AKIR2_RAT
ID AKIR2_RAT Reviewed; 201 AA.
AC Q25C79;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Akirin-2 {ECO:0000305};
DE AltName: Full=Fourteen-three-three beta interactant 1 {ECO:0000303|PubMed:18460465};
DE AltName: Full=Fourteen-three-three beta interacting-protein 1 {ECO:0000303|PubMed:18460465};
GN Name=Akirin2 {ECO:0000250|UniProtKB:Q53H80};
GN Synonyms=FBI1 {ECO:0000303|PubMed:18460465};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAE81786.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH YWHAB, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF SER-31; THR-103; SER-111; SER-119
RP AND SER-131.
RX PubMed=18460465; DOI=10.1074/jbc.m802530200;
RA Komiya Y., Kurabe N., Katagiri K., Ogawa M., Sugiyama A., Kawasaki Y.,
RA Tashiro F.;
RT "A novel binding factor of 14-3-3beta functions as a transcriptional
RT repressor and promotes anchorage-independent growth, tumorigenicity, and
RT metastasis.";
RL J. Biol. Chem. 283:18753-18764(2008).
RN [2] {ECO:0000312|EMBL:EDL98593.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Also plays a role in facilitating interdigital
CC tissue regression during limb development (By similarity).
CC {ECO:0000250|UniProtKB:B1AXD8, 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 (PubMed:18460465).
CC {ECO:0000250|UniProtKB:B1AXD8, ECO:0000250|UniProtKB:Q53H80,
CC ECO:0000269|PubMed:18460465}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18460465}. 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 -!- TISSUE SPECIFICITY: Highly expressed in testis, cerebrum and
CC cerebellum, and barely detectable in liver, heart, spleen and muscle.
CC Also highly expressed in various tumor cells from hepatoma,
CC glioblastoma and pheochromocytoma. {ECO:0000269|PubMed:18460465}.
CC -!- SIMILARITY: Belongs to the akirin family. {ECO:0000305}.
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DR EMBL; AB234867; BAE81786.1; -; mRNA.
DR EMBL; CH473962; EDL98593.1; -; Genomic_DNA.
DR RefSeq; NP_001035003.1; NM_001039914.2.
DR AlphaFoldDB; Q25C79; -.
DR SMR; Q25C79; -.
DR IntAct; Q25C79; 1.
DR MINT; Q25C79; -.
DR STRING; 10116.ENSRNOP00000010962; -.
DR iPTMnet; Q25C79; -.
DR PhosphoSitePlus; Q25C79; -.
DR PaxDb; Q25C79; -.
DR PRIDE; Q25C79; -.
DR Ensembl; ENSRNOT00000010962; ENSRNOP00000010962; ENSRNOG00000008288.
DR GeneID; 297968; -.
DR KEGG; rno:297968; -.
DR UCSC; RGD:1307791; rat.
DR CTD; 55122; -.
DR RGD; 1307791; Akirin2.
DR eggNOG; KOG4330; Eukaryota.
DR GeneTree; ENSGT00940000156096; -.
DR HOGENOM; CLU_119227_0_0_1; -.
DR InParanoid; Q25C79; -.
DR OMA; RRCAPIM; -.
DR OrthoDB; 1420469at2759; -.
DR PhylomeDB; Q25C79; -.
DR TreeFam; TF317123; -.
DR PRO; PR:Q25C79; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Proteomes; UP000234681; Chromosome 5.
DR Bgee; ENSRNOG00000008288; Expressed in testis and 19 other tissues.
DR Genevisible; Q25C79; RN.
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; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:RGD.
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:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0010950; P:positive regulation of endopeptidase activity; IMP:RGD.
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; ISO:RGD.
DR InterPro; IPR024132; Akirin.
DR PANTHER; PTHR13293; PTHR13293; 1.
PE 1: Evidence at protein 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..201
FT /note="Akirin-2"
FT /id="PRO_0000355122"
FT MOTIF 22..27
FT /note="Nuclear localization signal"
FT MOTIF 198..201
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:0007744|PubMed:22673903"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AXD8"
FT MUTAGEN 31
FT /note="S->A: Abolishes binding to YWHAB. Reduces
FT transcriptional repressor activity; when associated with A-
FT 111 and A-119."
FT /evidence="ECO:0000269|PubMed:18460465"
FT MUTAGEN 103
FT /note="T->A: Abolishes binding to YWHAB. Loss of
FT transcriptional repressor activity; when associated with A-
FT 111; A-119 and A-131."
FT /evidence="ECO:0000269|PubMed:18460465"
FT MUTAGEN 111
FT /note="S->A: Abolishes binding to YWHAB. Loss of
FT transcriptional repressor activity; when associated with A-
FT 103; A-119 and A-131. Reduces transcriptional repressor
FT activity; when associated with A-31 and A-119."
FT /evidence="ECO:0000269|PubMed:18460465"
FT MUTAGEN 119
FT /note="S->A: Abolishes binding to YWHAB. Loss of
FT transcriptional repressor activity; when associated with A-
FT 103; A-111 and A-131. Reduces transcriptional repressor
FT activity; when associated with A-31 and A-111."
FT /evidence="ECO:0000269|PubMed:18460465"
FT MUTAGEN 131
FT /note="S->A: Abolishes binding to YWHAB. Loss of
FT transcriptional repressor activity; when associated with A-
FT 103; A-111 and A-119."
FT /evidence="ECO:0000269|PubMed:18460465"
SQ SEQUENCE 201 AA; 22129 MW; 2DEC2AA36F95C1BB CRC64;
MACGATLKRT LDFDPLLSPA SPKRRRCAPL SAPASAAASP AAATAAAAAS AAAASPQKYL
RMEPSPFGDV SSRLTTEQIL YNIKQEYKRM QKRRHLEASF QQTDPGCSSD SQPHAFLISG
PASPGTSSAT SSPLKKEQPL FTLRQVGMIC ERLLKEREEK VREEYEEILN TKLAEQYDAF
VKFTHDQIMR RYGEQPASYV S
