ID G3WR51_SARHA Unreviewed; 1215 AA.
AC G3WR51;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 58.
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=LOC100933824 {ECO:0000313|Ensembl:ENSSHAP00000017906.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000017906.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000017906.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000017906.2}
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 AlphaFoldDB; G3WR51; -.
DR STRING; 9305.ENSSHAP00000017906; -.
DR Ensembl; ENSSHAT00000018054.2; ENSSHAP00000017906.2; ENSSHAG00000015200.2.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR HOGENOM; CLU_005067_1_0_1; -.
DR OrthoDB; 5354237at2759; -.
DR TreeFam; TF314604; -.
DR Proteomes; UP000007648; 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:SF2; SCD DOMAIN-CONTAINING PROTEIN; 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:UP000007648}.
FT DOMAIN 334..419
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1215
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1215 AA; 140035 MW; 41A3BCDB8C835F8C CRC64;
MIAEPSPASD TSQKCGMPSA SYSSVCPVEK ENDGQEATAP ASAVQNGGCV KNSSNSTPKE
RKKVQEQCEN VRKKNISRRK RSSQPENDED EVEEMVEAVT LFEVVSLGKR AMQSVVDDWI
EAYKEDRDLA LLDLINFFIQ CSGCQGMVTA EMYQSLHSSD ILKKMIEKFD EETGLQYKRI
MARPWILTVT WPMELEDEGY PLVKPGPHWK KFKANFCEFT AVLIQQCQYS ILYDGYLMNT
ITSLLSGLTG SVVRAFRHTS TLAAMKLVTA LVSVIQNLDV SIHNAQQLYE VEKNRTPEGE
TGPRLDELDR KRKECQQKPV EIENMMNALF KGTFVQRYRD VIPEIRIVCI EEMGSWLKLY
PNMFLNDSYL KYVGWMLYDK QAEVRLKCLQ GLRGLYEHKE LIFKMGLFNT RFKSRIVSMT
TDKEPEVAVE AMKLVMLMVL NCENTVSSEE CEAMYHFVYA TYRPLAVVAG ELLCKRLFCL
PSGEEEPPNA KKKNKFVYSL RRLKKLITFF LNHGFHKHVT YLVDSLWDWE DGLLRDWECL
TNLLRDKPMR KEEAFTDAQE SVLVEIIAAA VRQTAEGHPP VGRGSRKTLT AKERKTQMEE
CARMTERFII VLPELLAKYS SDTEKVTNFL QIPQYYNLNV YVAGRLEQYL DALLTEMKEL
VHRHTDLNVL EACSKVYSIL CGEQLAIYPF VSEALHHLID EMVMDFSQLI GEFFQEEDGL
GVNEEHIFRM SCILKKLTAF HNAHDLTRWH IGDWTLKILN FEKENGGLPA ETLIPALQCS
YFALLWQLEL VTESLVTETP SSQETLSELS EKMTCFRLIC ESYLNHHNKD VSEKAFILLC
DLLIVLSHQG VDEDEDFSLL KFLPDHDLQS RMIEFVKDHV FGENNLPEEM NREEAHRLDS
VYRKRIILAE YCKLIAYNVV EMMTAVEIYK HYMQTYHDFG DIIKETINRT RHNDKIESAR
TLIVCLQELY QNHMATYRSN NSRKKQVDSS ASFASIKELA RRFSLTFGWD QMNSRESIAM
IHKEGIDFAF HGDSQDIDYY LPPNLTFLAI ISEFSNKLLK PDKKLVYYYL QEFVTDHMLL
TCKGEKWHPL YCYRSSLIGT DDDAESTIAS SFREWPPPDK SKVFATKRKF SDGSIMDISL
PGSSRQTMDL QSDSQLSYFS WKSKTVTSED IVDEPGPTEQ DIAPRMGDSP ESLHEEETEE
LNEDIDVVEI DEGNL
//
