREHPD FNFVGRILGP RGMTAKQLEQ ETGCKIMVRG
KGSMRDKKKE DANRGKPNWE HLSDDLHVLI TVEDTENRAT VKLAQAVAEV QKLLVPQAEG
EDELKKRQLM ELAIINGTYR DTTAKSVAVC DEEWRRLVAA SDSRLLTSTG LPGLAAQIRA
PAAAPLGAPL ILNPRMTVPT TAASILSAQA APTAAFDQTG HGMIFAPYDY ANYAALAGNP
LLTEYADHSV GAIKQQRRLA TNREHPYQRA TVGVPAKPAG FIEIQ
