ID   STAG1_XENLA             Reviewed;        1265 AA.
AC   Q9DGN1; Q5D028;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Cohesin subunit SA-1;
DE            Short=xSA-1;
DE   AltName: Full=SCC3 homolog 1;
DE   AltName: Full=Stromal antigen 1 homolog;
GN   Name=stag1; Synonyms=sa1;
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 [MRNA], PROTEIN SEQUENCE OF 328-340; 451-459 AND
RP   620-625, SUBUNIT OF A COMPLEX COMPOSED OF SMC1; SMC3 AND RAD21, AND
RP   PHOSPHORYLATION.
RC   TISSUE=Egg;
RX   PubMed=10931856; DOI=10.1083/jcb.150.3.405;
RA   Losada A., Yokochi T., Kobayashi R., Hirano T.;
RT   "Identification and characterization of SA/Scc3p subunits in the Xenopus
RT   and human cohesin complexes.";
RL   J. Cell Biol. 150:405-416(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PHOSPHORYLATION BY PLK1.
RX   PubMed=11931760; DOI=10.1016/s1097-2765(02)00473-2;
RA   Sumara I., Vorlaufer E., Stukenberg P.T., Kelm O., Redemann N., Nigg E.A.,
RA   Peters J.-M.;
RT   "The dissociation of cohesin from chromosomes in prophase is regulated by
RT   Polo-like kinase.";
RL   Mol. Cell 9:515-525(2002).
CC   -!- FUNCTION: Component of cohesin complex, a complex required for the
CC       cohesion of sister chromatids after DNA replication. The cohesin
CC       complex apparently forms a large proteinaceous ring within which sister
CC       chromatids can be trapped. At anaphase, the complex is cleaved and
CC       dissociates from chromatin, allowing sister chromatids to segregate.
CC       The cohesin complex may also play a role in spindle pole assembly
CC       during mitosis.
CC   -!- SUBUNIT: Interacts directly with RAD21 in cohesin complex. Cohesin
CC       complexes are composed of a heterodimer between and SMC3, which are
CC       attached via their hinge domain, and RAD21 which link them at their
CC       heads, and one STAG protein (STAG1 OR STAG2). In cohesin complexes,
CC       STAG1 is mutually exclusive with STAG2. {ECO:0000269|PubMed:10931856}.
CC   -!- INTERACTION:
CC       Q9DGN1; O93309: smc3; NbExp=2; IntAct=EBI-80622, EBI-80653;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Chromosome, centromere.
CC       Note=Associates with chromatin. Before prophase it is scattered along
CC       chromosome arms. During prophase, most of cohesin complexes dissociate
CC       from chromatin probably because of phosphorylation by PLK1, except at
CC       centromeres, where cohesin complexes remain. At anaphase, the RAD21
CC       subunit of cohesin is cleaved, leading to the dissociation of the
CC       complex from chromosomes, allowing chromosome separation.
CC   -!- PTM: Phosphorylated by PLK1. The large dissociation of cohesin from
CC       chromosome arms during prophase is partly due to its phosphorylation
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
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DR   EMBL; AF255017; AAG00430.1; -; mRNA.
DR   EMBL; BC068770; AAH68770.1; -; mRNA.
DR   RefSeq; NP_001083864.1; NM_001090395.1.
DR   AlphaFoldDB; Q9DGN1; -.
DR   SMR; Q9DGN1; -.
DR   BioGRID; 100488; 1.
DR   IntAct; Q9DGN1; 8.
DR   DNASU; 399163; -.
DR   GeneID; 399163; -.
DR   KEGG; xla:399163; -.
DR   CTD; 399163; -.
DR   Xenbase; XB-GENE-1006159; stag1.S.
DR   OrthoDB; 167826at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 399163; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
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; Cell division; Centromere; Chromosome; Chromosome partition;
KW   Direct protein sequencing; Mitosis; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..1265
FT                   /note="Cohesin subunit SA-1"
FT                   /id="PRO_0000120184"
FT   DOMAIN          303..388
FT                   /note="SCD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1063..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1111..1130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..75
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1064..1083
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1265 AA;  145244 MW;  700ED07D76B7E824 CRC64;
     MITSELSVLQ DSTNESAVMH TDMTAVSADL STELVEDLEV KGKRKRGRPG RPPSAIKKPR
     KTPGDRSRAE PGSRGRGRAN GHPQQNGEGD PVTLFEVVKM GKSAMQAVVD DWIESYKQDR
     DIALLDLINF FIQCSGCKGT VRIEMFRNMQ NAEIIRKMTE EFDEDSGDYP LTMPGPHWKK
     FRCNFCEFIS VLIRQCQYSI IYDEYMMDTV ISLLTGLSDS QVRAFRHTST LAAMKLMTAL
     VNVALNLSIH QDNTQRQYET ERNKIINKRA NERLELLLQK RKELQENQDE IENMMNSIFK
     GIFVHRYRDA IAEIRAICIE EIGVWMKMYS DAFLNDSYLK YVGWTLHDRQ GEVRLKCLKA
     LQSLYTNREL FPKLELFTNR FKDRIVSMTL DKEYDVAVEA IRLVTLILHG SEEALSNEDC
     ENVYHLVYSA HRPVAVAAGE FLHKKLFSRH DPQAEEALAK RRGRSSPNGN LVKMLVLFFL
     ESELHEHAAY LVDSLWESSQ ELLKDWECMT ELLVEEPMQG EEVMSERQES ALVELMVCTI
     RQAAEAHPPV GRGTGKRVLT AKERKTQLDD KTKLTEHFIV ALPVLLSKYS ADAEKVANLL
     QIPQYFDLEL YSTGRMEKHL DSLLKQIRFV VEKHIESDVL EACSKTYSIL CSEEYTIQNR
     VEIAHSQLID ELADRFSHAV EELLQEAEEA DEDEIYNVMA SLKRLTCFHN AHDLTKWDFF
     GNCYRLLRAG IEHEGMMEQI VVQALQCSHY SILWQLVKIT EGNPSKEEML ALRKTVKSFL
     AVCQQCLSSM TTLVKEQAFM LLCDLLMIFS HQLTTGGREN LLLLVFNPDV GLQSELLSFV
     MDHVFIDQDD ENQSMEGDEE DEANKIEALH KRRNLLASFC KLIIYDIVDM NAAADIFKHY
     MKYYNDYGDI IKETLSKTRQ MDKIQCAKTL ILSLQQLFNE LVQEQGPNLD RTSAHVSGIK
     ELARRFALTF GLDQIKTREA VATLHKDGIE FAFKYQNPKG PEYPPLNLAF LEVLSEFSSK
     LLRQDKKTVH SYLEKFLTDL MMERREDVWL PLISYRNSLV TGGDEDRLSV NSGGSNSKGS
     SVRSKKGRPP LHKKRVIEEE SIDNSWVTRN DTIQTPGALT TPQLTSTVLR ENPRQIPEQI
     PEQESEPSSE PDFLHSPQMQ MSWLGQQKLE DLNRKDRTSM SYMKVRSGVR HAVRGLMEDD
     AEPIFEDVMM SSRGQLEDMN EEFEDTMVID LPPSRNRRER AELRPDFFDS AAIIEDDSGF
     GMPMF