SRA_DROME
ID SRA_DROME Reviewed; 292 AA.
AC Q9XZL8; Q9V391;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein sarah;
DE AltName: Full=Protein nebula;
GN Name=sra; Synonyms=nla; ORFNames=CG6072;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA McCormick A.V., Goldberg M.L.;
RT "Gene required for elongation of meiosis I spindle in Drosophila females.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
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]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=15611177; DOI=10.1534/genetics.104.029934;
RA Ejima A., Tsuda M., Takeo S., Ishii K., Matsuo T., Aigaki T.;
RT "Expression level of sarah, a homolog of DSCR1, is critical for ovulation
RT and female courtship behavior in Drosophila melanogaster.";
RL Genetics 168:2077-2087(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH PP2B-14D.
RX PubMed=16860743; DOI=10.1016/j.cub.2006.05.058;
RA Takeo S., Tsuda M., Akahori S., Matsuo T., Aigaki T.;
RT "The calcineurin regulator sra plays an essential role in female meiosis in
RT Drosophila.";
RL Curr. Biol. 16:1435-1440(2006).
RN [7]
RP FUNCTION.
RX PubMed=16860744; DOI=10.1016/j.cub.2006.06.024;
RA Horner V.L., Czank A., Jang J.K., Singh N., Williams B.C., Puro J.,
RA Kubli E., Hanes S.D., McKim K.S., Wolfner M.F., Goldberg M.L.;
RT "The Drosophila calcipressin sarah is required for several aspects of egg
RT activation.";
RL Curr. Biol. 16:1441-1446(2006).
RN [8]
RP FUNCTION, INTERACTION WITH CANA-14F; CANB2 AND PP2B-14D, PHOSPHORYLATION AT
RP SER-67; SER-72; SER-100; THR-102; THR-196; SER-215; SER-219 AND THR-246,
RP AND MUTAGENESIS OF SER-67; SER-72; SER-100; THR-102; THR-196; SER-199;
RP SER-215; SER-219 AND THR-246.
RX PubMed=22421435; DOI=10.1073/pnas.1120367109;
RA Takeo S., Swanson S.K., Nandanan K., Nakai Y., Aigaki T., Washburn M.P.,
RA Florens L., Hawley R.S.;
RT "Shaggy/glycogen synthase kinase 3beta and phosphorylation of
RT Sarah/regulator of calcineurin are essential for completion of Drosophila
RT female meiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:6382-6389(2012).
CC -!- FUNCTION: Required for elongation of meiosis I spindle. Critical for
CC ovulation, meiotic progression in oocytes and female courtship
CC behavior, including their postmating changes. Regulates female meiosis
CC by controlling calcineurin activity in the germline. Has a role in
CC calcium signaling during egg activation; bcd mRNA polyadenylation and
CC translation in the oocyte. {ECO:0000269|PubMed:15611177,
CC ECO:0000269|PubMed:16860743, ECO:0000269|PubMed:16860744,
CC ECO:0000269|PubMed:22421435}.
CC -!- SUBUNIT: Interacts with Pp2B-14D, CanA-14F and CanB2.
CC {ECO:0000269|PubMed:16860743, ECO:0000269|PubMed:22421435}.
CC -!- TISSUE SPECIFICITY: Expressed in central nervous system of the third
CC instar larvae, with a relatively intense signal in the brain and weak
CC signals in the ventral ganglion. Relatively low, but ubiquitous
CC expression level is observed in leg and wing imaginal disks, no signal
CC is detected in the eye-antennal disks. Expressed in all neurons in the
CC adult brain. {ECO:0000269|PubMed:15611177}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:15611177}.
CC -!- PTM: Phosphorylation at Ser-215 and Ser-219 is essential for
CC calcineurin activation and completion of female meiosis. Sgg is
CC required for phosphorylation of Ser-215 in activated eggs. Ser-100,
CC Thr-102 and Ser-219 are highly phosphorylated in both ovaries and
CC activated eggs; however, phosphorylation at Ser-100 or Thr-102 is not
CC required for sra function in completion of female meiosis.
CC {ECO:0000269|PubMed:22421435}.
CC -!- DISRUPTION PHENOTYPE: Flies exhibit spontaneous ovulation in virgins,
CC female sterility with impaired meiotic progression (eggs are arrested
CC at anaphase of meiosis I, they fail to fully polyadenylate and
CC translate bicoid mRNA and the male pronucleus fails to mature), and
CC compromised postmating responses with lower ovulation level, higher
CC remating rate, and shorter period for restoration of receptivity.
CC {ECO:0000269|PubMed:15611177}.
CC -!- SIMILARITY: Belongs to the RCAN family. {ECO:0000305}.
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DR EMBL; AF147700; AAD33987.1; -; mRNA.
DR EMBL; AE014297; AAF55285.1; -; Genomic_DNA.
DR EMBL; AY061194; AAL28742.1; -; mRNA.
DR RefSeq; NP_001287361.1; NM_001300432.1.
DR RefSeq; NP_524378.1; NM_079654.3.
DR AlphaFoldDB; Q9XZL8; -.
DR SMR; Q9XZL8; -.
DR BioGRID; 70782; 7.
DR IntAct; Q9XZL8; 3.
DR STRING; 7227.FBpp0082709; -.
DR iPTMnet; Q9XZL8; -.
DR PaxDb; Q9XZL8; -.
DR PRIDE; Q9XZL8; -.
DR DNASU; 47384; -.
DR EnsemblMetazoa; FBtr0083255; FBpp0082709; FBgn0086370.
DR EnsemblMetazoa; FBtr0344473; FBpp0310844; FBgn0086370.
DR GeneID; 47384; -.
DR KEGG; dme:Dmel_CG6072; -.
DR CTD; 47384; -.
DR FlyBase; FBgn0086370; sra.
DR VEuPathDB; VectorBase:FBgn0086370; -.
DR eggNOG; KOG4019; Eukaryota.
DR GeneTree; ENSGT00940000170734; -.
DR HOGENOM; CLU_076190_1_0_1; -.
DR InParanoid; Q9XZL8; -.
DR OMA; RMRVNYN; -.
DR OrthoDB; 1585262at2759; -.
DR PhylomeDB; Q9XZL8; -.
DR SignaLink; Q9XZL8; -.
DR BioGRID-ORCS; 47384; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 47384; -.
DR PRO; PR:Q9XZL8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0086370; Expressed in capitellum (Drosophila) and 27 other tissues.
DR ExpressionAtlas; Q9XZL8; baseline and differential.
DR Genevisible; Q9XZL8; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0007343; P:egg activation; IMP:FlyBase.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0035039; P:male pronucleus assembly; IMP:FlyBase.
DR GO; GO:0051321; P:meiotic cell cycle; IGI:FlyBase.
DR GO; GO:0007005; P:mitochondrion organization; IMP:FlyBase.
DR GO; GO:0008355; P:olfactory learning; IMP:FlyBase.
DR GO; GO:0048477; P:oogenesis; IEA:UniProtKB-KW.
DR GO; GO:0070884; P:regulation of calcineurin-NFAT signaling cascade; IMP:UniProtKB.
DR GO; GO:0045924; P:regulation of female receptivity; IMP:FlyBase.
DR GO; GO:0046008; P:regulation of female receptivity, post-mating; IMP:FlyBase.
DR GO; GO:0030431; P:sleep; IDA:FlyBase.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR006931; Calcipressin.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR PANTHER; PTHR10300; PTHR10300; 1.
DR Pfam; PF04847; Calcipressin; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW Behavior; Calcium; Cell cycle; Developmental protein; Differentiation;
KW Meiosis; Oogenesis; Phosphoprotein; Reference proteome.
FT CHAIN 1..292
FT /note="Protein sarah"
FT /id="PRO_0000211422"
FT REGION 1..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22421435"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22421435"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22421435"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22421435"
FT MOD_RES 196
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22421435"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22421435"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:22421435"
FT MOD_RES 246
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:22421435"
FT MUTAGEN 67
FT /note="S->A: No effect on function in completion of female
FT meiosis."
FT /evidence="ECO:0000269|PubMed:22421435"
FT MUTAGEN 72
FT /note="S->A: No effect on function in completion of female
FT meiosis."
FT /evidence="ECO:0000269|PubMed:22421435"
FT MUTAGEN 100
FT /note="S->A: No effect on function in completion of female
FT meiosis."
FT /evidence="ECO:0000269|PubMed:22421435"
FT MUTAGEN 102
FT /note="T->A: No effect on function in completion of female
FT meiosis."
FT /evidence="ECO:0000269|PubMed:22421435"
FT MUTAGEN 196
FT /note="T->A: No effect on function in completion of female
FT meiosis."
FT /evidence="ECO:0000269|PubMed:22421435"
FT MUTAGEN 199
FT /note="S->A: No effect on function in completion of female
FT meiosis."
FT /evidence="ECO:0000269|PubMed:22421435"
FT MUTAGEN 215
FT /note="S->A: Loss of function in completion of female
FT meiosis. Loss of function in completion of female meiosis;
FT when associated with A-219."
FT /evidence="ECO:0000269|PubMed:22421435"
FT MUTAGEN 215
FT /note="S->E,D: Loss of function in completion of female
FT meiosis."
FT /evidence="ECO:0000269|PubMed:22421435"
FT MUTAGEN 219
FT /note="S->A: Impairs function in completion of female
FT meiosis. Loss of function in completion of female meiosis;
FT when associated with A-215."
FT /evidence="ECO:0000269|PubMed:22421435"
FT MUTAGEN 219
FT /note="S->E,D: Slightly impairs function in completion of
FT female meiosis."
FT /evidence="ECO:0000269|PubMed:22421435"
FT MUTAGEN 246
FT /note="T->A: No effect on function in completion of female
FT meiosis."
FT /evidence="ECO:0000269|PubMed:22421435"
SQ SEQUENCE 292 AA; 31424 MW; 64F1BBF5F6EA6CF9 CRC64;
MSDAAKSNNN ASADAPDPTT PDATGEADAA NAATPTTPRG NHNNNNSANG RSKNKLKSTQ
NSSGGGSIDK LSPDQDIFIN AADGLPNQHP SLPKEGDVDS DTEPEVDADS FDDLPTSIIV
TNIHSEVFAN PELKHAMEEL FRTFSESATF QWLRSFRRLR VNYDNAIAAA NARIKLHQYE
FNKKTVITCY FAQPVTPVSN KNLQPPAPVK QFLISPPASP PAGWEPREEG EPLVNHDLLA
ALASLTPGES HELHPQSEDQ PAIIVHTAML AETGPGLQVK APIVQTKCPE RA
