LAB1_CAEEL
ID LAB1_CAEEL Reviewed; 161 AA.
AC Q17604; Q17605;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Long arms of the bivalent protein 1 {ECO:0000312|WormBase:C03D6.6};
GN Name=lab-1 {ECO:0000303|PubMed:18923084, ECO:0000312|WormBase:C03D6.6};
GN ORFNames=C03D6.6 {ECO:0000312|WormBase:C03D6.6};
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=18923084; DOI=10.1101/gad.1691208;
RA de Carvalho C.E., Zaaijer S., Smolikov S., Gu Y., Schumacher J.M.,
RA Colaiacovo M.P.;
RT "LAB-1 antagonizes the Aurora B kinase in C. elegans.";
RL Genes Dev. 22:2869-2885(2008).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH GSP-1 AND GSP-2, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 73-VAL--TRP-75.
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).
RN [4] {ECO:0000305}
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29483514; DOI=10.1038/s41467-018-03229-5;
RA Ferrandiz N., Barroso C., Telecan O., Shao N., Kim H.M., Testori S.,
RA Faull P., Cutillas P., Snijders A.P., Colaiacovo M.P., Martinez-Perez E.;
RT "Spatiotemporal regulation of Aurora B recruitment ensures release of
RT cohesion during C. elegans oocyte meiosis.";
RL Nat. Commun. 9:834-834(2018).
RN [5]
RP ERRATUM OF PUBMED:29483514.
RX PubMed=30158624; DOI=10.1038/s41467-018-05848-4;
RA Ferrandiz N., Barroso C., Telecan O., Shao N., Kim H.M., Testori S.,
RA Faull P., Cutillas P., Snijders A.P., Colaiacovo M.P., Martinez-Perez E.;
RL Nat. Commun. 9:3558-3558(2018).
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=30921322; DOI=10.1371/journal.pgen.1008004;
RA Billmyre K.K., Doebley A.L., Spichal M., Heestand B., Belicard T.,
RA Sato-Carlton A., Flibotte S., Simon M., Gnazzo M., Skop A., Moerman D.,
RA Carlton P.M., Sarkies P., Ahmed S.;
RT "The meiotic phosphatase GSP-2/PP1 promotes germline immortality and small
RT RNA-mediated genome silencing.";
RL PLoS Genet. 15:E1008004-E1008004(2019).
CC -!- FUNCTION: Involved in sister chromatid cohesion during mitosis and
CC meiosis (PubMed:18923084, PubMed:22927794, PubMed:30921322). In
CC association with the gsp-2 phosphatase, it both restricts the
CC localization and antagonizes the function of the air-2 kinase during
CC meiosis I and mitosis to promote chromatid cohesion and spindle
CC attachment (PubMed:18923084, PubMed:22927794, PubMed:29483514,
CC PubMed:30921322). This in turn, drives germ cell immortality
CC (PubMed:30921322). Furthermore, may play a role in ensuring the timely
CC assembly of the synaptonemal complex during prophase I of meiosis
CC (PubMed:18923084, PubMed:22927794). {ECO:0000269|PubMed:18923084,
CC ECO:0000269|PubMed:22927794, ECO:0000269|PubMed:29483514,
CC ECO:0000269|PubMed:30921322}.
CC -!- SUBUNIT: Interacts with gsp-1 and gsp-2; the interaction is direct.
CC {ECO:0000269|PubMed:22927794}.
CC -!- INTERACTION:
CC Q17604; Q27497: gsp-1; NbExp=3; IntAct=EBI-16011794, EBI-2416859;
CC Q17604; P48727: gsp-2; NbExp=2; IntAct=EBI-16011794, EBI-2418500;
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:18923084,
CC ECO:0000269|PubMed:22927794, ECO:0000269|PubMed:29483514,
CC ECO:0000269|PubMed:30921322}. Nucleus {ECO:0000269|PubMed:30921322}.
CC Note=Recruited to chromosomes by smc-3 which is a component of the
CC cohesin complex, and the proteins htp-1, htp-2 and htp-3
CC (PubMed:22927794, PubMed:29483514). Localizes to chromosomes in the
CC mid-pachytene phase of prophase I to the end of meiosis I
CC (PubMed:18923084, PubMed:30921322). Localizes to the long arms of
CC chromosomes during diakinesis phase of prophase I of meiosis
CC (PubMed:18923084, PubMed:30921322). Does not localize to chromosomes in
CC meiosis II (PubMed:18923084). Localizes to chromosomes in prophase of
CC mitosis in the first embryonic division and subsequently from late
CC prophase to anaphase during early embryonic division (PubMed:18923084).
CC {ECO:0000269|PubMed:18923084, ECO:0000269|PubMed:22927794,
CC ECO:0000269|PubMed:29483514, ECO:0000269|PubMed:30921322}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 1- to 100-cell stage embryos.
CC {ECO:0000269|PubMed:18923084}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryonic
CC lethality in 57% of animals, and of the surviving progeny, there is a
CC 6% increase in the number of males (Him phenotype) (PubMed:18923084).
CC Defective sister chromatid cohesion during meiosis and mitosis
CC (PubMed:18923084, PubMed:22927794). Mis-localized air-2 in oocytes at
CC the diakinesis phase of prophase I in meiosis (PubMed:18923084,
CC PubMed:22927794). Impaired meiotic DNA double-strand break repair as
CC evidenced by increased rad-51 positive nuclei throughout late pachytene
CC to early diplotene in gonads, and impaired number of crossover
CC recombination events between chromatids (PubMed:22927794). Absent syp-
CC 1, a core component of the synaptonemal complex, at the pachytene stage
CC of meiosis (PubMed:22927794). Reduced expression of the gsp-2
CC phosphatase (PubMed:30921322). {ECO:0000269|PubMed:18923084,
CC ECO:0000269|PubMed:22927794, ECO:0000269|PubMed:30921322}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX284601; CAA99761.1; -; Genomic_DNA.
DR PIR; T18881; T18881.
DR RefSeq; NP_492566.1; NM_060165.4.
DR AlphaFoldDB; Q17604; -.
DR DIP; DIP-59875N; -.
DR IntAct; Q17604; 19.
DR STRING; 6239.C03D6.6; -.
DR PaxDb; Q17604; -.
DR EnsemblMetazoa; C03D6.6.1; C03D6.6.1; WBGene00007278.
DR GeneID; 182160; -.
DR KEGG; cel:CELE_C03D6.6; -.
DR UCSC; C03D6.6; c. elegans.
DR CTD; 182160; -.
DR WormBase; C03D6.6; CE15580; WBGene00007278; lab-1.
DR eggNOG; ENOG502TIER; Eukaryota.
DR HOGENOM; CLU_1612273_0_0_1; -.
DR InParanoid; Q17604; -.
DR OMA; ETMENCE; -.
DR OrthoDB; 1630530at2759; -.
DR PRO; PR:Q17604; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00007278; Expressed in germ line (C elegans) and 3 other tissues.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0008157; F:protein phosphatase 1 binding; IPI:WormBase.
DR GO; GO:0034089; P:establishment of meiotic sister chromatid cohesion; IMP:WormBase.
DR GO; GO:0034090; P:maintenance of meiotic sister chromatid cohesion; IMP:WormBase.
DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IMP:WormBase.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:WormBase.
PE 1: Evidence at protein level;
KW Chromosome; Nucleus; Reference proteome.
FT CHAIN 1..161
FT /note="Long arms of the bivalent protein 1"
FT /id="PRO_0000448965"
FT REGION 85..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 72..75
FT /note="PP1 binding motif"
FT /evidence="ECO:0000305|PubMed:22927794"
FT COMPBIAS 97..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 73..75
FT /note="VIW->AIA: Does not impair binding to gsp-1 and gsp-
FT 2."
FT /evidence="ECO:0000269|PubMed:22927794"
SQ SEQUENCE 161 AA; 18577 MW; F141C402011CE0B9 CRC64;
MVSHKKNDRP RPLWILKIHK RLSLFEFKRY ATGIGKDDGQ DISWVLKGNA KNNVYQVTVE
TMENCETDEC KKVIWVPDEL AESTGTMFED FKEDQPQESV SSISNNEANW GSSVNELDEN
YEKMQKEETF DPYDSDSDTS EDSDFDEDFE DSDKTMCSGQ S
