SMC3_XENLA
ID SMC3_XENLA Reviewed; 1209 AA.
AC O93309; Q505N2;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Structural maintenance of chromosomes protein 3;
DE Short=SMC protein 3;
DE Short=SMC-3;
GN Name=smc3; Synonyms=smc3l1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 976-1209, FUNCTION, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1 AND RAD21.
RX PubMed=9649503; DOI=10.1101/gad.12.13.1986;
RA Losada A., Hirano M., Hirano T.;
RT "Identification of Xenopus SMC protein complexes required for sister
RT chromatid cohesion.";
RL Genes Dev. 12:1986-1997(1998).
RN [3]
RP IDENTIFICATION IN A COHESIN COMPLEX WITH SMC1; RAD21; STAG1 OR STAG2.
RX PubMed=10931856; DOI=10.1083/jcb.150.3.405;
RA Losada A., Yokochi T., Kobayashi R., Hirano T.;
RT "Identification and characterization of SA/Scc3p subunits in the Xenopus
RT and human cohesin complexes.";
RL J. Cell Biol. 150:405-416(2000).
CC -!- FUNCTION: Central component of cohesin, a complex required for
CC chromosome cohesion during the cell cycle. The cohesin complex may form
CC a large proteinaceous ring within which sister chromatids can be
CC trapped. At anaphase, the complex is cleaved and dissociates from
CC chromatin, allowing sister chromatids to segregate. Cohesion is coupled
CC to DNA replication and is involved in DNA repair. The cohesin complex
CC also plays an important role in spindle pole assembly during mitosis
CC and in chromosomes movement. {ECO:0000269|PubMed:9649503}.
CC -!- SUBUNIT: Forms a heterodimer with SMC1 in cohesin complex. The cohesin
CC complex is composed of the SMC1 and SMC3 heterodimer attached via their
CC SMC hinge domain, RAD21 which link them, and one STAG protein (STAG1 or
CC STAG2), which interacts with RAD21. {ECO:0000269|PubMed:10931856,
CC ECO:0000269|PubMed:9649503}.
CC -!- INTERACTION:
CC O93309; Q4QXM3: pds5a-a; NbExp=2; IntAct=EBI-80653, EBI-1386928;
CC O93309; Q9DGN1: stag1; NbExp=2; IntAct=EBI-80653, EBI-80622;
CC O93309; Q9DGN0: stag2; NbExp=2; IntAct=EBI-80653, EBI-80675;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9649503}. Chromosome
CC {ECO:0000269|PubMed:9649503}. Chromosome, centromere
CC {ECO:0000269|PubMed:9649503}. Note=Associates with chromatin. Before
CC prophase it is scattered along chromosome arms. During prophase, most
CC of cohesin complexes dissociate from chromatin probably because of
CC phosphorylation by PLK, except at centromeres, where cohesin complexes
CC remain. At anaphase, the RAD21 subunit of the cohesin complex is
CC cleaved, leading to the dissociation of the complex from chromosomes,
CC allowing chromosome separation.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC3, forming a V-shaped heterodimer.
CC The two heads of the heterodimer are then connected by different ends
CC of the cleavable RAD21 protein, forming a ring structure (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Acetylation at Lys-113 and Lys-114 by ESCO1 is important for
CC genome stability and S phase sister chromatid cohesion. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily. {ECO:0000305}.
CC -!- CAUTION: Was originally isolated as a proteoglycan protein. Although
CC not excluded, such secreted function is not clear. {ECO:0000305}.
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DR EMBL; BC094474; AAH94474.1; -; mRNA.
DR EMBL; AF051785; AAC26808.1; -; mRNA.
DR PDB; 5N1W; X-ray; 2.30 A; C/D=101-106.
DR PDB; 5N22; X-ray; 1.99 A; E/G/J/L=99-111.
DR PDBsum; 5N1W; -.
DR PDBsum; 5N22; -.
DR AlphaFoldDB; O93309; -.
DR SMR; O93309; -.
DR IntAct; O93309; 8.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0030893; C:meiotic cohesin complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006275; P:regulation of DNA replication; ISS:UniProtKB.
DR CDD; cd03272; ABC_SMC3_euk; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR041741; SMC3_ABC_euk.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 1.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Centromere; Chromosome; Coiled coil; DNA damage; DNA repair; Meiosis;
KW Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1209
FT /note="Structural maintenance of chromosomes protein 3"
FT /id="PRO_0000119005"
FT DOMAIN 530..642
FT /note="SMC hinge"
FT REGION 239..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 179..350
FT /evidence="ECO:0000255"
FT COILED 393..503
FT /evidence="ECO:0000255"
FT COILED 670..857
FT /evidence="ECO:0000255"
FT COILED 958..989
FT /evidence="ECO:0000255"
FT COMPBIAS 1067..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT CONFLICT 1052..1054
FT /note="KAT -> RPL (in Ref. 2; AAC26808)"
FT /evidence="ECO:0000305"
FT CONFLICT 1075
FT /note="T -> A (in Ref. 2; AAC26808)"
FT /evidence="ECO:0000305"
FT CONFLICT 1082
FT /note="V -> F (in Ref. 2; AAC26808)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109
FT /note="G -> R (in Ref. 2; AAC26808)"
FT /evidence="ECO:0000305"
FT CONFLICT 1118
FT /note="A -> R (in Ref. 2; AAC26808)"
FT /evidence="ECO:0000305"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:5N22"
SQ SEQUENCE 1209 AA; 140723 MW; 829012FA838CF97C CRC64;
MYIKQVIIQG FRSYRDQTIV DPFSSKHNVI VGRNGSGKSN FFYAIQFVLS DEFSHLRPEQ
RLALLHEGTG PRVISAFVEI IFDNSDNRLP IDKEEVSLRR VIGAKKDQYF LDKKMVTKND
VMNLLESAGF SRSNPYYIVK QGKINQMATA PDSQRLKLLR EVAGTRVYDE RKEESISLMK
ETEGKRDKIN ELLKYIEERL HTLEEEKEEL AQYQKWDKMR RALEYTIYNQ ELNETRAKLD
ELSSKRETSG EKSRQLRDAQ QDARDKMEEI ERQVRELKSK ISAMKEEKEQ LSSERQEQIK
QRTKLELKTK DLQDELAGNS EQRKRLLKER QKLLEKIEEK QKELAETEPK FSSVKQKEES
GIARLAQATQ ERTDLYAKQG RGSQFTSKEE RDKWIKKELK SLDQAINDKK RQIAAINKDL
EETEVNKEKN LEQYTKLDQD LNEVKTRVEE LDKKYYEVKN KKDELQSERN YLWREENAEQ
QSLAAKREDL EKKQQLLRAA TGKAILNGID SINKVLEHFR RKGINQHVIN GYHGIVMNNF
DCEPAFYTCV EVTAGNRLFY HIVESDEVST KILMEFNKMN LPGEVTFLPL NKLDVRDTAY
PETNDAIPMI SKLRYNLRFD KAFKHVFGKT LICRSMEVST QLARAFTMDC ITLEGDQVSH
RGALTGGYYD TRKSRLELQK DVRKVEDELH ALEAKLNENL RRNIERINNE IDQLMNQMQQ
IETQQRKFKA SRDSILSEMK MLKEKRQQSE KTFMPKQRSL QSLEASLHAM ESTRESLKAE
LGTDLLSQLS LEDQKRVDAL NDEIRQLQQE NRQLLNERIK LEGTITRVET YLNENLRKRL
DQVEQELNEL RETEGGTVLT ATTSELEAIN KRVKDTLARS EGLDITIDKT EVESKDLVKS
MDRWKNMEKD HMDAINHDTK ELEKMTNRQG MLLKKKEECM KKIRELGSLP QEAFEKYQTL
SLKQLFRKLE QCNTELKKYS HVNKKALDQF VNFSEQKEKL IKRQEELDRG HKSIMELMNV
LELRKYEAIQ LTFKQVSKNF SEVFQKLVPG GKATLVMKKG DVEGSQSQDE GEGSTQSSVP
SVDQFTGVGI RVSFTGKQAE MREMQQLSGG QKSLVALALI FAIQKCDPAP FYLFDEIDQA
LDAQHRKAVS DMIMELASHA QFITTTFRPE LLESADKFYG VKFRNKVSHI DVITAEQAKD
FVEDDTTHG
