SCC3_ARATH
ID SCC3_ARATH Reviewed; 1098 AA.
AC O82265; Q8LFH0; Q9XGM9;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=Sister-chromatid cohesion protein 3 {ECO:0000303|PubMed:11276426, ECO:0000303|PubMed:16176934};
DE Short=AtSCC3 {ECO:0000303|PubMed:11276426, ECO:0000303|PubMed:16176934};
DE AltName: Full=Stromalin protein {ECO:0000303|Ref.1};
GN Name=SCC3 {ECO:0000303|PubMed:11276426, ECO:0000303|PubMed:16176934};
GN Synonyms=SA {ECO:0000303|Ref.1};
GN OrderedLocusNames=At2g47980 {ECO:0000312|Araport:AT2G47980};
GN ORFNames=T9J23.3 {ECO:0000312|EMBL:AAM15132.1};
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].
RC STRAIN=cv. Columbia;
RA Valdeolmillos A., Barbero J.;
RT "Molecular cloning and expression of stromalin protein from Arabidopsis
RT thaliana.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY.
RX PubMed=11276426; DOI=10.1186/gb-2001-2-3-research0009;
RA Jones S., Sgouros J.;
RT "The cohesin complex: sequence homologies, interaction networks and shared
RT motifs.";
RL Genome Biol. 2:RESEARCH0009.1-RESEARCH0009.12(2001).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia, and cv. Wassilewskija;
RX PubMed=16176934; DOI=10.1242/jcs.02583;
RA Chelysheva L., Diallo S., Vezon D., Gendrot G., Vrielynck N., Belcram K.,
RA Rocques N., Marquez-Lema A., Bhatt A.M., Horlow C., Mercier R., Mezard C.,
RA Grelon M.;
RT "AtREC8 and AtSCC3 are essential to the monopolar orientation of the
RT kinetochores during meiosis.";
RL J. Cell Sci. 118:4621-4632(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
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).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [10]
RP INTERACTION WITH DEK3, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=cv. Columbia;
RX PubMed=25387881; DOI=10.1105/tpc.114.129254;
RA Waidmann S., Kusenda B., Mayerhofer J., Mechtler K., Jonak C.;
RT "A DEK domain-containing protein modulates chromatin structure and function
RT in Arabidopsis.";
RL Plant Cell 26:4328-4344(2014).
CC -!- FUNCTION: Essential component of cohesin complex, a complex required
CC for the cohesion of sister chromatids after DNA replication. The
CC cohesin complex apparently forms a large proteinaceous ring within
CC which sister chromatids can be trapped. At anaphase, the complex is
CC cleaved and dissociates from chromatin, allowing sister chromatids to
CC segregate. The cohesin complex may also play a role in spindle pole
CC assembly during mitosis. Required for centromere cohesion maintenance
CC at anaphase I and for the monopolar orientation of the kinetochores
CC during both male and female meiosis. Also involved in mitosis.
CC {ECO:0000269|PubMed:16176934, ECO:0000269|PubMed:19533160}.
CC -!- SUBUNIT: Part of the cohesin complex. Interacts with DEK3
CC (PubMed:25387881). {ECO:0000250, ECO:0000269|PubMed:25387881}.
CC -!- INTERACTION:
CC O82265; Q9SUA1: DEK3; NbExp=2; IntAct=EBI-9397077, EBI-1787282;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750,
CC ECO:0000269|PubMed:16176934}. Chromosome {ECO:0000269|PubMed:16176934}.
CC Note=In pollen mother cells (PMC), localized in nucleus from meiotic
CC interphase up to and including metaphase I. During interphase, detected
CC as foci in the nucleus. During leptotene and by zygotene and pachytene,
CC localized in condensing chromosomes on chromatin, delineating the
CC chromosome axis. At diplotene and diakinesis, remains on the chromosome
CC axis at lower levels. At metaphase I, confined to the arms of each
CC bivalent chromosomes. Excluded from centromeric regions.
CC -!- TISSUE SPECIFICITY: Expressed in roots, mature leaves, buds and
CC seedlings. {ECO:0000269|PubMed:16176934}.
CC -!- DEVELOPMENTAL STAGE: Expressed in mitotic and meitotic cells. In
CC meiotic nuclei, first detected at interphase, and binds to the
CC chromosome axis from early leptotene through to anaphase I.
CC {ECO:0000269|PubMed:16176934}.
CC -!- DISRUPTION PHENOTYPE: The null allele scc3-2 is embryo lethal. The weak
CC allele scc3-1 exhibits mitotic and meiotic defects. Heterozygote plants
CC are dwarf and partly sterile. Reduced chromatid alignment during
CC interphase. {ECO:0000269|PubMed:16176934, ECO:0000269|PubMed:19533160}.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
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DR EMBL; AJ242965; CAB45374.1; -; mRNA.
DR EMBL; AC005309; AAC63652.2; -; Genomic_DNA.
DR EMBL; AC006072; AAM15132.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10920.1; -; Genomic_DNA.
DR EMBL; AY063915; AAL36271.1; -; mRNA.
DR EMBL; AY091270; AAM14209.1; -; mRNA.
DR EMBL; AY084846; AAM61411.1; -; mRNA.
DR PIR; H84921; H84921.
DR RefSeq; NP_566119.1; NM_130365.4.
DR AlphaFoldDB; O82265; -.
DR SMR; O82265; -.
DR BioGRID; 4745; 38.
DR IntAct; O82265; 1.
DR STRING; 3702.AT2G47980.1; -.
DR iPTMnet; O82265; -.
DR PaxDb; O82265; -.
DR PRIDE; O82265; -.
DR ProteomicsDB; 226596; -.
DR EnsemblPlants; AT2G47980.1; AT2G47980.1; AT2G47980.
DR GeneID; 819410; -.
DR Gramene; AT2G47980.1; AT2G47980.1; AT2G47980.
DR KEGG; ath:AT2G47980; -.
DR Araport; AT2G47980; -.
DR TAIR; locus:2043318; AT2G47980.
DR eggNOG; KOG2011; Eukaryota.
DR HOGENOM; CLU_004086_0_0_1; -.
DR InParanoid; O82265; -.
DR OMA; ICDLLII; -.
DR OrthoDB; 167826at2759; -.
DR PhylomeDB; O82265; -.
DR PRO; PR:O82265; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O82265; baseline and differential.
DR Genevisible; O82265; AT.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005694; C:chromosome; IDA:TAIR.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051754; P:meiotic sister chromatid cohesion, centromeric; IMP:TAIR.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:TAIR.
DR GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IMP:TAIR.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039662; Cohesin_Scc3/SA.
DR InterPro; IPR020839; SCD.
DR InterPro; IPR013721; STAG.
DR PANTHER; PTHR11199; PTHR11199; 1.
DR Pfam; PF08514; STAG; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51425; SCD; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Chromosome partition; Coiled coil;
KW Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..1098
FT /note="Sister-chromatid cohesion protein 3"
FT /id="PRO_0000425660"
FT DOMAIN 275..360
FT /note="SCD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 245..265
FT /evidence="ECO:0000255"
FT COILED 632..653
FT /evidence="ECO:0000255"
FT COILED 888..908
FT /evidence="ECO:0000255"
FT COILED 1009..1032
FT /evidence="ECO:0000255"
FT COMPBIAS 1..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1042..1077
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 621
FT /note="S -> I (in Ref. 5; AAM61411)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1098 AA; 125759 MW; 293ACEA3D335471A CRC64;
MEDSPQGLKR SRDPDQDQDD DSGEAGKADG SGGENQERSS DQIELDDDDF QETRPKPKRS
RTHPPQQNLI EVVKGNGDLI SKAVKIWVER YEDSPSLATT ELLSMLFQAC GAKYSIKDDL
LDETDVDDVV VSLVNLARAG ELEDYQSSRK KELKNFKENL VSFWNNLIIE CQNGPLFDRV
LFDKCMDYII ALSCTPPRVY RQTATLMGLQ LVTSFISVAN TLGSQRETTQ RQLNAESKKR
ADGPRVDSLN KRLSVTHEQI TTLEDMMRKI FTGLFVHRYR DIDNDIRMSC IQSLGIWILS
YPSLFLQDLY LKYLGWTLND KNAGVRKASL LALQKLYEMD ENVPTLGLFT QRFSNRMIEM
ADDVDMSAAV CAIGLVKQLL RHQLIPDDDL GPLYDLLIDQ PQEIRRAIGE LVYDHLIAQK
FNSSPSSLTG HDDSSSEIHI FRMLQILREF STDPILCVYV IDDVWEYMKA MKDWKCIISM
LLDQNPRTGS TTDEDSTNLI RLLFVSIRKA VGEKIIPSTD NRKQYHSKAQ REIFENNRKD
ITVAMMKNYP QLLRKFMADK AKVSSLVEII IFMKLELYSL KRQEQSFKAA VRLIKDAFFK
HGEKEALRSC VKAITFCASE SKGELQDFSR GKLKDLEDEL LDKITSAIRE VKDGNDEYSL
LVNLKRLYEL QLSKPVLVES MFDEIALTLH NFRNLDEEVI CFLLLNMHMY LAWYLHSIIN
CEAISEASLS SLISKRDTLF EELSYFLNGI EESKKYGNQL SNRICAILAE TWCLFRKSNY
DSGKLERLGY CPDSVFLEKF WKLCAEMFNT SDETDEEDEN KEYIEETNRD VSVIAACKLV
ASDVVPKDYL GPEIISHLGM HGPGVTGIIK NLITFLRKKE DDISNIYLES LKRAYHRYSS
ELSSGREESR VDKCLEEWRE LAGGLSGMYI GAARNKYRLE ILSVVKEGVE FAFRDAPKQL
LFLEVAILPF ATRLSVSDII DIKKDVQGRI VHVNTDEDPS GWRPCFTFLE TLEEKCLKNE
DLQDDKEAAN VRRRGRPRKR PETERKRLFD EQSGSDEDES ISGGSDREDK LDEDAPLIET
IRSAARRKAL KGERSKGH
