AN32A_CANLF
ID AN32A_CANLF Reviewed; 249 AA.
AC Q8HY67;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member A;
DE AltName: Full=Inhibitor-1 of protein phosphatase type 2A;
GN Name=ANP32A;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Mishra S., Rastogi S., Gupta R.C., Sabbah H.N.;
RL Submitted (OCT-2002) 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).
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. Cytoplasm. Endoplasmic reticulum
CC {ECO:0000250}. Note=Shuttles between nucleus and cytoplasm.
CC Translocates to the cytoplasm during the process of neuritogenesis (By
CC similarity). {ECO:0000250}.
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; AY162293; AAN85118.1; -; mRNA.
DR STRING; 9612.ENSCAFP00000025783; -.
DR PaxDb; Q8HY67; -.
DR PRIDE; Q8HY67; -.
DR eggNOG; KOG2739; Eukaryota.
DR InParanoid; Q8HY67; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; 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 InterPro; IPR003603; U2A'_phosphoprotein32A_C.
DR PANTHER; PTHR11375; PTHR11375; 1.
DR SMART; SM00446; LRRcap; 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..249
FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT member A"
FT /id="PRO_0000240184"
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 147..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..174
FT /note="Necessary for tumor-suppressive function"
FT /evidence="ECO:0000250"
FT REGION 165..249
FT /note="Interaction with E4F1"
FT /evidence="ECO:0000250"
FT COMPBIAS 161..229
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..249
FT /note="Basic and 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 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P39687"
SQ SEQUENCE 249 AA; 28537 MW; E0ECFE9E4D3C0B82 CRC64;
MEMGRRIHLE LRNRTPSDVK ELVLDNCRSI EGKIEGLTDE FEELEFLSTI NVGLTSVANL
PKLNKLKKLE LSDNRISGGL EVLAEKCPNL THLNLSGNKI KDLSTIEPLK KLENLKSLDL
FNCEVTNLND YRENVFKLLP QLTYLDGYDR DDKEAPDSDA EGYVEGLDDD EEDEDEEEYD
EDAQVVEDEE DEEEEEEGEE EDVSGEEEED EEGYNDGEVD DEEDEEDVGE EERGQKRKRE
PXDXGEDDD
