WAPL_CAEEL
ID WAPL_CAEEL Reviewed; 748 AA.
AC H2L0H5;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Wings apart-like protein homolog 1 {ECO:0000312|WormBase:R08C7.10b};
GN Name=wapl-1 {ECO:0000312|WormBase:R08C7.10b};
GN ORFNames=R08C7.10 {ECO:0000312|WormBase:R08C7.10b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18202360; DOI=10.1534/genetics.107.075275;
RA Stanvitch G., Moore L.L.;
RT "cin-4, a gene with homology to topoisomerase II, is required for
RT centromere resolution by cohesin removal from sister kinetochores during
RT mitosis.";
RL Genetics 178:83-97(2008).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=26841696; DOI=10.7554/elife.10851;
RA Crawley O., Barroso C., Testori S., Ferrandiz N., Silva N.,
RA Castellano-Pozo M., Jaso-Tamame A.L., Martinez-Perez E.;
RT "Cohesin-interacting protein WAPL-1 regulates meiotic chromosome structure
RT and cohesion by antagonizing specific cohesin complexes.";
RL Elife 5:E10851-E10851(2016).
CC -!- FUNCTION: Regulator of meiotic chromosome structure and function,
CC playing a role in sister chromatid cohesion, possibly via antagonizing
CC the coh-3/-4 association with axial elements in nuclei during late
CC prophase, cohesin association with chromatin, DNA double strand break
CC repair and polar body positioning following meiotic divisions during
CC oogenesis (PubMed:26841696). Regulates the morphogenesis and temporal
CC assembly of axial elements to control the organization of meiotic
CC chromosomes in pachytene nuclei and is also involved in meiotic
CC chromosomal remodeling in late pachytene nuclei (PubMed:26841696).
CC Required for the removal of the cohesin component scc-1 from mitotic
CC chromosomes (PubMed:18202360). {ECO:0000269|PubMed:18202360,
CC ECO:0000269|PubMed:26841696}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26841696}.
CC Note=Expressed in mitotic and meiotic nuclei, with low expression in
CC nuclei during the early meiotic prophase stages leptotene and zygotene,
CC and increased expression in late pachytene nuclei which then continues
CC to remain high in diplotene and diakinesis oocytes.
CC {ECO:0000269|PubMed:26841696}.
CC -!- DISRUPTION PHENOTYPE: Mutants have an egg-laying defect and reduced
CC brood size with 20.8% displaying embryonic lethality whilst 28.38%
CC arrest at the larval stage. Recombination intermediates accumulate in
CC mid pachytene nuclei resulting in delayed meiotic double stranded break
CC repair. Irregular polar body extrusion from the egg pronucleus and
CC localization following meiotic divisions which can lead to aneuploidy
CC in the embryo. Altered meiotic chromosomal organization due to shorter
CC axial elements in late pachytene nuclei. Defective chromatin remodeling
CC in late pachytene meiotic chromosomes characterized by increased
CC cohesin associated with diplotene chromosomes, but reduced association
CC in late diakinesis oocytes, changes in axial element composition
CC including absent axial element coiling, accumulation of cohesin and a
CC more linear appearance of axial elements, and altered disassembly of
CC the synaptonemal complex in diplotene and diakinesis oocytes
CC (PubMed:26841696). RNAi-mediated knockdown leads to aberrant
CC localization of the cohesin component scc-1 to mitotic metaphase
CC chromosomes (PubMed:18202360). {ECO:0000269|PubMed:18202360,
CC ECO:0000269|PubMed:26841696}.
CC -!- SIMILARITY: Belongs to the WAPL family. {ECO:0000305}.
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DR EMBL; BX284604; CCD73092.1; -; Genomic_DNA.
DR RefSeq; NP_500566.1; NM_068165.3.
DR AlphaFoldDB; H2L0H5; -.
DR SMR; H2L0H5; -.
DR STRING; 6239.R08C7.10b; -.
DR EPD; H2L0H5; -.
DR PaxDb; H2L0H5; -.
DR PeptideAtlas; H2L0H5; -.
DR EnsemblMetazoa; R08C7.10b.1; R08C7.10b.1; WBGene00019953.
DR GeneID; 177211; -.
DR CTD; 177211; -.
DR WormBase; R08C7.10b; CE28750; WBGene00019953; wapl-1.
DR eggNOG; KOG2152; Eukaryota.
DR HOGENOM; CLU_371419_0_0_1; -.
DR InParanoid; H2L0H5; -.
DR OMA; INVMMTS; -.
DR OrthoDB; 690399at2759; -.
DR PhylomeDB; H2L0H5; -.
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 PRO; PR:H2L0H5; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00019953; Expressed in germ line (C elegans) and 4 other tissues.
DR ExpressionAtlas; H2L0H5; baseline and differential.
DR GO; GO:0043073; C:germ cell nucleus; IDA:WormBase.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071923; P:negative regulation of cohesin loading; IMP:WormBase.
DR GO; GO:0045875; P:negative regulation of sister chromatid cohesion; ISS:WormBase.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IMP:WormBase.
DR GO; GO:0060623; P:regulation of chromosome condensation; IBA:GO_Central.
DR GO; GO:0071922; P:regulation of cohesin loading; ISS:WormBase.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR039874; WAPL.
DR InterPro; IPR022771; WAPL_C.
DR InterPro; IPR012502; WAPL_dom.
DR PANTHER; PTHR22100; PTHR22100; 1.
DR Pfam; PF07814; WAPL; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51271; WAPL; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; Meiosis; Nucleus; Reference proteome.
FT CHAIN 1..748
FT /note="Wings apart-like protein homolog 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436007"
FT DOMAIN 205..723
FT /note="WAPL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00603"
FT REGION 23..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..630
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 84332 MW; B24EDE5F8D90C4E9 CRC64;
MSSDANSDDP FSKPIVRKRF QATLAQQGIE DDQLPSVRSS DSPDVPDTPD VPVNQLSSPP
LSLPETLSEG NAETLQNLSD DSEPEMLSQS STSSLNRRME DSAIDPSRGT RKSQSRGFDY
DPAGERTTAP VQKKKKDEID MGGAKFFPKQ EKKHVYTHKW TTEEDDEDEK TISSSSNRYS
SRPNQPAVSA RPRQPVYATT STYSKPLASG YGSRVRHIKE ANELRESGEY DDFKQDLVYI
LSSLQSSDAS MKVKCLSAIS LAKKCVSPDF RQFIKSENMT KSIVKALMDS PEDDLFALAA
STVLYLLTRD FNSIKIDFPS LRLVSQLLRI EKFEQRPEDK DKVVNMVWEV FNSYIEKQEV
GGQKVSFDMR KESLTPSSLI IEALVFICSR SVNDDNLKSE LLNLGILQFV VAKIETNVNL
IADNADDTYS ILILNRCFRI LESSSVFHKK NQAFLISHRS NILISSLAKF LQVILDRVHQ
LAEEEVKKYI SCLALMCRLL INISHDNELC CSKLGQIEGF LPNAITTFTY LAPKFGKENS
YDINVMMTSL LTNLVERCNA NRKVLIAQTV KMVIPGHDVE EVPALEAITR LFVYHESQAQ
IVDADLDREL AFDEGGCGDE EEEEEGGDES SDEDGVRKDG RLDRNKMDRM DQVDVVHALQ
QVMNKASAHM EGSVIASYHA LLVGFVLQQN EDHLDEVRKH LPGKNFQNMI SQLKRLYDFT
KATMAKRVES NSGFRAIERV IEYLERLE
