ID   AN32E_XENLA             Reviewed;         263 AA.
AC   Q7ZY40;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member E;
GN   Name=anp32e;
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 MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION.
RX   PubMed=8601433; DOI=10.1016/0014-5793(96)00010-5;
RA   Kurihara T., Hori M., Takeda H., Inoue M., Yoneda Y.;
RT   "Partial purification and characterization of a protein kinase that is
RT   activated by nuclear localization signal peptides.";
RL   FEBS Lett. 380:241-245(1996).
RN   [3]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15895553; DOI=10.1080/14734220410019020;
RA   Matilla A., Radrizzani M.;
RT   "The Anp32 family of proteins containing leucine-rich repeats.";
RL   Cerebellum 4:7-18(2005).
CC   -!- FUNCTION: Histone chaperone that specifically mediates the genome-wide
CC       removal of histone H2A.Z/H2AZ1 from the nucleosome: removes H2A.Z/H2AZ1
CC       from its normal sites of deposition, especially from enhancer and
CC       insulator regions. Not involved in deposition of H2A.Z/H2AZ1 in the
CC       nucleosome. May stabilize the evicted H2A.Z/H2AZ1-H2B dimer, thus
CC       shifting the equilibrium towards dissociation and the off-chromatin
CC       state. Inhibits activity of protein phosphatase 2A (PP2A). Does not
CC       inhibit protein phosphatase 1. May play a role in cerebellar
CC       development and synaptogenesis (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of a SWR1-like complex. Interacts with H2A.Z/H2AZ1
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The H2A.Z-interacting domain (ZID) mediates a direct
CC       interaction with H2A.Z/H2AZ1. {ECO:0000250}.
CC   -!- PTM: Phosphorylated. The phosphorylation is nuclear localization signal
CC       (NLS)-dependent. {ECO:0000269|PubMed:8601433}.
CC   -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
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DR   EMBL; BC043985; AAH43985.1; -; mRNA.
DR   RefSeq; NP_001080287.1; NM_001086818.1.
DR   AlphaFoldDB; Q7ZY40; -.
DR   SMR; Q7ZY40; -.
DR   MaxQB; Q7ZY40; -.
DR   DNASU; 379979; -.
DR   GeneID; 379979; -.
DR   KEGG; xla:379979; -.
DR   CTD; 379979; -.
DR   Xenbase; XB-GENE-991621; anp32e.L.
DR   OMA; MPNNQVS; -.
DR   OrthoDB; 1622194at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 379979; Expressed in gastrula and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR045081; AN32.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR11375; PTHR11375; 1.
DR   PROSITE; PS51450; LRR; 4.
PE   1: Evidence at protein level;
KW   Chaperone; Chromatin regulator; Cytoplasm; Leucine-rich repeat; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..263
FT                   /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT                   member E"
FT                   /id="PRO_0000240193"
FT   REPEAT          43..64
FT                   /note="LRR 1"
FT   REPEAT          65..84
FT                   /note="LRR 2"
FT   REPEAT          89..110
FT                   /note="LRR 3"
FT   DOMAIN          123..161
FT                   /note="LRRCT"
FT   REGION          146..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          202..263
FT                   /note="ZID domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        150..205
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..242
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   263 AA;  30108 MW;  36E6FED33B586002 CRC64;
     MEMKKRISLE LRNRSPAEVA ELVLDNCRSV DGEIEGLNDS YKELEFLSMA NVELKSLSKL
     PKLPKLRKLE LSDNSISGGL DVLTERCPNI TYLNLSGNKI KDLSTVEALA SLKNLKSLDL
     FNCEITNLED YRENIFQRLS QITYLDGFDQ EDNEAPDSEE DDDDDDYDDD EEPGPRRYEA
     EEDEEDEESA SDLGEEEEEE EEVGLSYLMK EEIRDEEDDD DYVEDGAEGE EEEEEDEEDE
     AAAADQGEKR KRDPEDEGDE DED