ID   AN32E_CHICK             Reviewed;         256 AA.
AC   Q5F4A3;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member E;
GN   Name=ANP32E; ORFNames=RCJMB04_1l3;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
RN   [2]
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   -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
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DR   EMBL; AJ851397; CAH65031.1; -; mRNA.
DR   RefSeq; NP_001006564.2; NM_001006564.2.
DR   AlphaFoldDB; Q5F4A3; -.
DR   SMR; Q5F4A3; -.
DR   STRING; 9031.ENSGALP00000021907; -.
DR   PaxDb; Q5F4A3; -.
DR   Ensembl; ENSGALT00000075671; ENSGALP00000049926; ENSGALG00000039891.
DR   GeneID; 426109; -.
DR   KEGG; gga:426109; -.
DR   CTD; 81611; -.
DR   VEuPathDB; HostDB:geneid_426109; -.
DR   eggNOG; KOG2739; Eukaryota.
DR   GeneTree; ENSGT00950000182907; -.
DR   InParanoid; Q5F4A3; -.
DR   OrthoDB; 1622194at2759; -.
DR   PRO; PR:Q5F4A3; -.
DR   Proteomes; UP000000539; Chromosome 25.
DR   Bgee; ENSGALG00000039891; Expressed in spleen and 13 other tissues.
DR   ExpressionAtlas; Q5F4A3; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR   GO; GO:0031410; C:cytoplasmic vesicle; ISS:AgBase.
DR   GO; GO:0005634; C:nucleus; ISS:AgBase.
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:0019212; F:phosphatase inhibitor activity; ISS:AgBase.
DR   GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR   GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Chaperone; Chromatin regulator; Cytoplasm; Leucine-rich repeat; Nucleus;
KW   Reference proteome; Repeat.
FT   CHAIN           1..256
FT                   /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT                   member E"
FT                   /id="PRO_0000280065"
FT   REPEAT          43..64
FT                   /note="LRR 1"
FT   REPEAT          65..87
FT                   /note="LRR 2"
FT   REPEAT          89..110
FT                   /note="LRR 3"
FT   DOMAIN          123..161
FT                   /note="LRRCT"
FT   REGION          147..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          204..256
FT                   /note="ZID domain"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        150..204
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..234
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..249
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   256 AA;  28926 MW;  50380963AB9C0F43 CRC64;
     MEMKKRINLE LRNQAPEEVT ELVLDNCKSS NGEIEGLNDS FKELEFLSMA NVQLTSLAKL
     PTLSKLRKLE LSDNIISGGL EVLAERCPNL TYLNLSGNKI KDLGTVEALQ NLKNLKSLDL
     FNCEITNLED YRDSIFDLLQ QITYLDGFDQ EDNEAPDSED DDDEGDEDDN DEDEDEAGPP
     GEYEEEDDED DGGSDLGEGE EEEEVGLSYL MKEEIQDEDD DDDYVEEGGD EEEEAEGIRG
     EKRKRDPEDE GEEEDD