ID   SGO2_MOUSE              Reviewed;        1164 AA.
AC   Q7TSY8; Q811I4; Q8C9C4; Q8CGJ4; Q9CS55;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   24-JAN-2024, entry version 156.
DE   RecName: Full=Shugoshin 2 {ECO:0000250|UniProtKB:Q562F6};
DE   AltName: Full=Shugoshin-2;
DE   AltName: Full=Shugoshin-like 2;
GN   Name=Sgo2 {ECO:0000250|UniProtKB:Q562F6};
GN   Synonyms=Sgol2, Sgol2a {ECO:0000312|MGI:MGI:1098767};
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary tumor;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-593.
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   PROTEIN SEQUENCE OF 95-103; 259-269; 579-588 AND 1056-1065, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17205076; DOI=10.1038/sj.embor.7400877;
RA   Gomez R., Valdeolmillos A., Parra M.T., Viera A., Carreiro C., Roncal F.,
RA   Rufas J.S., Barbero J.L., Suja J.A.;
RT   "Mammalian SGO2 appears at the inner centromere domain and redistributes
RT   depending on tension across centromeres during meiosis II and mitosis.";
RL   EMBO Rep. 8:173-180(2007).
RN   [5]
RP   DISRUPTION PHENOTYPE, AND FUNCTION.
RX   PubMed=18765791; DOI=10.1101/gad.475308;
RA   Llano E., Gomez R., Gutierrez-Caballero C., Herran Y., Sanchez-Martin M.,
RA   Vazquez-Quinones L., Hernandez T., de Alava E., Cuadrado A., Barbero J.L.,
RA   Suja J.A., Pendas A.M.;
RT   "Shugoshin-2 is essential for the completion of meiosis but not for mitotic
RT   cell division in mice.";
RL   Genes Dev. 22:2400-2413(2008).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=18084284; DOI=10.1038/ncb1667;
RA   Lee J., Kitajima T.S., Tanno Y., Yoshida K., Morita T., Miyano T.,
RA   Miyake M., Watanabe Y.;
RT   "Unified mode of centromeric protection by shugoshin in mammalian oocytes
RT   and somatic cells.";
RL   Nat. Cell Biol. 10:42-52(2008).
CC   -!- FUNCTION: Cooperates with PPP2CA to protect centromeric cohesin from
CC       separase-mediated cleavage in oocytes specifically during meiosis I.
CC       Has a crucial role in protecting REC8 at centromeres from cleavage by
CC       separase. During meiosis, protects centromeric cohesion complexes until
CC       metaphase II/anaphase II transition, preventing premature release of
CC       meiosis-specific REC8 cohesin complexes from anaphase I centromeres. Is
CC       thus essential for an accurate gametogenesis. May act by targeting
CC       PPP2CA to centromeres, thus leading to cohesin dephosphorylation.
CC       Essential for recruiting KIF2C to the inner centromere and for
CC       correcting defective kinetochore attachments. Involved in centromeric
CC       enrichment of AUKRB in prometaphase. {ECO:0000250|UniProtKB:Q562F6,
CC       ECO:0000269|PubMed:18084284, ECO:0000269|PubMed:18765791}.
CC   -!- SUBUNIT: Interacts with PPP2CA. Part of an astrin (SPAG5)-kinastrin
CC       (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2.
CC       Interacts with CDCA8 (By similarity). {ECO:0000250|UniProtKB:Q562F6}.
CC   -!- INTERACTION:
CC       Q7TSY8; Q9Z1B5: Mad2l1; NbExp=3; IntAct=EBI-2552468, EBI-2552918;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q562F6}.
CC       Chromosome, centromere {ECO:0000269|PubMed:17205076,
CC       ECO:0000269|PubMed:18084284}. Chromosome, centromere, kinetochore
CC       {ECO:0000269|PubMed:17205076}. Note=Centromeric localization requires
CC       the presence of BUB1 and AUKRB (By similarity). During meiosis I,
CC       accumulates at centromeres during diplotene, and colocalizes
CC       differentially with the cohesin subunits RAD21 and REC8 at metaphase I
CC       centromeres (PubMed:17205076) (PubMed:18084284). SGO2 and RAD21 change
CC       their relative distributions during telophase I when sister-kinetochore
CC       association is lost (PubMed:17205076). During meiosis II, it shows a
CC       striking tension-dependent redistribution within centromeres throughout
CC       chromosome congression during prometaphase II, as it does during
CC       mitosis (PubMed:17205076). {ECO:0000250|UniProtKB:Q562F6,
CC       ECO:0000269|PubMed:17205076, ECO:0000269|PubMed:18084284}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed in proliferating cells.
CC       Highly expressed in the testis and oocytes.
CC       {ECO:0000269|PubMed:18084284}.
CC   -!- DISRUPTION PHENOTYPE: Mice develop normally and survive to adulthood
CC       without any apparent alteration. However, both males and females are
CC       infertile. This defect appears cytologically as complete loss of
CC       centromere cohesion at metaphase II, leading to single chromatids, and
CC       physiologically as formation of aneuploid gametes that gave rise to
CC       infertility. {ECO:0000269|PubMed:18765791}.
CC   -!- MISCELLANEOUS: Shugoshin is Japanese for guardian spirit (as it is
CC       known to be a protector of centromeric cohesin).
CC   -!- SIMILARITY: Belongs to the shugoshin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH23855.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; BC023855; AAH23855.1; ALT_SEQ; mRNA.
DR   EMBL; BC044797; AAH44797.1; -; mRNA.
DR   EMBL; BC052742; AAH52742.1; -; mRNA.
DR   EMBL; AK017868; BAB30980.1; -; mRNA.
DR   EMBL; AK042448; BAC31263.1; -; mRNA.
DR   CCDS; CCDS35574.1; -.
DR   RefSeq; NP_001171338.1; NM_001177867.1.
DR   RefSeq; NP_950172.1; NM_199007.2.
DR   AlphaFoldDB; Q7TSY8; -.
DR   SMR; Q7TSY8; -.
DR   BioGRID; 212920; 58.
DR   IntAct; Q7TSY8; 59.
DR   MINT; Q7TSY8; -.
DR   STRING; 10090.ENSMUSP00000027202; -.
DR   GlyGen; Q7TSY8; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q7TSY8; -.
DR   PhosphoSitePlus; Q7TSY8; -.
DR   EPD; Q7TSY8; -.
DR   MaxQB; Q7TSY8; -.
DR   PaxDb; 10090-ENSMUSP00000027202; -.
DR   PeptideAtlas; Q7TSY8; -.
DR   ProteomicsDB; 256987; -.
DR   Pumba; Q7TSY8; -.
DR   DNASU; 68549; -.
DR   Ensembl; ENSMUST00000027202.9; ENSMUSP00000027202.9; ENSMUSG00000026039.10.
DR   GeneID; 68549; -.
DR   KEGG; mmu:68549; -.
DR   UCSC; uc007bbk.2; mouse.
DR   AGR; MGI:1098767; -.
DR   CTD; 68549; -.
DR   MGI; MGI:1098767; Sgol2a.
DR   VEuPathDB; HostDB:ENSMUSG00000026039; -.
DR   eggNOG; ENOG502S9Y1; Eukaryota.
DR   GeneTree; ENSGT00940000154107; -.
DR   HOGENOM; CLU_264434_0_0_1; -.
DR   InParanoid; Q7TSY8; -.
DR   OMA; LNWNNEI; -.
DR   OrthoDB; 5263725at2759; -.
DR   PhylomeDB; Q7TSY8; -.
DR   TreeFam; TF350100; -.
DR   Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR   Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-MMU-68877; Mitotic Prometaphase.
DR   Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR   BioGRID-ORCS; 68549; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Sgo2a; mouse.
DR   PRO; PR:Q7TSY8; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q7TSY8; Protein.
DR   Bgee; ENSMUSG00000026039; Expressed in undifferentiated genital tubercle and 128 other cell types or tissues.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR   GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR   GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR   GO; GO:0030892; C:mitotic cohesin complex; ISO:MGI.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0007143; P:female meiotic nuclear division; IMP:MGI.
DR   GO; GO:0035875; P:maintenance of meiotic sister chromatid cohesion, centromeric; IMP:MGI.
DR   GO; GO:0007140; P:male meiotic nuclear division; IMP:MGI.
DR   GO; GO:0051177; P:meiotic sister chromatid cohesion; IBA:GO_Central.
DR   GO; GO:0010789; P:meiotic sister chromatid cohesion involved in meiosis I; IMP:MGI.
DR   GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IMP:MGI.
DR   GO; GO:2000711; P:positive regulation of maintenance of meiotic sister chromatid cohesion, centromeric; IMP:MGI.
DR   GO; GO:0008104; P:protein localization; IMP:MGI.
DR   InterPro; IPR038889; Shugoshin1/2.
DR   PANTHER; PTHR21577; SHUGOSHIN; 1.
DR   PANTHER; PTHR21577:SF3; SHUGOSHIN 1-RELATED; 1.
DR   Genevisible; Q7TSY8; MM.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW   Coiled coil; Direct protein sequencing; Kinetochore; Meiosis; Nucleus;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..1164
FT                   /note="Shugoshin 2"
FT                   /id="PRO_0000055440"
FT   REGION          160..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          521..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          917..992
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1092..1164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          62..113
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        174..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        219..251
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..434
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..477
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        522..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        931..952
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1042
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q562F6"
FT   CONFLICT        78
FT                   /note="Q -> R (in Ref. 2; BAB30980)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1164 AA;  130277 MW;  64BCDCE5738576D6 CRC64;
     MEYPGIKVDT VTSGIQRRVK GRIAKTNLNV SLASKIKAKI LNNSSIFKIS LKHNNRALAR
     ALSKEKENSR RITTEKMQLQ KEVEKLNFEN TFLRLKLNTL NKKLVEIESH VSNDLLTAIE
     ISSLSEFHQG SFLLSATKKQ RNSKQCKPAH LPYARVLLTS ENDDDDGADD KWQTKCNNRT
     ISKTSPDSTS SVSRQPSSLH QCNLKAFPPK EDNQKTCGSG HLEHTSSVDI LPNESHSDQS
     PKSSLSEMKT APSPSLRREK LSHGNVTMRK KCVSSTPDIL YVTDLDHQPT SSPGSNWNNE
     IHGHTNETSN NTQRNAECFL DLPSESSSEP DAKRMELVQK NTDSFHFQKT VYDAADMELT
     ATDIGKIVAV SKSKKNQNKK KADCRKETFR KVKGASSDKK RESSKRECKD GSEVGAEEEA
     DAARAERGAG VLDGRGDSEE PNCISSTEQP SQVNTQKKRT LQNSSDQENI QNTKRRQTYT
     TDEQEETNPF SRHSVKFLQD GKFDLCQKTL HHNLSKPSRQ TFVIRKSEKD NLFPNQEDKD
     TISENLEVTN EFHIDDLSIE ANENVCDHET QTMLDLKKSV SAQQNQTKIN KTKQKINRRT
     KIISVMSQVY EDNDKDIHVL EKDNFPFHTQ ANKETTSGNL ESSKEFESPL LFTRDNGSLR
     DCKTQNVLDL HKQIPDLYPD RNESQISKIP RQKVNRKTEV ISGVKCFSND QGVHCSEKDK
     SLLLQKDKDF PGTLKDLSEF DTPAFCNKDS AKSCDYKSEM LLGLKKHDPN MQPACQDDSK
     AGKKLRQKVN RKTEIISKIT QIHENDRGST HDSLNKKLCQ KVNISKIISQ MNQIYETINE
     DGNGFKSSIK DCEDIKSCDF GEINSNKKEN YDPIQDPCTL VKKTKRKGSC KAGSSLAGAK
     NRCGLQLTDS SQVQSVPLDS GLRHHPNEAD SGPGEQTNLP KMQKQSAGRS LGDAFSVSLG
     KEGSRPAKAV SKMTPKSKKR KLPLGCSPET HGTVEITPNT DLAKAVDSQQ TEKENYLEKE
     KIAKRKPDFC TKVLKPLSET CSSNIKNSSL DSMCKSSLPL SISSRKTLML EESSSLESTC
     IFQVGDAAHE KITTGTRNPH HRTQKSTPGS RTSLVLVDTS SVSDTNPANP ENESEGQSSH
     PMRRKRQCVP LNLTEPSLRS KMRR
//