STAG2_XENLA
ID STAG2_XENLA Reviewed; 1194 AA.
AC Q9DGN0;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cohesin subunit SA-2;
DE Short=xSA-2;
DE AltName: Full=SCC3 homolog 2;
DE AltName: Full=Stromal antigen 2 homolog;
GN Name=stag2; Synonyms=sa2;
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], AND IDENTIFICATION IN A COHESIN COMPLEX WITH
RP SMC1; SMC3 AND RAD21.
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 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. {ECO:0000250|UniProtKB:Q8N3U4}.
CC -!- SUBUNIT: Part of the cohesin complex which is composed of a heterodimer
CC between a SMC1 protein (SMC1A or SMC1B) and SMC3, which are attached
CC via their hinge domain, and RAD21 which link them at their heads, and
CC one STAG protein (STAG1, STAG2 or STAG3). In cohesin complexes, STAG2
CC is mutually exclusive with STAG1 and STAG3. Interacts directly with
CC RAD21 in cohesin complex. {ECO:0000269|PubMed:10931856}.
CC -!- INTERACTION:
CC Q9DGN0; O93309: smc3; NbExp=2; IntAct=EBI-80675, 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 {ECO:0000269|PubMed:11931760}.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF255018; AAG00431.1; -; mRNA.
DR RefSeq; NP_001080997.1; NM_001087528.1.
DR AlphaFoldDB; Q9DGN0; -.
DR SMR; Q9DGN0; -.
DR BioGRID; 98921; 5.
DR IntAct; Q9DGN0; 8.
DR PRIDE; Q9DGN0; -.
DR GeneID; 394319; -.
DR KEGG; xla:394319; -.
DR CTD; 394319; -.
DR Xenbase; XB-GENE-17332484; stag2.L.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 394319; Expressed in gastrula and 19 other tissues.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007062; P:sister chromatid cohesion; ISS:UniProtKB.
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 Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1194
FT /note="Cohesin subunit SA-2"
FT /id="PRO_0000120187"
FT DOMAIN 224..309
FT /note="SCD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT REGION 986..1027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 137825 MW; 804FC73E468B13CE CRC64;
MNGHHQQNGV ENMMLFEVVK MGKSAMQSVV DDWIEAYKHS KDVALLDLIN FFIQCSGCKG
VVSGEMFRHM QNSEIIRRMT EEFDEDSGDY PLTMAGPQWK KFKFSFCEFI GVLVRQCQYS
IIYDEYMMDT VISLLTGLSD SQVRAFRHTS TLAAMKLMTA LVNVALNLSI NMDNTQRQYE
AERNKMIGKR ANDRLELLLQ KRKELQENQD EIENMMNAIF KGVFVHRYRD AIAEIRAICI
EEIGVWMKMY SDAFLNDSYL KYVGWTMHDK QGEVRLKCLT ALQGLYYNRE LNTKLELFTS
RFKDRIVSMT LDKEYDVAVQ AIKLLTLVLQ SSDEVLTAED CENVYHLVYS AHRPVAVAAG
EFLYKKLFSC RDPEEDGIMK RRGRLSPNAN LVKTLVFFFL ESELHEHAAY LVDSMWDCAT
ELLKDWDCMN SLLLDDPLNG EEALTDRQES ALIEILLCTV RQAAECHPPV GRGTGKRVLT
AKEKKSQMDD KTHLTELFAV SLPQLLAKYS VDAEKVTNLL QLPQYFDLEI YTTGRLEKHL
EALLRQIRNI VEKHTDTDVL EACSKTYHAL CNEEFTIYNR VDIAKSQLID ELADKFNRLL
EDFLQEEEEL DEDDAYQVLS TLKRITAFHN AHDLSRWDLF SGNYKLLKTG IENGDMPEQI
VVHALQCTHY VILWQLAKFS ETGSSKEELI TLKRQMRVFC QICQHYLTNV NTAVKEQAFT
ILCDVLMIFS HQIVVGGREA LEPLVYSPDS SLQSELLSFI LDHVFIDQDD DNSSSDGQQD
DEASKIEALH KRRNLLAAFC KLIVYNVVEM NTAADIFKQY MRYYNDYGDI IKETMSKTRQ
IDKIQCAKTL ILSLQQLFNE MIQEHSYNFD RSSPTFSAIK ELARRFALTF GLDQLKTREA
IAMLHKDGIE FAFKEPSPQG EAHPPLNMAF LDILSEFSSK LLRQDKKTVY AYLERFMTFQ
MSLRREDVWL PLMSYRNSLL AGGDDDTMSV MSGMSGRGSS TRSKKIKPPT GKRKLPEAEE
SSSSDSMWLN REQTMNTPVM LQTPQLTSTI MREPKRLRPE ESYMPVYPMQ PEHHQPSLDY
NTQVTWMLAQ RQQEEAARQQ QERAAMNYVK LRSNLQHAIR RNTGLMEDDE EPIVEDVMMS
SEGRIEDLNE GMDFDTMDID LPPSKNRRER TELKPDFFDP ASIMDESVLG VSMF
