AKIR1_MOUSE
ID AKIR1_MOUSE Reviewed; 191 AA.
AC Q99LF1; Q9JJB7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Akirin-1 {ECO:0000305};
DE AltName: Full=protein mighty {ECO:0000303|PubMed:18255059};
GN Name=Akirin1 {ECO:0000303|PubMed:18066067};
GN Synonyms=Mighty {ECO:0000303|PubMed:18255059}; ORFNames=MNCb-2831;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from mouse brain cDNA library made by
RT oligo-capping method.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Heart, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, INDUCTION, AND FUNCTION.
RX PubMed=18255059; DOI=10.1016/j.yexcr.2008.01.004;
RA Marshall A., Salerno M.S., Thomas M., Davies T., Berry C., Dyer K.,
RA Bracegirdle J., Watson T., Dziadek M., Kambadur R., Bower R., Sharma M.;
RT "Mighty is a novel promyogenic factor in skeletal myogenesis.";
RL Exp. Cell Res. 314:1013-1029(2008).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=18066067; DOI=10.1038/ni1543;
RA Goto A., Matsushita K., Gesellchen V., El Chamy L., Kuttenkeuler D.,
RA Takeuchi O., Hoffmann J.A., Akira S., Boutros M., Reichhart J.-M.;
RT "Akirins are highly conserved nuclear proteins required for NF-kappaB-
RT dependent gene expression in Drosophila and mice.";
RL Nat. Immunol. 9:97-104(2008).
RN [6]
RP ERRATUM OF PUBMED:18066067.
RA Goto A., Matsushita K., Gesellchen V., El Chamy L., Kuttenkeuler D.,
RA Takeuchi O., Hoffmann J.A., Akira S., Boutros M., Reichhart J.-M.;
RL Nat. Immunol. 9:216-216(2008).
RN [7]
RP INDUCTION, TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19406121; DOI=10.1016/j.yexcr.2009.04.014;
RA Salerno M.S., Dyer K., Bracegirdle J., Platt L., Thomas M., Siriett V.,
RA Kambadur R., Sharma M.;
RT "Akirin1 (Mighty), a novel promyogenic factor regulates muscle regeneration
RT and cell chemotaxis.";
RL Exp. Cell Res. 315:2012-2021(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INDUCTION.
RX PubMed=23516508; DOI=10.1371/journal.pone.0058554;
RA Dong Y., Pan J.S., Zhang L.;
RT "Myostatin suppression of Akirin1 mediates glucocorticoid-induced satellite
RT cell dysfunction.";
RL PLoS ONE 8:E58554-E58554(2013).
RN [10]
RP FUNCTION.
RX PubMed=30746755; DOI=10.1002/jcb.28406;
RA Rao V.V., Sangiah U., Mary K.A., Akira S., Mohanty A.;
RT "Role of Akirin1 in the regulation of skeletal muscle fiber-type switch.";
RL J. Cell. Biochem. 0:0-0(2019).
CC -!- FUNCTION: Molecular adapter that acts as a bridge between proteins, and
CC which is involved skeletal muscle development (PubMed:18255059,
CC PubMed:19406121, PubMed:30746755). Functions as signal transducer for
CC MSTN during skeletal muscle regeneration and myogenesis
CC (PubMed:18255059, PubMed:19406121). May regulate chemotaxis of both
CC macrophages and myoblasts by reorganising actin cytoskeleton, leading
CC to more efficient lamellipodia formation via a PI3 kinase dependent
CC pathway (PubMed:19406121). In contrast to AKIRIN2, not involved in
CC nuclear import of proteasomes (By similarity).
CC {ECO:0000250|UniProtKB:Q9H9L7, ECO:0000269|PubMed:18255059,
CC ECO:0000269|PubMed:19406121, ECO:0000269|PubMed:30746755}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H9L7}.
CC -!- TISSUE SPECIFICITY: Expressed in macrophages and satellite cells.
CC {ECO:0000269|PubMed:18255059, ECO:0000269|PubMed:19406121}.
CC -!- INDUCTION: Up-regulated in activated satellite cells and in the
CC regenerating muscle (PubMed:19406121). Down-regulated by MSTN in
CC skeletal muscle (PubMed:19406121, PubMed:18255059, PubMed:23516508).
CC Down-regulated by dexamethasone by a MSTN (PubMed:23516508).
CC {ECO:0000269|PubMed:18255059, ECO:0000269|PubMed:19406121,
CC ECO:0000269|PubMed:23516508}.
CC -!- DISRUPTION PHENOTYPE: Mice grow normally and do not display gross
CC developmental abnormalities (PubMed:18066067). Embryonic fibroblasts
CC obtained from null mutant mice do not express Akirin1
CC (PubMed:18066067). {ECO:0000269|PubMed:18066067}.
CC -!- MISCELLANEOUS: 'Akiraka ni suru' means 'making things clear' in
CC Japanese. The name is given based on the presence of the clear nuclear
CC localization signal. {ECO:0000305|PubMed:18066067}.
CC -!- SIMILARITY: Belongs to the akirin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95077.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB041594; BAA95077.1; ALT_INIT; mRNA.
DR EMBL; AK146017; BAE26835.1; -; mRNA.
DR EMBL; AK159632; BAE35246.1; -; mRNA.
DR EMBL; AK160087; BAE35618.1; -; mRNA.
DR EMBL; AK168201; BAE40161.1; -; mRNA.
DR EMBL; AK168214; BAE40172.1; -; mRNA.
DR EMBL; AK168530; BAE40408.1; -; mRNA.
DR EMBL; BC003291; AAH03291.1; -; mRNA.
DR CCDS; CCDS18619.1; -.
DR RefSeq; NP_075912.2; NM_023423.3.
DR AlphaFoldDB; Q99LF1; -.
DR SMR; Q99LF1; -.
DR STRING; 10090.ENSMUSP00000099696; -.
DR iPTMnet; Q99LF1; -.
DR PhosphoSitePlus; Q99LF1; -.
DR jPOST; Q99LF1; -.
DR MaxQB; Q99LF1; -.
DR PaxDb; Q99LF1; -.
DR PeptideAtlas; Q99LF1; -.
DR PRIDE; Q99LF1; -.
DR ProteomicsDB; 282065; -.
DR Antibodypedia; 31846; 134 antibodies from 21 providers.
DR DNASU; 68050; -.
DR Ensembl; ENSMUST00000102636; ENSMUSP00000099696; ENSMUSG00000023075.
DR GeneID; 68050; -.
DR KEGG; mmu:68050; -.
DR UCSC; uc008upv.1; mouse.
DR CTD; 79647; -.
DR MGI; MGI:1915300; Akirin1.
DR VEuPathDB; HostDB:ENSMUSG00000023075; -.
DR eggNOG; KOG4330; Eukaryota.
DR GeneTree; ENSGT00940000158787; -.
DR HOGENOM; CLU_119227_0_0_1; -.
DR InParanoid; Q99LF1; -.
DR OMA; TSESHPH; -.
DR OrthoDB; 1420469at2759; -.
DR PhylomeDB; Q99LF1; -.
DR TreeFam; TF317123; -.
DR BioGRID-ORCS; 68050; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Akirin1; mouse.
DR PRO; PR:Q99LF1; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q99LF1; protein.
DR Bgee; ENSMUSG00000023075; Expressed in lens of camera-type eye and 108 other tissues.
DR Genevisible; Q99LF1; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0014839; P:myoblast migration involved in skeletal muscle regeneration; IMP:UniProtKB.
DR GO; GO:1902725; P:negative regulation of satellite cell differentiation; IMP:UniProtKB.
DR GO; GO:1902723; P:negative regulation of skeletal muscle satellite cell proliferation; IMP:UniProtKB.
DR GO; GO:0010592; P:positive regulation of lamellipodium assembly; IMP:UniProtKB.
DR GO; GO:0010759; P:positive regulation of macrophage chemotaxis; IMP:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR InterPro; IPR024132; Akirin.
DR PANTHER; PTHR13293; PTHR13293; 1.
PE 1: Evidence at protein level;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..191
FT /note="Akirin-1"
FT /id="PRO_0000274319"
FT REGION 17..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 23..28
FT /note="Nuclear localization signal"
FT MOTIF 188..191
FT /note="SYVS motif"
FT /evidence="ECO:0000250|UniProtKB:Q53H80"
FT COMPBIAS 27..60
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 71
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9L7"
SQ SEQUENCE 191 AA; 21676 MW; 52AFC483184A86A7 CRC64;
MACGATLKRP MEFEAALLSP GSPKRRRCAP LPGPTPGLRP PDAEPPPLQM QTPPASLQQP
APPGSERRLP TPEQIFQNIK QEYNRYQRWR HLEVVLSQSE ACTSETQPSS SALTAPGSPG
AFWMKKDQPT FTLRQVGIIC ERLLKDYEDK VREEYEQILS TKLAEQYESF VKFTHDQIMR
RYGTRPTSYV S
