SMC22_ARATH
ID SMC22_ARATH Reviewed; 1171 AA.
AC Q9SN90; Q9STX7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Structural maintenance of chromosomes protein 2-2;
DE Short=AtSMC2-2;
DE AltName: Full=Chromosome-associated protein E-2;
DE Short=AtCAP-E2;
GN Name=SMC2-2; Synonyms=CAP-E2; OrderedLocusNames=At3g47460;
GN ORFNames=F1P2.10, T21L8.210;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
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 [3]
RP 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).
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.
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}.
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DR EMBL; AL096860; CAB51218.1; -; Genomic_DNA.
DR EMBL; AL132955; CAB61972.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78284.1; -; Genomic_DNA.
DR PIR; T45706; T45706.
DR RefSeq; NP_190330.1; NM_114614.4.
DR AlphaFoldDB; Q9SN90; -.
DR SMR; Q9SN90; -.
DR BioGRID; 9220; 5.
DR STRING; 3702.AT3G47460.1; -.
DR iPTMnet; Q9SN90; -.
DR PaxDb; Q9SN90; -.
DR PRIDE; Q9SN90; -.
DR ProteomicsDB; 226746; -.
DR EnsemblPlants; AT3G47460.1; AT3G47460.1; AT3G47460.
DR GeneID; 823900; -.
DR Gramene; AT3G47460.1; AT3G47460.1; AT3G47460.
DR KEGG; ath:AT3G47460; -.
DR Araport; AT3G47460; -.
DR TAIR; locus:2079107; AT3G47460.
DR eggNOG; KOG0933; Eukaryota.
DR HOGENOM; CLU_001042_9_0_1; -.
DR InParanoid; Q9SN90; -.
DR OMA; HNKIAME; -.
DR PhylomeDB; Q9SN90; -.
DR PRO; PR:Q9SN90; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SN90; baseline and differential.
DR Genevisible; Q9SN90; 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; IBA:GO_Central.
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..1171
FT /note="Structural maintenance of chromosomes protein 2-2"
FT /id="PRO_0000284895"
FT DOMAIN 2..1158
FT /note="Zinc-hook"
FT DOMAIN 518..635
FT /note="SMC hinge"
FT COILED 172..510
FT /evidence="ECO:0000255"
FT COILED 674..1026
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1171 AA; 132315 MW; 2FB6BFC4F00F4C95 CRC64;
MHIKEICLEG FKSYATRTVV PGFDPHFNAI TGLNGSGKSN ILDSICFVLG ITNLQQVRAA
NLQELVYKQG QAGITRATVS VTFDNSERNR SPLGHEDHSE ITVTRQIVVG GKNKYLINGK
LAQPNQVQNL FHSVQLNVNN PHFLIMQGRI TKVLNMKPME ILSMLEEAAG TRMYENKKEA
ALKTLEKKQT KVDEINKLLE KDILPALEKL RREKSQYMQW ANGNAELDRL KRFCVAFEYV
QAEKIRDNSI HVVEEMKIKM TGIDEQTDKT QGEISELEKQ IKALTQAREA SMGGEVKALS
DKVDSLSNEV TRELSKLTNM EDTLQGEEKN AEKMVHNIED LKKSVEERAS ALNKCDEGAA
ELKQKFQEFS TTLEECEREH QGILAGKSSG DEEKCLEDQL RDAKISVGTA ETELKQLNTK
ISHCEKELKE KKSQLMSKQD EAVAVENELD ARKNDVESVK RAFDSLPYKE GQMEALEKDR
ESELEIGHRL KDKVHELSAQ LANVQFTYRD PVKNFDRSKV KGVVAKLIKV NDRSSMTALE
VTAGGKLFNV IVDTEDTGKQ LLQKGDLRRR VTIIPLNKIQ SHLVPPRVQQ ATVGKGNAEL
ALSLVGYSEE LKNAMEYVFG STFVCKTTDA AKEVAFNREI RTPSVTLEGD VFQPSGLLTG
GSRKGGGDLL RQLHDLAEAE TKFRAHQKSL SEIEANIKEL QPLQTKFTDM KAQLELKMYD
MSLFLKRAEQ NEHHKLGDAV KKLEEEVEEM RSQIKEKEGL YKSCADTVST LEKSIKDHDK
NREGRLKDLE KNIKTLKARI QASSKDLKGH ENVRERLVME QEAVTQEQSY LKSQLTSLRT
QISTLASDVG NQRAKVDAIQ KDHDQSLSEL KLIHAKMKEC DTQISGSIAE QEKCLQKISD
MKLDRKKLEN EVTRMEMEHK NCSVKVDKLV EKHTWITSEK RLFGNGGTDY DFESRDPHKA
REELERLQTD QSSLEKRVNK KVTAMFEKAE DEYNALMTKK NIIETDKSKI KKVIEELDEK
KKETLKVTWV KVNQDFGSIF STLLPGTMSK LEPPEGGTFL DGLEVRVAFG DVWKQSLSEL
SGGQRSLLAL SLILALLLFK PAPIYILDEV DAALDLSHTQ NIGRMIKSHF PHSQFIVVSL
KEGMFSNADV LFRTKFVDGV STVQRTVTKQ S
