SMC5_CAEEL
ID SMC5_CAEEL Reviewed; 1076 AA.
AC Q18237;
DT 12-APR-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Structural maintenance of chromosomes protein 5 {ECO:0000305};
GN Name=smc-5 {ECO:0000312|WormBase:C27A2.1};
GN ORFNames=C27A2.1 {ECO:0000312|WormBase:C27A2.1};
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, INTERACTION WITH SMC-6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=20661436; DOI=10.1371/journal.pgen.1001028;
RA Bickel J.S., Chen L., Hayward J., Yeap S.L., Alkers A.E., Chan R.C.;
RT "Structural maintenance of chromosomes (SMC) proteins promote homolog-
RT independent recombination repair in meiosis crucial for germ cell genomic
RT stability.";
RL PLoS Genet. 6:E1001028-E1001028(2010).
RN [3] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLY-965.
RX PubMed=24424777; DOI=10.1534/genetics.113.158295;
RA Wolters S., Ermolaeva M.A., Bickel J.S., Fingerhut J.M., Khanikar J.,
RA Chan R.C., Schumacher B.;
RT "Loss of Caenorhabditis elegans BRCA1 promotes genome stability during
RT replication in smc-5 mutants.";
RL Genetics 196:985-999(2014).
RN [4] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27011106; DOI=10.1371/journal.pbio.1002412;
RA Jagut M., Hamminger P., Woglar A., Millonigg S., Paulin L., Mikl M.,
RA Dello Stritto M.R., Tang L., Habacher C., Tam A., Gallach M.,
RA von Haeseler A., Villeneuve A.M., Jantsch V.;
RT "Separable roles for a Caenorhabditis elegans RMI1 homolog in promoting and
RT antagonizing meiotic crossovers ensure faithful chromosome inheritance.";
RL PLoS Biol. 14:E1002412-E1002412(2016).
RN [5] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27010650; DOI=10.1371/journal.pgen.1005872;
RA Hong Y., Sonneville R., Agostinho A., Meier B., Wang B., Blow J.J.,
RA Gartner A.;
RT "The SMC-5/6 complex and the HIM-6 (BLM) helicase synergistically promote
RT meiotic recombination intermediate processing and chromosome maturation
RT during Caenorhabditis elegans meiosis.";
RL PLoS Genet. 12:E1005872-E1005872(2016).
CC -!- FUNCTION: Core component of the smc-5/smc-6 complex (PubMed:20661436).
CC Functions in DNA double strand break repair by promoting sister-
CC chromatid homologous recombination during meiosis (PubMed:20661436,
CC PubMed:27011106, PubMed:27010650, PubMed:24424777). Acts in a DNA
CC repair pathway for removal of ionizing radiation- and ultraviolet (UV)
CC radiation-induced DNA lesions that is distinct from classical
CC nucleotide excision repair and the translesion synthesis pathway
CC (PubMed:20661436, PubMed:24424777). Also involved in the recovery of
CC stalled replication forks (PubMed:24424777).
CC {ECO:0000269|PubMed:20661436, ECO:0000269|PubMed:24424777,
CC ECO:0000269|PubMed:27010650, ECO:0000269|PubMed:27011106}.
CC -!- SUBUNIT: Interacts with smc-6. {ECO:0000269|PubMed:20661436}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20661436}. Chromosome
CC {ECO:0000269|PubMed:20661436}. Note=Localizes on chromosomes during
CC diplotene and diakinesis in oocytes. {ECO:0000269|PubMed:20661436}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline (at protein level).
CC {ECO:0000269|PubMed:20661436}.
CC -!- DOMAIN: The flexible hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of smc-6, forming a V-shaped heterodimer.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Reduced fecundity and transgenerational sterility
CC (PubMed:20661436). Increased apoptosis in germ cells and
CC hypersensitivity to ultraviolet and ionizing radiation and hydroxyurea-
CC induced replication stress (PubMed:20661436, PubMed:24424777).
CC Increased rad-51 foci in the mitotic and meiotic germline
CC (PubMed:20661436, PubMed:27010650, PubMed:24424777). Chromosome
CC fragmentation defects and unresolved diakinesis chromosomes in meiotic
CC oocytes (PubMed:20661436, PubMed:27010650). Increased accumulation of
CC homologous recombination intermediates during meiosis (PubMed:20661436,
CC PubMed:27011106, PubMed:27010650). Impaired DNA replication in germ
CC cells (PubMed:24424777). Accumulation of brd-1 and rmh-1 on chromosomes
CC in mitotic germ cells (PubMed:24424777, PubMed:27011106). In a spo-11
CC mutant background, no accumulation of meiotic rad-51 foci and decrease
CC in chromosome fragmentation (PubMed:20661436). In a him-3 mutant
CC background, increase in rad-51 foci and chromosome fragmentation
CC (PubMed:20661436). RNAi-mediated knockdown of syp-2 leads to an
CC increase of chromosome fragmentation (PubMed:20661436). In a xpc-1
CC mutant background, increased ultraviolet sensitivity (PubMed:24424777).
CC In a xpc-1 or csb-1 mutant background, enhanced ultraviolet-induced
CC delay in somatic development (PubMed:24424777). In a rmh-1 mutant
CC background, increased embryonic lethality and larval arrest
CC (PubMed:27011106). In a him-6 mutant background, increased cross-over
CC frequency, formation of chromatin bridges, defects in diakinetic
CC chiasmata formation, aberrant distribution of the condensin II subunit
CC hcp-6 and compromised chromosome segregation in meiosis, leading to
CC embryonic lethality (PubMed:27010650). {ECO:0000269|PubMed:20661436,
CC ECO:0000269|PubMed:24424777, ECO:0000269|PubMed:27010650,
CC ECO:0000269|PubMed:27011106}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily. {ECO:0000305}.
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DR EMBL; BX284602; CCD63066.1; -; Genomic_DNA.
DR RefSeq; NP_494935.1; NM_062534.4.
DR AlphaFoldDB; Q18237; -.
DR SMR; Q18237; -.
DR STRING; 6239.C27A2.1; -.
DR EPD; Q18237; -.
DR PaxDb; Q18237; -.
DR PeptideAtlas; Q18237; -.
DR EnsemblMetazoa; C27A2.1.1; C27A2.1.1; WBGene00016151.
DR GeneID; 173874; -.
DR KEGG; cel:CELE_C27A2.1; -.
DR UCSC; C27A2.1; c. elegans.
DR CTD; 173874; -.
DR WormBase; C27A2.1; CE27096; WBGene00016151; smc-5.
DR eggNOG; KOG0979; Eukaryota.
DR GeneTree; ENSGT00550000074816; -.
DR HOGENOM; CLU_004969_1_0_1; -.
DR InParanoid; Q18237; -.
DR OMA; SAEFFPG; -.
DR OrthoDB; 100993at2759; -.
DR PhylomeDB; Q18237; -.
DR Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:Q18237; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00016151; Expressed in adult organism and 4 other tissues.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030915; C:Smc5-Smc6 complex; 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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0010705; P:meiotic DNA double-strand break processing involved in reciprocal meiotic recombination; IGI:WormBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR027131; SMC5.
DR PANTHER; PTHR45916; PTHR45916; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromosome; Coiled coil; DNA damage; DNA recombination;
KW DNA repair; DNA replication; Meiosis; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1076
FT /note="Structural maintenance of chromosomes protein 5"
FT /id="PRO_0000439582"
FT REGION 375..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..617
FT /note="Flexible hinge"
FT /evidence="ECO:0000305"
FT COILED 190..415
FT /evidence="ECO:0000255"
FT COILED 627..713
FT /evidence="ECO:0000255"
FT COILED 749..786
FT /evidence="ECO:0000255"
FT COMPBIAS 375..416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
FT MUTAGEN 965
FT /note="G->R: In sbj2; hypersensitive to UVB irradiation."
FT /evidence="ECO:0000269|PubMed:24424777"
SQ SEQUENCE 1076 AA; 123461 MW; C20E6428B1A5865F CRC64;
MASQDSDEAL PANYKDYPDG SLLRVVFHNF LTYEHTSFLP TASLNMILGH NGSGKSSIIC
GICLACGGSP KSLGRSERIV EYIRHGCTEG YVEIAIADKQ KGPQVVRLTI RVGEQPKYRL
NDSATTQSEI ADLRKHYNIQ IDNPCAFLAQ DKVKSFSEQS SIELLRNTEK AASADLDQQH
IDLMKQREDS TSIEDKCTTS ENAIKRLEDE IGKIMPLVEN YRKKLALQSK LRLLEKKMKI
MEFEKFDREY KAELQNMDGA MIEYREVEKS IAECEKHRKN LEDRIKKDRS QISQMQRSCN
EILAKVQEKG DKKLMEDMMQ RAKAKLESAK KAADQHEKDV EKARKMIDQA RARLQEAVDT
LNGYEEFQSE MKSLEQKYST AERDSRQEED AIQKKSYEMR QLENKKRDEE QNSQLNRQDR
YRVLQNFSSD ASKAYRWYQQ NRSQFKGDVY MPIMDMVLKT PEAAKALENS VGVRDRTMFV
CCYKEDELLI NGKQHSWRIN TSVVPAEKIY SEDIDAQLPS ELSRLGFKYL VSNCFDAPAP
LKQFLCNVSG LNRIPFGGSD VEKKIAEVSQ AIEQTRYSVF LTANIRCQNS KSRYANNTLQ
SQSATREANT WRDQFFKVSP VAKRTDNSIL EEIQKLKAEI DIRSEQLREK RGAIQKERDV
LRQEQMQWKS KKQVHTKWKT ELASEMAKLE ALENEVVDIS AIEEEYANVE KKAILETKKM
LENSIRWHKE IIDKHRLIGI FELSESICKS RVNKSNSEAE THRSKLEDLK SVKDAAEDLL
KTALNHKKAA ASALMKECSL KTLDESKMSP AENKIYSSLV KMFEEADVPT DMNTLDQAIT
SEKTRLKLAE DSGEDGSIVH EQRLKVLDDD LVLEKTRQEK LIENRARIHD KLGDEINNWR
KEVETMIEQI NVNYVQFFDS LGCRGEVSLE VPENPLDIEK YGIMIMVCFR KGESMKRLDN
KVQSGGERSV ATMLYLLALQ QLCPVPFRCI DEINQGMDPT NERKVFDIMV GMWNGTTGTL
SKTQYFLLSP KLLHGLDMRE NVNIVMVNST LTNSHGKHYD TSAKIDATFA KMGISA
