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Database: UniProt
Entry: M3YW48_MUSPF
LinkDB: M3YW48_MUSPF
Original site: M3YW48_MUSPF 
ID   M3YW48_MUSPF            Unreviewed;      1249 AA.
AC   M3YW48;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 55.
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:ENSMPUP00000015558.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000015558.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000015558.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-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   EMBL; AEYP01053095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01053096; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01053097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AEYP01053098; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004761546.1; XM_004761489.2.
DR   AlphaFoldDB; M3YW48; -.
DR   STRING; 9669.ENSMPUP00000015558; -.
DR   Ensembl; ENSMPUT00000015799.1; ENSMPUP00000015558.1; ENSMPUG00000015668.1.
DR   KEGG; mpuf:101689444; -.
DR   eggNOG; KOG2011; Eukaryota.
DR   GeneTree; ENSGT00950000182972; -.
DR   HOGENOM; CLU_005067_1_0_1; -.
DR   InParanoid; M3YW48; -.
DR   OMA; WDCAAPL; -.
DR   OrthoDB; 5354237at2759; -.
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; 2.
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}.
FT   DOMAIN          321..406
FT                   /note="SCD"
FT                   /evidence="ECO:0000259|PROSITE:PS51425"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1085..1249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..92
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1097..1120
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1121..1143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1161..1180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1216..1234
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1249 AA;  140716 MW;  15F77E2E2D712AF5 CRC64;
     MPTLRSSSSP SSVSSPLRRA AGGGQRGLSA SSSSSVSVPY GNRDSGQTSQ GDSDSLSADE
     GSDFEDSLRR SVRKRAARRP LKTTPVAKHP KKGSRMIRGD GQKDSEVPAS HLFDAVKAAK
     SDMQSLVDEW LDSYKQDQDA GFLELINFFI RSCGCKGNVT PEMFKKMSNS EIIRHLTEQF
     NEDSGDYPLT APGPSWKKFQ GSFCEFVKTL VFQCQYSLLY DGFPMDNLIS LLTGLSDSQV
     RAFRHTSTLA AMKLMTSLVR VALQLSLHKD NNQRQYEAER NKGPGQRAPE RLESLLEKRK
     ELQEHQEEIE GMMNALFRGV FVHRYRDVLP EIRAICIEEI GSWMQSYSTS FLTDSYLKYI
     GWTLHDKHRE VRLKCLKALK ALYSSRDLTA RLELFTSRFK DRMVSMVMDR EYDVAVEAVK
     LLTIILKNME GVLTDADCEG IYPVVYASHR ALASAAGEFL YWKLFYPECE TRAEGGRQRR
     RSPRAQRTFF HLLLSFFVES ELHDHAAYLV DSLWDCAGAQ LKDWESLTSL LLEKDQSACR
     VTAGGGGLSP PNLGDVQEST LIEILVSSVR QASEGHPPVG RLTGKKGLTP KERKTQADDK
     VKLTEHLIPL LPQLLAKFSA DAEKVAPLLQ LLNHFDLNIY CTRRLEKHLE LFLQQLQEVV
     VKHAEPAVLE AGAHALYLLC NPEFTFFGRV DFARSQLVDL LTDRFQQELE ELLQSPFLDE
     DEVYSLAATL KRLSAFYNAH DLSRWELYEP CYRLLRKAVD TGEVPHQVIL PALTLVYFSI
     LWTLSHLSES DASQKQLLSL KGRVVAFCEL CQSCLSDVDS DIQEQAFVLL SDLLLVFSPQ
     MILGGRDFLR PLVFFPEATL QSELASFLMD HVFIQPGELG SGHSQEDHVH IEQLHQRRRL
     LAGFCKLLLY GVLEMDAASD VFKHYNKFYN DYGDIIKETL TRARQIDRSH CSRILLLSLK
     QLYTELLQEQ GPQGLNELPA FGEMRDLARR FALSFGPQQL QNRDLVVALH KEGIRFSLSE
     PPPAGSSGQP PNLAFLELLS EFSPRLFHQD KQLLLSYLGK GLQRVSQSLD CPWGPVTTYC
     HSLSPVESTA EASPQGYPRS KKRRTEGPPR RQREDVRPSQ EESLQLTSIP PSPTLTSTAV
     KRGQPQRALG EAEEEGSSEP EHSAQGSQPL SGNQRPRFSS PRRFRTLLHP PGPGLGSRLT
     RLSLMEEDED ELEAHSELSE GWQDADKHSS PSEHGLDLLD STELNLEDF
//
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