SGO1_SCHPO
ID SGO1_SCHPO Reviewed; 319 AA.
AC Q9P7A0;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Shugoshin-1;
GN Name=sgo1; ORFNames=SPBP35G2.03c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, PROBABLE UBIQUITINATION, AND MUTAGENESIS OF
RP ASN-29; ILE-50; PRO-293; SER-294; ARG-296; THR-297; LYS-298; LEU-299 AND
RP ARG-300.
RX PubMed=14730319; DOI=10.1038/nature02312;
RA Kitajima T.S., Kawashima S.A., Watanabe Y.;
RT "The conserved kinetochore protein shugoshin protects centromeric cohesion
RT during meiosis.";
RL Nature 427:510-517(2004).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14972679; DOI=10.1016/j.cub.2004.01.051;
RA Rabitsch K.P., Gregan J., Schleiffer A., Javerzat J.-P., Eisenhaber F.,
RA Nasmyth K.;
RT "Two fission yeast homologs of Drosophila Mei-S332 are required for
RT chromosome segregation during meiosis I and II.";
RL Curr. Biol. 14:287-301(2004).
RN [4]
RP FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Plays a central role in chromosome cohesion during meiosis by
CC preventing premature dissociation of cohesin complex from centromeres
CC after prophase, when most of cohesin complex dissociates from
CC chromosomes arms. May act by protecting centromeric rec8 from separase
CC degradation during anaphase I. {ECO:0000269|PubMed:14730319,
CC ECO:0000269|PubMed:14972679, ECO:0000269|PubMed:16303567}.
CC -!- INTERACTION:
CC Q9P7A0; Q10428: par1; NbExp=4; IntAct=EBI-989427, EBI-989357;
CC Q9P7A0; P40381: swi6; NbExp=3; IntAct=EBI-989427, EBI-926939;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere
CC {ECO:0000269|PubMed:14730319}. Note=Localizes to the centromere. Bub1
CC is required for centromeric localization (PubMed:14730319). At the
CC onset of anaphase I, it is degraded. {ECO:0000269|PubMed:14730319}.
CC -!- PTM: Ubiquitinated by the anaphase promoting complex (APC) at the onset
CC of anaphase, conducting to its degradation. {ECO:0000305}.
CC -!- MISCELLANEOUS: 'Shugoshin' means 'guardian spirit' in Japanese.
CC -!- SIMILARITY: Belongs to the shugoshin family. {ECO:0000305}.
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DR EMBL; CU329671; CAB87365.1; -; Genomic_DNA.
DR RefSeq; NP_595378.1; NM_001021285.2.
DR AlphaFoldDB; Q9P7A0; -.
DR SMR; Q9P7A0; -.
DR BioGRID; 277838; 27.
DR DIP; DIP-36613N; -.
DR IntAct; Q9P7A0; 2.
DR STRING; 4896.SPBP35G2.03c.1; -.
DR PaxDb; Q9P7A0; -.
DR PRIDE; Q9P7A0; -.
DR EnsemblFungi; SPBP35G2.03c.1; SPBP35G2.03c.1:pep; SPBP35G2.03c.
DR GeneID; 2541326; -.
DR KEGG; spo:SPBP35G2.03c; -.
DR PomBase; SPBP35G2.03c; sgo1.
DR VEuPathDB; FungiDB:SPBP35G2.03c; -.
DR HOGENOM; CLU_847752_0_0_1; -.
DR InParanoid; Q9P7A0; -.
DR OMA; SKCILAD; -.
DR PhylomeDB; Q9P7A0; -.
DR PRO; PR:Q9P7A0; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0000939; C:inner kinetochore; IDA:PomBase.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0072687; C:meiotic spindle; IDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR GO; GO:0140483; F:kinetochore adaptor activity; EXP:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045143; P:homologous chromosome segregation; IMP:PomBase.
DR GO; GO:1990813; P:meiotic centromeric cohesion protection; IMP:PomBase.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0045144; P:meiotic sister chromatid segregation; EXP:PomBase.
DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IMP:PomBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IMP:PomBase.
DR InterPro; IPR038889; Shugoshin.
DR InterPro; IPR011515; Shugoshin_C.
DR InterPro; IPR011516; Shugoshin_N.
DR PANTHER; PTHR21577; PTHR21577; 3.
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; Meiosis; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..319
FT /note="Shugoshin-1"
FT /id="PRO_0000055451"
FT COILED 33..62
FT /evidence="ECO:0000255"
FT MUTAGEN 29
FT /note="N->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:14730319"
FT MUTAGEN 50
FT /note="I->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:14730319"
FT MUTAGEN 293
FT /note="P->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:14730319"
FT MUTAGEN 294
FT /note="S->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:14730319"
FT MUTAGEN 296
FT /note="R->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:14730319"
FT MUTAGEN 297
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:14730319"
FT MUTAGEN 298
FT /note="K->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:14730319"
FT MUTAGEN 299
FT /note="L->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:14730319"
FT MUTAGEN 300
FT /note="R->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:14730319"
SQ SEQUENCE 319 AA; 37135 MW; 32F52DD0A1E0542A CRC64;
MNFQFINSNI NNEDKLPMES LKKKFLKQNR EIIKINTQLS IKIRESENEI QDLIQENFTL
KSYLVKLEAR FRNQSQTEDL LKNFFPEIQT IHKKISQVQS LLKIIEKKCS SDFLEANVKS
QFTTCENKDS KEDYQILHNK RLEYVSFNDE LKSLETGQPL YCFQDFQKKV HGPPALSEKP
GKCILKDKTN AHVNKIPQDE VNYSLPQKNI TIFSKELKEN EFESINEGET EEEKAKTSNV
CVCIPCKSAE QITDLKGQAT GDSSPCDFEE SQPRINGREK LRRSVKVINY AIPSLRTKLR
RDFDLPSDRK RKRHPRGKA
