AN32A_RAT
ID AN32A_RAT Reviewed; 247 AA.
AC P49911;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 151.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member A;
DE AltName: Full=Leucine-rich acidic nuclear protein;
DE Short=LANP;
GN Name=Anp32a; Synonyms=Lanp;
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=7937870; DOI=10.1073/pnas.91.21.9670;
RA Matsuoka K., Taoka M., Satozawa N., Nakayama H., Ichimura T., Takahashi N.,
RA Yamakuni T., Song S.-Y., Isobe T.;
RT "A nuclear factor containing the leucine-rich repeats expressed in murine
RT cerebellar neurons.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9670-9674(1994).
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: 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. Participates in
CC other biochemical processes such as regulation of mRNA nuclear-to-
CC cytoplasmic translocation and stability by its association with ELAVL1
CC (Hu-antigen R). Plays a role in E4F1-mediated transcriptional
CC repression as well as inhibition of protein phosphatase 2A.
CC {ECO:0000250|UniProtKB:P39687}.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Endoplasmic reticulum {ECO:0000250}. Note=Translocates to the cytoplasm
CC during the process of neuritogenesis. Shuttles between nucleus and
CC cytoplasm (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely distributed in the central nervous system,
CC with an abundant expression in the cerebellum.
CC {ECO:0000269|PubMed:7937870}.
CC -!- DEVELOPMENTAL STAGE: It is moderately expressed in the cerebellum on
CC postnatal day 7 in the external granule and Perkinje cells, increases
CC in the second postnatal week and thereafter decreases to an adult
CC level. {ECO:0000269|PubMed:7937870}.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
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DR EMBL; D32209; BAA06908.1; -; mRNA.
DR PIR; I59334; I59334.
DR RefSeq; NP_037035.1; NM_012903.1.
DR AlphaFoldDB; P49911; -.
DR BMRB; P49911; -.
DR SMR; P49911; -.
DR BioGRID; 247418; 3.
DR IntAct; P49911; 2.
DR MINT; P49911; -.
DR STRING; 10116.ENSRNOP00000020443; -.
DR iPTMnet; P49911; -.
DR PhosphoSitePlus; P49911; -.
DR SwissPalm; P49911; -.
DR jPOST; P49911; -.
DR PaxDb; P49911; -.
DR PRIDE; P49911; -.
DR GeneID; 25379; -.
DR KEGG; rno:25379; -.
DR UCSC; RGD:2116; rat.
DR CTD; 8125; -.
DR RGD; 11508551; Anp32a.
DR eggNOG; KOG2739; Eukaryota.
DR InParanoid; P49911; -.
DR OrthoDB; 1622194at2759; -.
DR PhylomeDB; P49911; -.
DR Reactome; R-RNO-450520; HuR (ELAVL1) binds and stabilizes mRNA.
DR PRO; PR:P49911; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0035067; P:negative regulation of histone acetylation; IMP:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IMP:RGD.
DR GO; GO:0006913; P:nucleocytoplasmic transport; ISS:UniProtKB.
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 Cytoplasm; Endoplasmic reticulum; Leucine-rich repeat; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..247
FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT member A"
FT /id="PRO_0000137594"
FT REPEAT 18..41
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:0000250"
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"
SQ SEQUENCE 247 AA; 28565 MW; 0919739645557462 CRC64;
MEMDKRIYLE LRNRTPSDVK ELVLDNCRSI EGKIEGLTDE FEELEFLSTI NVGLTSISNL
PKLNKLKKLE LSENRISGDL EVLAEKCPNL KHLNLSGNKI KDLSTIEPLK KLENLKSLDL
FNCEVTNLNA YRENVFKLLP QVMYLDGYDR DNKEAPDSDV EGYVEDDDEE DEDEEEYDEY
AQLVEDEEEE DEEEEGEEED VSGEEEEDEE GYNDGEVDDE EDEEDAAEEE GSQKRKREPD
DEGQEDD
