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Database: UniProt
Entry: M3XDE3_FELCA
LinkDB: M3XDE3_FELCA
Original site: M3XDE3_FELCA 
ID   M3XDE3_FELCA            Unreviewed;      1195 AA.
AC   M3XDE3;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   24-JAN-2024, entry version 67.
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|Ensembl:ENSFCAP00000024649.3,
GN   ECO:0000313|VGNC:VGNC:65744};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000024649.3, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000024649.3, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000024649.3,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000024649.3, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000024649.3,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000024649.3}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000024649.3};
RG   Ensembl;
RL   Submitted (SEP-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; AANG04004457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; M3XDE3; -.
DR   Ensembl; ENSFCAT00000028339.4; ENSFCAP00000024649.3; ENSFCAG00000027633.4.
DR   VGNC; VGNC:65744; STAG2.
DR   eggNOG; KOG2011; Eukaryota.
DR   GeneTree; ENSGT00950000182972; -.
DR   HOGENOM; CLU_005067_1_0_1; -.
DR   Proteomes; UP000011712; Chromosome X.
DR   Bgee; ENSFCAG00000027633; Expressed in embryonic head and 10 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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleus {ECO:0000256|RuleBase:RU369063};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011712}.
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          1028..1047
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   1195 AA;  137348 MW;  3F740EEE0070DF2C 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 RKELQENQDE IENMMNAIFK GVFVHRYRDA
     IAEIRAICIE EIGIWMKMYS DAFLNDSYLK YVGWTMHDKQ GEVRLKCLTA LQGLYYNKEL
     NSKLELFTSR FKDRIVSMTL DKEYDVAVQA IKLLTLVLQL FSRRDPEEDG MMKRRGRQGP
     NANLVKTLVF FFLESELHEH AAYLVDSMWD CATELLKDWE CMNSLLLEEP LSGEEALTDR
     QESALIEIML CTIRQAAECH PPVGRGTGKR VLTAKEKKTQ LDDRTKITEL FAVALPQLLA
     KYSIDAEKVT NLLQLPQYFD LEIYTTGRLE KHLDALLRQI RNIVEKHTDT DVLEACSKTY
     HALCNEEFTI FNRVDISRSQ LIDELADKFN RLLEDFLQEG EEPDEDDAYQ VLSTLKRITA
     FHNAHDLSKW DLFACNYKLL KTGIENGDMP EQIVIHALQC THYVILWQLA KITESSSTKE
     DLLRLKKQMR VFCQICQHYL TNVNTTVKEQ AFTILCDILM IFSHQIMSGG RDMLEPLVYT
     PDSSLQSELL SFILDHVFIE QDDDNNSADG QQEDEASKIE ALHKRRNLLA AFCKLIVYTV
     VEMNTAADIF KQYMKYYNDY GDIIKETMSK TRQIDKIQCA KTLILSLQQL FNEMIQENGY
     NFDRSSSTFS GIKELARRFA LTFGLDQLKT REAIAMLHKD GIEFAFKEPN PQGESHPPLN
     LAFLDILSEF SSKLLRQDKR TVYVYLEKFM TFQMSLRRED VWLPLMSYRN SLLAGGDDDT
     MSVISGISSR GSTVRSKKSK PSTGKRKVVE GMQLSLTEES SSSDSMWLSR EQTLHTPVMM
     QTPQLTSTIM REPKRLRPED SFMSVYPMQT EHHQTPLDYN RRGTSLMEDD EEPIVEDVMM
     SSEGRIEDLN EGMDFDTMDI DLPPSKNRRE RTELKPDFFD PASIMDESVL GVSMF
//
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