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Database: UniProt
Entry: O70576
LinkDB: O70576
Original site: O70576 
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   24-JAN-2024, entry version 159.
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   SwissPalm; O70576; -.
DR   MaxQB; O70576; -.
DR   PaxDb; 10090-ENSMUSP00000040945; -.
DR   PeptideAtlas; O70576; -.
DR   ProteomicsDB; 258655; -.
DR   Antibodypedia; 30623; 180 antibodies from 27 providers.
DR   DNASU; 50878; -.
DR   Ensembl; ENSMUST00000048028.15; ENSMUSP00000040945.9; ENSMUSG00000036928.15.
DR   Ensembl; ENSMUST00000162245.8; ENSMUSP00000125523.2; ENSMUSG00000036928.15.
DR   GeneID; 50878; -.
DR   KEGG; mmu:50878; -.
DR   UCSC; uc009afn.2; mouse.
DR   AGR; MGI:1355311; -.
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; 5354237at2759; -.
DR   PhylomeDB; O70576; -.
DR   TreeFam; TF314604; -.
DR   BioGRID-ORCS; 50878; 3 hits in 78 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 102 other cell types or 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: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:0034089; P:establishment of meiotic sister chromatid cohesion; ISS:UniProtKB.
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:SF8; COHESIN SUBUNIT SA-3; 1.
DR   PANTHER; PTHR11199; STROMAL ANTIGEN; 1.
DR   Pfam; PF21581; SCD; 1.
DR   Pfam; PF08514; STAG; 1.
DR   SUPFAM; SSF48371; ARM repeat; 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
//
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