ID F7HJH8_MACMU Unreviewed; 1342 AA.
AC F7HJH8;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 27-MAR-2024, entry version 59.
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=STAG3 {ECO:0000313|Ensembl:ENSMMUP00000024210.4,
GN ECO:0000313|VGNC:VGNC:81766};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000024210.4, ECO:0000313|Proteomes:UP000006718};
RN [1] {ECO:0000313|Proteomes:UP000006718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2] {ECO:0000313|Ensembl:ENSMMUP00000024210.4}
RP IDENTIFICATION.
RC STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000024210.4};
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 SMR; F7HJH8; -.
DR STRING; 9544.ENSMMUP00000024210; -.
DR PaxDb; 9544-ENSMMUP00000024209; -.
DR Ensembl; ENSMMUT00000025873.4; ENSMMUP00000024210.4; ENSMMUG00000018405.4.
DR VEuPathDB; HostDB:ENSMMUG00000018405; -.
DR VGNC; VGNC:81766; STAG3.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR InParanoid; F7HJH8; -.
DR OMA; WDCAAPL; -.
DR Proteomes; UP000006718; Chromosome 3.
DR Bgee; ENSMMUG00000018405; Expressed in spermatocyte and 14 other cell types or tissues.
DR ExpressionAtlas; F7HJH8; baseline.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0000800; C:lateral element; IEA:Ensembl.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0030893; C:meiotic cohesin complex; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000802; C:transverse filament; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IEA:Ensembl.
DR GO; GO:0034502; P:protein localization to chromosome; IEA:Ensembl.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
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:UP000006718}.
FT DOMAIN 309..394
FT /note="SCD"
FT /evidence="ECO:0000259|PROSITE:PS51425"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1178..1211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..87
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1076..1093
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1094..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1178..1192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1342 AA; 151825 MW; C8FFCE6A56F7B285 CRC64;
MSSPLQRAAG GAKTALSASS SSSASLPFDD RDSNHTSEGN SDSLLADEGS DFEDSLNRSV
KKRAAKRPPK TTPVAKHPKK GSRVVHRHSR KQSEPPANDL FSAVKAAKSD MQSLVDEWLD
SYKQDQDAGF LELVNFFIRS CGCKGTVTPE MFKKMSNSEI IQHLTEQFNE DSGDYPLTAP
GPSWKKFQGS FCEFVRTLVC QCQYSLLYDG FPMDNLISLL TGLSDSQVRA FRHTSTLAAM
KLMTSLVRVA LQLSLHQDNN QRQYEAERNK GPGQRAPERL ESLLEKRKEL QEHQEEIEGM
MNALFRGVFV HRYRDVLPEI RAICIEEIGC WMQSYSTSFL TDSYLKYIGW TLHDKHREVR
LKCLKALKGL YGNRDLTARL ELFTSRFKDR MVSMVMDKEY DVAVEAVRLL ILILKNMEGV
LTDADCESIY PVVYASNRGL ASAAGEFLYW KLFYPECEIR TMGGRERRQS PGAQRTFFQL
LLSFFVESEL HDHAAYLVDS LWDCAGAQLK DWESLTSLLL EKDQNLGDVQ ESTLIEILVS
SARQASEGHP PVGRVTGRKG LTSKERKTQA DDRVKLTEHL IPLLPQLLAK FSADAEKVTP
LLRLLSSFDL HIYCTGRLEK HLELFLQQLQ EVVVKHAEPA VLEAGAHALY LLCNPEFTFF
SRADFARSQL VDLLTDRFQQ ELEELLQSSF LDEDEVYNLA ATLKRLSAFY NAHDLTRWEL
YEPCCQLLQK AVDTGEVPHQ VILPALTLVY FSILWTLTHI SKSDASQKQL SSLRDRMVAF
CELCQSCLSD VDTEIQEQAF VLLSDLLLIF SPQMIVGGRD FLRPLVFFPE ATLQSELASF
LMDHVFIQLG DLGSGDSQED HLQIERLHQR RRLLAGFCKL LLYGVLEMDA ASDVFKHYNK
FYNDYGDIIK ETLTRARQID RSHCSRILLL SLKQLYTELL QDHGPQGLNE LPAFIEMRDL
ARRFALSFGP QQLQNRDLVV MLHKEGIKFS LSELPPAGSS DQPPNLAFLE LLSEFSPRLI
HQDKQLLLSY LEKCLQQVSQ APGRPWGPVT TYCHSLSPVE NTAETSPQVL PSSKRRRVEG
PAKHDREDVS SSQEESLKLN SIPPTPTLTS TAVKSRQPLW GLEEMEEEDD SELDFAQGQP
LAGTQRSRFL GPQYFQTPRN PSGPGLGNQL MRLSLMEENE EEELEIQDES SEERQDTDMQ
ASSYSSPSER GLDLLDSTEL DVEVSVPRAG GVCVLGKCWQ ATHVLIKLTE RPQPGGGPLS
CLWGFYGNPG EDGLPIGLLL CPVYSFHLSH YRISDMTGPL PSSTPYLKDV TIWKRQREKE
QNEAFPQAFP WALRGRSWAL FF
//
