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 08-NOV-2023, entry version 74.
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 PaxDb; 9940-ENSOARP00000008546; -.
DR eggNOG; KOG2739; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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; ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32; 1.
DR PANTHER; PTHR11375:SF2; ACIDIC LEUCINE-RICH NUCLEAR PHOSPHOPROTEIN 32 FAMILY MEMBER B; 1.
DR Pfam; PF14580; LRR_9; 1.
DR SMART; SM00446; LRRcap; 1.
DR SUPFAM; SSF52058; L domain-like; 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
//
