SMC1_ARATH
ID SMC1_ARATH Reviewed; 1218 AA.
AC Q6Q1P4; F4JE01; F4JE02; Q0WSY5; Q9M1T3;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Structural maintenance of chromosomes protein 1;
DE Short=SMC protein 1;
DE Short=SMC-1;
DE AltName: Full=Chromosome segregation protein SMC-1;
DE AltName: Full=Cohesin complex subunit SMC-1;
DE AltName: Full=Protein TITAN8;
GN Name=SMC1; Synonyms=TTN8; OrderedLocusNames=At3g54670; ORFNames=T5N23.30;
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], 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 [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-332.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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:0000250}. Chromosome {ECO:0000250}.
CC Note=Associates with chromatin. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flower buds and stems, and, to
CC a lower extent, in leaves and roots. {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 -!- 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. SMC1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB77587.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY567966; AAS68515.1; -; mRNA.
DR EMBL; AL138650; CAB77587.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79263.2; -; Genomic_DNA.
DR EMBL; AK227781; BAE99763.1; -; mRNA.
DR PIR; T47626; T47626.
DR RefSeq; NP_001319748.1; NM_001339686.1.
DR AlphaFoldDB; Q6Q1P4; -.
DR SMR; Q6Q1P4; -.
DR BioGRID; 9948; 2.
DR STRING; 3702.AT3G54670.3; -.
DR iPTMnet; Q6Q1P4; -.
DR PaxDb; Q6Q1P4; -.
DR PRIDE; Q6Q1P4; -.
DR ProteomicsDB; 228196; -.
DR EnsemblPlants; AT3G54670.1; AT3G54670.1; AT3G54670.
DR GeneID; 824632; -.
DR Gramene; AT3G54670.1; AT3G54670.1; AT3G54670.
DR KEGG; ath:AT3G54670; -.
DR Araport; AT3G54670; -.
DR TAIR; locus:2102420; AT3G54670.
DR eggNOG; KOG0018; Eukaryota.
DR HOGENOM; CLU_001042_0_1_1; -.
DR InParanoid; Q6Q1P4; -.
DR OMA; YIRDHTT; -.
DR OrthoDB; 326079at2759; -.
DR PRO; PR:Q6Q1P4; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q6Q1P4; baseline and differential.
DR Genevisible; Q6Q1P4; AT.
DR GO; GO:0008278; C:cohesin complex; ISS:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F: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:0007062; P:sister chromatid cohesion; IMP:TAIR.
DR CDD; cd03275; ABC_SMC1_euk; 2.
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; IPR028468; Smc1_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; 2.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Chromosome; Coiled coil;
KW DNA damage; DNA repair; Meiosis; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..1218
FT /note="Structural maintenance of chromosomes protein 1"
FT /id="PRO_0000421562"
FT DOMAIN 11..1200
FT /note="Zinc-hook"
FT DOMAIN 518..632
FT /note="SMC hinge"
FT COILED 159..505
FT /evidence="ECO:0000255"
FT COILED 671..938
FT /evidence="ECO:0000255"
FT COILED 1003..1035
FT /evidence="ECO:0000255"
FT MOTIF 183..190
FT /note="Nuclear localization signal 1"
FT /evidence="ECO:0000250"
FT MOTIF 425..432
FT /note="Nuclear localization signal 2"
FT /evidence="ECO:0000250"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 818
FT /note="L -> P (in Ref. 1; AAS68515)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1218 AA; 140912 MW; 07F9768B155397CA CRC64;
MPAIQSPSGK ILQLEMENFK SYKGHQLVGP FKDFTAIIGP NGSGKSNLMD AISFVLGVRT
GQLRGSQLKD LIYAFDDRDK EQRGRKAFVR LVYQMDDGVE LRFTRSITSA GGSEYRIDNR
VVNLDEYNGK LRSLGILVKA RNFLVFQGDV ESIASKNPKE LTGLLEEISG SEELKKEYEG
LEEKKASAEE KAALIYQKKK TIGNEKKLKK AQKEEAEKHL RLQEELKALK RERFLWQLYN
IENDIEKANE DVDSEKSNRK DVMRELEKFE REAGKRKVEQ AKYLKEIAQR EKKIAEKSSK
LGKIQPELLR FKEEIARIKA KIETNRKDVD KRKKEKGKHS KEIEQMQKSI KELNKKMELF
NKKRQDSSGK LPMLDSQLQD YFRLKEEAGM KTIKLRDEHE VLERQRRTDL EALRNLEENY
QQLINRKNDL DEQIKRFKDR QGEIETSSSK YKNETTSLKT ELRALQEKHV NAREASAKLK
TRIAELEDQL SDLTAERYEN ERDSRLTQAV ESLKRLFQGV HGRMTDLCRP NRKKYNLAVT
VAMGRFMDAV VVEDENTGKD CIKYLKEQRL PPMTFIPLQS VRVKQVFERL RNLGGTAKLV
FDVIQFDPEL EKAVLYAVGN TLVCDELEEA KVLSWSGERF KVVTVDGILL TKAGTMTGGT
SGGMEAKSNK WDDKKIEGLK KNKEDFEQQL ENIGSIREMQ MKESEISGKI SGLEKKIQYA
EIEKKSIKDK LPQLEQEERN IIEEIDRIKP ELSKARTEVD KRKTEMNKLE KRMNEIVDRI
YKDFSQSVGV PNIRVYEETQ LKTAEKEAEE RLELSNQLAK LKYQLEYEQN RDVGSRIRKI
ESSISSLETD LEGIQKTMSE RKETAVKITN EINNWKKEME ECKQKSEEYE KEILDWKKQA
SQATTSITKL NRQIHSKETQ IEQLISQKQE ITEKCELEHI TLPVLSDAME EDDSDGPQFD
FSELGRAYLQ ERRPSAREKV EAEFRQKIES KTSEIERTAP NLRALDQYEA IQEKEKQVSQ
EFEAARKEEK QVADAFNTVK QKRYELFMEA FNHIASNIDK IYKQLTKSNT HPLGGTAYLN
LENEDDPFLH GIKYTTMPPT KRFRDMEQLS GGEKTVAALA LLFSIHSYRP SPFFILDEVD
AALDNLNVAK VAKFIRSKSC QAARDNQDAE DGNGFQSIVI SLKDSFYDKA EALVGVYRDT
ERSCSSTMSF DLRNYQES
