SMCL1_CAEEL
ID SMCL1_CAEEL Reviewed; 537 AA.
AC Q18616;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Structural maintenance of chromosomes-like protein 1 {ECO:0000312|WormBase:C44C10.4};
GN Name=smcl-1 {ECO:0000303|PubMed:28301465, ECO:0000312|WormBase:C44C10.4};
GN ORFNames=C44C10.4 {ECO:0000312|WormBase:C44C10.4};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
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 DPY-27; MIX-1; DPY-28; DPY-26; CAPG-1 AND SMC-4,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28301465; DOI=10.1371/journal.pgen.1006614;
RA Chao L.F., Singh M., Thompson J., Yates J.R. III, Hagstrom K.A.;
RT "An SMC-like protein binds and regulates Caenorhabditis elegans
RT condensins.";
RL PLoS Genet. 13:E1006614-E1006614(2017).
CC -!- FUNCTION: Acts as a modulator of condensin function, possibly by
CC binding to the condensin SMC subunits and thereby inhibiting their
CC function. Negatively regulates the condensin I complex in mitotic
CC chromosome segregation. Negatively regulates the condensin I-like
CC dosage compensation complex, which functions in the regulation of X
CC chromosome-linked gene transcription, by limiting the association of
CC the complex with the X chromosomes. {ECO:0000269|PubMed:28301465}.
CC -!- SUBUNIT: Interacts with dpy-27, mix-1, dpy-28, dpy-26, capg-1 and smc-
CC 4. {ECO:0000269|PubMed:28301465}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28301465}.
CC -!- TISSUE SPECIFICITY: Expressed in the germline.
CC {ECO:0000269|PubMed:28301465}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development and in adult
CC animals. {ECO:0000269|PubMed:28301465}.
CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000305}.
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DR EMBL; BX284606; CAA93638.2; -; Genomic_DNA.
DR PIR; T19925; T19925.
DR RefSeq; NP_509956.2; NM_077555.4.
DR AlphaFoldDB; Q18616; -.
DR SMR; Q18616; -.
DR DIP; DIP-27235N; -.
DR STRING; 6239.C44C10.4; -.
DR EPD; Q18616; -.
DR PaxDb; Q18616; -.
DR PeptideAtlas; Q18616; -.
DR EnsemblMetazoa; C44C10.4.1; C44C10.4.1; WBGene00008085.
DR GeneID; 183453; -.
DR KEGG; cel:CELE_C44C10.4; -.
DR UCSC; C44C10.4; c. elegans.
DR CTD; 183453; -.
DR WormBase; C44C10.4; CE31442; WBGene00008085; smcl-1.
DR eggNOG; KOG0018; Eukaryota.
DR GeneTree; ENSGT00970000197297; -.
DR HOGENOM; CLU_507388_0_0_1; -.
DR InParanoid; Q18616; -.
DR OMA; EWFINER; -.
DR PhylomeDB; Q18616; -.
DR PRO; PR:Q18616; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00008085; Expressed in embryo and 4 other tissues.
DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007062; P:sister chromatid cohesion; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Mitosis; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..537
FT /note="Structural maintenance of chromosomes-like protein
FT 1"
FT /id="PRO_0000441025"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00499"
SQ SEQUENCE 537 AA; 62991 MW; F9C93CD011640F13 CRC64;
MTYPQQRLLT VDILNFKCYQ HHKSFGPFDH VTTFIGMNGC GKSIMIEAIA FVFGEDLPDP
KNPHNEHLFY DYNIRCVVSL KFEMPDGSTK RFTRIGLKTT YTYMIFNKYV TEEEYLLELG
KMNFRFAGQN ISVYNKTTLK VTRKSAEELG AFFDIVSNSI EFKPEYDELK AKLNFAESTV
LRWAKMIDSI ELEKEKFITL TLYKLYLCDK EIQETKEKFV AEQLKVNAKN AKMPLRISRY
SEAIPKQTPS PNFKNNAIVV RPKTHNHYDN LITVDKLNSY LNEKVTERRE LLQFAVNHPN
MNIRFSEEGP NIYAREIDYT ELPEYYKKES DDIIATSYKR SMLEKEIKKI RQCWLDENNI
KDDANIDNIN MRIKEATTKH TLALNIESEA RLNWEKLRVM RSARFNNFMA PLQTSLSRIY
AEIAQDEDSL AFLRPLDEEE PYLAIDAFVK ERHSEHISTR TFHGGSRMIV DLALIFAIHE
WKPSPLVVID DIDRNLYHEA SKKIEPYLSR QKQTQFIVTT KEDSYFTEVT KTITLEN
