SGO1_DROME
ID SGO1_DROME Reviewed; 401 AA.
AC Q24141;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Shugoshin;
DE AltName: Full=Meiotic protein S332;
GN Name=mei-S332; ORFNames=CG5303;
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:AAL13862.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF GLY-28; VAL-34; LEU-112; CYS-375; PRO-377 AND SER-384.
RC TISSUE=Testis;
RX PubMed=7585942; DOI=10.1016/0092-8674(95)90166-3;
RA Kerrebrock A.W., Moore D.P., Wu J.S., Orr-Weaver T.L.;
RT "Mei-S332, a Drosophila protein required for sister-chromatid cohesion, can
RT localize to meiotic centromere regions.";
RL Cell 83:247-256(1995).
RN [2] {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 [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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF ASN-13; GLY-28;
RP VAL-34; SER-277; GLU-382 AND SER-384.
RX PubMed=9869638; DOI=10.1101/gad.12.24.3843;
RA Tang T.-T., Bickel S.E., Young L.M., Orr-Weaver T.L.;
RT "Maintenance of sister-chromatid cohesion at the centromere by the
RT Drosophila MEI-S332 protein.";
RL Genes Dev. 12:3843-3856(1998).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9490715; DOI=10.1083/jcb.140.5.1003;
RA Moore D.P., Page A.W., Tang T.-T., Kerrebrock A.W., Orr-Weaver T.L.;
RT "The cohesion protein MEI-S332 localizes to condensed meiotic and mitotic
RT centromeres until sister chromatids separate.";
RL J. Cell Biol. 140:1003-1012(1998).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10654079; DOI=10.1007/s004120050392;
RA LeBlanc H.N., Tang T.-T., Wu J.S., Orr-Weaver T.L.;
RT "The mitotic centromeric protein MEI-S332 and its role in sister-chromatid
RT cohesion.";
RL Chromosoma 108:401-411(1999).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=10985388; DOI=10.1016/s0960-9822(00)00650-3;
RA Lopez J.M., Karpen G.H., Orr-Weaver T.L.;
RT "Sister-chromatid cohesion via MEI-S332 and kinetochore assembly are
RT separable functions of the Drosophila centromere.";
RL Curr. Biol. 10:997-1000(2000).
RN [9]
RP LACK OF DEGRADATION.
RX PubMed=15268859; DOI=10.1016/j.cub.2004.07.023;
RA Lee J.Y., Dej K.J., Lopez J.M., Orr-Weaver T.L.;
RT "Control of centromere localization of the MEI-S332 cohesion protection
RT protein.";
RL Curr. Biol. 14:1277-1283(2004).
RN [10]
RP PHOSPHORYLATION, PHOSPHORYLATION AT THR-331, AND MUTAGENESIS OF SER-234 AND
RP THR-331.
RX PubMed=15621529; DOI=10.1016/j.devcel.2004.12.003;
RA Clarke A.S., Tang T.-T., Ooi D.L.-Y., Orr-Weaver T.L.;
RT "POLO kinase regulates the Drosophila centromere cohesion protein MEI-
RT S332.";
RL Dev. Cell 8:53-64(2005).
RN [11]
RP INTERACTION WITH INCENP, PHOSPHORYLATION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 124-SER--SER-126.
RX PubMed=16824953; DOI=10.1016/j.devcel.2006.04.021;
RA Resnick T.D., Satinover D.L., MacIsaac F., Stukenberg P.T., Earnshaw W.C.,
RA Orr-Weaver T.L., Carmena M.;
RT "INCENP and Aurora B promote meiotic sister chromatid cohesion through
RT localization of the Shugoshin MEI-S332 in Drosophila.";
RL Dev. Cell 11:57-68(2006).
CC -!- FUNCTION: Plays a central role in chromosome cohesion during meiosis
CC and mitosis by preventing premature dissociation of cohesin complex
CC from centromeres after prophase, when most of cohesin complex
CC dissociates from chromosomes arms. May act by protecting or Rad21 from
CC cleavage by Sse/separase. Required during meiosis in both males and
CC females. {ECO:0000269|PubMed:10654079, ECO:0000269|PubMed:7585942,
CC ECO:0000269|PubMed:9490715, ECO:0000269|PubMed:9869638}.
CC -!- SUBUNIT: Homodimer. Interacts with Incenp.
CC {ECO:0000269|PubMed:16824953, ECO:0000269|PubMed:9869638}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere
CC {ECO:0000269|PubMed:10654079, ECO:0000269|PubMed:7585942,
CC ECO:0000269|PubMed:9490715, ECO:0000269|PubMed:9869638}. Note=Localizes
CC to the centromere of meiotic and mitotic chromosomes (PubMed:9490715,
CC PubMed:10654079). During meiosis, it assembles onto centromeres during
CC prometaphase I, remains attached until anaphase II, during which it is
CC displaced from centromeres without being degraded (PubMed:9490715).
CC Localization onto centromeres is independent of kinetochore formation
CC and cohesin complex (PubMed:10985388). {ECO:0000269|PubMed:10654079,
CC ECO:0000269|PubMed:10985388, ECO:0000269|PubMed:9490715}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Present
CC throughout embryogenesis and larval stages.
CC -!- PTM: Phosphorylation by polo-like kinase (PLK) on Thr-331 antagonizes
CC cohesive function. Phosphorylation on Thr-331 at the metaphase anaphase
CC transition leads to its dissociation from centromeres. In contrast,
CC phosphorylation by aurB/ial on either Ser-124, Ser-125 or Ser-126 is
CC required for association with centromeres.
CC {ECO:0000269|PubMed:15621529, ECO:0000269|PubMed:16824953}.
CC -!- SIMILARITY: Belongs to the shugoshin family. {ECO:0000305}.
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DR EMBL; U36583; AAA87038.1; -; mRNA.
DR EMBL; AE013599; AAF46802.1; -; Genomic_DNA.
DR EMBL; AY058633; AAL13862.1; -; mRNA.
DR PIR; A57226; A57226.
DR RefSeq; NP_001286705.1; NM_001299776.1.
DR RefSeq; NP_476634.1; NM_057286.5.
DR AlphaFoldDB; Q24141; -.
DR SMR; Q24141; -.
DR BioGRID; 63143; 43.
DR DIP; DIP-17412N; -.
DR IntAct; Q24141; 10.
DR STRING; 7227.FBpp0071675; -.
DR iPTMnet; Q24141; -.
DR PaxDb; Q24141; -.
DR DNASU; 37523; -.
DR EnsemblMetazoa; FBtr0071761; FBpp0071675; FBgn0002715.
DR EnsemblMetazoa; FBtr0342979; FBpp0309743; FBgn0002715.
DR GeneID; 37523; -.
DR KEGG; dme:Dmel_CG5303; -.
DR CTD; 37523; -.
DR FlyBase; FBgn0002715; mei-S332.
DR VEuPathDB; VectorBase:FBgn0002715; -.
DR eggNOG; ENOG502TCIV; Eukaryota.
DR HOGENOM; CLU_632032_0_0_1; -.
DR InParanoid; Q24141; -.
DR OMA; SENTDMS; -.
DR OrthoDB; 1145243at2759; -.
DR PhylomeDB; Q24141; -.
DR SignaLink; Q24141; -.
DR BioGRID-ORCS; 37523; 0 hits in 1 CRISPR screen.
DR ChiTaRS; mei-S332; fly.
DR GenomeRNAi; 37523; -.
DR PRO; PR:Q24141; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0002715; Expressed in testis and 18 other tissues.
DR ExpressionAtlas; Q24141; baseline and differential.
DR Genevisible; Q24141; DM.
DR GO; GO:0005694; C:chromosome; IDA:FlyBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:FlyBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0007065; P:male meiosis sister chromatid cohesion; IEP:FlyBase.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:FlyBase.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:FlyBase.
DR GO; GO:0007062; P:sister chromatid cohesion; IDA:UniProtKB.
DR InterPro; IPR011515; Shugoshin_C.
DR InterPro; IPR011516; Shugoshin_N.
DR Pfam; PF07557; Shugoshin_C; 1.
DR Pfam; PF07558; Shugoshin_N; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Coiled coil; Developmental protein; Meiosis; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..401
FT /note="Shugoshin"
FT /id="PRO_0000055443"
FT REGION 82..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3..49
FT /evidence="ECO:0000255"
FT COMPBIAS 97..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..187
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 124
FT /note="Phosphoserine; by AurB"
FT /evidence="ECO:0000305"
FT MOD_RES 125
FT /note="Phosphoserine; by AurB"
FT /evidence="ECO:0000305"
FT MOD_RES 126
FT /note="Phosphoserine; by AurB"
FT /evidence="ECO:0000305"
FT MOD_RES 331
FT /note="Phosphothreonine; by PLK1"
FT /evidence="ECO:0000305|PubMed:15621529"
FT MUTAGEN 13
FT /note="N->I: In mei-S332-9; induces missegregation of
FT chromatids during meiosis."
FT /evidence="ECO:0000269|PubMed:9869638"
FT MUTAGEN 28
FT /note="G->D: In mei-S332-3; induces missegregation of
FT chromatids during meiosis."
FT /evidence="ECO:0000269|PubMed:7585942,
FT ECO:0000269|PubMed:9869638"
FT MUTAGEN 34
FT /note="V->E: In mei-S332-8; induces missegregation of
FT chromatids during meiosis."
FT /evidence="ECO:0000269|PubMed:7585942,
FT ECO:0000269|PubMed:9869638"
FT MUTAGEN 112
FT /note="L->M: In mei-S332-4; induces missegregation of
FT chromatids during meiosis; when associated with H-."
FT /evidence="ECO:0000269|PubMed:7585942"
FT MUTAGEN 124..126
FT /note="SSS->AAA: Does not stably associate with centromeres
FT during mitosis."
FT /evidence="ECO:0000269|PubMed:16824953"
FT MUTAGEN 234
FT /note="S->A: Does not affect phosphorylation."
FT /evidence="ECO:0000269|PubMed:15621529"
FT MUTAGEN 277
FT /note="S->F: In mei-S332-5; induces missegregation of
FT chromatids during meiosis."
FT /evidence="ECO:0000269|PubMed:9869638"
FT MUTAGEN 331
FT /note="T->A: Affects phosphorylation and localization to
FT centromeres."
FT /evidence="ECO:0000269|PubMed:15621529"
FT MUTAGEN 375
FT /note="C->Y: In mei-S332-2; induces missegregation of
FT chromatids during meiosis."
FT /evidence="ECO:0000269|PubMed:7585942"
FT MUTAGEN 377
FT /note="P->H: In mei-S332-4; induces missegregation of
FT chromatids during meiosis; when associated with M-112."
FT /evidence="ECO:0000269|PubMed:7585942"
FT MUTAGEN 382
FT /note="E->K: In mei-S332-10; induces missegregation of
FT chromatids during meiosis."
FT /evidence="ECO:0000269|PubMed:9869638"
FT MUTAGEN 384
FT /note="S->R: In mei-S332-6; induces missegregation of
FT chromatids during meiosis."
FT /evidence="ECO:0000269|PubMed:7585942,
FT ECO:0000269|PubMed:9869638"
SQ SEQUENCE 401 AA; 44402 MW; 76D3EA53577B315F CRC64;
MGSKVEQQYK LLNAELMDQV QKQRLEIGEY RKRVISLERE IMDIREEHVL QNHRQRMENI
SIVRSLMLSL NVDSDSLAVR QEPAPAAQIN RPSGPRRSSR EICKDMRRTC ALARTTRPIS
PRRSSSVTST VSSTSRRSSA EVQSEVVTTR IPEDRRANKP TPPPRRPAEL VFDEDDSDDD
FDEAVSPVEE TQTEQNEENN RLFSIIEENG SEGESTDSSS SCEAIYCDTT FESSPPNAQV
TVTPSGRALR EVDTNIPVAV SLSRGKETGK GSWLAISVAV EDSPQEPSIQ CPRLAVTRPS
QSSGIFPDVN GLTPRRSLFN GIGKMAGSTS TPKSFLVEEM PSIRTRSRTA ANKKSENTDM
SSSFCNNSAR PSRSCRPTSL VEPSLKNKLR NGSKGKAKAK K
