SCC1_CAEEL
ID SCC1_CAEEL Reviewed; 645 AA.
AC Q19325;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Sister chromatid cohesion protein 1 {ECO:0000250|UniProtKB:Q12158};
GN Name=scc-1 {ECO:0000312|WormBase:F10G7.4};
GN Synonyms=coh-2 {ECO:0000312|WormBase:F10G7.4},
GN rad-21.1 {ECO:0000312|WormBase:F10G7.4};
GN ORFNames=F10G7.4 {ECO:0000312|WormBase:F10G7.4};
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, DEVELOPMENTAL STAGE, AND DISRUPTION
RP 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 IN THE COHESIN COMPLEX, INTERACTION WITH SCC-3;
RP SMC-1; SMC-3 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).
CC -!- FUNCTION: Cleavable component of the cohesin complex involved in
CC chromosome cohesion during cell cycle (PubMed:12827206,
CC PubMed:12808038). The cohesin complex is required for the cohesion of
CC sister chromatids after DNA replication (PubMed:12827206,
CC PubMed:12808038). The cohesin complex apparently forms a large
CC proteinaceous ring within which sister chromatids can be trapped (By
CC similarity). At metaphase-anaphase transition, this protein is cleaved
CC and dissociates from chromatin, allowing sister chromatids to segregate
CC (By similarity). {ECO:0000250|UniProtKB:Q12158,
CC ECO:0000269|PubMed:12808038, ECO:0000269|PubMed:12827206}.
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. Interacts with smc-1, smc-3, scc-3 and tim-1.
CC {ECO:0000269|PubMed:12827206}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12808038,
CC ECO:0000269|PubMed:12827206}. Chromosome {ECO:0000269|PubMed:12808038,
CC ECO:0000269|PubMed:12827206}. Cytoplasm {ECO:0000269|PubMed:12808038}.
CC Note=Shows cell-cycle dependent localization to chromosomes, with an
CC accumulation on chromosomes apparent during mitotic interphase and
CC telephase, but more diffuse nuclear expression during prometaphase,
CC metaphase and anaphase. {ECO:0000269|PubMed:12808038,
CC ECO:0000269|PubMed:12827206}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in actively dividing
CC cells, during all stages of development. {ECO:0000269|PubMed:12808038}.
CC -!- DISRUPTION PHENOTYPE: Postembryonic RNAi-mediated knock-down results in
CC either larval arrest, or adult sterility with a protruding vulva
CC phenotype (PubMed:12808038, PubMed:12827206). Worms have defective
CC chromosome segregation (PubMed:12808038). {ECO:0000269|PubMed:12808038,
CC ECO:0000269|PubMed:12827206}.
CC -!- SIMILARITY: Belongs to the rad21 family. {ECO:0000305}.
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DR EMBL; FO081114; CCD69206.1; -; Genomic_DNA.
DR PIR; G88130; G88130.
DR RefSeq; NP_494836.1; NM_062435.4.
DR AlphaFoldDB; Q19325; -.
DR SMR; Q19325; -.
DR ComplexPortal; CPX-967; Nuclear mitotic cohesin complex.
DR DIP; DIP-24317N; -.
DR IntAct; Q19325; 11.
DR MINT; Q19325; -.
DR STRING; 6239.F10G7.4; -.
DR EPD; Q19325; -.
DR PaxDb; Q19325; -.
DR PeptideAtlas; Q19325; -.
DR EnsemblMetazoa; F10G7.4.1; F10G7.4.1; WBGene00004737.
DR GeneID; 173808; -.
DR KEGG; cel:CELE_F10G7.4; -.
DR UCSC; F10G7.4; c. elegans.
DR CTD; 173808; -.
DR WormBase; F10G7.4; CE02628; WBGene00004737; scc-1.
DR eggNOG; KOG1213; Eukaryota.
DR GeneTree; ENSGT00940000154655; -.
DR HOGENOM; CLU_015775_1_1_1; -.
DR InParanoid; Q19325; -.
DR OMA; YCPVELE; -.
DR OrthoDB; 1253899at2759; -.
DR PhylomeDB; Q19325; -.
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:Q19325; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00004737; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0008278; C:cohesin complex; IPI:WormBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0034990; C:nuclear mitotic cohesin complex; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003684; F:damaged DNA binding; ISS:WormBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; IDA:ComplexPortal.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:WormBase.
DR GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IBA:GO_Central.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR GO; GO:0007130; P:synaptonemal complex assembly; TAS:WormBase.
DR Gene3D; 1.10.10.580; -; 1.
DR InterPro; IPR039781; Rad21/Rec8-like.
DR InterPro; IPR006909; Rad21/Rec8_C_eu.
DR InterPro; IPR006910; Rad21_Rec8_N.
DR InterPro; IPR023093; ScpA-like_C.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR12585; PTHR12585; 1.
DR Pfam; PF04824; Rad21_Rec8; 1.
DR Pfam; PF04825; Rad21_Rec8_N; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chromosome; Cytoplasm; Mitosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..645
FT /note="Sister chromatid cohesion protein 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000432843"
FT REGION 292..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 73409 MW; BFB2DAB771B8943B CRC64;
MFYAQFVLAK KGPLAKVWLA AHWEKKLTKA QIFETDVPQA IEEVIRPKVK MALRTVGHLL
LGIVRIYSKK TRYLLADTNE AYQKMKINFR NGFSFEVDIP ENAEIEEDFS NFIDKYNITV
PEFHDADYNE QLIMANVSRR EDITMKETVN FNVEFNIDAD FDGFGDEGES WQLDHLYGSV
EPLSLRPTPQ PESLMEVERD RDVAANGTEI SRIDADSVIF SEGPTRPNLI FDNQEGGNFM
PEMNLKVENQ TLENDGGVGP ADMFSSMIHP VREHAVADVQ NDDGMDFDYQ PFEPENVEPS
RPQSPESFAL EPLDVEHMEG RKKRQRKARK LIVDAETMIS NDAFREQQED FSDTMRVVEM
APPTRKMFNL CVSGDLQHLS REPGCKMFNR ELLQRYRRCL VTREFDLNYT MQELSDSSSF
TPSMEAQAEP WEDLNLNEDI QEDIQAQGPA VDEFFNDVRM DDDDDRQPAQ EMDFGDNFDF
PQEVEHQECA PIPIQSGFAG ENKENEDAED WSDPFGSSNS SRRGQLEAYG FGNTSTYKED
DGKWAKRAKH ILKKVSADIE TSGQADFSSV TATAKNRKQA AEQFYSLLTL AKSQAISVDQ
SEPYGEIVIR PGANFKEACP LSSPKPMGLG NTMENSTMRT PMRPV
