AN32E_RAT
ID AN32E_RAT Reviewed; 258 AA.
AC Q5XIE0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member E;
GN Name=Anp32e;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [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, composed of EP400,
CC KAT5/TIP60, TRRAP, BRD8, RUVBL1, RUVBL2, ING3 and ANP32E; the complex
CC does not contain SRCAP. Interacts with H2A.Z/H2AZ1. Interacts with the
CC importin alpha KPNA1 and KPNA2 (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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
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DR EMBL; BC083744; AAH83744.1; -; mRNA.
DR RefSeq; NP_001013218.1; NM_001013200.1.
DR AlphaFoldDB; Q5XIE0; -.
DR SMR; Q5XIE0; -.
DR BioGRID; 263117; 3.
DR STRING; 10116.ENSRNOP00000028744; -.
DR iPTMnet; Q5XIE0; -.
DR PhosphoSitePlus; Q5XIE0; -.
DR jPOST; Q5XIE0; -.
DR PaxDb; Q5XIE0; -.
DR PRIDE; Q5XIE0; -.
DR Ensembl; ENSRNOT00000028744; ENSRNOP00000028744; ENSRNOG00000021168.
DR GeneID; 361999; -.
DR KEGG; rno:361999; -.
DR UCSC; RGD:1310611; rat.
DR CTD; 81611; -.
DR RGD; 1310611; Anp32e.
DR eggNOG; KOG2739; Eukaryota.
DR GeneTree; ENSGT00950000182907; -.
DR HOGENOM; CLU_063314_1_1_1; -.
DR InParanoid; Q5XIE0; -.
DR OMA; MPNNQVS; -.
DR OrthoDB; 1622194at2759; -.
DR PRO; PR:Q5XIE0; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000021168; Expressed in thymus and 20 other tissues.
DR Genevisible; Q5XIE0; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0043486; P:histone exchange; ISO:RGD.
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 Acetylation; Chaperone; Chromatin regulator; Cytoplasm; Isopeptide bond;
KW Leucine-rich repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..258
FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT member E"
FT /id="PRO_0000236251"
FT REPEAT 18..38
FT /note="LRR 1"
FT REPEAT 43..64
FT /note="LRR 2"
FT REPEAT 65..87
FT /note="LRR 3"
FT REPEAT 89..110
FT /note="LRR 4"
FT DOMAIN 123..161
FT /note="LRRCT"
FT REGION 149..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..258
FT /note="ZID domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 150..201
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTT0"
FT CROSSLNK 68
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BTT0"
SQ SEQUENCE 258 AA; 29418 MW; 2312700EA7157B37 CRC64;
MEMKKKINME LKNRAPEEVT ELVLDNCLCV NGEIEGLNDT FKELEFLSMA NVELSSLARL
PSLNKLRKLE LSDNIISGGL EVLAEKCPNL TYLNLSGNKI KDLSTVEALQ NLKNLKSLDL
FNCEITNLED YRESIFELLQ QITYLDGFDQ EDNEAPDSEE EEEDEDGDED EEDEEEDEAG
PPEGYEDEDE DEDEAGSEVG EGEEEVGLSY LMKEEIQDEE DDDDYVDEGE EEEEEEEEGP
RGEKRKRDAE DDGEEDDD
