ID G5AN26_HETGA Unreviewed; 1167 AA.
AC G5AN26;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
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 ORFNames=GW7_15809 {ECO:0000313|EMBL:EHA98436.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHA98436.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHA98436.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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; JH166116; EHA98436.1; -; Genomic_DNA.
DR AlphaFoldDB; G5AN26; -.
DR STRING; 10181.G5AN26; -.
DR eggNOG; KOG2011; Eukaryota.
DR InParanoid; G5AN26; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
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: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:UP000006813}.
FT DOMAIN 330..415
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1064..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..103
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 960..981
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1082..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1167 AA; 131744 MW; A2E8BE8DF2C12D62 CRC64;
MPTLKSSGSS PQLHSSSSPS SVSSSLQRTV GVAQRALSAS SSSSINLPCE DKDSELASKG
AGPSLSGDEG SDFEDSLRRN VKKRRAKRPH KTTPVAKHPK KGSQIICRKV QKKSELPACD
LFDAVKAAKS DMQSLVDEWL ESYKQDEDTG FLELVNFFIR SCGCKGTVTP EMFKKMSNSE
VIRHLTEQFN EDSGDYPLTA SGPSWKKFQG SFCEFVKMLV CQCQYSLLYD GFPMDNLISL
LTGLSDSQVR AFRHTSTLAA MKLMTSLVRV ALQLSLHKDN SQRQYESERN KGPEQRSPER
LESLLEKRKE LQEHQEEIEG MMNAIFRGVF VHRYRDILPE IRAICIEEIG CWMQSYGTSF
LTDSYLKYIG WTLHDKHRDV RLTCLKALQG LYSNRELTAR LELFTSRFKD RMVSMVMDRE
YDVAVEAVRL LILILKNMEG VLTSADCESV YPVVYASHRP LAAAAGEFLY WKLFYPEFEM
RAVFGRERHR SPHAQRTFFH LLLYFFMEIE LHDHATYLVD SLWDCAGPHL KDWESLTSLL
LEKDQNLSDV QENTLIEILV SSARQAVEGH PPVGRVSGRK GLSAKERKVQ ADDKVKLTEH
LIPLLPQLLA KFSADAEKVA PLLQLLNYFD LSIYCTGRLE KQLQEVVVKH TEPPVLEAGA
QALYVLCKPE FTFFSRVDFA RSQLVDLLTD RFQQELEELL QKQLLSLKGK MVAVCELCQN
YLSGVDLQIQ EQAFVLLTDL LLIFSPQMIA GGRDFLRPLI FFPEATLQSE LASFLMDHVF
LQSGDLGSGQ TQDDHKQIEQ LNQRRRLLAG FCKLLLYGVL ELDAASDVFK HYNKFYNDYG
DIIKETLTRA RQIDRSHCSR ILLLSLKQLY TELLQEQGPQ GLSELPAFME MRDLARKFAL
SFGPQQLQNR DIVMKLHRLS YLEKCLQRVP QTPGCPWGPV TTYRHSLSPV ESTAEANPQG
HSRSKKRRIE GPSKHQRADQ EESLQLNSVP PTPTLTSTAV KSKQPLGVLG ETEEEDGLES
EFSQSRFLSG TQRPRFSGAQ YFQTSSSPSG PGLDNKLTRL SLMEEDEEEL ESLDESSEEW
QNTKKQPGSH SSLSEHGLDL LDSTELNIEV SVPGARDCVL GNAAGQPVKW TERLKPLGGP
LVVSGALAGE VRFNQGYAVF CFPFGIL
//
