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Database: UniProt
Entry: U3F944_CALJA
LinkDB: U3F944_CALJA
Original site: U3F944_CALJA 
ID   U3F944_CALJA            Unreviewed;      1231 AA.
AC   U3F944; F7CRJ9;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
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=STAG2 {ECO:0000313|EMBL:JAB31825.1,
GN   ECO:0000313|Ensembl:ENSCJAP00000049766.2};
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|EMBL:JAB31825.1};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000049766.2}
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|EMBL:JAB31825.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Bladder {ECO:0000313|EMBL:JAB08804.1}, Cerebellum
RC   {ECO:0000313|EMBL:JAB51947.1}, Cerebral cortex
RC   {ECO:0000313|EMBL:JAB31825.1}, Hippocampus
RC   {ECO:0000313|EMBL:JAB22408.1}, and Skeletal muscle
RC   {ECO:0000313|EMBL:JAB39190.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
RN   [3] {ECO:0000313|Ensembl:ENSCJAP00000049766.2}
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   EMBL; GAMT01003057; JAB08804.1; -; mRNA.
DR   EMBL; GAMS01000728; JAB22408.1; -; mRNA.
DR   EMBL; GAMR01002107; JAB31825.1; -; mRNA.
DR   EMBL; GAMQ01002661; JAB39190.1; -; mRNA.
DR   EMBL; GAMP01000808; JAB51947.1; -; mRNA.
DR   Ensembl; ENSCJAT00000061307.4; ENSCJAP00000049766.2; ENSCJAG00000020559.5.
DR   GeneTree; ENSGT00950000182972; -.
DR   HOGENOM; CLU_005067_1_0_1; -.
DR   Proteomes; UP000008225; Chromosome X.
DR   Bgee; ENSCJAG00000020559; Expressed in cerebellum and 6 other cell types or tissues.
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:SF3; COHESIN SUBUNIT SA-2; 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   2: Evidence at transcript 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   Reference proteome {ECO:0000313|Proteomes:UP000008225}.
FT   DOMAIN          293..378
FT                   /note="SCD"
FT                   /evidence="ECO:0000259|PROSITE:PS51425"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1064..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          234..287
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        21..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1231 AA;  141312 MW;  22C14B141617EEBE CRC64;
     MIAAPEIPTD FNILQESETH FSSDTDFEDI EGKNQKQGKG KTCKKGKKGP AEKGKGGNGG
     GKPPSGPNRM NGHHQQNGVE NMMLFEVVKM GKSAMQSVVD DWIESYKHDR DIALLDLINF
     FIQCSGCKGV VTAEMFRHMQ NSEIIRKMTE EFDEDSGDYP LTMAGPQWKK FKSSFCEFIG
     VLVRQCQYSI IYDEYMMDTV ISLLTGLSDS QVRAFRHTST LAAMKLMTAL VNVALNLSIN
     MDNTQRQYEA ERNKMIGKRA NERLELLLQK RKELQENQDE IENMMNAIFK GVFVHRYRDA
     IAEIRAICIE EIGIWMKMYS DAFLNDSYLK YVGWTMHDKQ GEVRLKCLTA LQGLYYNKEL
     NSKLELFTSR FKDRIVSMTL DKEYDVAVQA IKLLTLVLQS SEEVLTAEDC ENVYHLVYSA
     HRPVAVAAGE FLYKKLFSRR DPEEDGMMKR RGRQGPNANL VKTLVFFFLE SELHEHAAYL
     VDSMWDCATE LLKDWECMNS LLLEEPLSGE EALTDRQESA LIEIMLCTIR QAAECHPPVG
     RGTGKRVLTA KEKKTQLDDR TKITELFAVA LPQLLGKYSV DAEKVTNLLQ LPQYFDLEIY
     TTGRLEKHLD ALLRQIRNIV EKHTDTDVLE ACSKTYHALC NEEFTIFNRV DISRSQLIDE
     LADKFNRLLE DFLQEGEEPD EDDAYQVLST LKRITAFHNA HDLSKWDLFA CNYKLLKTGI
     ENGDMPEQIV IHALQCTHYV ILWQLAKITE SSSTKEDLLR LKKQMRVFCQ ICQHYLTNVN
     TTVKEQAFTI LCDILMIFSH QIMSGGRDML EPLVYTPDSS LQSELLSFIL DHVFIEQDDD
     NNSADGQQED EASKIEALHK RRNLLAAFCK LIVYTVVEMN TAADIFKQYM KYYNDYGDII
     KETMSKTRQI DKIQCAKTLI LSLQQLFNEM IQENGYNFDR SSSTFSGIKE LARRFALTFG
     LDQLKTREAI AMLHKDGIEF AFKEPNPQGE SHPPLNLAFL DILSEFSSKL LRQDKRTVYV
     YLEKFMTFQM SLRREDVWLP LMSYRNSLLA GGDDDTMSVI SGISSRGSTV RSKKSKPSTG
     KRKVVEGMQL SLTEESSSSD SMWLSREQTL HTPVMMQTPQ LTSTIMREPK RLRPEDSFMS
     VYPMQTEHHQ TPLDYNRRGT SLMEDDEEPI VEDVMMSSEG RIEDLNEGMD FDTMDIDLPP
     SKNRRERTEL KPDFFDPASI MDESVLGVSM F
//
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