SGO1_XENLA
ID SGO1_XENLA Reviewed; 663 AA.
AC Q4KLP8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Shugoshin 1 {ECO:0000250|UniProtKB:Q5FBB7};
DE AltName: Full=Shugoshin-like 1;
GN Name=sgo1 {ECO:0000250|UniProtKB:Q5FBB7}; Synonyms=sgo, sgol1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, PROBABLE UBIQUITINATION, DEVELOPMENTAL
RP STAGE, AND INTERACTION WITH MICROTUBULES.
RX PubMed=15339662; DOI=10.1016/j.cell.2004.08.016;
RA Salic A., Waters J.C., Mitchison T.J.;
RT "Vertebrate shugoshin links sister centromere cohesion and kinetochore
RT microtubule stability in mitosis.";
RL Cell 118:567-578(2004).
CC -!- FUNCTION: Plays a central role in chromosome cohesion during mitosis 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 preventing phosphorylation of the stag2
CC subunit of cohesin complex at the centromere, ensuring cohesin
CC persistence at centromere until cohesin cleavage by espl1/separase at
CC anaphase. May regulate kinetochore microtubule stability in mitosis,
CC possibly to sense tension on mitotic chromosomes.
CC {ECO:0000269|PubMed:15339662}.
CC -!- SUBUNIT: Binds microtubules.
CC -!- INTERACTION:
CC Q4KLP8; Q91912: Mad2; NbExp=16; IntAct=EBI-6977619, EBI-6977603;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15339662}.
CC Chromosome, centromere {ECO:0000269|PubMed:15339662}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:15339662}. Note=Localizes
CC to the centromere. At anaphase, it dissociates from centromeres when
CC chromatids separate. Localizes to kinetochores.
CC -!- DEVELOPMENTAL STAGE: High level during prophase and prometaphase and
CC weaker after the chromosomes attach to the spindle and align at the
CC metaphase plate. During anaphase, it is degraded, allowing the
CC separation of sister centromeres (at protein level).
CC {ECO:0000269|PubMed:15339662}.
CC -!- PTM: Ubiquitinated by the anaphase promoting complex (APC) at the onset
CC of anaphase, conducting to its degradation. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the shugoshin family. {ECO:0000305}.
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DR EMBL; BC099060; AAH99060.1; -; mRNA.
DR RefSeq; NP_001090071.1; NM_001096602.1.
DR RefSeq; XP_018122216.1; XM_018266727.1.
DR RefSeq; XP_018122217.1; XM_018266728.1.
DR AlphaFoldDB; Q4KLP8; -.
DR IntAct; Q4KLP8; 2.
DR MINT; Q4KLP8; -.
DR DNASU; 735145; -.
DR GeneID; 735145; -.
DR KEGG; xla:735145; -.
DR CTD; 735145; -.
DR Xenbase; XB-GENE-940797; sgo1.L.
DR OMA; CQWNKDQ; -.
DR OrthoDB; 1414582at2759; -.
DR Proteomes; UP000186698; Chromosome 6L.
DR Bgee; 735145; Expressed in egg cell and 19 other tissues.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0045132; P:meiotic chromosome segregation; IEA:InterPro.
DR GO; GO:0071962; P:mitotic sister chromatid cohesion, centromeric; IEA:InterPro.
DR InterPro; IPR028321; Sgo1.
DR InterPro; IPR038889; Shugoshin.
DR InterPro; IPR011515; Shugoshin_C.
DR InterPro; IPR011516; Shugoshin_N.
DR PANTHER; PTHR21577; PTHR21577; 1.
DR PANTHER; PTHR21577:SF3; PTHR21577:SF3; 1.
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; Kinetochore; Microtubule; Mitosis; Nucleus;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..663
FT /note="Shugoshin 1"
FT /id="PRO_0000055438"
FT REGION 207..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 8..29
FT /evidence="ECO:0000255"
FT COILED 110..132
FT /evidence="ECO:0000255"
FT COMPBIAS 208..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 663 AA; 74638 MW; 1FF8F3D40E0DE65A CRC64;
MVKERCPKQA FQDSLEDIKE RMKEKRIKKL AKVATVNKTL CTKVQILNSG STAIKNYKAN
NTALALALEA EKLKTRQAQD LILGLKREHQ RLIFEIFMLR RRLQSQQGRD TAESKLASLK
DIIAKVTHNL LETASLLEPA HLLCSSANNN TPNPSKVEEK LSSGASAILR LPSHAPISDT
LPKNVIPNRL EPEQRNFKDK VVLEANRNTA GVNRQSRGRR SHSNQPSFTS RLEECNNEDK
TESGATMNKN VSLRRRASSL NICLEESLPL EDTNVNSEHT VVETERPFPT EEFSNESRTD
REIDNVDNPA SPLKVKCFPH ANGSKMTGLA SEAKQTSNKN KEEPRVGRER VKKGKAERVA
VSQMKKPWEN SKPRARSKSR DRSASKKSVA KEKMNSSLNS GDAFDFACEE SIHVTPFRQN
KQEESQNESS LEISSSEGEL DDSLYKPYKD KSKNKNLKPD IAPVPLRSRS KRNTARKNSI
AENELMSDVQ AEANEKKITR NGLKRKSENS FTESAETYRE KSFMPTCINT NNAIAENPEV
KVFSDECNGG IIYTADEPSG ASTPRISLSD VTNLPGNTDA KKHINLLFNE DEMKRSSTPS
RKRRCKVSIN YAEPKLSGKL RRGDPFTDSE FLQSPIFKNE SKRNSLNRQS LSRYNEVFVG
CRR
