SMC21_ARATH
ID SMC21_ARATH Reviewed; 1175 AA.
AC Q9C5Y4; Q9FJK1; Q9FUY9;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Structural maintenance of chromosomes protein 2-1;
DE Short=AtSMC2-1;
DE AltName: Full=Chromosome-associated protein E-1;
DE Short=AtCAP-E1;
DE AltName: Full=Protein TITAN 3;
GN Name=SMC2-1; Synonyms=CAP-E1, TTN3; OrderedLocusNames=At5g62410;
GN ORFNames=MMI9.19, MMI9.24;
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 [GENOMIC DNA / MRNA], AND FUNCTION.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12783798; DOI=10.1242/dev.00542;
RA Siddiqui N.U., Stronghill P.E., Dengler R.E., Hasenkampf C.A., Riggs C.D.;
RT "Mutations in Arabidopsis condensin genes disrupt embryogenesis, meristem
RT organization and segregation of homologous chromosomes during meiosis.";
RL Development 130:3283-3295(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9872454; DOI=10.1093/dnares/5.5.297;
RA Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT features of the regions of 1,013,767 bp covered by sixteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:297-308(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [5]
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).
CC -!- FUNCTION: Central component of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases. Also involved in chromosome
CC segregation in meiosis. {ECO:0000269|PubMed:11846874,
CC ECO:0000269|PubMed:12783798}.
CC -!- SUBUNIT: Forms a heterodimer with SMC4. Component of the condensin
CC complex, which contains the SMC2 and SMC4 heterodimer, and three non
CC SMC subunits that probably regulate the complex: CAPH, CAPD2 and CAPG.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with chromatin.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots and young floral buds.
CC {ECO:0000269|PubMed:12783798}.
CC -!- DOMAIN: The SMC hinge domain, which separates the large intramolecular
CC coiled coil regions, allows the heterodimerization with SMC4, forming a
CC V-shaped heterodimer.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG27593.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAK58634.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF271730; AAG27593.2; ALT_FRAME; Genomic_DNA.
DR EMBL; AF271731; AAK58634.1; ALT_FRAME; mRNA.
DR EMBL; AF306547; AAG53093.1; -; mRNA.
DR EMBL; AB015469; BAB11491.1; -; Genomic_DNA.
DR EMBL; AB019235; BAB11491.1; JOINED; Genomic_DNA.
DR EMBL; CP002688; AED97605.1; -; Genomic_DNA.
DR RefSeq; NP_201047.1; NM_125635.3.
DR AlphaFoldDB; Q9C5Y4; -.
DR SMR; Q9C5Y4; -.
DR BioGRID; 21606; 5.
DR STRING; 3702.AT5G62410.1; -.
DR iPTMnet; Q9C5Y4; -.
DR PaxDb; Q9C5Y4; -.
DR PRIDE; Q9C5Y4; -.
DR ProteomicsDB; 228025; -.
DR EnsemblPlants; AT5G62410.1; AT5G62410.1; AT5G62410.
DR GeneID; 836362; -.
DR Gramene; AT5G62410.1; AT5G62410.1; AT5G62410.
DR KEGG; ath:AT5G62410; -.
DR Araport; AT5G62410; -.
DR TAIR; locus:2167973; AT5G62410.
DR eggNOG; KOG0933; Eukaryota.
DR HOGENOM; CLU_001042_9_0_1; -.
DR InParanoid; Q9C5Y4; -.
DR OMA; ECAGTTI; -.
DR OrthoDB; 119789at2759; -.
DR PhylomeDB; Q9C5Y4; -.
DR PRO; PR:Q9C5Y4; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C5Y4; baseline and differential.
DR Genevisible; Q9C5Y4; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000793; C:condensed chromosome; IBA:GO_Central.
DR GO; GO:0000796; C:condensin complex; ISS:TAIR.
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:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0007076; P:mitotic chromosome condensation; IBA:GO_Central.
DR CDD; cd03273; ABC_SMC2_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; IPR027120; Smc2_ABC.
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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Coiled coil; DNA condensation;
KW Meiosis; Mitosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1175
FT /note="Structural maintenance of chromosomes protein 2-1"
FT /id="PRO_0000284894"
FT DOMAIN 2..1161
FT /note="Zinc-hook"
FT DOMAIN 518..638
FT /note="SMC hinge"
FT COILED 172..508
FT /evidence="ECO:0000255"
FT COILED 673..1028
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 107
FT /note="I -> V (in Ref. 1; AAK58634/AAG27593)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="E -> K (in Ref. 2; AAG53093)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="G -> GVG (in Ref. 1; AAK58634/AAG27593)"
FT /evidence="ECO:0000305"
FT CONFLICT 439
FT /note="L -> R (in Ref. 1; AAK58634/AAG27593 and 2;
FT AAG53093)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="E -> G (in Ref. 2; AAG53093)"
FT /evidence="ECO:0000305"
FT CONFLICT 965
FT /note="E -> V (in Ref. 1; AAK58634/AAG27593)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1175 AA; 132600 MW; 51EA64A11C3FFF62 CRC64;
MHIKEICLEG FKSYATRTVV SGFDPHFNAI TGLNGSGKSN ILDSICFVLG ITNLQQVRAA
NLQELVYKQG QAGITKATVS VTFDNSERHR SPLGYEEHPE ITVTRQIVVG GRNKYLINGK
LAQPSQVQNL FHSVQLNVNN PHFLIMQGRI TKVLNMKPPE ILSMLEEAAG TRMYENKKEA
ALKTLEKKQT KVDEINKLLD HEILPALEKL RKEKSQYMQW ANGNAELDRL RRFCIAFEYV
QAEKIRDNAV LGVGEMKAKL GKIDAETEKT QEEIQEFEKQ IKALTQAKEA SMGGEVKTLS
EKVDSLAQEM TRESSKLNNK EDTLLGEKEN VEKIVHSIED LKKSVKERAA AVKKSEEGAA
DLKQRFQELS TTLEECEKEH QGVLAGKSSG DEEKCLEDQL RDAKIAVGTA GTELKQLKTK
IEHCEKELKE RKSQLMSKLE EAIEVENELG ARKNDVEHVK KALESIPYNE GQMEALEKDR
GAELEVVQRL EDKVRGLSAQ LANFQFTYSD PVRNFDRSKV KGVVAKLIKV KDRSSMTALE
VTAGGKLYDV VVDSEDTGKQ LLQNGALRRR VTIIPLNKIQ SYVVQPRVQQ ATARLVGKDN
AELALSLVGY SDELKNAMEY VFGSTFVCKT TDVAKEVAFN RDIRTPSVTL EGDIFQPSGL
LTGGSRKGGG DRLRKLHDLA EAESELQGHQ KRLADVESQI KELQPLQMKF TDVYAQLELK
TYDLSLFLKR AEQNEHHKLG EAVKKLEEEL EEAKSQIKEK ELAYKNCFDA VSKLENSIKD
HDKNREGRLK DLEKNIKTIK AQMQAASKDL KSHENEKEKL VMEEEAMKQE QSSLESHLTS
LETQISTLTS EVDEQRAKVD ALQKIHDESL AELKLIHAKM KECDTQISGF VTDQEKCLQK
LSDMKLERKK LENEVVRMET DHKDCSVKVD KLVEKHTWIA SEKQLFGKGG TDYDFESCDP
YVAREKLEKL QSDQSGLEKR VNKKVMAMFE KAEDEYNALI SKKNTIENDK SKITKVIEEL
DEKKKETLKV TWVKVNQDFG SIFSTLLPGT MAKLEPPEDG NFLDGLEVRV AFGKVWKQSL
SELSGGQRSL LALSLILALL LFKPAPLYIL DEVDAALDLS HTQNIGRMIR AHFPHSQFIV
VSLKEGMFNN ANVLFRTKFV DGVSTVQRTV TKQTK
