AN32A_MOUSE
ID AN32A_MOUSE Reviewed; 247 AA.
AC O35381; P97437;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member A;
DE AltName: Full=Acidic nuclear phosphoprotein pp32;
DE AltName: Full=Leucine-rich acidic nuclear protein;
DE Short=LANP;
DE AltName: Full=Potent heat-stable protein phosphatase 2A inhibitor I1PP2A;
GN Name=Anp32a; Synonyms=Anp32, Lanp;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8970164; DOI=10.1091/mbc.7.12.2045;
RA Chen T.-H., Brody J.R., Romantsev F.E., Yu J.-G., Kayler A.E., Voneiff E.,
RA Kuhajda F.P., Pasternack G.R.;
RT "Structure of pp32, an acidic nuclear protein which inhibits oncogene-
RT induced formation of transformed foci.";
RL Mol. Biol. Cell 7:2045-2056(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH SCA1.
RC TISSUE=Cerebellum;
RX PubMed=9353121; DOI=10.1038/40159;
RA Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T., Zoghbi H.Y.;
RT "The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-
RT 1.";
RL Nature 389:974-978(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MAP1B.
RX PubMed=12807913; DOI=10.1074/jbc.m302785200;
RA Opal P., Garcia J.J., Propst F., Matilla A., Orr H.T., Zoghbi H.Y.;
RT "Mapmodulin/leucine-rich acidic nuclear protein binds the light chain of
RT microtubule-associated protein 1B and modulates neuritogenesis.";
RL J. Biol. Chem. 278:34691-34699(2003).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=15060138; DOI=10.1128/mcb.24.8.3140-3149.2004;
RA Opal P., Garcia J.J., McCall A.E., Xu B., Weeber E.J., Sweatt J.D.,
RA Orr H.T., Zoghbi H.Y.;
RT "Generation and characterization of LANP/pp32 null mice.";
RL Mol. Cell. Biol. 24:3140-3149(2004).
RN [6]
RP GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
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 [7]
RP FUNCTION, AND INTERACTION WITH E4F1.
RX PubMed=17557114; DOI=10.1038/sj.embor.7400983;
RA Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y.,
RA Opal P.;
RT "The role of LANP and ataxin 1 in E4F-mediated transcriptional
RT repression.";
RL EMBO Rep. 8:671-677(2007).
RN [8]
RP GLYCYLATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29467488; DOI=10.1038/s41375-018-0010-7;
RA Yang X., Lu B., Sun X., Han C., Fu C., Xu K., Wang M., Li D., Chen Z.,
RA Opal P., Wen Q., Crispino J.D., Wang Q.F., Huang Z.;
RT "ANP32A regulates histone H3 acetylation and promotes leukemogenesis.";
RL Leukemia 32:1587-1597(2018).
CC -!- FUNCTION: Multifunctional protein that is involved in the regulation of
CC many processes including tumor suppression, apoptosis, cell cycle
CC progression or transcription. Promotes apoptosis by favouring the
CC activation of caspase-9/CASP9 and allowing apoptosome formation. In
CC addition, plays a role in the modulation of histone acetylation and
CC transcription as part of the INHAT (inhibitor of histone
CC acetyltransferases) complex. Inhibits the histone-acetyltranferase
CC activity of EP300/CREBBP (CREB-binding protein) and EP300/CREBBP-
CC associated factor by histone masking. Preferentially binds to
CC unmodified histone H3 and sterically inhibiting its acetylation and
CC phosphorylation leading to cell growth inhibition (PubMed:29467488).
CC Participates in other biochemical processes such as regulation of mRNA
CC nuclear-to-cytoplasmic translocation and stability by its association
CC with ELAVL1 (Hu-antigen R). Plays a role in E4F1-mediated
CC transcriptional repression as well as inhibition of protein phosphatase
CC 2A (By similarity) (PubMed:17557114, PubMed:29467488).
CC {ECO:0000250|UniProtKB:P39687, ECO:0000269|PubMed:17557114,
CC ECO:0000269|PubMed:29467488}.
CC -!- SUBUNIT: Component of the SET complex, composed of at least ANP32A,
CC APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with SET.
CC Interacts with ATXN1/SCA1. Interacts with MAP1B. Interacts with ELAVL1.
CC Part of the INHAT (inhibitor of histone acetyltransferases) complex.
CC Interacts with E4F1. {ECO:0000269|PubMed:12807913,
CC ECO:0000269|PubMed:17557114, ECO:0000269|PubMed:9353121}.
CC -!- INTERACTION:
CC O35381; Q8CCE9: E4f1; NbExp=2; IntAct=EBI-643140, EBI-7450874;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12807913}. Cytoplasm
CC {ECO:0000269|PubMed:12807913}. Endoplasmic reticulum {ECO:0000250}.
CC Note=Shuttles between nucleus and cytoplasm. Translocates to the
CC cytoplasm during the process of neuritogenesis.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the cerebellum.
CC Expressed also in cortex, lung, skeletal muscle, gastrointestinal
CC tract, spleen, liver and heart. {ECO:0000269|PubMed:15895553}.
CC -!- PTM: Phosphorylated on serine residues, at least in part by casein
CC kinase 2/CK2. {ECO:0000250|UniProtKB:P39687}.
CC -!- PTM: Some glutamate residues are glycylated by TTLL8. This modification
CC occurs exclusively on glutamate residues and results in a glycine chain
CC on the gamma-carboxyl group.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile. They have no
CC derangements in any of the major organ systems, including the nervous
CC systems. Moreover, bone marrow cells from mutant mice only show mild
CC decrease of colony-forming unit(CFU)-myeloid.
CC {ECO:0000269|PubMed:15060138, ECO:0000269|PubMed:29467488}.
CC -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U73478; AAB39707.1; -; mRNA.
DR EMBL; AF022957; AAB91546.1; -; mRNA.
DR EMBL; BC062899; AAH62899.1; -; mRNA.
DR CCDS; CCDS40663.1; -.
DR RefSeq; NP_033802.2; NM_009672.3.
DR PDB; 2JQD; NMR; -; A=1-164.
DR PDBsum; 2JQD; -.
DR AlphaFoldDB; O35381; -.
DR BMRB; O35381; -.
DR SMR; O35381; -.
DR BioGRID; 198104; 10.
DR IntAct; O35381; 11.
DR MINT; O35381; -.
DR STRING; 10090.ENSMUSP00000082652; -.
DR iPTMnet; O35381; -.
DR PhosphoSitePlus; O35381; -.
DR SwissPalm; O35381; -.
DR REPRODUCTION-2DPAGE; IPI00314736; -.
DR CPTAC; non-CPTAC-3633; -.
DR EPD; O35381; -.
DR jPOST; O35381; -.
DR MaxQB; O35381; -.
DR PaxDb; O35381; -.
DR PeptideAtlas; O35381; -.
DR PRIDE; O35381; -.
DR ProteomicsDB; 281978; -.
DR DNASU; 11737; -.
DR Ensembl; ENSMUST00000085519; ENSMUSP00000082652; ENSMUSG00000032249.
DR GeneID; 11737; -.
DR KEGG; mmu:11737; -.
DR UCSC; uc009qah.3; mouse.
DR CTD; 8125; -.
DR MGI; MGI:108447; Anp32a.
DR VEuPathDB; HostDB:ENSMUSG00000032249; -.
DR eggNOG; KOG2739; Eukaryota.
DR GeneTree; ENSGT00950000182907; -.
DR HOGENOM; CLU_063314_1_1_1; -.
DR InParanoid; O35381; -.
DR OMA; DKRSAFC; -.
DR OrthoDB; 1622194at2759; -.
DR PhylomeDB; O35381; -.
DR TreeFam; TF317206; -.
DR Reactome; R-MMU-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR BioGRID-ORCS; 11737; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Anp32a; mouse.
DR EvolutionaryTrace; O35381; -.
DR PRO; PR:O35381; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O35381; protein.
DR Bgee; ENSMUSG00000032249; Expressed in retinal neural layer and 275 other tissues.
DR ExpressionAtlas; O35381; baseline and differential.
DR Genevisible; O35381; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IPI:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006913; P:nucleocytoplasmic transport; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Endoplasmic reticulum; Leucine-rich repeat;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..247
FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT member A"
FT /id="PRO_0000137593"
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 150..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..172
FT /note="Necessary for tumor-suppressive function"
FT /evidence="ECO:0000250"
FT REGION 165..247
FT /note="Interaction with E4F1"
FT /evidence="ECO:0000269|PubMed:17557114"
FT COMPBIAS 160..228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P39687"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39687"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39687"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39687"
FT CONFLICT 191
FT /note="D -> V (in Ref. 1; AAB39707)"
FT /evidence="ECO:0000305"
FT HELIX 3..11
FT /evidence="ECO:0007829|PDB:2JQD"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:2JQD"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:2JQD"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:2JQD"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:2JQD"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:2JQD"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2JQD"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:2JQD"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:2JQD"
FT TURN 103..106
FT /evidence="ECO:0007829|PDB:2JQD"
FT HELIX 107..111
FT /evidence="ECO:0007829|PDB:2JQD"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2JQD"
FT HELIX 124..127
FT /evidence="ECO:0007829|PDB:2JQD"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:2JQD"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2JQD"
SQ SEQUENCE 247 AA; 28538 MW; 82EEDCF72ECC2918 CRC64;
MEMDKRIYLE LRNRTPSDVK ELVLDNCKSI EGKIEGLTDE FEELEFLSTI NVGLTSISNL
PKLNKLKKLE LSENRISGDL EVLAEKCPNL KHLNLSGNKI KDLSTIEPLK KLENLKSLDL
FNCEVTNLNA YRENVFKLLP QVMYLDGYDR DNKEAPDSDV EGYVEDDDEE DEDEEEYDEY
AQLVEDEEEE DEEEEGEEED VSGEEEEDEE GYNDGEVDDE EDEEEAGEEE GSQKRKREPD
DEGEEDD
