ID F6WTL9_CALJA Unreviewed; 1243 AA.
AC F6WTL9;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Cohesin subunit SA {ECO:0000256|RuleBase:RU369063};
DE AltName: Full=SCC3 homolog {ECO:0000256|RuleBase:RU369063};
DE AltName: Full=Stromal antigen {ECO:0000256|RuleBase:RU369063};
GN Name=STAG3 {ECO:0000313|Ensembl:ENSCJAP00000028428.4};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000028428.4, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000028428.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000028428.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|RuleBase:RU369063}.
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. {ECO:0000256|RuleBase:RU369063}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369063}.
CC Chromosome {ECO:0000256|RuleBase:RU369063}. Chromosome, centromere
CC {ECO:0000256|RuleBase:RU369063}.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000256|ARBA:ARBA00005486,
CC ECO:0000256|RuleBase:RU369063}.
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DR RefSeq; XP_017821919.1; XM_017966430.1.
DR AlphaFoldDB; F6WTL9; -.
DR STRING; 9483.ENSCJAP00000028428; -.
DR Ensembl; ENSCJAT00000030040.4; ENSCJAP00000028428.4; ENSCJAG00000015392.4.
DR GeneID; 100385764; -.
DR KEGG; cjc:100385764; -.
DR CTD; 10734; -.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR InParanoid; F6WTL9; -.
DR OMA; WDCAAPL; -.
DR TreeFam; TF314604; -.
DR Proteomes; UP000008225; Chromosome 2.
DR Bgee; ENSCJAG00000015392; Expressed in ovary and 1 other cell type or tissue.
DR GO; GO:0000785; C:chromatin; IEA:UniProtKB-UniRule.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0000800; C:lateral element; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0030893; C:meiotic cohesin complex; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000802; C:transverse filament; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IEA:Ensembl.
DR GO; GO:0034502; P:protein localization to chromosome; IEA:Ensembl.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199:SF8; COHESIN SUBUNIT SA-3; 1.
DR PANTHER; PTHR11199; STROMAL ANTIGEN; 1.
DR Pfam; PF21581; SCD; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR PROSITE; PS51425; SCD; 1.
PE 3: Inferred from homology;
KW Cell cycle {ECO:0000256|RuleBase:RU369063};
KW Cell division {ECO:0000256|RuleBase:RU369063};
KW Chromosome {ECO:0000256|RuleBase:RU369063};
KW Chromosome partition {ECO:0000256|RuleBase:RU369063};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369063};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT DOMAIN 327..412
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..105
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1213
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1243 AA; 140959 MW; 7CB0D4B26EE16793 CRC64;
MPTLPSSSSW PRSSSSPNLS SPLQRAVGGA KRALSESSSS SASLPFDDRD SSHTSEGNSD
SLSADEGSDF EDSFSRSVRK RAAKRPPKTT PVAKHPKKGS RVVHRHSRKQ SEPPANDLFS
AVKAAKSDMQ SLVDEWLDSY KQDQDAGFLE LVNFFTRSCG CKGTVTPEMF KKMSNSEIIQ
HLTEQFNEDS GDYPLTAPGP SWKKFRGSFC EFVRTLVCQC QYSLLYDGFP MDNLISLLTG
LSDSQVRAFR HTSTLAAMKL MTSLVRVALQ LSLHQDNNQR QYEAERNKGP GQRAPERLES
LLEKRKELQE HQEEIEGMMN ALFRGVFVHR YRDVLPEIRA ICIEEIGCWM QSYSTSFLTD
SYLKYIGWTL HDKHREVRLK CLKALKGLYG NRDLTTRLEL FTSRFKDRMV SMVMDREYDV
AVEAVRLLIL ILKNMEGVLT DTDCESIYPI VYASNRALAS AAGEFLYWKL FYPECKIRTV
GGREQRQSPG AQRTFFQLLL SFFVESELHD HAAYLVDSLW DCAGTQLKDW ESLTSLLLEK
DQNLGDVQES TLIEILVSSA RQASEGHPPV GRVTGRKGLT SKERKTQADD RVKLTEHLIP
LLPQLLAKFS ADAEKVTPLL QLLSCFDLHI YCTGRLEKHL ELLLKQLQEV VVKHTEPAVL
EAGAHALYLL CNPEFTFFSR ADFARSQLVD LLTDRFQQEL EELLQSSFLD EDEVYNLATT
LKRLSAFYNA HDLTRWELYE PCCQLLQKAV DTGEVPHQVI LPALTLVYFS ILWTLTHISK
SDASQKQLSS LRERMVAFCE LCQSCLSDVD PEIREQAFVL LSDLLLIFSP QMIVGGRDFL
RPLVFFPEAT LQSELASFLM DHVFIQPGDL GSGDSKEDHL QIEQLHQRRR LLAGFCKLLL
YGVLEMDAAS DVFKHYNKFY NDYGDIIKET LTRARQIDRS HCSRILLLSL KQLYTELLQE
HGPQGLNEHP AFIEIRDLAR RFALSFGPQQ LQNRDLVVLL HKEGIKFSLS ELPPAGSSDQ
PPNLAFLELL SEFSPRLFHQ DKQLLLSYLE KCLKHISQAP GHPWGPVTAY CHSLSPVENT
AETSPQVLPR SKKRRVEGPA KPDREEISSS QEESLQLNSI PPTPTLTSTA VKSRQPLWGL
EEMEEDDSEL DFAQGSQPLA GTQRSRFLGP QSIQTPHNPS GPGLGNQLMR LNLMEEDEEK
ELEIQDESSE EWQDTDMQAS TYSSPSERRL DLLDSTELDI EDF
//
