ID STAG3_RAT Reviewed; 1256 AA.
AC Q99M76;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 24-JAN-2024, entry version 135.
DE RecName: Full=Cohesin subunit SA-3;
DE AltName: Full=SCC3 homolog 3;
DE AltName: Full=Stromal antigen 3;
DE AltName: Full=Stromalin-3;
GN Name=Stag3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=11599053; DOI=10.1002/mrd.1104;
RA Bayes M., Prieto I., Noguchi J., Barbero J.L., Perez Jurado L.A.;
RT "Evaluation of the Stag3 gene and the synaptonemal complex in a rat model
RT (as/as) for male infertility.";
RL Mol. Reprod. Dev. 60:414-417(2001).
CC -!- FUNCTION: Meiosis specific component of cohesin complex. The cohesin
CC complex is required for the cohesion of sister chromatids after DNA
CC replication. The cohesin complex apparently forms a large proteinaceous
CC ring within which sister chromatids can be trapped. At anaphase, the
CC complex is cleaved and dissociates from chromatin, allowing sister
CC chromatids to segregate. The meiosis-specific cohesin complex probably
CC replaces mitosis specific cohesin complex when it dissociates from
CC chromatin during prophase I. {ECO:0000250|UniProtKB:O70576}.
CC -!- SUBUNIT: Component of the meiosis-specific cohesin complex, which also
CC contains the SMC1 (SMC1A or SMC1B) and SMC3 heterodimer. Such complex
CC likely contains RAD21, or the meiosis-specific related protein REC8.
CC Interacts with CCDC79/TERB1; recruiting cohesin to telomeres to develop
CC structural rigidity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750}.
CC Chromosome {ECO:0000250}. Note=Associates with chromatin. In prophase I
CC stage of meiosis, it is found along the axial elements of synaptonemal
CC complexes. In late-pachytene-diplotene, the bulk of protein dissociates
CC from the chromosome arms probably because of phosphorylation by PLK1,
CC except at centromeres, where cohesin complexes remain. It however
CC remains chromatin associated at the centromeres up to metaphase I.
CC During anaphase I, it probably dissociates from centromeres, allowing
CC chromosomes segregation (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Testis specific.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
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DR EMBL; AY027880; AAK13052.1; -; mRNA.
DR RefSeq; NP_446182.1; NM_053730.1.
DR RefSeq; XP_006249082.1; XM_006249020.3.
DR AlphaFoldDB; Q99M76; -.
DR SMR; Q99M76; -.
DR STRING; 10116.ENSRNOP00000072692; -.
DR iPTMnet; Q99M76; -.
DR PhosphoSitePlus; Q99M76; -.
DR jPOST; Q99M76; -.
DR PaxDb; 10116-ENSRNOP00000041918; -.
DR Ensembl; ENSRNOT00000042006.5; ENSRNOP00000041918.4; ENSRNOG00000001360.7.
DR GeneID; 114522; -.
DR KEGG; rno:114522; -.
DR UCSC; RGD:621333; rat.
DR AGR; RGD:621333; -.
DR CTD; 10734; -.
DR RGD; 621333; Stag3.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR InParanoid; Q99M76; -.
DR OMA; WDCAAPL; -.
DR OrthoDB; 5354237at2759; -.
DR PhylomeDB; Q99M76; -.
DR PRO; PR:Q99M76; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001360; Expressed in testis and 2 other cell types or tissues.
DR Genevisible; Q99M76; RN.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:RGD.
DR GO; GO:0000800; C:lateral element; ISO:RGD.
DR GO; GO:0001673; C:male germ cell nucleus; ISO:RGD.
DR GO; GO:0030893; C:meiotic cohesin complex; ISO:RGD.
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:0000795; C:synaptonemal complex; ISO:RGD.
DR GO; GO:0000802; C:transverse filament; ISO:RGD.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0034089; P:establishment of meiotic sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISO:RGD.
DR GO; GO:0051321; P:meiotic cell cycle; TAS:RGD.
DR GO; GO:0034502; P:protein localization to chromosome; ISO:RGD.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
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 2: Evidence at transcript level;
KW Cell cycle; Chromosome; Chromosome partition; Meiosis; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1256
FT /note="Cohesin subunit SA-3"
FT /id="PRO_0000120190"
FT DOMAIN 324..409
FT /note="SCD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1230..1256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..91
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1144..1166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O70576"
SQ SEQUENCE 1256 AA; 141951 MW; 1C0B3F49D4B8B85D CRC64;
MPTLWSPSTQ HHGSSSGSMS SPLRKSVRCA QMALSPCSSN IQPCDDRDSQ GTAEWDSSST
SEDSDFEDSL RRNVRKRAAK RPPKAIPVAK HPKKQSHIVP GGNDKNKSVP PTSDLFDAVK
AARSCAQSLV DEWLENYKQD ENAGFLELVN FFIRACGCKS TVTPEMFKTM SNSEIIQHLT
EEFNEDSGDY PLTAPGPSWK KFQGSFCEFV KTLVCQCQYS LLFDGFPMDD LISLLIGLSD
SQVRAFRHTS TLAAMKLMTS LVKVALQLSL HKDNNQRQYE AERNKGPEQR APERLESLLE
KRKEFQENQE EIEGMMNAIF RGVFVHRYRD ILPEIRAVCI EEIGCWMQSY STSFLNDSYL
KYIGWTLHDK HKEVRLKCVK ALAGLYSNQE LSSRMELFTN RFKDRMVSMV MDRESEVAVE
AIRLLTLILK NMEGVLTSAD CEKIYSIVYI SNRAMASSAG EFVYWKIFHP ECGAKAVSGR
ERRRSPQAQR TFIYLLLAFF MESEHHDHAA YLVDSLWDCA GSYLKDWESL TSLLLQKDQN
LGDMQERMLI EILVSSARQA AEGHPPVGRI TGKKSLTAKE RKLQAYDKVK LAEHLIPLLP
QLLAKFSADA ENVAPLLRLL SYFDLNIYCT QRLEKHLELL LQQLQEVVVK HVEPEVLEAA
AHALYLLCKP EFTFFSRVDF ARSQLVDLLT DRFQQELDDL MQSSFLDEDE VYSLTATLKR
LSAFYNAHDL TRWEISEPCS RLLRKAVDTG EVPHQVILPA LTLVYFSILW TVTHISESTS
QKQLMSLKKR MVAFCELCQS CLSDVDPEIQ EQAFVLLSDL LLIFSPQMVV GGRDFLRPLV
FFPEATLQSE LASFLMDHVF LQPGELGNGQ SQEDHVQIEL LHQRRRLLAG FCKLLLYGVL
ELDAASDVFK HYNKFYEDYG DIIKETLTRA RQIDRCQCSR ILLLSLKQLY TELIQEQGPQ
DLTELPAFIE MRDLARRFAL SFGPQQLHNR DLVVMLHKEG IKFSLSELPP AGSSREPPNI
AFLELLSEFS PRLFHQDKQL LLSYLEKCLQ RVSMAPSHPW GPVTTYCHSL HLVENTAEAS
SQGPPHSKKR CIEVPRRLQE EESSSQGESL QLNSGPTTPT LTSTAVKRRQ SPRTVGKRQK
GGPGPGPGPG PGPGPGPGPG PGPGPGPELI CSQQLSGTQR LKMSSAPCFQ IRCDPSGSGL
GKQMTRLSLM EEDEEEELRL LDEEWQCGDK LLHSPSSPSE HGLDLLDTTE LNMEDF
//
