WAPL_MOUSE
ID WAPL_MOUSE Reviewed; 1200 AA.
AC Q65Z40; B9EIG8; Q6ZQE9;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Wings apart-like protein homolog;
DE AltName: Full=Dioxin-inducible factor 2;
DE Short=DIF-2;
DE AltName: Full=WAPL cohesin release factor {ECO:0000312|MGI:MGI:2675859};
GN Name=Wapl {ECO:0000312|MGI:MGI:2675859}; Synonyms=Kiaa0261, Wapal;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=15620708; DOI=10.1016/j.febslet.2004.11.070;
RA Kuroda M., Oikawa K., Ohbayashi T., Yoshida K., Yamada K., Mimura J.,
RA Matsuda Y., Fujii-Kuriyama Y., Mukai K.;
RT "A dioxin sensitive gene, mammalian WAPL, is implicated in
RT spermatogenesis.";
RL FEBS Lett. 579:167-172(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP INTERACTION WITH THE COHESIN COMPLEX.
RX PubMed=17113138; DOI=10.1016/j.cell.2006.09.040;
RA Kueng S., Hegemann B., Peters B.H., Lipp J.J., Schleiffer A., Mechtler K.,
RA Peters J.M.;
RT "Wapl controls the dynamic association of cohesin with chromatin.";
RL Cell 127:955-967(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND SER-470, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-226; THR-286; SER-468
RP AND SER-470, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Regulator of sister chromatid cohesion in mitosis which
CC negatively regulates cohesin association with chromatin. Involved in
CC both sister chromatid cohesion during interphase and sister-chromatid
CC resolution during early stages of mitosis. Couples DNA replication to
CC sister chromatid cohesion. Cohesion ensures that chromosome
CC partitioning is accurate in both meiotic and mitotic cells and plays an
CC important role in DNA repair (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with the cohesin complex throughout the cell cycle;
CC interacts with both chromatin-bound and soluble pools of the complex.
CC Interacts with RAD21; the interaction is direct (By similarity).
CC Interacts with PDS5A; the interaction is direct, cohesin-dependent and
CC competitive with CDCA5/SORORIN (By similarity). Interacts (via FGF
CC motifs) with PDS5B; the interaction is direct (By similarity).
CC Interacts with a SMC1 protein (SMC1A or SMC1B) and SMC3 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Cytoplasm {ECO:0000250}. Note=Associates with chromatin through the
CC cohesin complex during interphase. Released in the cytoplasm from
CC nuclear envelope breakdown until anaphase, it reaccumulates in nucleus
CC at telophase (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Highly expressed in large pachytene spermatocytes
CC of testis. Down-regulated by dioxin in testis.
CC {ECO:0000269|PubMed:15620708}.
CC -!- SIMILARITY: Belongs to the WAPL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97915.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB167349; BAD44717.1; -; mRNA.
DR EMBL; AK129105; BAC97915.1; ALT_INIT; mRNA.
DR EMBL; BC139434; AAI39435.1; -; mRNA.
DR CCDS; CCDS36880.1; -.
DR RefSeq; NP_001004436.2; NM_001004436.4.
DR RefSeq; NP_001288259.1; NM_001301330.1.
DR AlphaFoldDB; Q65Z40; -.
DR SMR; Q65Z40; -.
DR BioGRID; 230082; 9.
DR IntAct; Q65Z40; 2.
DR MINT; Q65Z40; -.
DR STRING; 10090.ENSMUSP00000040232; -.
DR iPTMnet; Q65Z40; -.
DR PhosphoSitePlus; Q65Z40; -.
DR SwissPalm; Q65Z40; -.
DR EPD; Q65Z40; -.
DR jPOST; Q65Z40; -.
DR MaxQB; Q65Z40; -.
DR PaxDb; Q65Z40; -.
DR PRIDE; Q65Z40; -.
DR ProteomicsDB; 299961; -.
DR Antibodypedia; 30070; 173 antibodies from 30 providers.
DR DNASU; 218914; -.
DR Ensembl; ENSMUST00000048263; ENSMUSP00000040232; ENSMUSG00000041408.
DR Ensembl; ENSMUST00000169910; ENSMUSP00000130547; ENSMUSG00000041408.
DR GeneID; 218914; -.
DR KEGG; mmu:218914; -.
DR UCSC; uc007tbi.2; mouse.
DR CTD; 23063; -.
DR MGI; MGI:2675859; Wapl.
DR VEuPathDB; HostDB:ENSMUSG00000041408; -.
DR eggNOG; KOG2152; Eukaryota.
DR GeneTree; ENSGT00390000015768; -.
DR InParanoid; Q65Z40; -.
DR OMA; PPHRASY; -.
DR OrthoDB; 81845at2759; -.
DR PhylomeDB; Q65Z40; -.
DR TreeFam; TF323477; -.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2468052; Establishment of Sister Chromatid Cohesion.
DR Reactome; R-MMU-2470946; Cohesin Loading onto Chromatin.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR BioGRID-ORCS; 218914; 6 hits in 24 CRISPR screens.
DR ChiTaRS; Wapl; mouse.
DR PRO; PR:Q65Z40; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q65Z40; protein.
DR Bgee; ENSMUSG00000041408; Expressed in cleaving embryo and 227 other tissues.
DR ExpressionAtlas; Q65Z40; baseline and differential.
DR Genevisible; Q65Z40; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000278; P:mitotic cell cycle; IMP:MGI.
DR GO; GO:0035562; P:negative regulation of chromatin binding; ISS:UniProtKB.
DR GO; GO:0008156; P:negative regulation of DNA replication; ISS:UniProtKB.
DR GO; GO:0045875; P:negative regulation of sister chromatid cohesion; ISS:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0071168; P:protein localization to chromatin; ISS:UniProtKB.
DR GO; GO:0060623; P:regulation of chromosome condensation; IMP:MGI.
DR GO; GO:0051983; P:regulation of chromosome segregation; IMP:MGI.
DR GO; GO:0071922; P:regulation of cohesin loading; IMP:MGI.
DR GO; GO:0009636; P:response to toxic substance; IDA:MGI.
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 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Chromosome; Coiled coil; Cytoplasm;
KW Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1200
FT /note="Wings apart-like protein homolog"
FT /id="PRO_0000245233"
FT DOMAIN 635..1179
FT /note="WAPL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00603"
FT REGION 1..668
FT /note="Mediates interaction with the cohesin complex"
FT /evidence="ECO:0000250"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1061..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 266..293
FT /evidence="ECO:0000255"
FT COILED 751..791
FT /evidence="ECO:0000255"
FT MOTIF 73..75
FT /note="FGF motif 1"
FT MOTIF 437..439
FT /note="FGF motif 2"
FT MOTIF 462..464
FT /note="FGF motif 3"
FT COMPBIAS 53..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..521
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1083
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1095..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 168
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5K2"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5K2"
FT MOD_RES 286
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5K2"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5K2"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5K2"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z5K2"
FT CONFLICT 757
FT /note="L -> V (in Ref. 1; BAD44717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1200 AA; 134070 MW; 7697FA31AABBC573 CRC64;
MTSRFGKTYS RKGGNGSSKF DEVFSNKRTT LSTKWGETTF MAKLGQKRPN FKPDIQEIPK
KPKVEEEDTG DPFGFDSDDE SLPVSSKNLA QGKGSSYSES SEAAQLEEVT SVFEANSKCS
HVVGEDSFAS DRCLLVEDTL IGKEKSISRI PEDNANKSSC TKLLTSDKVE NFSEEHEKNS
HHFHKNAEDS TKKPNAETAV ASEYKADETK ETNDTWNSQS GKRTESPSES CPVKGSVRTG
LYEWDNDFED IRSEDCILSL DNESLLEMKD EDLKNRIGGL ENLNETFEED IIQSVLRPSN
CRTYCRANKA RSSQGASNFD KLMDGTSQSL AKANSESSKD GLNQAKKGSA SCGTSFRGTV
GRTRDYTVLH PSCLSVCNVT IQDTMERSMD EFTASTPADL GEAGRLRKKA DIATSKTTTR
FRPSNTKSKK DVKLEFFGFE DHDETGGDEG GSGSSNYKIK YFGFDDLSES EDDDDDDCQV
ERKKDKKRTK TAPSPSQQPP PESSDNSQDS QSSTNNAENL DFTEDLPGVP ESVKKPISKQ
GDKSKENTRK IFSGPKRSPT KAVYNARHWN HPDSEELPGP PIAKPQRVTV RLSSKEPNQK
DDGVFKAPAP PLKVIKTVTI PTQPYQEIVT ALKCRKEDKE LYTVVQHVKH FNDVVEFGEN
QEFTDDIEYL LSGLKSTQPL NTRCLSVISL ATKCAMPSFR MHLRAHGMVA MVFKTLDDSQ
HHQNLSLCTA ALMYILSRDR LNMDLDRASL DLMIRLLELE QDASSAKLLN EKDMNKIKEK
IRRLCETVHN KHLDLENITT GHLAMETLLS LTSKRAGDWF KEELRLLGGL DHIVDKVKEC
VDHLSRDDED EEKLVASLWG AERCLRVLES VTVHNPENQS YLIAYKDSQL IISSAKALQH
CEDLIQQYNR AENSICVADS NPLPYQNVTN HVGKAVEDCM RAIIGVLLNL TNDNEWGSTK
TGEQEGLIGT AMNCVLQVPK YLPQEQRFDI RVLGLGLLIN LVEYSARNRH CLVNMQTSCS
FDSSFSSGEG DHSLRLAGQV HAVQALVQLF LERERAAQLA ESKTDELIKD APTTQHDKSG
EWQETSGEIQ WVSTEKTDGA EEKQKKEEED EELDLNKALQ HAGKHMEDCI VASYTALLLG
CLCQESPINV TTVREYLPEG DFSIMTEMLK KFLSFMNLTC AVGTTGQKSI SRVIEYLEHC
