AASD1_MOUSE
ID AASD1_MOUSE Reviewed; 412 AA.
AC Q3THG9; Q3UWH8; Q8BVJ6; Q99JS9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Alanyl-tRNA editing protein Aarsd1;
DE AltName: Full=Alanyl-tRNA deacylase alaX;
DE Short=AlaX;
DE Short=AlaXp-II;
DE AltName: Full=Alanyl-tRNA synthetase domain-containing protein 1;
GN Name=Aarsd1; Synonyms=Alax;
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=BALB/cJ, and C57BL/6J; TISSUE=Embryonic head, and Embryonic testis;
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 STRAIN=FVB/N; TISSUE=Mammary gland;
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 FUNCTION AS TRNA(ALA) EDITING PROTEIN.
RX PubMed=18172502; DOI=10.1038/nature06454;
RA Beebe K., Mock M., Merriman E., Schimmel P.;
RT "Distinct domains of tRNA synthetase recognize the same base pair.";
RL Nature 451:90-93(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Pancreas, Spleen, and Testis;
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).
CC -!- FUNCTION: Functions in trans to edit the amino acid moiety from
CC incorrectly charged Ser-tRNA(Ala). {ECO:0000269|PubMed:18172502}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC -!- INTERACTION:
CC Q3THG9; Q62406-1: Irak1; NbExp=4; IntAct=EBI-646572, EBI-488313;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Alax-L subfamily. {ECO:0000305}.
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DR EMBL; AK078016; BAC37098.1; -; mRNA.
DR EMBL; AK136332; BAE22937.1; -; mRNA.
DR EMBL; AK168281; BAE40227.1; -; mRNA.
DR EMBL; BC005711; AAH05711.1; -; mRNA.
DR CCDS; CCDS25467.1; -.
DR RefSeq; NP_659078.1; NM_144829.1.
DR AlphaFoldDB; Q3THG9; -.
DR SMR; Q3THG9; -.
DR BioGRID; 213614; 17.
DR IntAct; Q3THG9; 1.
DR STRING; 10090.ENSMUSP00000067912; -.
DR iPTMnet; Q3THG9; -.
DR PhosphoSitePlus; Q3THG9; -.
DR SwissPalm; Q3THG9; -.
DR EPD; Q3THG9; -.
DR jPOST; Q3THG9; -.
DR MaxQB; Q3THG9; -.
DR PaxDb; Q3THG9; -.
DR PeptideAtlas; Q3THG9; -.
DR PRIDE; Q3THG9; -.
DR ProteomicsDB; 285626; -.
DR DNASU; 69684; -.
DR Ensembl; ENSMUST00000070395; ENSMUSP00000067912; ENSMUSG00000075528.
DR GeneID; 69684; -.
DR KEGG; mmu:69684; -.
DR UCSC; uc007los.1; mouse.
DR CTD; 80755; -.
DR MGI; MGI:1916934; Aarsd1.
DR VEuPathDB; HostDB:ENSMUSG00000075528; -.
DR eggNOG; KOG2105; Eukaryota.
DR GeneTree; ENSGT00940000156241; -.
DR HOGENOM; CLU_004485_7_0_1; -.
DR InParanoid; Q3THG9; -.
DR OMA; CMHTSQH; -.
DR OrthoDB; 910848at2759; -.
DR PhylomeDB; Q3THG9; -.
DR TreeFam; TF323735; -.
DR BioGRID-ORCS; 69684; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Aarsd1; mouse.
DR PRO; PR:Q3THG9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q3THG9; protein.
DR Bgee; ENSMUSG00000075528; Expressed in proximal tubule and 63 other tissues.
DR Genevisible; Q3THG9; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:InterPro.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0002196; F:Ser-tRNA(Ala) hydrolase activity; IDA:MGI.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:InterPro.
DR GO; GO:0006450; P:regulation of translational fidelity; IDA:MGI.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF07973; tRNA_SAD; 1.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Phosphoprotein; Protein biosynthesis;
KW Reference proteome; Zinc.
FT CHAIN 1..412
FT /note="Alanyl-tRNA editing protein Aarsd1"
FT /id="PRO_0000277466"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BTE6"
FT CONFLICT 80
FT /note="D -> G (in Ref. 1; BAE22937)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="L -> M (in Ref. 1; BAE40227)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="L -> H (in Ref. 1; BAE22937)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 412 AA; 44971 MW; 3FFD32304A379B44 CRC64;
MAFLCQRDSY AREFTTTVVS CSPAELQTDA SGGKKEVLSG FHVVLEDTLL FPEGGGQPDD
RGTINDISVL RVTRRGAQAD HFTESPLSPG SQVQVRVDWE RRFDHMQQHS GQHLITAVAD
LLFGLKTTSW ELGRLRSVIE LDSPSVTAEQ VAAIEQSVNQ KIRDRLPVSV RELSLDDPEV
EQVRGRGLPD DHAGPIRVVT IEGVDSNMCC GTHVSNLSDL QVIKILGTEK GKKNKSNLIF
LAGNRVLKWM ERSHGSEKAL TSLLKCGVED HVEAVKKLQN ATKLLQKNNL NLLRDLAVHT
AHSLRSSPAW GGVVTLHRKE GDSEFMNIIA NEIGSEETLL FLTVGDEKGA GLFLLAGPAE
AVETLGPRVA EVLEGKGAGK KGRFQGKATK MSRRAEAQAL LQDYVSTQSA EE
