ID   A0A1S2ZTL6_ERIEU        Unreviewed;      1273 AA.
AC   A0A1S2ZTL6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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|RefSeq:XP_007524352.2};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_007524352.2};
RN   [1] {ECO:0000313|RefSeq:XP_007524352.2}
RP   IDENTIFICATION.
RG   RefSeq;
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_007524352.2; XM_007524290.2.
DR   AlphaFoldDB; A0A1S2ZTL6; -.
DR   STRING; 9365.ENSEEUP00000006851; -.
DR   CTD; 10735; -.
DR   eggNOG; KOG2011; Eukaryota.
DR   InParanoid; A0A1S2ZTL6; -.
DR   OrthoDB; 5354237at2759; -.
DR   Proteomes; UP000079721; Unplaced.
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   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|RuleBase:RU369063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721}.
FT   DOMAIN          298..383
FT                   /note="SCD"
FT                   /evidence="ECO:0000259|PROSITE:PS51425"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1273 AA;  146022 MW;  0FD87DBB19DB7C67 CRC64;
     MIAAPEIPTD FNLLQESETH FSSDTDFEDI EGKNQKQGKG KTCKKGKKGP GEKGKSGNGG
     GKPPSGPNRM NGHHQQNGVE NMMLFEVVKM GKSAMQSVVD DWIESYKHDR DIALLDLINF
     FIQCSGCKGV VTAEMFRHMQ NSEIIRKMTE EFDEDSGDYP LTMAGPQWKK FKSSFCEFIG
     VLVRQCQYSI IYDEYMMDTV ISLLTGLSDS QVRAFRHTST LAAMKLMTAL VNVALNLSIN
     MDNTQRQYEA ERNKMIGKRA NERLELLLQK RKELSDIQIQ IELCLNALWC CGTNNVIFLS
     LFSDAIAEIR AICIEEIGIW MKMYSDAFLN DSYLKYVGWT MHDKQGEVRL KCLTALQGLY
     YNKELNSKLE LFTSRFKDRI VSMTLDKEYD VAVQAIKLLT LVLQSSEEVL TAEDCENVYH
     LVYSAHRPVA VAAGEFLYKK LFSRRDPEEE GIMKRRGRQG PNANLVKTLV FFFLESELHE
     HAAYLVDSMW DCATELLKDW ECMNSLLLEE PLSGEEALTD RQESALIEIM LCTIRQAAEC
     HPPVGRGTGK RVLTAKEKKT QLDDRTKITE LFAVALPQLL AKYSIDAEKV TNLLQLPQYF
     DLEIYTTGRL EKHLDALLRQ IRNIVEKHTD TDVLEACSKT YHALCNEEFT IFNRVDISRS
     QLIDELADKF NRLLEDFLQE GEEPDEDDAY QVLSTLKRIT AFHNAHDLSK WDLFACNYKL
     LKTGIENGDM PEQIVIHALQ CTHYVILWQL AKITESSSTK EDLLRLKKQM RVFCQICQHY
     LTNVNTTVKE QAFTILCDIL MIFSHQIMSG GRDMLEPLVY TPDSSLQSEL LSFILDHVFI
     EQDDDSNSAD GQQEDEASKI EALHKRRNLL AAFCKLIVYT VVEMNTAADI FKQYMKYYND
     YGDIIKETMS KTRQIDKIQC AKTLILSLQQ LFNEMIQENG YNFDRSSTTF SGIKELARRF
     ALTFGLDQLK TREAIAMLHK DGIEFAFKEP NPQGESHPPL NLAFLDILSE FSSKLLRQDK
     RTVYVYLEKF MTFQMSLRRE DVWLPLMSYR NSLLAGGDDD TMSVISGISS RGSTVRSKKS
     KPSTGKRKIV EGMQLALTEE SSSSDSMWLS REQTLHTPVM MQTPQLTSTI MREPKRLRPE
     DSFMSVYPMQ AEHHQTPLDY NTQVTWMLAQ RQQEEARQQQ ERAAMSYVKL RTNLQHAIRR
     GTSLMEDDEE PIVEDVMMSS EGRIEDLNEG MDFDTMDIDL PPSKNRRERT ELKPDFFDPA
     SIMDESVLGV SMF
//