ID   PWP2A_XENLA             Reviewed;         784 AA.
AC   A0A1L8GR68;
DT   27-SEP-2017, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2017, sequence version 2.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=PWWP domain-containing protein 2A;
GN   Name=pwwp2a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA   Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA   Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA   Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA   Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA   Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA   Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA   Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA   Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA   Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA   Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28645917; DOI=10.15252/embj.201695757;
RA   Puenzeler S., Link S., Wagner G., Keilhauer E.C., Kronbeck N.,
RA   Spitzer R.M., Leidescher S., Markaki Y., Mentele E., Regnard C.,
RA   Schneider K., Takahashi D., Kusakabe M., Vardabasso C., Zink L.M.,
RA   Straub T., Bernstein E., Harata M., Leonhardt H., Mann M., Rupp R.A.,
RA   Hake S.B.;
RT   "Multivalent binding of PWWP2A to H2A.Z regulates mitosis and neural crest
RT   differentiation.";
RL   EMBO J. 36:2263-2279(2017).
CC   -!- FUNCTION: H2A.Z-specific chromatin binding protein which plays an
CC       important role in the neural crest cell differentiation and/or
CC       migration during early development and is essential for the development
CC       of the head and eye (PubMed:28645917). Acts as an adapter between
CC       distinct nucleosome components (H3K36me3 or H2A.Z) and chromatin-
CC       modifying complexes, contributing to the regulation of the levels of
CC       histone acetylation at actively transcribed genes (By similarity).
CC       {ECO:0000250|UniProtKB:Q96N64, ECO:0000269|PubMed:28645917}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96N64}.
CC   -!- DISRUPTION PHENOTYPE: Embryos exhibit lack of retinal tissue combined
CC       with a reduced head size. Defects in neural crest stem cell migration
CC       and differentiation seen. {ECO:0000269|PubMed:28645917}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=OCT86276.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CM004471; OCT86276.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A0A1L8GR68; -.
DR   SMR; A0A1L8GR68; -.
DR   STRING; 8355.A0A1L8GR68; -.
DR   Proteomes; UP000186698; Genome assembly.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR   GO; GO:0001654; P:eye development; IMP:UniProtKB.
DR   GO; GO:0060322; P:head development; IMP:UniProtKB.
DR   GO; GO:1901675; P:negative regulation of histone H3-K27 acetylation; ISS:UniProtKB.
DR   GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; ISS:UniProtKB.
DR   GO; GO:0014033; P:neural crest cell differentiation; IMP:UniProtKB.
DR   GO; GO:0001755; P:neural crest cell migration; IMP:UniProtKB.
DR   InterPro; IPR000313; PWWP_dom.
DR   Pfam; PF00855; PWWP; 1.
DR   SMART; SM00293; PWWP; 1.
DR   PROSITE; PS50812; PWWP; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..784
FT                   /note="PWWP domain-containing protein 2A"
FT                   /id="PRO_0000441729"
FT   DOMAIN          684..744
FT                   /note="PWWP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          468..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..655
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        476..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..522
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   784 AA;  87011 MW;  3169A6DB5865D28F CRC64;
     MAAVAAAPGP GEAGESEQDS KTTPGEWRLG ELQCEPIVAV LDSERQSLIR CEMDSDTLEK
     AGPVVEQLGG SGTDQVYGID KNSDFESVSV MDYKPPYRGI NQERIAGENK KARHEQLPRH
     TFLQKEPTPM ILSEVRDSGV HTEMCLEEAT LSSNNDGSET SLNDPDCDIG SMGTSEGSVV
     TSGIGSLIPG SEVQVTLDHI IQDALVVSFC HGNRIFSGVL MDLSKRFGPH GIPVTVHPRR
     EYKNKPVESI QEESKSFHEE TLLKSEENVT PPEDVTPIQQ SESCEIQNLW TTKPPPLFHE
     GAPYPPPLFI RDTYNQSIPQ PPPRKIKRPK KKIYREEPTS IINAIKLRPR QVLCDKCKNN
     VVADKKEIRK VATDSYKTEE GKRRRHETIT TVNKKLKTDH KVNGKGQHES QKRAGVTKVP
     NLAHGRGKVV KVPSQTSAAK TQLHTKKVLQ NKNMDHVKAR EVLKMAKEKA QKKQKVTTSS
     KNAHSKVHFT RRLQNSNSGT LPPRLRIKPQ RYRNEENDSS LKPGLETLRS SKMGIKPQTR
     YSATRSAGEA PSEIQSPSNG PEEVSSEIQD TNVCVPPEEQ DLQQTLGKRG SKSNITVYMA
     INQKKANSSS ASVCSSDSTD DMKSSHSECS STENFDFPPG SMHTPSSSSA SSKEEKKLSN
     SLKIKMFSKN VSKCVTPDGR TICVGDIVWA KIYGFPWWPA RILAITISRK DNGLLIRQEA
     RISWFGSPTT SFLALSQLAP FLENFQSRFN KKRKGLYRKA ITEAAKAAKQ LTPEVRALLT
     QFET