AN32E_DANRE
ID AN32E_DANRE Reviewed; 250 AA.
AC Q6NUW5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member E;
GN Name=anp32e; ORFNames=zgc:65995, zgc:85827;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Embryo, and Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
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).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18307296; DOI=10.1021/pr700667w;
RA Lemeer S., Pinkse M.W.H., Mohammed S., van Breukelen B., den Hertog J.,
RA Slijper M., Heck A.J.R.;
RT "Online automated in vivo zebrafish phosphoproteomics: from large-scale
RT analysis down to a single embryo.";
RL J. Proteome Res. 7:1555-1564(2008).
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
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DR EMBL; BC056543; AAH56543.1; -; mRNA.
DR EMBL; BC068403; AAH68403.1; -; mRNA.
DR EMBL; BC098881; AAH98881.1; -; mRNA.
DR RefSeq; NP_998442.1; NM_213277.1.
DR AlphaFoldDB; Q6NUW5; -.
DR SMR; Q6NUW5; -.
DR STRING; 7955.ENSDARP00000071527; -.
DR iPTMnet; Q6NUW5; -.
DR PaxDb; Q6NUW5; -.
DR PRIDE; Q6NUW5; -.
DR Ensembl; ENSDART00000077059; ENSDARP00000071527; ENSDARG00000054804.
DR GeneID; 406562; -.
DR KEGG; dre:406562; -.
DR CTD; 81611; -.
DR ZFIN; ZDB-GENE-040426-2448; anp32e.
DR eggNOG; KOG2739; Eukaryota.
DR GeneTree; ENSGT00950000182907; -.
DR HOGENOM; CLU_063314_1_1_1; -.
DR InParanoid; Q6NUW5; -.
DR OMA; MPNNQVS; -.
DR OrthoDB; 1622194at2759; -.
DR PhylomeDB; Q6NUW5; -.
DR TreeFam; TF317206; -.
DR PRO; PR:Q6NUW5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000054804; Expressed in gastrula and 26 other tissues.
DR ExpressionAtlas; Q6NUW5; baseline.
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:0019212; F:phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
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 InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR PANTHER; PTHR11375; PTHR11375; 1.
DR SMART; SM00446; LRRcap; 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..250
FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT member E"
FT /id="PRO_0000240192"
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 149..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..247
FT /note="ZID domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 150..192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18307296"
SQ SEQUENCE 250 AA; 28135 MW; F5A4582115198A5A CRC64;
MEMKKRISLE LRNRTPAEVA ELVVDNCRSS DGEIEGLTDD FKELEFLSMV NVGLTSLAKL
PSLPKLRKLE LSDNNISGTL ETLAEKCANL TYLNLSGNKI KELSTLEALQ NLKNLKSLDL
FNCEITTLED YRESIFELLP QVTYLDGFDA EDNEAPDSEA DDDDDDEDGD EGAGQLGEYE
EEEEEDEEGS EGGEVGLSYL MKEDIQDEED DDDYVEEEEE EGGEEEADVR GEKRKREAED
EGEDDDEDDD
