SISA_DROME
ID SISA_DROME Reviewed; 189 AA.
AC Q9VZ09; Q24525; Q4V6W9;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein sisterless A {ECO:0000312|EMBL:AAF48022.1};
GN Name=sisA; ORFNames=CG1641;
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}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF LYS-128.
RC STRAIN=Oregon-R {ECO:0000269|PubMed:8370520};
RC TISSUE=Embryo {ECO:0000269|PubMed:8370520};
RX PubMed=8370520; DOI=10.1101/gad.7.9.1688;
RA Erickson J.W., Cline T.W.;
RT "A bZIP protein, sisterless-a, collaborates with bHLH transcription factors
RT early in Drosophila development to determine sex.";
RL Genes Dev. 7:1688-1702(1993).
RN [2] {ECO:0000312|EMBL:AAC97604.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000312|EMBL:AAC97604.1};
RX PubMed=9671597; DOI=10.1242/dev.125.16.3259;
RA Erickson J.W., Cline T.W.;
RT "Key aspects of the primary sex determination mechanism are conserved
RT across the genus Drosophila.";
RL Development 125:3259-3268(1998).
RN [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP 108-ASP--GLU-118.
RX PubMed=10790394; DOI=10.1093/genetics/155.1.191;
RA Walker J.J., Lee K.K., Desai R.N., Erickson J.W.;
RT "The Drosophila melanogaster sex determination gene sisA is required in
RT yolk nuclei for midgut formation.";
RL Genetics 155:191-202(2000).
RN [4] {ECO:0000312|EMBL:AAF48022.1}
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 [5] {ECO:0000312|EMBL:AAF48022.1}
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 [6] {ECO:0000312|EMBL:AAY51581.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA Park S., Wan K., Yu C., Celniker S.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305}
RP HOMODIMERIZATION, AND INTERACTION WITH DPN AND DA.
RX PubMed=7651341; DOI=10.1007/bf02190799;
RA Liu Y., Belote J.M.;
RT "Protein-protein interactions among components of the Drosophila primary
RT sex determination signal.";
RL Mol. Gen. Genet. 248:182-189(1995).
RN [8] {ECO:0000305}
RP INTERACTION WITH BAP60.
RX PubMed=16083904; DOI=10.1016/j.jmb.2005.07.009;
RA Moller A., Avila F.W., Erickson J.W., Jackle H.;
RT "Drosophila BAP60 is an essential component of the Brahma complex, required
RT for gene activation and repression.";
RL J. Mol. Biol. 352:329-337(2005).
CC -!- FUNCTION: Involved in sex determination and dosage compensation.
CC Required for proper expression of Sxl in embryonic somatic cells. Also
CC has an essential function in the yolk nuclei. Involved in endoderm
CC migration and midgut formation. {ECO:0000269|PubMed:10790394,
CC ECO:0000269|PubMed:8370520}.
CC -!- SUBUNIT: Homodimer. Interacts with dpn (via bHLH motif). Interacts with
CC da (via bHLH motif). Interacts with Bap60.
CC {ECO:0000269|PubMed:16083904, ECO:0000269|PubMed:7651341}.
CC -!- INTERACTION:
CC Q9VZ09; Q86PA6: da; NbExp=3; IntAct=EBI-147605, EBI-367267;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:8370520}.
CC -!- TISSUE SPECIFICITY: Localizes to all the embryonic nuclei until nuclear
CC cycle 9, when expression ceases in the prepole cell nuclei. Associates
CC with the somatic nuclei through cycle 10. By nuclear cycle 12,
CC distributes uniformly in the somatic portion of the embryo and no
CC longer associates with the nuclei. After early cycle 14 (beginning of
CC cellularization) there is very little or no expression in the periphery
CC of the embryo or in either the somatic or germ cells. In the yolk,
CC accumulates at the nuclei from nuclear cycle 8 until 10-11 hours after
CC fertilization. {ECO:0000269|PubMed:10790394,
CC ECO:0000269|PubMed:8370520}.
CC -!- DEVELOPMENTAL STAGE: Expressed zygotically in embryos from 0 to 12
CC hours after fertilization, with a peak of expression during the 2 to 4
CC hour period. {ECO:0000269|PubMed:10790394, ECO:0000269|PubMed:8370520}.
CC -!- DISRUPTION PHENOTYPE: Homozygous embryonic female lethality. Hemizygous
CC embryonic male lethality. Mutant embryos fail to form the midgut due to
CC the failure of endoderm migration. Consequently, the yolk is left as an
CC unenclosed mass that moves to ectopic locations as development
CC progresses causing a variety of terminal phenotypes.
CC {ECO:0000269|PubMed:10790394}.
CC -!- CAUTION: Reported to be a member of the bZIP family but does not match
CC diagnostic signatures for this family and has low similarity to other
CC family members. {ECO:0000305|PubMed:8370520}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAY51581.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF046044; AAC97604.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF48022.1; -; Genomic_DNA.
DR EMBL; BT022187; AAY51581.1; ALT_INIT; mRNA.
DR RefSeq; NP_511116.2; NM_078561.3.
DR AlphaFoldDB; Q9VZ09; -.
DR SMR; Q9VZ09; -.
DR BioGRID; 58480; 32.
DR DIP; DIP-18301N; -.
DR IntAct; Q9VZ09; 10.
DR STRING; 7227.FBpp0073317; -.
DR PaxDb; Q9VZ09; -.
DR DNASU; 32068; -.
DR EnsemblMetazoa; FBtr0073461; FBpp0073317; FBgn0003411.
DR GeneID; 32068; -.
DR KEGG; dme:Dmel_CG1641; -.
DR UCSC; CG1641-RA; d. melanogaster.
DR CTD; 32068; -.
DR FlyBase; FBgn0003411; sisA.
DR VEuPathDB; VectorBase:FBgn0003411; -.
DR eggNOG; ENOG502TB94; Eukaryota.
DR HOGENOM; CLU_1397715_0_0_1; -.
DR InParanoid; Q9VZ09; -.
DR OMA; GHVYAPY; -.
DR OrthoDB; 1354446at2759; -.
DR PhylomeDB; Q9VZ09; -.
DR BioGRID-ORCS; 32068; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 32068; -.
DR PRO; PR:Q9VZ09; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003411; Expressed in yolk nucleus (Drosophila) and 8 other tissues.
DR Genevisible; Q9VZ09; DM.
DR GO; GO:0005634; C:nucleus; IC:FlyBase.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:FlyBase.
DR GO; GO:0007496; P:anterior midgut development; IMP:FlyBase.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007492; P:endoderm development; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0007497; P:posterior midgut development; IMP:FlyBase.
DR GO; GO:0007538; P:primary sex determination; IMP:FlyBase.
DR GO; GO:0007530; P:sex determination; IGI:FlyBase.
DR GO; GO:0007540; P:sex determination, establishment of X:A ratio; TAS:FlyBase.
DR GO; GO:0007548; P:sex differentiation; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Developmental protein; Differentiation; Nucleus; Reference proteome;
KW Sexual differentiation; Transcription; Transcription regulation.
FT CHAIN 1..189
FT /note="Protein sisterless A"
FT /id="PRO_0000421979"
FT REGION 93..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 108..118
FT /note="DVKDAQRQRAE->GCPASEGR: In sisA3; embryonic lethal."
FT /evidence="ECO:0000269|PubMed:10790394"
FT MUTAGEN 128
FT /note="K->E: In sisA1; embryonic female lethal."
FT /evidence="ECO:0000269|PubMed:8370520"
FT CONFLICT 177
FT /note="E -> D (in Ref. 1; AAC97604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 189 AA; 21290 MW; A62684A03F125B21 CRC64;
MERSHLYLPT LSYAAMGHVY APYRGSSSPA LSTASSTSSK PEQIEELVSQ QLHHLKMHYA
DEEQRYVDQM LLENPIVVER RAPPPLKTEL AMDCRGSGSG SGSGSGSDVK DAQRQRAESC
RKSRYNNKIK KAKLRFRHKF VSGQLKKSAV MLDTMRDVIA QAERQLLERG YPAATLERMR
ATFGLEMEQ
