ANR16_MOUSE
ID ANR16_MOUSE Reviewed; 361 AA.
AC A2AS55; Q8BH84;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ankyrin repeat domain-containing protein 16 {ECO:0000305};
GN Name=Ankrd16 {ECO:0000312|MGI:MGI:2444796};
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Heart, and Lung;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AARS, DOMAIN, DISRUPTION
RP PHENOTYPE, TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-102; LYS-135 AND
RP LYS-165.
RX PubMed=29769718; DOI=10.1038/s41586-018-0137-8;
RA Vo M.N., Terrey M., Lee J.W., Roy B., Moresco J.J., Sun L., Fu H., Liu Q.,
RA Weber T.G., Yates J.R. III, Fredrick K., Schimmel P., Ackerman S.L.;
RT "ANKRD16 prevents neuron loss caused by an editing-defective tRNA
RT synthetase.";
RL Nature 557:510-515(2018).
CC -!- FUNCTION: Required to prevent the misactivation of serine (Ser) with
CC tRNA(Ala) by promoting the hydrolysis of Ser-mischarged tRNA(Ala),
CC thereby playing a role in translational fidelity (PubMed:29769718).
CC Binds directly to the catalytic domain of AARS/AlaRS and captures Ser
CC that is misactivated by AARS/AlaRS, preventing the charging of Ser
CC adenylates to tRNA(Ala) and precluding Ser misincorporation in nascent
CC peptides (PubMed:29769718). {ECO:0000269|PubMed:29769718}.
CC -!- SUBUNIT: Interacts with AARS; the interaction is direct.
CC {ECO:0000269|PubMed:29769718}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29769718}. Nucleus
CC {ECO:0000269|PubMed:29769718}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A2AS55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2AS55-2; Sequence=VSP_031593, VSP_031594;
CC -!- TISSUE SPECIFICITY: Widely expressed in brain (at protein level).
CC {ECO:0000269|PubMed:29769718}.
CC -!- DOMAIN: Side chains of Lys-102, Lys-135 and Lys-165 capture Ser that is
CC misactivated by AARS/AlaRS. {ECO:0000269|PubMed:29769718}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:29769718). Loss of
CC Ankrd16 in mice with a 'sticky' phenotype (mice homozygous for the
CC variant 'Glu-734' in Aars/AlaRS) results in early embryonic lethality
CC (PubMed:29769718). Conditional deletion in postnatal Purkinje cells in
CC mice with a 'sticky' phenotype exacerbates the 'sticky' phenotype and
CC causes widespread protein aggregation and neuron loss
CC (PubMed:29769718). {ECO:0000269|PubMed:29769718}.
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DR EMBL; AK052460; BAC35002.1; -; mRNA.
DR EMBL; AK085853; BAC39552.1; -; mRNA.
DR EMBL; AL845548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC116229; AAI16230.1; -; mRNA.
DR EMBL; BC116230; AAI16231.1; -; mRNA.
DR CCDS; CCDS50502.1; -. [A2AS55-1]
DR RefSeq; NP_796242.2; NM_177268.4. [A2AS55-1]
DR AlphaFoldDB; A2AS55; -.
DR SMR; A2AS55; -.
DR STRING; 10090.ENSMUSP00000052056; -.
DR PhosphoSitePlus; A2AS55; -.
DR EPD; A2AS55; -.
DR MaxQB; A2AS55; -.
DR PaxDb; A2AS55; -.
DR PRIDE; A2AS55; -.
DR ProteomicsDB; 296254; -. [A2AS55-1]
DR ProteomicsDB; 296255; -. [A2AS55-2]
DR Antibodypedia; 51456; 34 antibodies from 15 providers.
DR DNASU; 320816; -.
DR Ensembl; ENSMUST00000056108; ENSMUSP00000052056; ENSMUSG00000047909. [A2AS55-1]
DR GeneID; 320816; -.
DR KEGG; mmu:320816; -.
DR UCSC; uc008ijg.2; mouse. [A2AS55-2]
DR UCSC; uc012bqv.1; mouse. [A2AS55-1]
DR CTD; 54522; -.
DR MGI; MGI:2444796; Ankrd16.
DR VEuPathDB; HostDB:ENSMUSG00000047909; -.
DR eggNOG; KOG0504; Eukaryota.
DR GeneTree; ENSGT00940000153969; -.
DR InParanoid; A2AS55; -.
DR OMA; QYEPDCK; -.
DR OrthoDB; 1073161at2759; -.
DR PhylomeDB; A2AS55; -.
DR TreeFam; TF329520; -.
DR BioGRID-ORCS; 320816; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ankrd16; mouse.
DR PRO; PR:A2AS55; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; A2AS55; protein.
DR Bgee; ENSMUSG00000047909; Expressed in metanephric renal vesicle and 232 other tissues.
DR ExpressionAtlas; A2AS55; baseline and differential.
DR Genevisible; A2AS55; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR Gene3D; 1.25.40.20; -; 3.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF13637; Ank_4; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 9.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; ANK repeat; Cytoplasm; Nucleus; Reference proteome;
KW Repeat.
FT CHAIN 1..361
FT /note="Ankyrin repeat domain-containing protein 16"
FT /id="PRO_0000320068"
FT REPEAT 36..66
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 70..99
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 103..132
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 136..165
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 170..200
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 204..233
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 238..268
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 273..302
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT REPEAT 306..335
FT /note="ANK 9"
FT /evidence="ECO:0000255"
FT SITE 102
FT /note="Required to capture Ser that is misactivated by
FT AARS/AlaRS"
FT /evidence="ECO:0000269|PubMed:29769718"
FT SITE 135
FT /note="Required to capture Ser that is misactivated by
FT AARS/AlaRS"
FT /evidence="ECO:0000269|PubMed:29769718"
FT SITE 165
FT /note="Required to capture Ser that is misactivated by
FT AARS/AlaRS"
FT /evidence="ECO:0000269|PubMed:29769718"
FT VAR_SEQ 179..187
FT /note="AMHGCLEAV -> GTPCKLWSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031593"
FT VAR_SEQ 188..361
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_031594"
FT MUTAGEN 102
FT /note="K->R: In ANKRD16(3XR); abolished ability to enhance
FT hydrolysis of Ser-mischarged tRNA(Ala); when associated
FT with R-135 and R-165."
FT /evidence="ECO:0000269|PubMed:29769718"
FT MUTAGEN 135
FT /note="K->R: In ANKRD16(3XR); abolished ability to enhance
FT hydrolysis of Ser-mischarged tRNA(Ala); when associated
FT with R-102 and R-165."
FT /evidence="ECO:0000269|PubMed:29769718"
FT MUTAGEN 165
FT /note="K->R: In ANKRD16(3XR); abolished ability to enhance
FT hydrolysis of Ser-mischarged tRNA(Ala); when associated
FT with R-102 and R-135."
FT /evidence="ECO:0000269|PubMed:29769718"
SQ SEQUENCE 361 AA; 39776 MW; 4570C30C3B1316CA CRC64;
MALPGDPRRL CRLVQEGRLR DLQEELAVAR GCRGPAGDTL LHCAARHGRQ DILAYLVEAW
SMDIEATNRD YKRPLHEAAS MGHRDCVRYL LGRGAVVDSL KKADWTPLMM ACTRKNLDVI
QDLVEHGANP LLKNKDGWNS FHIASREGHP VILRYLLTVC PDAWKTESNI RRTPLHTAAM
HGCLEAVQVL LERCHYEPDC RDNCGVTPFM DAIQCGHVSI AKLLLEQHKA CSSAADSMGA
QALHRAAVTG QDEAIRFLVC GLGIDVDVRA KSSQLTALHY AAKEGQTNTV QTLLSLGADI
NSTDERNRSV LHLACAGQHV ACTRLLLQSG LKDSEDLTGT LAQQLTRSVD ILQDFDHDVK
S
