AKIR2_BOVIN
ID AKIR2_BOVIN Reviewed; 203 AA.
AC A8YXY8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Akirin-2;
GN Name=AKIRIN2 {ECO:0000312|EMBL:AAI04620.1};
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] {ECO:0000312|EMBL:AAI04620.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI04620.1};
RC TISSUE=Uterus {ECO:0000312|EMBL:AAI04620.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular adapter that acts as a bridge between a variety of
CC multiprotein complexes, and which is involved in embryonic development,
CC immunity, myogenesis and brain development (By similarity). Plays a key
CC role in nuclear protein degradation by promoting import of proteasomes
CC into the nucleus: directly binds to fully assembled 20S proteasomes at
CC one end and to nuclear import receptor IPO9 at the other end, bridging
CC them together and mediating the import of pre-assembled proteasome
CC complexes through the nuclear pore (By similarity). Involved in innate
CC immunity by regulating the production of interleukin-6 (IL6) downstream
CC of Toll-like receptor (TLR): acts by bridging the NF-kappa-B inhibitor
CC NFKBIZ and the SWI/SNF complex, leading to promote induction of IL6.
CC Also involved in adaptive immunity by promoting B-cell activation.
CC Involved in brain development: required for the survival and
CC proliferation of cerebral cortical progenitor cells. Involved in
CC myogenesis: required for skeletal muscle formation and skeletal
CC development, possibly by regulating expression of muscle
CC differentiation factors (By similarity). {ECO:0000250|UniProtKB:B1AXD8,
CC ECO:0000250|UniProtKB:Q53H80}.
CC -!- SUBUNIT: Homodimer. Interacts with IPO9; the interaction is direct.
CC Associates with 20S and 26S proteasomes (By similarity). Interacts with
CC SMARCD1; promoting SWI/SNF complex recruitment. Interacts with NFKBIZ
CC (By similarity). Interacts with YWHAB (By similarity).
CC {ECO:0000250|UniProtKB:B1AXD8, ECO:0000250|UniProtKB:Q25C79,
CC ECO:0000250|UniProtKB:Q53H80}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B1AXD8}. Cytoplasm
CC {ECO:0000250|UniProtKB:B1AXD8}. Membrane
CC {ECO:0000250|UniProtKB:B1AXD8}. Note=Present mainly in the nuclear
CC fraction, and at much lower level in the cytoplasmic and membrane
CC fractions. {ECO:0000250|UniProtKB:B1AXD8}.
CC -!- SIMILARITY: Belongs to the akirin family. {ECO:0000305}.
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DR EMBL; BC104619; AAI04620.1; -; mRNA.
DR RefSeq; NP_001103557.1; NM_001110087.1.
DR AlphaFoldDB; A8YXY8; -.
DR SMR; A8YXY8; -.
DR STRING; 9913.ENSBTAP00000004897; -.
DR PaxDb; A8YXY8; -.
DR PRIDE; A8YXY8; -.
DR Ensembl; ENSBTAT00000004897; ENSBTAP00000004897; ENSBTAG00000003764.
DR GeneID; 614292; -.
DR KEGG; bta:614292; -.
DR CTD; 55122; -.
DR VEuPathDB; HostDB:ENSBTAG00000003764; -.
DR VGNC; VGNC:25794; AKIRIN2.
DR eggNOG; KOG4330; Eukaryota.
DR GeneTree; ENSGT00940000156096; -.
DR HOGENOM; CLU_119227_0_0_1; -.
DR InParanoid; A8YXY8; -.
DR OMA; RRCAPIM; -.
DR OrthoDB; 1420469at2759; -.
DR TreeFam; TF317123; -.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000003764; Expressed in oocyte and 102 other tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0021987; P:cerebral cortex development; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISS:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; ISS:UniProtKB.
DR GO; GO:0002821; P:positive regulation of adaptive immune response; ISS:UniProtKB.
DR GO; GO:0050871; P:positive regulation of B cell activation; IEA:Ensembl.
DR GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0031144; P:proteasome localization; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0051147; P:regulation of muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR InterPro; IPR024132; Akirin.
DR PANTHER; PTHR13293; PTHR13293; 1.
PE 2: Evidence at transcript level;
KW Adaptive immunity; Cytoplasm; Developmental protein; Immunity;
KW Innate immunity; Membrane; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Transport.
FT CHAIN 1..203
FT /note="Akirin-2"
FT /id="PRO_0000355120"
FT REGION 115..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 22..27
FT /note="Nuclear localization signal"
FT MOTIF 200..203
FT /note="SYVS motif"
FT /evidence="ECO:0000250|UniProtKB:Q53H80"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53H80"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q53H80"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AXD8"
SQ SEQUENCE 203 AA; 22510 MW; 1771B0C09074EDC8 CRC64;
MACGATLKRT LDFDPLLSPA SPKRRRCAPL SAPTSAAATP SSAAAATAAS FSAAAASPQK
YLRMEPSPFG DVSSRLTTEQ ILYNIKQEYK RMQKRRHLET SFQQTDPCCT SDAQPHAFLL
SGPASPGTPS GTSSPLKKEQ PLFTLRQVGM ICERLLKERE EKVREEYEEI LNTKLAEQYD
AFVKFTHDQI MRRYGEQPAS YVS
