ID SYCC_MOUSE Reviewed; 831 AA.
AC Q9ER72; O88303; Q8BP81; Q8CAY7; Q8CCE3; Q8K0S4; Q9ER68;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 24-JAN-2024, entry version 165.
DE RecName: Full=Cysteine--tRNA ligase, cytoplasmic;
DE EC=6.1.1.16 {ECO:0000250|UniProtKB:P49589};
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
GN Name=Cars1; Synonyms=Cars;
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 (ISOFORM 1).
RC STRAIN=129/Sv;
RX PubMed=11063728; DOI=10.1093/hmg/9.18.2691;
RA Engemann S., Stroedicke M., Paulsen M., Franck O., Reinhardt R., Lane N.,
RA Reik W., Walter J.;
RT "Sequence and functional comparison in the Beckwith-Wiedemann region:
RT implications for a novel imprinting centre and extended imprinting.";
RL Hum. Mol. Genet. 9:2691-2706(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Skin, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Retina;
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 NUCLEOTIDE SEQUENCE OF 129-614.
RC STRAIN=C57BL/10;
RA Yatsuki H., Mukai T.;
RT "Mouse cysteinyl-tRNA synthetase mRNA, partial cds.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102 AND SER-390, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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: Catalyzes the ATP-dependent ligation of cysteine to
CC tRNA(Cys). {ECO:0000250|UniProtKB:P49589}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC ChEBI:CHEBI:456215; EC=6.1.1.16;
CC Evidence={ECO:0000250|UniProtKB:P49589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17774;
CC Evidence={ECO:0000250|UniProtKB:P49589};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P21888};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P21888};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49589}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49589}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ER72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ER72-2; Sequence=VSP_010258;
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AJ276505; CAC16398.1; -; Genomic_DNA.
DR EMBL; AJ276796; CAC16403.1; -; mRNA.
DR EMBL; AK033328; BAC28234.1; -; mRNA.
DR EMBL; AK037227; BAC29766.1; -; mRNA.
DR EMBL; AK077558; BAC36862.1; -; mRNA.
DR EMBL; BC030473; AAH30473.1; -; mRNA.
DR EMBL; BC054717; AAH54717.1; -; mRNA.
DR EMBL; BC058954; AAH58954.1; -; mRNA.
DR EMBL; AB015589; BAA29032.1; -; mRNA.
DR CCDS; CCDS40198.1; -. [Q9ER72-1]
DR CCDS; CCDS57597.1; -. [Q9ER72-2]
DR RefSeq; NP_001239522.1; NM_001252593.1. [Q9ER72-2]
DR RefSeq; NP_038770.3; NM_013742.5. [Q9ER72-1]
DR AlphaFoldDB; Q9ER72; -.
DR SMR; Q9ER72; -.
DR BioGRID; 205152; 17.
DR STRING; 10090.ENSMUSP00000010899; -.
DR GlyGen; Q9ER72; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9ER72; -.
DR PhosphoSitePlus; Q9ER72; -.
DR SwissPalm; Q9ER72; -.
DR EPD; Q9ER72; -.
DR jPOST; Q9ER72; -.
DR MaxQB; Q9ER72; -.
DR PaxDb; 10090-ENSMUSP00000010899; -.
DR PeptideAtlas; Q9ER72; -.
DR ProteomicsDB; 258681; -. [Q9ER72-1]
DR ProteomicsDB; 258682; -. [Q9ER72-2]
DR Pumba; Q9ER72; -.
DR Antibodypedia; 1044; 273 antibodies from 30 providers.
DR DNASU; 27267; -.
DR Ensembl; ENSMUST00000010899.14; ENSMUSP00000010899.8; ENSMUSG00000010755.18. [Q9ER72-1]
DR Ensembl; ENSMUST00000105909.4; ENSMUSP00000101529.4; ENSMUSG00000010755.18. [Q9ER72-2]
DR GeneID; 27267; -.
DR KEGG; mmu:27267; -.
DR UCSC; uc009kpn.2; mouse. [Q9ER72-1]
DR AGR; MGI:1351477; -.
DR CTD; 833; -.
DR MGI; MGI:1351477; Cars1.
DR VEuPathDB; HostDB:ENSMUSG00000010755; -.
DR eggNOG; KOG1668; Eukaryota.
DR eggNOG; KOG2007; Eukaryota.
DR GeneTree; ENSGT00390000006347; -.
DR HOGENOM; CLU_013528_3_3_1; -.
DR InParanoid; Q9ER72; -.
DR OMA; FHNDMKS; -.
DR OrthoDB; 2140072at2759; -.
DR PhylomeDB; Q9ER72; -.
DR TreeFam; TF300384; -.
DR BioGRID-ORCS; 27267; 24 hits in 80 CRISPR screens.
DR ChiTaRS; Cars; mouse.
DR PRO; PR:Q9ER72; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9ER72; Protein.
DR Bgee; ENSMUSG00000010755; Expressed in retinal neural layer and 254 other cell types or tissues.
DR ExpressionAtlas; Q9ER72; baseline and differential.
DR Genevisible; Q9ER72; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; ISS:UniProtKB.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; ISS:UniProtKB.
DR CDD; cd00672; CysRS_core; 1.
DR CDD; cd10310; GST_C_CysRS_N; 1.
DR Gene3D; 1.20.1050.130; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR NCBIfam; TIGR00435; cysS; 1.
DR PANTHER; PTHR10890:SF3; CYSTEINE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR10890; CYSTEINYL-TRNA SYNTHETASE; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding;
KW Cytoplasm; Ligase; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P49589"
FT CHAIN 2..831
FT /note="Cysteine--tRNA ligase, cytoplasmic"
FT /id="PRO_0000159551"
FT REGION 736..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 140..150
FT /note="'HIGH' region"
FT MOTIF 184..187
FT /note="'KIIK' region"
FT MOTIF 489..493
FT /note="'KMSKS' region"
FT COMPBIAS 736..762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 139
FT /ligand="L-cysteine"
FT /ligand_id="ChEBI:CHEBI:35235"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 179
FT /ligand="L-cysteine"
FT /ligand_id="ChEBI:CHEBI:35235"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 456
FT /ligand="L-cysteine"
FT /ligand_id="ChEBI:CHEBI:35235"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 456
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 460
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P21888"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P49589"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49589"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49589"
FT VAR_SEQ 9..92
FT /note="AADYRSILSISDEAARVQALDQHLSTRSYIQGYSLSQADVDVFRQLSAPPAD
FT SRLFHVARWFRHIEALLGGPQGRDEPCRLQAS -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010258"
FT CONFLICT 161
FT /note="R -> P (in Ref. 3; AAH30473)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="L -> R (in Ref. 3; AAH30473)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="M -> K (in Ref. 2; BAC28234)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="L -> P (in Ref. 4; BAA29032)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="E -> G (in Ref. 2; BAC28234)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="S -> G (in Ref. 1; CAC16398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 831 AA; 94860 MW; 5FE338D27AE32B92 CRC64;
MAGSSAEQAA DYRSILSISD EAARVQALDQ HLSTRSYIQG YSLSQADVDV FRQLSAPPAD
SRLFHVARWF RHIEALLGGP QGRDEPCRLQ ASKGRRVQPQ WSPPAGTEPC RLRLYNSLTR
NKDVFIPQDG KKVTWYCCGP TVYDASHMGH ARSYISFDIL RRVLRDYFQY DVFYCMNITD
IDDKIIRRAR QNYLFEQYRE QKPPATQLLK DVRDAMKPFS VKLSETTDPD KRQMLERIQN
SVKLATEPLE QAVRSSLSGE EVDSKVQVLL EEAKDLLSDW LDSTGGSEVT DNSIFSKLPK
FWEEEFHKDM EALNVLPPDV LTRVSEYVPE IVNFVQKIVD NGYGYASNGS VYFDTAKFAA
SEKHSYGKLV PEAVGDQKAL QEGEGDLSIS ADRLSEKRSP NDFALWKASK PGEPSWPCPW
GKGRPGWHIE CSAMAGTLLG ASMDIHGGGF DLRFPHHDNE LAQSEAYFEN DCWVRYFLHT
GHLTIAGCKM SKSLKNFITI KDALKKHSAR QLRLAFLMHS WKDTLDYSSN TMESALQYEK
FMNEFFLNVK DILRAPVDIT GQFEKWEAEE VELNKNFYGK KTAVHEALCD NIDTRTVMEE
MRALVSQCNL YMAARKAERR RPNRALLENI AMYLTHMLKI FGAIEEESPL GFPVGGPGTN
LNLESTVMPY LQVLSEFREG VRKIAREKKV LEVLQLSDAL RDDILPELGV RFEDHEGLPT
VVKLVDRDTL LKEKEGKKRA EEEKRRKKEE AARKKQEQEA AKLAKMKIPP SEMFLSEVNK
YSKFDENGLP THDTEGKELS KGQAKKLKKL FEAQEKLYKE YLQMLQNGSL Q
//
