AN32B_CHICK
ID AN32B_CHICK Reviewed; 262 AA.
AC Q5ZMN0;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member B;
GN Name=ANP32B; ORFNames=RCJMB04_1j7;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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 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. {ECO:0000250|UniProtKB:Q92688}.
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 -!- DOMAIN: Histone binding is mediated by the concave surface of the LRR
CC region. {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; AJ719354; CAG31013.1; -; mRNA.
DR RefSeq; NP_001026105.1; NM_001030934.1.
DR AlphaFoldDB; Q5ZMN0; -.
DR SMR; Q5ZMN0; -.
DR STRING; 9031.ENSGALP00000002398; -.
DR PaxDb; Q5ZMN0; -.
DR Ensembl; ENSGALT00000086550; ENSGALP00000062993; ENSGALG00000037483.
DR GeneID; 420087; -.
DR KEGG; gga:420087; -.
DR CTD; 10541; -.
DR VEuPathDB; HostDB:geneid_420087; -.
DR eggNOG; KOG2739; Eukaryota.
DR GeneTree; ENSGT00950000182907; -.
DR HOGENOM; CLU_063314_1_1_1; -.
DR InParanoid; Q5ZMN0; -.
DR OMA; VNDCEAS; -.
DR PhylomeDB; Q5ZMN0; -.
DR TreeFam; TF317206; -.
DR PRO; PR:Q5ZMN0; -.
DR Proteomes; UP000000539; Chromosome 28.
DR Bgee; ENSGALG00000037483; Expressed in spleen and 12 other tissues.
DR ExpressionAtlas; Q5ZMN0; baseline and differential.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:AgBase.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:AgBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:AgBase.
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 Chaperone; Leucine-rich repeat; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..262
FT /note="Acidic leucine-rich nuclear phosphoprotein 32 family
FT member B"
FT /id="PRO_0000280063"
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 150..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 240..243
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q92688"
FT COMPBIAS 150..233
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 262 AA; 29944 MW; A59C2750DA50D3DB CRC64;
MEMKKRLTLE LRNKKPGEVK ELVLDNCRSD DGKIVGLSSD FENLEFLSMI NVNLLSISNL
PKLNKLRKLE LSDNRISGGL EVLAERTPNL THLNLSGNKI KDINTLEPLK KLPNLHSLDL
FNCEVTMLIN YRESVFTLLP QLTYLDGFDA DEQEAPDSDP EADGDGLEDE YENGEGEEEE
DDDEEDDLDE EVIDEEDDED DDLEGEEEED GVDDEEEDEE EDGEDEEDDE ADDDLPRGEK
RKRNLEDEGE EDPEDEEDDE DD