ID   AKIR2_XENLA             Reviewed;         181 AA.
AC   Q6GQB5;
DT   25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Akirin-2 {ECO:0000303|PubMed:28193841};
DE            Short=XAkirin2 {ECO:0000303|PubMed:28193841};
GN   Name=akirin2.S {ECO:0000312|Xenbase:XB-GENE-951500};
GN   Synonyms=akirin2 {ECO:0000303|PubMed:28193841};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND INTERACTION WITH ACTL6A AND GMNN.
RX   PubMed=28193841; DOI=10.1074/jbc.m117.777110;
RA   Liu X., Xia Y., Tang J., Ma L., Li C., Ma P., Mao B.;
RT   "Dual roles of Akirin2 protein during Xenopus neural development.";
RL   J. Biol. Chem. 292:5676-5684(2017).
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 (PubMed:28193841). Plays a
CC       key role in nuclear protein degradation by promoting import of
CC       proteasomes into the nucleus: acts by bridging fully assembled 20S
CC       proteasomes with nuclear import receptor ipo9 (By similarity). Involved
CC       in both neural precursor maintenance and terminal neural
CC       differentiation: bridges gmnn and actl6a/baf53a in neural progenitor
CC       cells, antagonizing the activity of gmnn, thereby suppressing sox2
CC       expression (PubMed:28193841). Also required for proper activation of
CC       neurod1 and neuronal differentiation (PubMed:28193841). 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, ECO:0000269|PubMed:28193841}.
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with actl6a/baf53a
CC       (PubMed:28193841). Interacts with gmnn (PubMed:28193841).
CC       {ECO:0000250|UniProtKB:Q53H80, ECO:0000269|PubMed:28193841}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:B1AXD8}.
CC   -!- SIMILARITY: Belongs to the akirin family. {ECO:0000305}.
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DR   EMBL; BC072831; AAH72831.1; -; mRNA.
DR   RefSeq; NP_001085484.1; NM_001092015.1.
DR   DNASU; 443910; -.
DR   GeneID; 443910; -.
DR   KEGG; xla:443910; -.
DR   CTD; 443910; -.
DR   Xenbase; XB-GENE-951500; akirin2.S.
DR   OrthoDB; 1420469at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 443910; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProtKB.
DR   GO; GO:0022008; P:neurogenesis; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR024132; Akirin.
DR   PANTHER; PTHR13293; PTHR13293; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Nucleus; Protein transport; Reference proteome;
KW   Repressor; Transcription; Transcription regulation; Transport.
FT   CHAIN           1..181
FT                   /note="Akirin-2"
FT                   /id="PRO_0000455441"
FT   REGION          18..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           23..28
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H80"
FT   MOTIF           178..181
FT                   /note="SYVS motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q53H80"
SQ   SEQUENCE   181 AA;  20623 MW;  775C54A39C80ADE6 CRC64;
     MACGATLKRT IEFDPLLSPA ASPKRRRCAP LSPSGPSPQK YLRLEPSPFG EVSPRLTAEQ
     ILYNIKQEYK RMQKRRHLES SFQPTDPCCS SEGQPQTFIP SGPTLPGTSA TSPLRKEQPL
     FSLRQVGMIC ERLLKEREDN VREEYEEILT TKLAEQYDAF VKFTHDQIMR RFGEQPASYV
     S