SMC3_CAEEL
ID SMC3_CAEEL Reviewed; 1261 AA.
AC B2FDA8; I2HAB3; Q9U2C1;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Structural maintenance of chromosomes protein 3 {ECO:0000312|WormBase:Y47D3A.26b};
GN Name=smc-3 {ECO:0000312|WormBase:Y47D3A.26b};
GN ORFNames=Y47D3A.26 {ECO:0000312|WormBase:Y47D3A.26b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12808038; DOI=10.1091/mbc.e02-09-0603;
RA Mito Y., Sugimoto A., Yamamoto M.;
RT "Distinct developmental function of two Caenorhabditis elegans homologs of
RT the cohesin subunit Scc1/Rad21.";
RL Mol. Biol. Cell 14:2399-2409(2003).
RN [3] {ECO:0000305}
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP COHESIN COMPLEX, INTERACTION WITH SMC-1; SCC-1 AND TIM-1, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=12827206; DOI=10.1038/nature01697;
RA Chan R.C., Chan A., Jeon M., Wu T.F., Pasqualone D., Rougvie A.E.,
RA Meyer B.J.;
RT "Chromosome cohesion is regulated by a clock gene paralogue TIM-1.";
RL Nature 423:1002-1009(2003).
RN [4] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=21856158; DOI=10.1016/j.cub.2011.07.007;
RA Lightfoot J., Testori S., Barroso C., Martinez-Perez E.;
RT "Loading of meiotic cohesin by SCC-2 is required for early processing of
RT DSBs and for the DNA damage checkpoint.";
RL Curr. Biol. 21:1421-1430(2011).
RN [5] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-1081.
RX PubMed=21957461; DOI=10.1371/journal.pone.0024799;
RA Baudrimont A., Penkner A., Woglar A., Mamnun Y.M., Hulek M., Struck C.,
RA Schnabel R., Loidl J., Jantsch V.;
RT "A new thermosensitive smc-3 allele reveals involvement of cohesin in
RT homologous recombination in C. elegans.";
RL PLoS ONE 6:E24799-E24799(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22927794; DOI=10.1371/journal.pbio.1001378;
RA Tzur Y.B., Egydio de Carvalho C., Nadarajan S., Van Bostelen I., Gu Y.,
RA Chu D.S., Cheeseman I.M., Colaiacovo M.P.;
RT "LAB-1 targets PP1 and restricts Aurora B kinase upon entrance into meiosis
RT to promote sister chromatid cohesion.";
RL PLoS Biol. 10:E1001378-E1001378(2012).
CC -!- FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA
CC repair (PubMed:21957461). Involved in the repair of double strand
CC breaks during mitosis and meiosis (PubMed:21957461). Required for
CC chromosome segregation during mitosis (PubMed:12808038). Central
CC component of cohesin complex (PubMed:12827206, PubMed:12808038,
CC PubMed:21957461). The cohesin complex is required for the cohesion of
CC sister chromatids after DNA replication (PubMed:12827206). The cohesin
CC complex apparently forms a large proteinaceous ring within which sister
CC chromatids can be trapped (By similarity). At anaphase, the complex is
CC cleaved and dissociates from chromatin, allowing sister chromatids to
CC segregate (By similarity). Required for the localization of lab-1 to
CC meiotic and mitotic chromosomes (PubMed:22927794).
CC {ECO:0000250|UniProtKB:Q9UQE7, ECO:0000269|PubMed:12808038,
CC ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21957461,
CC ECO:0000269|PubMed:22927794}.
CC -!- SUBUNIT: Component of the cohesin complex, composed of the smc-1 and
CC smc-3 heterodimer attached via their SMC hinge domain, scc-1 which
CC links them, and scc-3. Interacts with scc-1, smc-1 and tim-1.
CC {ECO:0000269|PubMed:12827206}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12827206,
CC ECO:0000269|PubMed:21856158, ECO:0000269|PubMed:21957461}. Chromosome
CC {ECO:0000269|PubMed:12827206}. Note=Has diffuse nuclear appearance at
CC interphase during mitosis in somatic and germline tissues.
CC {ECO:0000269|PubMed:12827206}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=b {ECO:0000312|WormBase:Y47D3A.26b};
CC IsoId=B2FDA8-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:Y47D3A.26a};
CC IsoId=B2FDA8-2; Sequence=VSP_057591;
CC Name=c {ECO:0000312|WormBase:Y47D3A.26c};
CC IsoId=B2FDA8-3; Sequence=VSP_057590, VSP_057591;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knock-down is embryonic lethal and
CC results in aberrant chromosome segregation during mitosis. RNAi-
CC mediated knockdown at 20 degrees Celsius results in the mis-
CC localization of lab-1 in germ line nuclei (PubMed:22927794).
CC {ECO:0000269|PubMed:12808038, ECO:0000269|PubMed:12827206,
CC ECO:0000269|PubMed:22927794}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC3 subfamily. {ECO:0000305}.
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DR EMBL; BX284603; CAQ48406.1; -; Genomic_DNA.
DR EMBL; BX284603; CAB57898.4; -; Genomic_DNA.
DR EMBL; BX284603; CCH63820.1; -; Genomic_DNA.
DR RefSeq; NP_001129842.1; NM_001136370.2.
DR RefSeq; NP_001255118.1; NM_001268189.1. [B2FDA8-2]
DR RefSeq; NP_001255119.1; NM_001268190.1. [B2FDA8-3]
DR AlphaFoldDB; B2FDA8; -.
DR SMR; B2FDA8; -.
DR ComplexPortal; CPX-967; Nuclear mitotic cohesin complex.
DR STRING; 6239.Y47D3A.26b; -.
DR EPD; B2FDA8; -.
DR PaxDb; B2FDA8; -.
DR PRIDE; B2FDA8; -.
DR EnsemblMetazoa; Y47D3A.26a.1; Y47D3A.26a.1; WBGene00004873. [B2FDA8-2]
DR EnsemblMetazoa; Y47D3A.26c.1; Y47D3A.26c.1; WBGene00004873. [B2FDA8-3]
DR GeneID; 176559; -.
DR KEGG; cel:CELE_Y47D3A.26; -.
DR UCSC; Y47D3A.26.1; c. elegans.
DR CTD; 176559; -.
DR WormBase; Y47D3A.26a; CE41472; WBGene00004873; smc-3. [B2FDA8-2]
DR WormBase; Y47D3A.26b; CE37287; WBGene00004873; smc-3. [B2FDA8-1]
DR WormBase; Y47D3A.26c; CE47674; WBGene00004873; smc-3. [B2FDA8-3]
DR eggNOG; KOG0964; Eukaryota.
DR GeneTree; ENSGT00940000169262; -.
DR HOGENOM; CLU_001042_5_0_1; -.
DR InParanoid; B2FDA8; -.
DR OMA; DQHQSMR; -.
DR OrthoDB; 119789at2759; -.
DR PhylomeDB; B2FDA8; -.
DR Reactome; R-CEL-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-CEL-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-CEL-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:B2FDA8; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004873; Expressed in adult organism and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0008278; C:cohesin complex; IDA:WormBase.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IDA:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0061775; F:cohesin loading activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IDA:ComplexPortal.
DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IBA:GO_Central.
DR CDD; cd03272; ABC_SMC3_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; IPR041741; SMC3_ABC_euk.
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 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Chromosome; Coiled coil;
KW DNA damage; DNA repair; Mitosis; Nucleus; Reference proteome.
FT CHAIN 1..1261
FT /note="Structural maintenance of chromosomes protein 3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000432835"
FT DOMAIN 534..645
FT /note="SMC hinge"
FT COILED 188..332
FT /evidence="ECO:0000255"
FT COILED 406..450
FT /evidence="ECO:0000255"
FT COILED 677..826
FT /evidence="ECO:0000255"
FT COILED 857..930
FT /evidence="ECO:0000255"
FT COILED 1023..1085
FT /evidence="ECO:0000255"
FT MOTIF 1159..1193
FT /note="DA-box"
FT /evidence="ECO:0000250|UniProtKB:P47037"
FT VAR_SEQ 1..876
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057590"
FT VAR_SEQ 947..1002
FT /note="Missing (in isoform a and isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_057591"
FT MUTAGEN 1081
FT /note="L->F: In t2553; Thermosensitive mutant with reduced
FT stability of the cohesin complex on chromosomes and
FT defective DNA double-stranded break repair."
FT /evidence="ECO:0000269|PubMed:21957461"
SQ SEQUENCE 1261 AA; 146517 MW; DF6B14105AB52B01 CRC64;
MKIKEVRITG FRSYKDNTNV SGFSPRSNVV VGRNGSGKSN FFHAIQFVLS DEYAHLKEEQ
RLGLLHESTG PKVAHARVEI TFDNSEKRLM AFENSEVKIV RQVGKKKDQY YIDNKMVPRA
EVVNLMESAG FSRSNPYYIV KQGKINELAT SPDAYKLKLL REVAGTRVYD ERKEESLKIL
KETKMKTEKI QGLLKYIDER LQTLENEKED LKEYQKLDKT KRSVEYTMYD NTNKEAIKEK
TKLDEQKVEL NQKDNNVKSQ LNDVIAEMAK LKTDKKKLES LGRGLREDKE TLQAEETKMV
EEKMTLKLEI DSLNEENTRE RQGRQNAEHS LQGVGDEIFK NEEELDTIKP EYAKLLEEES
RLKTDIRIDE SRAKEILAKQ GQRSQFSSVD DRDKFLRNEI RRISGLIADN KEREETIQKE
LADVEREDEK LNNEIQSISR TIDENRYEMD TFAAKSTSLK QEYDAAYVAQ QTAAREEKAI
RDKIGNTEQD ISAANDQLRR IVARPVYNGI TGVRKVIEEF KHDNRNGQHD DVINGYYGTV
IELAEVPDMF RTAVEVIAQN RLFYHVVETD RIATKILRKF NEMQLPGEIN FFPMNRVSAP
RQRDLSNNSN ARPMSDVIDY EVQYDKVFKS ITANVIIVRT LDQAARDLRN EGFDVVSVDG
DQMSKKGVMT GGFIDKKRSK LELHTQKDRF TKELAELQKS LAEAEKMVRE RTQEAEKIRN
RMQQHENQIG DFHRKHRELT EAKNAISQQF YMVTSTKEPK KDQLLGIKNH LRELLAQKEN
FEQEIGSNMS SQLTSDEEQT VKKLRKKVDE MTKQLATVSR RRMDLMHRKN AIENLLTKKL
YKTKESLTAR VDDISDNERR HKLENANAQL TSLLTRMEST RKQLATAISE LQDYETKEKA
LQINIDNVLE QQRDLEKQQA DFQLQYDKIT AKEDEVKQKR EDSLKKLILS RYSIKTRKNQ
FSYEISDSEE VGAKREPIEH RKLKISTFCL EYRAKLEKVH SNMRLLGALP TDTFSKWQNV
KPRELEKKLL ECVNELKKYE NVNKKALDQY MTASSQKEEL TKRMAEQKKS EDSIEELLKV
LENRKYEAID LTFKQVKKNF EQVFKQLVPH GRGKMQMRAR EQRDDEEGIN SVELYEGISV
LVSFVSDDGD SETREMTQLS GGQKSLVALA IIFSIQKCDP APFYLFDEID AALDAQHRKS
VADMIQSLSD QAQFVTTTFR PELLATAEKF YGVRFRNKVS HIDSVTREQA YDFVEDDTTH
G
