ID   AN32B_SHEEP             Reviewed;         261 AA.
AC   Q6A1I3;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Acidic leucine-rich nuclear phosphoprotein 32 family member B;
DE   AltName: Full=Acidic protein rich in leucines;
DE   AltName: Full=Leucine-rich acidic nuclear protein;
DE            Short=LAN;
GN   Name=ANP32B; Synonyms=APRIL;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Fetal blood;
RA   Zhang J.;
RT   "Cloning and identification of SLAN expressed in fetal sheep blood using
RT   DDRT-PCR.";
RL   Submitted (JUL-2004) 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 working as a cell cycle progression
CC       factor as well as a cell survival factor. Required for the progression
CC       from the G1 to the S phase. Anti-apoptotic protein which functions as a
CC       caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity.
CC       Exhibits histone chaperone properties, stimulating core histones to
CC       assemble into a nucleosome (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Interacts with histones H3 and H4 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Accumulates in the nuclei at the S
CC       phase.
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   -!- SIMILARITY: Belongs to the ANP32 family. {ECO:0000305}.
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DR   EMBL; AJ783860; CAH04953.1; -; mRNA.
DR   AlphaFoldDB; Q6A1I3; -.
DR   BMRB; Q6A1I3; -.
DR   SMR; Q6A1I3; -.
DR   STRING; 9940.ENSOARP00000008546; -.
DR   PRIDE; Q6A1I3; -.
DR   eggNOG; KOG2739; Eukaryota.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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_0000137596"
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   COMPBIAS        158..243
FT                   /note="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;  29741 MW;  B778F10BD0700F53 CRC64;
     MDMKRRIHLE LRNRTPAAVR ELVLDNCKSN DGKIEGLTAE FVNLEFLSLI NVGLISVSNL
     PKLPKLKKLE LSDNRICGGL DMLAEKLPNL THLNLSGNKL KDIGTLEPLK KLECLKSLDL
     FNCEVTNLND YRESVFKLLP QLTYLDGYDR EDREAPDSDA EVDGVDEEED DEEGENEDKE
     EDEDGEEEEF DDEEDDDEDE DVEGEEDEDK VSGEEEEFGH DGEADEDDED EDEDEDEDEE
     EEESGKGEGR KRETDDEGED D