ID AN32E_MOUSE Reviewed; 260 AA.
AC P97822; E9Q5H9; Q3TH89; Q3TX26; Q8BPF8; Q8C2L4; Q8C7Q8; Q9CZD2;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 178.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member E;
DE AltName: Full=Cerebellar postnatal development protein 1;
DE AltName: Full=LANP-like protein;
DE Short=LANP-L;
GN Name=Anp32e; Synonyms=Cpd1;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=11430900; DOI=10.1016/s0006-8993(01)02351-4;
RA Radrizzani M., Vila-Ortiz G., Cafferata E.G.A., Di Tella M.C.,
RA Gonzalez-Guerrico A., Perandones C., Pivetta O.H., Carminatti H.,
RA Idoyaga Vargas V.P., Santa-Coloma T.A.;
RT "Differential expression of CPD1 during postnatal development in the mouse
RT cerebellum.";
RL Brain Res. 907:162-174(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH KPNA1 AND
RP KPNA2.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10692581; DOI=10.1016/s0014-5793(00)01218-7;
RA Matsubae M., Kurihara T., Tachibana T., Imamoto N., Yoneda Y.;
RT "Characterization of the nuclear transport of a novel leucine-rich acidic
RT nuclear protein-like protein.";
RL FEBS Lett. 468:171-175(2000).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Kidney, Spinal cord, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Mammary gland;
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 [6]
RP FUNCTION.
RX PubMed=14964690; DOI=10.1080/14734220310017212;
RA Santa-Coloma T.A.;
RT "Anp32e (Cpd1) and related protein phosphatase 2 inhibitors.";
RL Cerebellum 2:310-320(2003).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16420440; DOI=10.1111/j.1460-9568.2005.04555.x;
RA Costanzo R.V., Vila-Ortiz G.J., Perandones C., Carminatti H., Matilla A.,
RA Radrizzani M.;
RT "Anp32e/Cpd1 regulates protein phosphatase 2A activity at synapses during
RT synaptogenesis.";
RL Eur. J. Neurosci. 23:309-324(2006).
RN [8]
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 [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 DISRUPTION PHENOTYPE.
RX PubMed=20844742; DOI=10.1371/journal.pone.0012649;
RA Kular R.K., Gogliotti R.G., Opal P.;
RT "Cpd-1 null mice display a subtle neurological phenotype.";
RL PLoS ONE 5:0-0(2010).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=21049064; DOI=10.1371/journal.pone.0013597;
RA Reilly P.T., Afzal S., Wakeham A., Haight J., You-Ten A., Zaugg K.,
RA Dembowy J., Young A., Mak T.W.;
RT "Generation and characterization of the Anp32e-deficient mouse.";
RL PLoS ONE 5:E13597-E13597(2010).
RN [12]
RP DISRUPTION PHENOTYPE.
RX PubMed=23675506; DOI=10.1371/journal.pone.0063815;
RA Wong P., Leo V.I., Low M., Mak T.W., Zhang X., Reilly P.T.;
RT "Targeted ANP32E mutant mice do not demonstrate obvious movement defects.";
RL PLoS ONE 8:E63815-E63815(2013).
RN [13]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=24463511; DOI=10.1038/nature12922;
RA Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M.,
RA Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C.,
RA Hamiche A.;
RT "ANP32E is a histone chaperone that removes H2A.Z from chromatin.";
RL Nature 505:648-653(2014).
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 (PubMed:24463511). Inhibits activity of protein phosphatase 2A
CC (PP2A). Does not inhibit protein phosphatase 1. May play a role in
CC cerebellar development and synaptogenesis.
CC {ECO:0000269|PubMed:11430900, ECO:0000269|PubMed:14964690,
CC ECO:0000269|PubMed:16420440, ECO:0000269|PubMed:24463511}.
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 (By similarity).
CC Interacts with the importin alpha KPNA1 and KPNA2. {ECO:0000250,
CC ECO:0000269|PubMed:10692581}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P97822-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97822-2; Sequence=VSP_007373;
CC Name=3;
CC IsoId=P97822-3; Sequence=VSP_059599;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in cerebellum and
CC spleen. In the cerebellum, expressed mainly in granule cells and, to a
CC lesser extent, in Purkinje cells. {ECO:0000269|PubMed:11430900}.
CC -!- DEVELOPMENTAL STAGE: Low levels are found at postnatal day 4. Levels
CC increase from postnatal day 7 to postnatal day 17. Levels decrease and
CC remain low in the adult. {ECO:0000269|PubMed:11430900}.
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 -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are viable and fertile
CC (PubMed:20844742, PubMed:21049064, PubMed:23675506). They display a
CC subtle neurological clasping phenotype and mild motor deficits
CC (PubMed:20844742). Motor defects were not confirmed by a subsequent
CC analysis (PubMed:23675506). Deletion in embryonic fibroblasts results
CC in the appearance of a significant number of new H2A.Z/H2AZ1 around the
CC transcription start site as well as at other chromatin regions
CC (PubMed:24463511). {ECO:0000269|PubMed:20844742,
CC ECO:0000269|PubMed:21049064, ECO:0000269|PubMed:23675506,
CC ECO:0000269|PubMed:24463511}.
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; U89345; AAB49462.2; -; mRNA.
DR EMBL; AB037685; BAB03507.1; -; mRNA.
DR EMBL; AC092855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK012759; BAB28449.1; -; mRNA.
DR EMBL; AK049647; BAC33858.1; -; mRNA.
DR EMBL; AK076049; BAC36147.1; -; mRNA.
DR EMBL; AK088401; BAC40331.1; -; mRNA.
DR EMBL; AK147888; BAE28205.1; -; mRNA.
DR EMBL; AK159446; BAE35090.1; -; mRNA.
DR EMBL; AK168380; BAE40309.1; -; mRNA.
DR EMBL; BC005690; AAH05690.1; -; mRNA.
DR EMBL; BC080684; AAH80684.1; -; mRNA.
DR CCDS; CCDS17626.1; -. [P97822-1]
DR CCDS; CCDS57238.1; -. [P97822-2]
DR CCDS; CCDS57239.1; -. [P97822-3]
DR RefSeq; NP_001240686.1; NM_001253757.1. [P97822-2]
DR RefSeq; NP_001240687.1; NM_001253758.1. [P97822-3]
DR RefSeq; NP_075699.3; NM_023210.4. [P97822-1]
DR AlphaFoldDB; P97822; -.
DR SMR; P97822; -.
DR BioGRID; 211498; 3.
DR IntAct; P97822; 3.
DR STRING; 10090.ENSMUSP00000128483; -.
DR iPTMnet; P97822; -.
DR PhosphoSitePlus; P97822; -.
DR SwissPalm; P97822; -.
DR EPD; P97822; -.
DR jPOST; P97822; -.
DR MaxQB; P97822; -.
DR PaxDb; 10090-ENSMUSP00000128483; -.
DR PeptideAtlas; P97822; -.
DR ProteomicsDB; 282093; -. [P97822-1]
DR ProteomicsDB; 282094; -. [P97822-2]
DR ProteomicsDB; 357028; -.
DR Pumba; P97822; -.
DR Antibodypedia; 20276; 153 antibodies from 30 providers.
DR DNASU; 66471; -.
DR Ensembl; ENSMUST00000015893.13; ENSMUSP00000015893.7; ENSMUSG00000015749.13. [P97822-2]
DR Ensembl; ENSMUST00000165307.8; ENSMUSP00000128483.2; ENSMUSG00000015749.13. [P97822-1]
DR Ensembl; ENSMUST00000171368.8; ENSMUSP00000130599.2; ENSMUSG00000015749.13. [P97822-3]
DR GeneID; 66471; -.
DR KEGG; mmu:66471; -.
DR UCSC; uc008qlu.2; mouse. [P97822-1]
DR UCSC; uc008qlv.2; mouse. [P97822-2]
DR AGR; MGI:1913721; -.
DR CTD; 81611; -.
DR MGI; MGI:1913721; Anp32e.
DR VEuPathDB; HostDB:ENSMUSG00000015749; -.
DR eggNOG; KOG2739; Eukaryota.
DR GeneTree; ENSGT00950000182907; -.
DR InParanoid; P97822; -.
DR OMA; MPNNQVS; -.
DR OrthoDB; 1386993at2759; -.
DR PhylomeDB; P97822; -.
DR TreeFam; TF317206; -.
DR BioGRID-ORCS; 66471; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Anp32e; mouse.
DR PRO; PR:P97822; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P97822; Protein.
DR Bgee; ENSMUSG00000015749; Expressed in embryonic post-anal tail and 267 other cell types or tissues.
DR ExpressionAtlas; P97822; baseline and differential.
DR Genevisible; P97822; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0044183; F:protein folding chaperone; ISO:MGI.
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; Ribonuclease Inhibitor; 1.
DR InterPro; IPR045081; AN32.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR11375; ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32; 1.
DR PANTHER; PTHR11375:SF5; ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER E; 1.
DR Pfam; PF14580; LRR_9; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Chromatin regulator;
KW Cytoplasm; Isopeptide bond; Leucine-rich repeat; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..260
FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT member E"
FT /id="PRO_0000137600"
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..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..260
FT /note="ZID domain"
FT /evidence="ECO:0000250"
FT COMPBIAS 150..203
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..240
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"
FT VAR_SEQ 19..141
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_059599"
FT VAR_SEQ 208..219
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_007373"
FT CONFLICT 38
FT /note="N -> D (in Ref. 4; BAE35090)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="N -> D (in Ref. 4; BAB28449)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="S -> T (in Ref. 4; BAC33858)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 29622 MW; 7F94E46D72A04780 CRC64;
MEMKKKINME LKNRAPEEVT ELVLDNCLCV NGEIEGLNDT FKELEFLSMA NVELSSLARL
PSLNKLRKLE LSDNIISGGL EVLAEKCPNL TYLNLSGNKI KDLSTVEALQ NLKNLKSLDL
FNCEITNLED YRESIFELLQ QITYLDGFDQ EDNEAPDSEE EDDDDEDGDE DEEDEDEDEA
GPPEGYEEEE DDDEDEAGSE VGEGEEEVGL SYLMKDEIQD EEDDDDYVDE GEEEEEEEEE
GLRGEKRKRD AEDDGEEDDD
//
