STAG3_MOUSE
ID STAG3_MOUSE Reviewed; 1240 AA.
AC O70576; B2RSV0;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cohesin subunit SA-3;
DE AltName: Full=SCC3 homolog 3;
DE AltName: Full=Stromal antigen 3;
DE AltName: Full=Stromalin-3;
GN Name=Stag3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC TISSUE=Testis;
RX PubMed=10698974; DOI=10.1096/fasebj.14.3.581;
RA Pezzi N., Prieto I., Kremer L., Perez Jurado L.A., Valero C., Del Mazo J.,
RA Martinez-A C., Barbero J.L.;
RT "STAG3, a novel gene encoding a protein involved in meiotic chromosome
RT pairing and location of STAG3-related genes flanking the Williams-Beuren
RT syndrome deletion.";
RL FASEB J. 14:581-592(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION IN MEIOSIS, AND INTERACTION WITH SMC1A AND SMC3.
RX PubMed=11483963; DOI=10.1038/35087082;
RA Prieto I., Suja J.A., Pezzi N., Kremer L., Martinez-A C., Rufas J.S.,
RA Barbero J.L.;
RT "Mammalian STAG3 is a cohesin specific to sister chromatid arms in meiosis
RT I.";
RL Nat. Cell Biol. 3:761-766(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=22346761; DOI=10.1371/journal.pgen.1002485;
RA Fukuda T., Pratto F., Schimenti J.C., Turner J.M., Camerini-Otero R.D.,
RA Hoeoeg C.;
RT "Phosphorylation of chromosome core components may serve as axis marks for
RT the status of chromosomal events during mammalian meiosis.";
RL PLoS Genet. 8:E1002485-E1002485(2012).
RN [6]
RP INTERACTION WITH CCDC79.
RX PubMed=24413433; DOI=10.1038/ncb2896;
RA Shibuya H., Ishiguro K.I., Watanabe Y.;
RT "The TRF1-binding protein TERB1 promotes chromosome movement and telomere
RT rigidity in meiosis.";
RL Nat. Cell Biol. 16:145-156(2014).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=24597867; DOI=10.1056/nejmoa1309635;
RA Caburet S., Arboleda V.A., Llano E., Overbeek P.A., Barbero J.L., Oka K.,
RA Harrison W., Vaiman D., Ben-Neriah Z., Garcia-Tunon I., Fellous M.,
RA Pendas A.M., Veitia R.A., Vilain E.;
RT "Mutant cohesin in premature ovarian failure.";
RL N. Engl. J. Med. 370:943-949(2014).
CC -!- FUNCTION: Meiosis specific component of cohesin complex. The cohesin
CC complex is required for the cohesion of sister chromatids after DNA
CC replication. The cohesin complex apparently forms a large proteinaceous
CC ring within which sister chromatids can be trapped. At anaphase, the
CC complex is cleaved and dissociates from chromatin, allowing sister
CC chromatids to segregate. The meiosis-specific cohesin complex probably
CC replaces mitosis specific cohesin complex when it dissociates from
CC chromatin during prophase I. {ECO:0000269|PubMed:11483963,
CC ECO:0000269|PubMed:24597867}.
CC -!- SUBUNIT: Component of the meiosis-specific cohesin complex, which also
CC contains the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer. Such complex
CC likely contains RAD21, or the meiosis-specific related protein REC8 (By
CC similarity). Interacts with CCDC79/TERB1; recruiting cohesin to
CC telomeres to develop structural rigidity. {ECO:0000250,
CC ECO:0000269|PubMed:11483963, ECO:0000269|PubMed:24413433}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750,
CC ECO:0000269|PubMed:22346761}. Chromosome {ECO:0000269|PubMed:22346761}.
CC Chromosome, centromere {ECO:0000269|PubMed:22346761}. Note=Associates
CC with chromatin. In prophase I stage of meiosis, it is found along the
CC axial elements of synaptonemal complexes. In late-pachytene-diplotene,
CC the bulk of protein dissociates from the chromosome arms probably
CC because of phosphorylation by PLK1, except at centromeres, where
CC cohesin complexes remain. It however remains chromatin associated at
CC the centromeres up to metaphase I. During anaphase I, it probably
CC dissociates from centromeres, allowing chromosomes segregation.
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:22346761}.
CC -!- DISRUPTION PHENOTYPE: Deficient mice are sterile and their fetal
CC oocytes are arrested at early prophase I leading to oocyte depletion at
CC 1 week of age. {ECO:0000269|PubMed:24597867}.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
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DR EMBL; AJ005678; CAA06669.1; -; mRNA.
DR EMBL; BC139010; AAI39011.1; -; mRNA.
DR EMBL; BC139011; AAI39012.1; -; mRNA.
DR CCDS; CCDS39344.1; -.
DR PIR; T30834; T30834.
DR RefSeq; NP_058660.2; NM_016964.2.
DR RefSeq; XP_006504659.1; XM_006504596.2.
DR RefSeq; XP_011239250.1; XM_011240948.2.
DR AlphaFoldDB; O70576; -.
DR SMR; O70576; -.
DR BioGRID; 206141; 8.
DR CORUM; O70576; -.
DR DIP; DIP-60731N; -.
DR IntAct; O70576; 6.
DR MINT; O70576; -.
DR STRING; 10090.ENSMUSP00000040945; -.
DR iPTMnet; O70576; -.
DR PhosphoSitePlus; O70576; -.
DR MaxQB; O70576; -.
DR PaxDb; O70576; -.
DR PeptideAtlas; O70576; -.
DR PRIDE; O70576; -.
DR ProteomicsDB; 258655; -.
DR Antibodypedia; 30623; 168 antibodies from 27 providers.
DR DNASU; 50878; -.
DR Ensembl; ENSMUST00000048028; ENSMUSP00000040945; ENSMUSG00000036928.
DR Ensembl; ENSMUST00000162245; ENSMUSP00000125523; ENSMUSG00000036928.
DR GeneID; 50878; -.
DR KEGG; mmu:50878; -.
DR UCSC; uc009afn.2; mouse.
DR CTD; 10734; -.
DR MGI; MGI:1355311; Stag3.
DR VEuPathDB; HostDB:ENSMUSG00000036928; -.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR HOGENOM; CLU_005067_1_0_1; -.
DR InParanoid; O70576; -.
DR OMA; WDCAAPL; -.
DR OrthoDB; 167826at2759; -.
DR PhylomeDB; O70576; -.
DR TreeFam; TF314604; -.
DR BioGRID-ORCS; 50878; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Stag3; mouse.
DR PRO; PR:O70576; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O70576; protein.
DR Bgee; ENSMUSG00000036928; Expressed in spermatocyte and 99 other tissues.
DR ExpressionAtlas; O70576; baseline and differential.
DR Genevisible; O70576; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0000800; C:lateral element; IDA:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0030893; C:meiotic cohesin complex; IDA:UniProtKB.
DR GO; GO:0034991; C:nuclear meiotic cohesin complex; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR GO; GO:0000802; C:transverse filament; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0007066; P:female meiosis sister chromatid cohesion; ISS:MGI.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:MGI.
DR GO; GO:0007065; P:male meiosis sister chromatid cohesion; ISS:MGI.
DR GO; GO:0034502; P:protein localization to chromosome; IMP:MGI.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199; PTHR11199; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51425; SCD; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Centromere; Chromosome; Chromosome partition; Meiosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1240
FT /note="Cohesin subunit SA-3"
FT /id="PRO_0000120189"
FT DOMAIN 324..409
FT /note="SCD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1083..1104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 553
FT /note="L -> P (in Ref. 1; CAA06669)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="A -> D (in Ref. 1; CAA06669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1079
FT /note="A -> G (in Ref. 1; CAA06669)"
FT /evidence="ECO:0000305"
FT CONFLICT 1090
FT /note="R -> K (in Ref. 1; CAA06669)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1240 AA; 141167 MW; B3856012BFE76C1C CRC64;
MPTLWSPSTQ HHGSSSGSES SPLQKSVRRA QMALSPCSSS ILPCDDRDSQ GTAEWDSPST
NEDSDFEDSL RRNVKKRAAK QPPKAVPAAK HRKKQSRIVS SGNGKNESVP STNYLFDAVK
AARSCMQSLV DEWLDNYKQD ENAGFLELIN FFIRACGCKS TVTPEMFKTM SNSEIIQHLT
EEFNEDSGDY PLTAPGPSWK KFQGSFCEFV KTLVYQCQYS LLYDGFPMDD LISLLIGLSD
SQVRAFRHTS TLAAMKLMTS LVKVALQLSL HKDNNQRQYE AERNKGPEQR APERLESLLE
KRKEFQENQE DIEGMMNAIF RGVFVHRYRD ILPEIRAICI EEIGYWMQSY STSFLNDSYL
KYIGWTLHDK HKEVRLKCVK ALAGLYSNQE LSLRMELFTN RFKDRMVSMV MDRECEVAVE
AIRLLTLILK NMEGVLTSAD CEKIYSIVYI SNRAMASSAG EFVYWKIFHP ECGAKAVSDR
ERRRSPQAQK TFIYLLLAFF MESEHHNHAA YLVDSLWDCA GSYLKDWESL TNLLLQKDQN
LGDMQERMLI EILVSSARQA AEGHPPVGRI TGKKSLTAKE RKLQAYDKMK LAEHLIPLLP
QLLAKFSADA ENVAPLLQLL SYFDLSIYCT QRLEKHLELL LQQLQEVVVK HVEPEVLEAA
AHALYLLCKP EFTFFSRVDF ARSQLVDFLT DRFQQELDDL MQSSFLDEDE VYSLTATLKR
LSAFYNAHDL TRWEISEPCS RLLRKAVDTG EVPHQVILPA LTLVYFSILW TVTHISESTS
HKQLMSLKKR MVAFCELCQS CLSDVDPEIQ EQAFVLLSDL LLIFSPQMIV GGRDFLRPLV
FFPEATLQSE LASFLMDHVF LQPGELGNGQ SQEDHVQIEL LHQRRRLLAG FCKLLLYGVL
ELDAASDVFK HYNKFYEDYG DIIKETLTRA RQIDRCQCSR ILLLSLKQLY TELIQEQGPQ
GLTELPAFIE MRDLARRFAL SFGPQQLHNR DLVVMLHKEG IKFSLSELPP AGSSHEPPNL
AFLELLSEFS PRLFHQDKRL LLSYLEKCLQ RVSKAPNHPW GPVTTYCHSL HPLEITAEAS
PRGPPHSKKR CVEGPCRPQE EESSSQEESL QLNSGPTTPT LTSTAVKRKQ SLRTVGKKQK
GRPGPGPGPG PELICSQQLL GTQRLKMSSA PCFQIRCDPS GSGLGKQLTR LSLMEEDEEE
ELRLLDEEWQ RGDKMLHSPS SPSEHGLDLL DTTELNMEDF
