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Structural maintenance of chromosomes protein 2-1 (AtSMC2-1) (Chromosome-associated protein E-1) (AtCAP-E1) (Protein TITAN 3)

 SMC21_ARATH             Reviewed;        1175 AA.
Q9C5Y4; Q9FJK1; Q9FUY9;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 2.
25-OCT-2017, entry version 117.
RecName: Full=Structural maintenance of chromosomes protein 2-1;
Short=AtSMC2-1;
AltName: Full=Chromosome-associated protein E-1;
Short=AtCAP-E1;
AltName: Full=Protein TITAN 3;
Name=SMC2-1; Synonyms=CAP-E1, TTN3; OrderedLocusNames=At5g62410;
ORFNames=MMI9.19, MMI9.24;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
PubMed=11846874; DOI=10.1046/j.1365-313x.2002.01224.x;
Liu C.-M., McElver J., Tzafrir I., Joosen R., Wittich P., Patton D.,
Van Lammeren A.A.M., Meinke D.;
"Condensin and cohesin knockouts in Arabidopsis exhibit a titan seed
phenotype.";
Plant J. 29:405-415(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=cv. Landsberg erecta;
PubMed=12783798; DOI=10.1242/dev.00542;
Siddiqui N.U., Stronghill P.E., Dengler R.E., Hasenkampf C.A.,
Riggs C.D.;
"Mutations in Arabidopsis condensin genes disrupt embryogenesis,
meristem organization and segregation of homologous chromosomes during
meiosis.";
Development 130:3283-3295(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9872454; DOI=10.1093/dnares/5.5.297;
Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. VII.
Sequence features of the regions of 1,013,767 bp covered by sixteen
physically assigned P1 and TAC clones.";
DNA Res. 5:297-308(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10718197; DOI=10.1093/dnares/7.1.31;
Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
features of the regions of 3,076,755 bp covered by sixty P1 and TAC
clones.";
DNA Res. 7:31-63(2000).
[5]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Central component of the condensin complex, a complex
required for conversion of interphase chromatin into mitotic-like
condense chromosomes. The condensin complex probably introduces
positive supercoils into relaxed DNA in the presence of type I
topoisomerases and converts nicked DNA into positive knotted forms
in the presence of type II topoisomerases. Also involved in
chromosome segregation in meiosis. {ECO:0000269|PubMed:11846874,
ECO:0000269|PubMed:12783798}.
-!- SUBUNIT: Forms a heterodimer with SMC4. Component of the condensin
complex, which contains the SMC2 and SMC4 heterodimer, and three
non SMC subunits that probably regulate the complex: CAPH, CAPD2
and CAPG.
-!- SUBCELLULAR LOCATION: Nucleus. Note=Associates with chromatin.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in roots and young floral
buds. {ECO:0000269|PubMed:12783798}.
-!- DOMAIN: The hinge domain, which separates the large intramolecular
coiled coil regions, allows the heterodimerization with SMC4,
forming a V-shaped heterodimer.
-!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG27593.2; Type=Frameshift; Positions=168, 174; Evidence={ECO:0000305};
Sequence=AAK58634.1; Type=Frameshift; Positions=168, 174; Evidence={ECO:0000305};
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EMBL; AF271730; AAG27593.2; ALT_FRAME; Genomic_DNA.
EMBL; AF271731; AAK58634.1; ALT_FRAME; mRNA.
EMBL; AF306547; AAG53093.1; -; mRNA.
EMBL; AB015469; BAB11491.1; -; Genomic_DNA.
EMBL; AB019235; BAB11491.1; JOINED; Genomic_DNA.
EMBL; CP002688; AED97605.1; -; Genomic_DNA.
RefSeq; NP_201047.1; NM_125635.3.
UniGene; At.19029; -.
ProteinModelPortal; Q9C5Y4; -.
SMR; Q9C5Y4; -.
STRING; 3702.AT5G62410.1; -.
iPTMnet; Q9C5Y4; -.
PaxDb; Q9C5Y4; -.
EnsemblPlants; AT5G62410.1; AT5G62410.1; AT5G62410.
GeneID; 836362; -.
Gramene; AT5G62410.1; AT5G62410.1; AT5G62410.
KEGG; ath:AT5G62410; -.
Araport; AT5G62410; -.
TAIR; locus:2167973; AT5G62410.
eggNOG; KOG0933; Eukaryota.
eggNOG; COG1196; LUCA.
HOGENOM; HOG000163792; -.
InParanoid; Q9C5Y4; -.
KO; K06674; -.
OMA; HNKIAME; -.
OrthoDB; EOG093600ZC; -.
PhylomeDB; Q9C5Y4; -.
Reactome; R-ATH-2299718; Condensation of Prophase Chromosomes.
Reactome; R-ATH-2514853; Condensation of Prometaphase Chromosomes.
PRO; PR:Q9C5Y4; -.
Proteomes; UP000006548; Chromosome 5.
Genevisible; Q9C5Y4; AT.
GO; GO:0000796; C:condensin complex; ISS:TAIR.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005215; F:transporter activity; ISS:TAIR.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
CDD; cd03273; ABC_SMC2_euk; 1.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR003395; RecF/RecN/SMC_N.
InterPro; IPR024704; SMC.
InterPro; IPR027120; Smc2_ABC.
InterPro; IPR010935; SMC_hinge.
InterPro; IPR036277; SMC_hinge_sf.
Pfam; PF06470; SMC_hinge; 1.
Pfam; PF02463; SMC_N; 1.
PIRSF; PIRSF005719; SMC; 1.
SMART; SM00968; SMC_hinge; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF75553; SSF75553; 1.
2: Evidence at transcript level;
ATP-binding; Cell cycle; Cell division; Coiled coil;
Complete proteome; DNA condensation; Meiosis; Mitosis;
Nucleotide-binding; Nucleus; Reference proteome.
CHAIN 1 1175 Structural maintenance of chromosomes
protein 2-1.
/FTId=PRO_0000284894.
DOMAIN 2 1161 Zinc-hook.
NP_BIND 32 39 ATP. {ECO:0000255}.
REGION 509 672 Flexible hinge.
COILED 172 508 {ECO:0000255}.
COILED 673 1028 {ECO:0000255}.
CONFLICT 107 107 I -> V (in Ref. 1; AAK58634/AAG27593).
{ECO:0000305}.
CONFLICT 213 213 E -> K (in Ref. 2; AAG53093).
{ECO:0000305}.
CONFLICT 254 254 G -> GVG (in Ref. 1; AAK58634/AAG27593).
{ECO:0000305}.
CONFLICT 439 439 L -> R (in Ref. 1; AAK58634/AAG27593 and
2; AAG53093). {ECO:0000305}.
CONFLICT 602 602 E -> G (in Ref. 2; AAG53093).
{ECO:0000305}.
CONFLICT 965 965 E -> V (in Ref. 1; AAK58634/AAG27593).
{ECO:0000305}.
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


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