SCC3_CAEEL
ID SCC3_CAEEL Reviewed; 1096 AA.
AC Q19555;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Cohesin subunit scc-3 {ECO:0000250|UniProtKB:P40541};
GN Name=scc-3 {ECO:0000312|WormBase:F18E2.3};
GN ORFNames=F18E2.3 {ECO:0000312|WormBase:F18E2.3};
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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=14499625; DOI=10.1016/s0014-4827(03)00266-0;
RA Pasierbek P., Fodermayr M., Jantsch V., Jantsch M., Schweizer D., Loidl J.;
RT "The Caenorhabditis elegans SCC-3 homologue is required for meiotic
RT synapsis and for proper chromosome disjunction in mitosis and meiosis.";
RL Exp. Cell Res. 289:245-255(2003).
RN [3] {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 [4] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 800-GLN--PHE-1096.
RX PubMed=14560015; DOI=10.1128/mcb.23.21.7698-7707.2003;
RA Wang F., Yoder J., Antoshechkin I., Han M.;
RT "Caenorhabditis elegans EVL-14/PDS-5 and SCC-3 are essential for sister
RT chromatid cohesion in meiosis and mitosis.";
RL Mol. Cell. Biol. 23:7698-7707(2003).
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE COHESIN COMPLEX, INTERACTION WITH SMC-1;
RP SMC-3; SCC-1 AND TIM-1, SUBCELLULAR 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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16802858; DOI=10.1371/journal.pbio.0040242;
RA Seitan V.C., Banks P., Laval S., Majid N.A., Dorsett D., Rana A., Smith J.,
RA Bateman A., Krpic S., Hostert A., Rollins R.A., Erdjument-Bromage H.,
RA Tempst P., Benard C.Y., Hekimi S., Newbury S.F., Strachan T.;
RT "Metazoan Scc4 homologs link sister chromatid cohesion to cell and axon
RT migration guidance.";
RL PLoS Biol. 4:E242-E242(2006).
RN [7] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF 800-GLN--PHE-1096.
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).
CC -!- FUNCTION: Component of the cohesin complex, a complex required for the
CC cohesion of sister chromatids after DNA replication (PubMed:12827206).
CC The cohesin complex apparently forms a large proteinaceous ring within
CC which sister chromatids can be trapped (By similarity). At anaphase,
CC the scc-1 subunit of the complex is cleaved and dissociates from
CC chromatin, allowing sister chromatids to segregate (By similarity). The
CC cohesin complex may also play a role in spindle pole assembly during
CC mitosis (By similarity). Plays an essential role in cell division
CC during embryonic development (PubMed:12808038, PubMed:14560015,
CC PubMed:12827206, PubMed:16802858). Required for the assembly of the
CC synaptonemal complex between homologous chromosomes to promote sister
CC chromatid cohesion during mitosis and meiosis (PubMed:14499625,
CC PubMed:14560015). Has a role in stabilization of homologous chromosome
CC associations during meiotic synapsis (PubMed:12827206). Required for
CC chromosome segregation during mitosis and meiosis (PubMed:14499625,
CC PubMed:12808038, PubMed:14560015, PubMed:16802858). Plays a role in DNA
CC double-strand break (DSB) repair during meiotic recombination and
CC promotes the assembly of the 9-1-1 cell-cycle checkpoint response
CC complex which is required for inducing apoptosis in response to DNA
CC damage, at DNA damage sites (PubMed:21856158).
CC {ECO:0000250|UniProtKB:P40541, ECO:0000269|PubMed:12808038,
CC ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:14499625,
CC ECO:0000269|PubMed:14560015, ECO:0000269|PubMed:16802858,
CC ECO:0000269|PubMed:21856158}.
CC -!- SUBUNIT: Component of the cohesin complex, composed of the smc-1 and
CC smc-3 heterodimer attached via their hinge domain, scc-1 which links
CC them, and scc-3 (PubMed:12827206). Interacts with scc-1, smc-1 and tim-
CC 1 (PubMed:12827206). {ECO:0000269|PubMed:12827206}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750,
CC ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:14499625}. Chromosome
CC {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:14499625}. Note=Has
CC diffuse nuclear appearance at interphase during mitosis in somatic and
CC germline tissues (PubMed:12827206). Localizes to chromosomes at
CC pachytene during meiosis (PubMed:14499625).
CC {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:14499625}.
CC -!- TISSUE SPECIFICITY: Expressed in gonadal cells.
CC {ECO:0000269|PubMed:14499625}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryonic
CC lethality (PubMed:14560015, PubMed:12827206, PubMed:12808038,
CC PubMed:16802858). RNAi-mediated knockdown from early in larval
CC development results in sterile, uncoordinated (Unc), and protruding
CC vulva phenotypes, in abnormal embryonic cell nuclei morphology and in
CC defects in the mitotic and meiotic cells of gonads (PubMed:14499625,
CC PubMed:14560015). RNAi-mediated knockdown results in somatic gonad cell
CC division defects with a reduced number of pi uterine cells at the
CC early- to mid-L4 larval stage (PubMed:14560015). RNAi-mediated
CC knockdown results in chromosome segregation defects in early embryos
CC with lagging chromosomes at the anaphase phase of mitosis
CC (PubMed:14499625, PubMed:12808038, PubMed:16802858). RNAi-mediated
CC knockdown results in defective homologous alignment of chromosomes and
CC chromosome cohesion in meiosis (PubMed:14499625).
CC {ECO:0000269|PubMed:12808038, ECO:0000269|PubMed:12827206,
CC ECO:0000269|PubMed:14499625, ECO:0000269|PubMed:14560015,
CC ECO:0000269|PubMed:16802858}.
CC -!- SIMILARITY: Belongs to the SCC3 family. {ECO:0000305}.
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DR EMBL; BX284605; CAA99836.1; -; Genomic_DNA.
DR PIR; T21091; T21091.
DR RefSeq; NP_506193.1; NM_073792.3.
DR AlphaFoldDB; Q19555; -.
DR SMR; Q19555; -.
DR ComplexPortal; CPX-967; Nuclear mitotic cohesin complex.
DR DIP; DIP-26563N; -.
DR IntAct; Q19555; 2.
DR STRING; 6239.F18E2.3; -.
DR EPD; Q19555; -.
DR PaxDb; Q19555; -.
DR PeptideAtlas; Q19555; -.
DR EnsemblMetazoa; F18E2.3.1; F18E2.3.1; WBGene00004738.
DR GeneID; 179749; -.
DR KEGG; cel:CELE_F18E2.3; -.
DR UCSC; F18E2.3; c. elegans.
DR CTD; 179749; -.
DR WormBase; F18E2.3; CE05664; WBGene00004738; scc-3.
DR eggNOG; KOG2011; Eukaryota.
DR GeneTree; ENSGT00950000182972; -.
DR HOGENOM; CLU_005067_1_0_1; -.
DR InParanoid; Q19555; -.
DR OMA; ICDLLII; -.
DR OrthoDB; 167826at2759; -.
DR PhylomeDB; Q19555; -.
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:Q19555; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004738; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0008278; C:cohesin complex; IPI:WormBase.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISS:WormBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IMP:UniProtKB.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IDA:ComplexPortal.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IMP:WormBase.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:1905309; P:positive regulation of cohesin loading; IMP:UniProtKB.
DR GO; GO:2000001; P:regulation of DNA damage checkpoint; IMP:UniProtKB.
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; Coiled coil; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..1096
FT /note="Cohesin subunit scc-3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000432845"
FT DOMAIN 320..405
FT /note="SCD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00750"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1057..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 261..312
FT /evidence="ECO:0000255"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 800..1096
FT /note="Missing: In ku263; sterile. Vulval cell division
FT defects, resulting in asymmetric vulval invaginations at
FT the L4 larval stage. Gonad development defects, where the
FT gonad arms are shorter than in wild-type. Reduces the
FT number of oocytes in the proximal gonad arm. The
FT hermaphrodite gonad lacks a transition zone and pachytene
FT nuclei and oocytes have an abnormal morphology. Fewer
FT uterine cells, abnormal and small uteri and an endomitotic
FT oocyte phenotype (also called an Emo phenotype), in which
FT chromosomes have gone through endoreduplication without
FT cytokinesis and karyokinesis. Impairs assembly of the
FT synaptonemal complex between homologous chromosomes and
FT disrupts homologous chromosome pairing, sister chromatid
FT cohesion and localization of cohesin complex subunit rec-8
FT to chromosomes in the pachytene zone of the gonad.
FT Defective DNA double-strand break repair during meiosis
FT resulting in an accumulation of rad-51-positive
FT recombination intermediates in the mid and late pachytene
FT region of the germline. No increase in apoptosis in
FT response to the accumulation of recombination
FT intermediates, indicative of a defective DNA damage
FT response. Furthermore, hus-1, a component of the 9-1-1
FT cell-cycle checkpoint response complex which is required
FT for inducing apoptosis in response to DNA damage, does not
FT accumulate on the recombination intermediates."
FT /evidence="ECO:0000269|PubMed:14560015,
FT ECO:0000269|PubMed:21856158"
SQ SEQUENCE 1096 AA; 124775 MW; FC12008760DECD4A CRC64;
MSETPTDQSP QRMSTRNQAR VNYTDMAAGN NSVEKEPVFR SPTASTRGRK KRAANVDVAD
LSASFGNLNN FSTPPKRGRP RGGGLGSARG GRAPMVRRTT TEESAEVDDR ELVAAVKSGK
KITEAVDRWI GRYNEKFLVA IAEMHQFFFA ICGCKGIVTP QMSATLTYKD IICRMTEDFE
EDSADYPLVH GGSLKKVRAN LHNFIHTLII RTKASMLFDS NLMDGFVQLL TGMADSQVRA
FRHTATFCAM KITSALVDVT IELTQSKEKT SKQIEAEKAK LKNNSAGNEK YEALVAQRTQ
TEERAEEIRQ IIGYLFRSVF VHRYRDVVPD IRCICIQELG HWMDVYPEHF VEDSYLKYIG
WSMFDKVGDV RQRCIRALIP LFEKTLILDK LELFVNKFKD RLVSMLLDKD LETSIETVHL
MRVLYTVFPT LLTIKDVVPI YELIYASNRP LAVAAGMFLN TKVFRSAEKP GKAPTAANIP
LVKDLTTFFI EGDLHQHATY LVDALFESNP IVKDWATMGE LLINDQYQLD SNFETKLIEI
LTCSVVQSAT GEPPVGRHIV KKGAPSAKES RDLVEDRQRL TETLIPLIPR LITKFSSDNE
KIINLVNIPL HFQLETYLSA RMQTHLMELM EGLDSLIEKH LDEELLKAVA ELYYHLTTNS
SISALVEGHK MKLLDGVAAF IRKSMQQFDD DQMGEEEEAL FVSYIKRMAA FAGFMDLRHW
DLWDILLKVV SNYTREDTQR DVRERSMQML FMQLCFDSMN IKKEGETPKA DQVRKLKKRR
DQLIRIVTET LNEEACGVEQ AYLVICDLMI LFGSQLAEES KALEPLIWRP DAMVLGNLKI
FLDVNVFDVS NLDDMDQQEK IEVMHKMRQH VAQYAKLIIH GAMPVAEASH LIKRYQSHFQ
DFGDIFKNLL SKCREISFVE TGVMICETLK TLYSQLDEDQ GTDPLSESFN SIRDLAKRLG
PAFGVDYAKN RFAISSLHKK AIDFAFEEYD KENHQMPKNI FFLEIAIEFS GKLLAQDKMA
VVRYLNKIYT NRVGTSTVVW EPYRLYLGSL SDRNDDDNMS VRSGMTVTSN ATMRSTASST
RGRGRGRGRS RIADDF
