ID F8WHU7_MOUSE Unreviewed; 1221 AA.
AC F8WHU7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=Stag1 {ECO:0000313|Ensembl:ENSMUSP00000040724.7,
GN ECO:0000313|MGI:MGI:1098658};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000040724.7, ECO:0000313|Proteomes:UP000000589};
RN [1] {ECO:0000313|Ensembl:ENSMUSP00000040724.7, ECO:0000313|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000040724.7,
RC ECO:0000313|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2] {ECO:0007829|PubMed:21183079}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3] {ECO:0000313|Ensembl:ENSMUSP00000040724.7}
RP IDENTIFICATION.
RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000040724.7};
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_006510988.1; XM_006510925.2.
DR AlphaFoldDB; F8WHU7; -.
DR SMR; F8WHU7; -.
DR EPD; F8WHU7; -.
DR MaxQB; F8WHU7; -.
DR PeptideAtlas; F8WHU7; -.
DR ProteomicsDB; 345586; -.
DR Antibodypedia; 17829; 294 antibodies from 29 providers.
DR DNASU; 20842; -.
DR Ensembl; ENSMUST00000041418.13; ENSMUSP00000040724.7; ENSMUSG00000037286.16.
DR GeneID; 20842; -.
DR AGR; MGI:1098658; -.
DR CTD; 10274; -.
DR MGI; MGI:1098658; Stag1.
DR VEuPathDB; HostDB:ENSMUSG00000037286; -.
DR GeneTree; ENSGT00950000182972; -.
DR HOGENOM; CLU_005067_1_0_1; -.
DR BioGRID-ORCS; 20842; 9 hits in 81 CRISPR screens.
DR ChiTaRS; Stag1; mouse.
DR Proteomes; UP000000589; Chromosome 9.
DR Bgee; ENSMUSG00000037286; Expressed in embryonic post-anal tail and 258 other cell types or tissues.
DR ExpressionAtlas; F8WHU7; baseline and differential.
DR GO; GO:0000785; C:chromatin; IEA:UniProtKB-UniRule.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0007062; P:sister chromatid cohesion; IEA:UniProtKB-UniRule.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199:SF6; COHESIN SUBUNIT SA-1; 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 1: Evidence at protein level;
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|RuleBase:RU369063};
KW Proteomics identification {ECO:0007829|EPD:F8WHU7,
KW ECO:0007829|MaxQB:F8WHU7};
KW Reference proteome {ECO:0000313|Proteomes:UP000000589}.
FT DOMAIN 296..381
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 260..290
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1221 AA; 140133 MW; 953A0F27A3565096 CRC64;
MITSELPVLQ DSTNETTAHS DAGSELEETE VKGKRKRGRP GRPPSTNKKP RKSPGEKSRI
EAGIRGAGRG RANGHPQQNG DGDPVTLFEV VKLGKSAMQS VVDDWIELYK QDRDIALLDL
INFFIQCSGC RGTVRIEMFR NMQNAEIIRK MTEEFDEDSG DYPLTMPGPQ WKKFRSNFCE
FIGVLIRQCQ YSIIYDEYMM DTVISLLTGL SDSQVRAFRH TSTLAAMKLM TALVNVALNL
SIHQDNTQRQ YEAERNKMIG KRANERLELL LQKRKELQEN QDEIENMMNS IFKGIFVHRY
RDAIAEIRAI CIEEIGVWMK MYSDAFLNDS YLKYVGWTLH DRQGEVRLKC LKALQSLYTN
RELFPKLELF TNRFKDRIVS MTLDKEYDVA VEAIRLVTLI LHGSEEALSN EDCENVYHLV
YSAHRPVAVA AGEFLHKKLF SRHDPQAEEA LAKRRGRNSP NGNLIRMLVL FFLESELHEH
AAYLVDSLWE SSQELLKDWE CMTELLLEEP VQGEEAMSDR QESALIELMV CTIRQAAEAH
PPVGRGTGKR VLTAKERKTQ IDDRNKLTEH FIITLPMLLS KYSADAEKVA NLLQIPQYFD
LEIYSTGRME KHLDALLKQI KFVVEKHVES DVLEACSKTY SILCSEEYTI QNRVDIARSQ
LIDEFVDRFN HSVEDLLQEG EEADDDDIYN VLSTLKRLTS FHNAHDLTKW DLFGNCYRLL
KTGIEHGAMP EQIVVQALQC SHYSILWQLV KITDGSPSKE DLLVLRKTVK SFLAVCQQCL
SNVNTPVKEQ AFMLLCDLLM IFSHQLMTGG REGLQPLVFN PDTGLQSELL SFVMDHVFID
QDEENQSMEG DEEDEANKIE ALHKRRNLLA AFSKLIIYDI VDMHAAADIF KHYMKYYNDY
GDIIKETLSK TRQIDKIQCA KTLILSLQQL FNELVQEQGP NLDRTSAHVS GIKELARRFA
LTFGLDQIKT REAVATLHKD GIEFAFKYQN QKGQEYPPPN LAFLEVLSEF SSKLLRQDKK
TVHSYLEKFL TEQMMERRED VWLPLISYRN SLVTGGEDDR MSVNSGSSSS KTSSVRSKKG
RPPLHRKRVE DESLDNTWLN RTDTMIQTPG PLPTPQLTST VLRENSRPMG EQIQEPESEH
GSEPDFLHNR GLMEEDAEPI FEDVMMSSRS QLEDMNEEFE DTMVIDLPPS RNRRERAELR
PDFFDSAAII EDDSGFGMPM F
//
