SMC3_ARATH
ID SMC3_ARATH Reviewed; 1204 AA.
AC Q56YN8; Q0WNE4; Q0WWN8; Q56ZJ9; Q6QU76; Q8H2D2; Q8S8B4; Q9SHT1;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Structural maintenance of chromosomes protein 3;
DE Short=SMC protein 3;
DE Short=SMC-3;
DE AltName: Full=Chromosome segregation protein SMC-3;
DE AltName: Full=Cohesin complex subunit SMC-3;
DE AltName: Full=Protein TITAN7;
GN Name=SMC3; Synonyms=TTN7; OrderedLocusNames=At2g27170; ORFNames=T22O13.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=14660695; DOI=10.1093/molbev/msh023;
RA Cobbe N., Heck M.M.S.;
RT "The evolution of SMC proteins: phylogenetic analysis and structural
RT implications.";
RL Mol. Biol. Evol. 21:332-347(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. Wassilewskija;
RX PubMed=15972315; DOI=10.1242/jcs.02443;
RA Lam W.S., Yang X., Makaroff C.A.;
RT "Characterization of Arabidopsis thaliana SMC1 and SMC3: evidence that
RT AtSMC3 may function beyond chromosome cohesion.";
RL J. Cell Sci. 118:3037-3048(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11846874; DOI=10.1046/j.1365-313x.2002.01224.x;
RA Liu C.-M., McElver J., Tzafrir I., Joosen R., Wittich P., Patton D.,
RA Van Lammeren A.A.M., Meinke D.;
RT "Condensin and cohesin knockouts in Arabidopsis exhibit a titan seed
RT phenotype.";
RL Plant J. 29:405-415(2002).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11788751; DOI=10.1104/pp.010911;
RA Tzafrir I., McElver J.A., Liu C.-M., Yang L.J., Wu J.Q., Martinez A.,
RA Patton D.A., Meinke D.W.;
RT "Diversity of TITAN functions in Arabidopsis seed development.";
RL Plant Physiol. 128:38-51(2002).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19533160; DOI=10.1007/s00412-009-0220-x;
RA Schubert V., Weissleder A., Ali H., Fuchs J., Lermontova I., Meister A.,
RA Schubert I.;
RT "Cohesin gene defects may impair sister chromatid alignment and genome
RT stability in Arabidopsis thaliana.";
RL Chromosoma 118:591-605(2009).
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 (By similarity). Essential protein plant
CC viability. Required for chromosome segregation (e.g. sister chromatid
CC alignment) and cell division during embryogenesis. {ECO:0000250,
CC ECO:0000269|PubMed:11788751, ECO:0000269|PubMed:11846874,
CC ECO:0000269|PubMed:19533160}.
CC -!- SUBUNIT: Cohesin complexes are composed of the SMC1 and SMC3
CC heterodimer attached via their SMC hinge domain, SCC3, and an alpha-
CC kleisin subunit SCC1 linked to one SYN subunit (SYN1, SYN2, SYN3 or
CC SYN4). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15972315}. Cytoplasm
CC {ECO:0000269|PubMed:15972315}. Nucleus matrix
CC {ECO:0000269|PubMed:15972315}. Chromosome
CC {ECO:0000269|PubMed:15972315}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:15972315}. Chromosome, centromere {ECO:0000250}.
CC Note=Primarily associated with the nuclear matrix during interphase and
CC with chromatin from prophase through anaphase in both somatic and
CC meiotic cells. During mitosis and meiosis the protein also colocalized
CC with the spindle from metaphase to telophase.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flower buds and leaves, and, to
CC a lower extent, in roots and stems. {ECO:0000269|PubMed:15972315}.
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 SMC1A or SMC1B, forming a V-shaped
CC heterodimer. The two heads of the heterodimer are then connected by
CC different ends of the cleavable RAD21 protein, forming a ring structure
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylation at Lys-105 and Lys-106 is important for genome
CC stability and S phase sister chromatid cohesion. {ECO:0000250}.
CC -!- PTM: Phosphorylated upon DNA damage. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Altered chromosome dynamics and cell division
CC during seed development, leading to aberrant mitoses and giant
CC polyploid nuclei in endosperm as well as arrested embryos with a few
CC small cells. {ECO:0000269|PubMed:11788751, ECO:0000269|PubMed:11846874,
CC ECO:0000269|PubMed:19533160}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD26882.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAM15423.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ504805; CAD43403.2; -; mRNA.
DR EMBL; AY525642; AAS09910.1; -; mRNA.
DR EMBL; AC007154; AAM15423.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007290; AAD26882.3; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC07948.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07949.1; -; Genomic_DNA.
DR EMBL; AK220965; BAD94521.1; -; mRNA.
DR EMBL; AK221283; BAD93989.1; -; mRNA.
DR EMBL; AK226305; BAE98460.1; -; mRNA.
DR EMBL; AK229499; BAF01356.1; -; mRNA.
DR PIR; F84669; F84669.
DR RefSeq; NP_001077968.1; NM_001084499.2.
DR RefSeq; NP_180285.4; NM_128275.5.
DR AlphaFoldDB; Q56YN8; -.
DR SMR; Q56YN8; -.
DR BioGRID; 2611; 1.
DR STRING; 3702.AT2G27170.2; -.
DR PaxDb; Q56YN8; -.
DR PRIDE; Q56YN8; -.
DR ProteomicsDB; 226747; -.
DR EnsemblPlants; AT2G27170.1; AT2G27170.1; AT2G27170.
DR EnsemblPlants; AT2G27170.2; AT2G27170.2; AT2G27170.
DR GeneID; 817259; -.
DR Gramene; AT2G27170.1; AT2G27170.1; AT2G27170.
DR Gramene; AT2G27170.2; AT2G27170.2; AT2G27170.
DR KEGG; ath:AT2G27170; -.
DR Araport; AT2G27170; -.
DR TAIR; locus:2045159; AT2G27170.
DR eggNOG; KOG0964; Eukaryota.
DR HOGENOM; CLU_001042_5_0_1; -.
DR InParanoid; Q56YN8; -.
DR OrthoDB; 119789at2759; -.
DR PhylomeDB; Q56YN8; -.
DR PRO; PR:Q56YN8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q56YN8; baseline and differential.
DR Genevisible; Q56YN8; AT.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0008278; C:cohesin complex; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0061775; F:cohesin loading activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:TAIR.
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; 2.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Centromere;
KW Chromosome; Coiled coil; Cytoplasm; Cytoskeleton; DNA damage; DNA repair;
KW Meiosis; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1204
FT /note="Structural maintenance of chromosomes protein 3"
FT /id="PRO_0000421563"
FT DOMAIN 2..1180
FT /note="Zinc-hook"
FT DOMAIN 522..633
FT /note="SMC hinge"
FT REGION 455..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 190..420
FT /evidence="ECO:0000255"
FT COILED 474..502
FT /evidence="ECO:0000255"
FT COILED 673..744
FT /evidence="ECO:0000255"
FT COILED 803..1009
FT /evidence="ECO:0000255"
FT MOTIF 171..178
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 457..464
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT MOTIF 650..657
FT /note="Nuclear localization signal 3"
FT /evidence="ECO:0000250"
FT MOTIF 799..806
FT /note="Nuclear localization signal 4"
FT /evidence="ECO:0000250"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 694..696
FT /note="LQV -> HVSL (in Ref. 1; CAD43403)"
FT /evidence="ECO:0000305"
FT CONFLICT 1055
FT /note="N -> H (in Ref. 2; AAS09910)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1204 AA; 139371 MW; E43EFABDD7C92E61 CRC64;
MFIKQVIIEG FKSYKEQVAT EEFSNKVNCV VGANGSGKSN FFHAIRFVLS DIYQNLRSED
RHALLHEGAG HQVVSAFVEI VFDNSDNRFP VDKEEIRLRR TVGLKKDDYF LDGKHITKGE
VMNLLESAGF SRANPYYVVQ QGKIASLTLM KDIERLDLLK EIGGTRVYEE RRRESLRIMQ
ETGNKRKQII EVVHYLDERL RELDEEKEEL RKYQQLDKQR KSLEYTIYDK ELHDAREKLE
QVEVARTKAS EESTKMYDRV EKAQDDSKSL DESLKELTKE LQTLYKEKET VEAQQTKALK
KKTKLELDVK DFQDRITGNI QSKNDALEQL NTVEREMQDS LRELEAIKPL YESQVDKENQ
TSKRINELEK TLSILYQKQG RATQFSNKAA RDKWLRKEIE DLKRVLDSNT VQEQKLQDEI
LRLNTDLTER DEHIKKHEVE IGELESRISK SHELFNTKKR ERDEEQRKRK EKWGEESQLS
SEIDKLKTEL ERAKKNLDHA TPGDVRRGLN SIRRICADYR INGVFGPLVE LVDCDEKFFT
AVEVTAGNSL FNVVVENDDI STKIIRHLNS LKGGRVTFLP LNRIKAPRVN YPKDSDAIPL
LKKLKFDSKF EPALGQVFGR TVVCRDLNVA TRVAKNDDLD CITMEGDQVS RKGGMTGGFY
DHRRSKLRFM NIIMQNTKSI NEKEKELEDV RRQLQVIDQQ ITQLVTEQQR LEADWTLCKL
QVEQLKQEIA NANKQKHAIH KAIEYKEKLL GDIRTRIDQV RSSMSMKEAE MGTELVDHLT
PEEREQLSKL NPEIKDLKEK KFAYQADRIE RETRKAELEA NIATNLKRRI TELQATIASI
DDDSLPSSAG TKEQELDDAK LSVNEAAKEL KSVCDSIDEK TKQIKKIKDE KAKLKTLEDD
CKGTLQDLDK KLEELFSLRN TLLAKQDEYT KKIRGLGPLS SDAFDTYKRK NIKELQKMLH
RCSEQLQQFS HVNKKALDQY VNFTEQREEL QNRQAELDAG DEKIKELITV LDQRKDESIE
RTFKGVAHHF RDVFSELVQD GYGNLIIMKK KDLDNDDEDD DDDDGGREAV TEGRVEKYIG
VKVKVSFTGQ GETQLMKQLS GGQKTVVALA LIFAIQRCDP APFYLFDEID AALDPQYRTA
VGNLIRRLAD DYGTQFITTT FRPELVRVAD KIYGVFHKNR VSIVNVISKD QALDFIEKDQ
SHDT
