ANR54_MOUSE
ID ANR54_MOUSE Reviewed; 299 AA.
AC Q91WK7; Q3UPC5; Q3UZL7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ankyrin repeat domain-containing protein 54;
DE AltName: Full=Lyn-interacting ankyrin repeat protein;
GN Name=Ankrd54; Synonyms=Liar;
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=Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=17971504; DOI=10.1152/physiolgenomics.00128.2007;
RA McClintock T.S., Glasser C.E., Bose S.C., Bergman D.A.;
RT "Tissue expression patterns identify mouse cilia genes.";
RL Physiol. Genomics 32:198-206(2008).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-98;
RP ARG-99; LEU-289 AND LEU-291, AND INTERACTION WITH LYN; HCLS1; ITSN2; VAV1;
RP DBNL AND LASP1.
RX PubMed=19064729; DOI=10.1182/blood-2008-04-153452;
RA Samuels A.L., Klinken S.P., Ingley E.;
RT "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that
RT influences erythropoietin-induced differentiation.";
RL Blood 113:3845-3856(2009).
CC -!- FUNCTION: Plays an important role in regulating intracellular signaling
CC events associated with erythroid terminal differentiation.
CC {ECO:0000269|PubMed:19064729}.
CC -!- SUBUNIT: Interacts (via ankyrin repeat region) with LYN (via SH3-
CC domain) in an activation-independent status of LYN. Forms a
CC multiprotein complex with LYN and HCLS1. Interacts with TSN2, VAV1,
CC DBNL AND LASP1. {ECO:0000269|PubMed:19064729}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19064729}. Cytoplasm
CC {ECO:0000269|PubMed:19064729}. Midbody {ECO:0000269|PubMed:19064729}.
CC Note=Shuttles between nucleus and cytoplasm during the cell cycle. EPO
CC stimulation induces nuclear accumulation.
CC -!- TISSUE SPECIFICITY: Expressed in a variety of hemopoietic cell lines
CC and tissue with high levels in testis. Highly expressed in ciliated
CC cells. {ECO:0000269|PubMed:17971504, ECO:0000269|PubMed:19064729}.
CC -!- DEVELOPMENTAL STAGE: Expressed in brachial arches, maxillary process,
CC fore and hind limb buds and in the developing gastrointestinal tract of
CC day 10 embryos.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE25471.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK133785; BAE21840.1; -; mRNA.
DR EMBL; AK143625; BAE25471.1; ALT_FRAME; mRNA.
DR EMBL; BC014743; AAH14743.1; -; mRNA.
DR CCDS; CCDS37139.1; -.
DR RefSeq; NP_659098.1; NM_144849.1.
DR AlphaFoldDB; Q91WK7; -.
DR SMR; Q91WK7; -.
DR BioGRID; 230175; 1.
DR CORUM; Q91WK7; -.
DR IntAct; Q91WK7; 2.
DR STRING; 10090.ENSMUSP00000047042; -.
DR iPTMnet; Q91WK7; -.
DR PhosphoSitePlus; Q91WK7; -.
DR EPD; Q91WK7; -.
DR MaxQB; Q91WK7; -.
DR PaxDb; Q91WK7; -.
DR PRIDE; Q91WK7; -.
DR ProteomicsDB; 281883; -.
DR Antibodypedia; 26115; 139 antibodies from 27 providers.
DR DNASU; 223690; -.
DR Ensembl; ENSMUST00000040676; ENSMUSP00000047042; ENSMUSG00000033055.
DR GeneID; 223690; -.
DR KEGG; mmu:223690; -.
DR UCSC; uc007wsi.1; mouse.
DR CTD; 129138; -.
DR MGI; MGI:2444209; Ankrd54.
DR VEuPathDB; HostDB:ENSMUSG00000033055; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000157805; -.
DR HOGENOM; CLU_072816_0_0_1; -.
DR InParanoid; Q91WK7; -.
DR OMA; DDMGNGA; -.
DR OrthoDB; 1559479at2759; -.
DR PhylomeDB; Q91WK7; -.
DR TreeFam; TF330790; -.
DR BioGRID-ORCS; 223690; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q91WK7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q91WK7; protein.
DR Bgee; ENSMUSG00000033055; Expressed in spermatocyte and 232 other tissues.
DR ExpressionAtlas; Q91WK7; baseline and differential.
DR Genevisible; Q91WK7; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030496; C:midbody; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0019887; F:protein kinase regulator activity; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:MGI.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IDA:MGI.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:MGI.
DR GO; GO:1902531; P:regulation of intracellular signal transduction; IDA:MGI.
DR GO; GO:0045859; P:regulation of protein kinase activity; IDA:MGI.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR SMART; SM00248; ANK; 4.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
PE 1: Evidence at protein level;
KW Acetylation; ANK repeat; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q6NXT1"
FT CHAIN 2..299
FT /note="Ankyrin repeat domain-containing protein 54"
FT /id="PRO_0000274494"
FT REPEAT 108..137
FT /note="ANK 1"
FT REPEAT 141..170
FT /note="ANK 2"
FT REPEAT 174..203
FT /note="ANK 3"
FT REPEAT 207..239
FT /note="ANK 4"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..240
FT /note="LYN-binding"
FT MOTIF 98..116
FT /note="Nuclear localization signal (NLS)"
FT MOTIF 282..292
FT /note="Nuclear export signal (NES)"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q6NXT1"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6NXT1"
FT MUTAGEN 98
FT /note="R->A: Increases the cytoplasmic protein content;
FT when associated with A-99."
FT /evidence="ECO:0000269|PubMed:19064729"
FT MUTAGEN 99
FT /note="R->A: Increases the cytoplasmic protein content;
FT when associated with A-98."
FT /evidence="ECO:0000269|PubMed:19064729"
FT MUTAGEN 289
FT /note="L->A: Accumulation within the nucleus; when
FT associated with A-291."
FT /evidence="ECO:0000269|PubMed:19064729"
FT MUTAGEN 291
FT /note="L->A: Accumulation within the nucleus; when
FT associated with A-289."
FT /evidence="ECO:0000269|PubMed:19064729"
FT CONFLICT 173
FT /note="G -> N (in Ref. 1; BAE21840)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 32486 MW; 88E91A10F1953AC3 CRC64;
MAATGGGADD ESRSGRSSSD GECAVAPEPL AEAGGLVSFA DFGVSLGSGA GLPGRSVGRA
QSSLRYLQVL WQQDVEPRDE LRCKIPAGRL RRAARPHRRL GPTGKEVHAL KRLRDSANAN
DVETVQQLLE DGADPCAADD KGRTALHFAS CNGNDQIVQL LLDHGADPNQ QDGLGNTPLH
LAACTNHVPV ITTLLRGGAR VDALDRAGRT PLHLAKSKLN ILQEGHSQCL EAVRLEVKQI
IHMLREYLER LGRHEQRERL DDLCTRLQMT STKEQVDEVT DLLASFTSLS LQMQSMEKR
