AKIRN_CAEEL
ID AKIRN_CAEEL Reviewed; 218 AA.
AC Q966L3;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Akirin {ECO:0000305};
GN Name=akir-1 {ECO:0000303|PubMed:23363597, ECO:0000312|WormBase:E01A2.6};
GN ORFNames=E01A2.6 {ECO:0000312|WormBase:E01A2.6};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-190.
RX PubMed=23363597; DOI=10.1091/mbc.e12-11-0841;
RA Clemons A.M., Brockway H.M., Yin Y., Kasinathan B., Butterfield Y.S.,
RA Jones S.J., Colaiacovo M.P., Smolikove S.;
RT "akirin is required for diakinesis bivalent structure and synaptonemal
RT complex disassembly at meiotic prophase I.";
RL Mol. Biol. Cell 24:1053-1067(2013).
RN [3]
RP FUNCTION, INTERACTION WITH CEH-18; HDA-1 AND LET-418, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=30036395; DOI=10.1371/journal.pgen.1007494;
RA Polanowska J., Chen J.X., Soule J., Omi S., Belougne J., Taffoni C.,
RA Pujol N., Selbach M., Zugasti O., Ewbank J.J.;
RT "Evolutionary plasticity in the innate immune function of Akirin.";
RL PLoS Genet. 14:E1007494-E1007494(2018).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND INTERACTION WITH
RP IMA-2.
RX PubMed=30563860; DOI=10.1534/genetics.118.301458;
RA Bowman R., Balukof N., Ford T., Smolikove S.;
RT "A novel role for alpha-importins and Akirin in establishment of meiotic
RT sister chromatid cohesion in Caenorhabditis elegans.";
RL Genetics 211:617-635(2019).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=31767636; DOI=10.1534/g3.119.400377;
RA Bowman R., Balukoff N., Clemons A., Koury E., Ford T., Baxi K.,
RA Egydio de Carvalho C., Smolikove S.;
RT "Akirin is required for muscle function and acts through the TGF-beta
RT Sma/Mab signaling pathway in Caenorhabditis elegans development.";
RL G3 (Bethesda) 10:387-400(2020).
CC -!- FUNCTION: Molecular adapter that acts as a bridge between a variety of
CC multiprotein complexes, and which is involved in antifungal innate
CC immunity, development of the muscle and sister chromatid cohesion
CC (PubMed:23363597, PubMed:30036395, PubMed:30563860, PubMed:31767636).
CC Plays a role in antifungal innate immunity by acting as a bridge
CC between components of the NuRD (Nucleosome Remodeling and Deacetylase)
CC and MEC chromatin remodeling complexes (PubMed:30036395). NuRD and MEC
CC complexes bind to the promoters of antimicrobial peptide genes and may
CC recruit other proteins such as ceh-18 to control gene expression in
CC response to fungal infection (PubMed:30036395). During meiotic prophase
CC I, plays a role in the disassembly of synaptonemal complex proteins and
CC in the regulation of chromosome condensation and segregation
CC (PubMed:23363597). Together with nuclear import receptor ima-2,
CC required for the import and load of cohesin complex proteins in meiotic
CC nuclei, possibly by acting as a bridge between ima-2 and cohesins
CC (PubMed:30563860). Required for embryonic development of muscle tissue
CC (PubMed:31767636). {ECO:0000269|PubMed:23363597,
CC ECO:0000269|PubMed:30036395, ECO:0000269|PubMed:30563860,
CC ECO:0000269|PubMed:31767636}.
CC -!- SUBUNIT: Interacts with hda-1, a component of the NuRD complex
CC (PubMed:30036395). Interacts with let-418, a component of the NuRD and
CC MEC complexes (PubMed:30036395). Interacts with the transcription
CC factor ceh-18 (PubMed:30036395). Interacts with ima-2
CC (PubMed:30563860). {ECO:0000269|PubMed:30036395,
CC ECO:0000269|PubMed:30563860}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30036395,
CC ECO:0000269|PubMed:30563860, ECO:0000269|PubMed:31767636}.
CC -!- TISSUE SPECIFICITY: Localizes to somatic tissues throughout the body,
CC including muscle cells (PubMed:31767636). Expressed in lateral
CC epithelial seam cells, the hyp7 epidermal syncytium, and multiple head
CC and tail neurons (PubMed:30036395). {ECO:0000269|PubMed:30036395,
CC ECO:0000269|PubMed:31767636}.
CC -!- DEVELOPMENTAL STAGE: Expressed from the late embryo stage onwards, with
CC high expression at the late L4 stage of larval development.
CC {ECO:0000269|PubMed:30036395}.
CC -!- DISRUPTION PHENOTYPE: 16% embryonic lethality, reduced egg laying and a
CC 0.9% increase in the number of male progeny (PubMed:23363597). Delayed
CC progression of meiosis, which most likely results from defective
CC disassembly of synaptonemal complex proteins, and defective chromosome
CC structure, alignment and condensation (PubMed:23363597). RNAi-mediated
CC knockdown results in reduced expression of the nlp-29 antimicrobial
CC peptide following fungal infection by D.coniospora (PubMed:30036395).
CC Worms show reduced body size and muscle function (PubMed:31767636).
CC Worms lacking both akir-1 and ima-2 show reduced gonad size and
CC aberrant diakinesis oocyte formation; defects are caused by impaired
CC meiotic recombination (PubMed:30563860). {ECO:0000269|PubMed:23363597,
CC ECO:0000269|PubMed:30036395, ECO:0000269|PubMed:30563860,
CC ECO:0000269|PubMed:31767636}.
CC -!- SIMILARITY: Belongs to the akirin family. {ECO:0000305}.
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DR EMBL; BX284601; CCD68578.1; -; Genomic_DNA.
DR RefSeq; NP_491304.1; NM_058903.6.
DR AlphaFoldDB; Q966L3; -.
DR SMR; Q966L3; -.
DR STRING; 6239.E01A2.6.1; -.
DR PaxDb; Q966L3; -.
DR EnsemblMetazoa; E01A2.6.1; E01A2.6.1; WBGene00017088.
DR GeneID; 171997; -.
DR KEGG; cel:CELE_E01A2.6; -.
DR UCSC; E01A2.6; c. elegans.
DR CTD; 171997; -.
DR WormBase; E01A2.6; CE24873; WBGene00017088; akir-1.
DR eggNOG; KOG4330; Eukaryota.
DR GeneTree; ENSGT00940000174557; -.
DR HOGENOM; CLU_1125694_0_0_1; -.
DR InParanoid; Q966L3; -.
DR OMA; RRCAPIM; -.
DR OrthoDB; 1420469at2759; -.
DR PhylomeDB; Q966L3; -.
DR PRO; PR:Q966L3; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00017088; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0051177; P:meiotic sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0045089; P:positive regulation of innate immune response; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IMP:UniProtKB.
DR InterPro; IPR024132; Akirin.
DR PANTHER; PTHR13293; PTHR13293; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Immunity; Innate immunity; Meiosis; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..218
FT /note="Akirin"
FT /id="PRO_0000447630"
FT REGION 96..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 190
FT /note="H->P: In rj1; 21% embryonic lethality, reduced egg
FT laying and a 0.6% increase in the number of male progeny.
FT Delayed progression of meiosis, which most likely results
FT from defective disassembly of synaptonemal complex
FT proteins, and defective chromosome alignment, segregation
FT and condensation."
FT /evidence="ECO:0000269|PubMed:23363597"
SQ SEQUENCE 218 AA; 24683 MW; 42971050BAC15F05 CRC64;
MACGLALKRP LQHEYESFLT DETYNGEAKR ARTQCPPFRA QMGTIAATLP STSTFAQKFK
EQEESVFQAA TLMTRLSRNQ LKTYLSSEVK NLRKRKAIPR SNDFDDDGDQ RGDGCSSNYS
KAYRAPSSPK SGSDSEGEAP STSVTDRSSA KREFTMANVQ MICERLLKQQ EIRLRNEFEM
VLTKKLDEQH QQYVQFAAEQ LNSKCVSTGD DYSYSYLS
