AN32B_BOVIN
ID AN32B_BOVIN Reviewed; 261 AA.
AC Q3SZC6;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member B;
GN Name=ANP32B;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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. As negative regulator of caspase-3-
CC dependent apoptosis, may act as an antagonist of ANP32A in regulating
CC tissue homeostasis. Exhibits histone chaperone properties, able to
CC recruit histones to certain promoters, thus regulating the
CC transcription of specific genes. Also plays an essential role in the
CC nucleocytoplasmic transport of specific mRNAs via the uncommon nuclear
CC mRNA export receptor XPO1/CRM1 (By similarity). Participates in the
CC regulation of adequate adaptive immune responses by acting on mRNA
CC expression and cell proliferation (By similarity).
CC {ECO:0000250|UniProtKB:Q92688, ECO:0000250|UniProtKB:Q9EST5}.
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:0000250|UniProtKB:Q92688}.
CC Note=Accumulates in the nuclei at the S phase.
CC {ECO:0000250|UniProtKB:Q92688}.
CC -!- DOMAIN: Histone binding is mediated by the concave surface of the LRR
CC region. {ECO:0000250}.
CC -!- PTM: Some Glu residues are glycylated by TTLL8; a modification that
CC generates a side chains of glycine on the gamma-carboxyl groups of
CC specific glutamate residues. {ECO:0000250}.
CC -!- PTM: Directly cleaved by caspase-3/CASP3.
CC {ECO:0000250|UniProtKB:Q92688}.
CC -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
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DR EMBL; BC102954; AAI02955.1; -; mRNA.
DR RefSeq; NP_001030246.1; NM_001035074.1.
DR AlphaFoldDB; Q3SZC6; -.
DR BMRB; Q3SZC6; -.
DR SMR; Q3SZC6; -.
DR IntAct; Q3SZC6; 1.
DR STRING; 9913.ENSBTAP00000028486; -.
DR PaxDb; Q3SZC6; -.
DR PeptideAtlas; Q3SZC6; -.
DR PRIDE; Q3SZC6; -.
DR Ensembl; ENSBTAT00000078479; ENSBTAP00000071807; ENSBTAG00000021367.
DR GeneID; 509685; -.
DR KEGG; bta:509685; -.
DR CTD; 10541; -.
DR VEuPathDB; HostDB:ENSBTAG00000021367; -.
DR VGNC; VGNC:25958; ANP32B.
DR eggNOG; KOG2739; Eukaryota.
DR GeneTree; ENSGT00950000182907; -.
DR InParanoid; Q3SZC6; -.
DR OrthoDB; 1622194at2759; -.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000021367; Expressed in pharyngeal tonsil and 102 other tissues.
DR ExpressionAtlas; Q3SZC6; baseline and differential.
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 Acetylation; Chaperone; Leucine-rich repeat; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..261
FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT member B"
FT /id="PRO_0000236249"
FT REPEAT 16..40
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..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 249..252
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q92688"
FT COMPBIAS 158..243
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92688"
FT MOD_RES 158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EST6"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92688"
SQ SEQUENCE 261 AA; 29872 MW; 25133BB762971990 CRC64;
MDMKRRIHLE LRNRTPAAVR ELVLDNCKSN DGKIEGLTAE FVNLEFLSLI NVGLISVSNL
PKLPKLKKLE LSDNRICGGL DMLAEKLPNL THLNLSGNKL KDISTLEPLK KLECLKSLDL
FNCEVTNLND YRESVFKLLP QLTYLDGYDR EDREAPDSDA EVDGVDEEED DEEGEDEDKE
EDEDGEEEEF DDEEDDDEDE DVEGEEDEDE VSGEEEEFGH DGEVDEDDED EDEDEDEDEE
EEESGKGEKR KRETDDEGED D
