AN32B_RAT
ID AN32B_RAT Reviewed; 272 AA.
AC Q9EST6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member B;
DE AltName: Full=Proliferation-related acidic leucine-rich protein PAL31;
GN Name=Anp32b; Synonyms=Pal31;
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar Imamichi; TISSUE=Brain;
RX PubMed=10913355; DOI=10.1006/bbrc.2000.3133;
RA Mutai H., Toyoshima Y., Sun W., Hattori N., Tanaka S., Shiota K.;
RT "PAL31, a novel nuclear protein, expressed in the developing brain.";
RL Biochem. Biophys. Res. Commun. 274:427-433(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
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 [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11162633; DOI=10.1006/bbrc.2000.4244;
RA Sun W., Hattori N., Mutai H., Toyoshima Y., Kimura H., Tanaka S.,
RA Shiota K.;
RT "PAL31, a nuclear protein required for progression to the S phase.";
RL Biochem. Biophys. Res. Commun. 280:1048-1054(2001).
RN [4]
RP FUNCTION.
RX PubMed=16499868; DOI=10.1016/j.bbrc.2006.02.026;
RA Sun W., Kimura H., Hattori N., Tanaka S., Matsuyama S., Shiota K.;
RT "Proliferation related acidic leucine-rich protein PAL31 functions as a
RT caspase-3 inhibitor.";
RL Biochem. Biophys. Res. Commun. 342:817-823(2006).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; SER-171 AND THR-265, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Multifunctional protein that is involved in the regulation of
CC many processes including cell proliferation, apoptosis, cell cycle
CC progression or transcription. Regulates the proliferation of neuronal
CC stem cells, differentiation of leukemic cells and progression from G1
CC to S phase of the cell cycle (PubMed:11162633). As negative regulator
CC of caspase-3-dependent apoptosis, may act as an antagonist of ANP32A in
CC regulating tissue homeostasis (PubMed:16499868). Exhibits histone
CC chaperone properties, able to recruit histones to certain promoters,
CC thus regulating the transcription of specific genes. Also plays an
CC essential role in the nucleocytoplasmic transport of specific mRNAs via
CC the uncommon nuclear mRNA export receptor XPO1/CRM1 (By similarity).
CC Participates in the regulation of adequate adaptive immune responses by
CC acting on mRNA expression and cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:Q92688, ECO:0000250|UniProtKB:Q9EST5,
CC ECO:0000269|PubMed:11162633, ECO:0000269|PubMed:16499868}.
CC -!- SUBUNIT: Interacts with histones H3 and H4. Interacts with KLF5; this
CC interaction induces promoter region-specific histone incorporation and
CC inhibition of histone acetylation by ANP32B.
CC {ECO:0000250|UniProtKB:Q92688}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10913355,
CC ECO:0000269|PubMed:11162633}. Note=Accumulates in the nuclei at the S
CC phase.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain. Expressed in the
CC entire embryonic brain, whereas in the adult brain its expression is
CC restricted to the subventricular zone where there are neural progenitor
CC cells. {ECO:0000269|PubMed:10913355}.
CC -!- INDUCTION: Expressed specifically during the late G1 and S phases.
CC -!- DOMAIN: Histone binding is mediated by the concave surface of the LRR
CC region. {ECO:0000250}.
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 -!- PTM: Directly cleaved by caspase-3/CASP3.
CC {ECO:0000250|UniProtKB:Q92688}.
CC -!- MISCELLANEOUS: Suppression of the expression of this gene by RNAi
CC induces apoptosis.
CC -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
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DR EMBL; AB025581; BAB12435.1; -; mRNA.
DR EMBL; BC086508; AAH86508.1; -; mRNA.
DR PIR; JC7357; JC7357.
DR RefSeq; NP_571986.1; NM_131911.2.
DR AlphaFoldDB; Q9EST6; -.
DR SMR; Q9EST6; -.
DR BioGRID; 250983; 2.
DR IntAct; Q9EST6; 1.
DR MINT; Q9EST6; -.
DR STRING; 10116.ENSRNOP00000012478; -.
DR iPTMnet; Q9EST6; -.
DR PhosphoSitePlus; Q9EST6; -.
DR SwissPalm; Q9EST6; -.
DR jPOST; Q9EST6; -.
DR PaxDb; Q9EST6; -.
DR PRIDE; Q9EST6; -.
DR Ensembl; ENSRNOT00000012478; ENSRNOP00000012478; ENSRNOG00000009266.
DR GeneID; 170724; -.
DR KEGG; rno:170724; -.
DR UCSC; RGD:621285; rat.
DR CTD; 10541; -.
DR RGD; 621285; Anp32b.
DR eggNOG; KOG2739; Eukaryota.
DR GeneTree; ENSGT00950000182907; -.
DR InParanoid; Q9EST6; -.
DR OrthoDB; 1622194at2759; -.
DR PhylomeDB; Q9EST6; -.
DR PRO; PR:Q9EST6; -.
DR Proteomes; UP000002494; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0070063; F:RNA polymerase binding; ISO:RGD.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0048839; P:inner ear development; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0045596; P:negative regulation of cell differentiation; ISO:RGD.
DR GO; GO:0006334; P:nucleosome assembly; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IMP:RGD.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0001944; P:vasculature development; ISO:RGD.
DR GO; GO:0021591; P:ventricular system development; ISO:RGD.
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; 2.
DR SMART; SM00446; LRRcap; 1.
DR PROSITE; PS51450; LRR; 3.
PE 1: Evidence at protein level;
KW Chaperone; Leucine-rich repeat; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..272
FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT member B"
FT /id="PRO_0000236253"
FT REPEAT 16..40
FT /note="LRR 1"
FT REPEAT 43..64
FT /note="LRR 2"
FT REPEAT 65..84
FT /note="LRR 3"
FT REPEAT 89..110
FT /note="LRR 4"
FT DOMAIN 123..161
FT /note="LRRCT"
FT REGION 149..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 260..263
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q92688"
FT COMPBIAS 152..254
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 265
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 272 AA; 31061 MW; 556AC9B169E9D996 CRC64;
MDMKRRIHLE LRNRTPAAVQ ELVLDNCKAN DGKIEGLTDE FVNLEFLSLI NVGLFSVSDL
PKLPKLKKLE LSENRIFGGL DRLAEELPSL THLNLSGNNL KDISTLEPLK RLDCLKSLDL
FGCEVTNRSD YRETVFRLLP QLSYLDGYDR EDQEAPDSDV EVDSVEEAPD SDGEVDGVDK
EEEDEEGEDE EEEEDEDGEE EEDEDEEDED EDEDVEGEDD EDEVSGEEEE FGHDGEVDED
EEDEDEDEDE EEEESGKGEK RKRETDDEGE DD
