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Serine--tRNA ligase, mitochondrial (EC 6.1.1.11) (SerRSmt) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase)

 SYSM_HUMAN              Reviewed;         518 AA.
Q9NP81; A6NHW7; B4DE10; Q9BVP3;
10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
05-DEC-2018, entry version 166.
RecName: Full=Serine--tRNA ligase, mitochondrial;
EC=6.1.1.11;
AltName: Full=SerRSmt;
AltName: Full=Seryl-tRNA synthetase;
Short=SerRS;
AltName: Full=Seryl-tRNA(Ser/Sec) synthetase;
Flags: Precursor;
Name=SARS2; Synonyms=SARSM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10764807; DOI=10.1074/jbc.M908473199;
Yokogawa T., Shimada N., Takeuchi N., Benkowski L., Suzuki T.,
Omori A., Ueda T., Nishikawa K., Spremulli L.L., Watanabe K.;
"Characterization and tRNA recognition of mammalian mitochondrial
seryl-tRNA synthetase.";
J. Biol. Chem. 275:19913-19920(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[7]
VARIANT HUPRAS GLY-390.
PubMed=21255763; DOI=10.1016/j.ajhg.2010.12.010;
Belostotsky R., Ben-Shalom E., Rinat C., Becker-Cohen R.,
Feinstein S., Zeligson S., Segel R., Elpeleg O., Nassar S.,
Frishberg Y.;
"Mutations in the mitochondrial seryl-tRNA synthetase cause
hyperuricemia, pulmonary hypertension, renal failure in infancy and
alkalosis, HUPRA syndrome.";
Am. J. Hum. Genet. 88:193-200(2011).
-!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also
probably able to aminoacylate tRNA(Sec) with serine, to form the
misacylated tRNA L-seryl-tRNA(Sec), which will be further
converted into selenocysteinyl-tRNA(Sec).
{ECO:0000250|UniProtKB:Q9N0F3}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) +
L-seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
Evidence={ECO:0000250|UniProtKB:Q9N0F3};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) +
L-seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
Evidence={ECO:0000250|UniProtKB:Q9N0F3};
-!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step
1/1.
-!- SUBUNIT: Homodimer. The tRNA molecule probably binds across the
dimer. {ECO:0000250|UniProtKB:Q9N0F3}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix
{ECO:0000250|UniProtKB:Q9N0F3}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NP81-1; Sequence=Displayed;
Name=2;
IsoId=Q9NP81-2; Sequence=VSP_043020;
Note=No experimental confirmation available.;
-!- DOMAIN: Consists of two distinct domains, a catalytic core and a
N-terminal extension that is involved in tRNA binding.
{ECO:0000250|UniProtKB:Q9N0F3}.
-!- DISEASE: Hyperuricemia, pulmonary hypertension, renal failure, and
alkalosis syndrome (HUPRAS) [MIM:613845]: A multisystem disorder
characterized by onset in infancy of progressive renal failure
leading to electrolyte imbalances, metabolic alkalosis, pulmonary
hypertension, hypotonia, and delayed development. Affected
individuals are born prematurely. {ECO:0000269|PubMed:21255763}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. Type-1 seryl-tRNA synthetase subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH01020.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB029948; BAA99557.1; -; mRNA.
EMBL; AK000457; BAA91176.1; -; mRNA.
EMBL; AK293414; BAG56921.1; -; mRNA.
EMBL; AC011455; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001020; AAH01020.2; ALT_INIT; mRNA.
EMBL; BC042912; AAH42912.1; -; mRNA.
CCDS; CCDS33017.1; -. [Q9NP81-1]
CCDS; CCDS54265.1; -. [Q9NP81-2]
RefSeq; NP_001139373.1; NM_001145901.1. [Q9NP81-2]
RefSeq; NP_060297.1; NM_017827.3. [Q9NP81-1]
UniGene; Hs.709416; -.
ProteinModelPortal; Q9NP81; -.
SMR; Q9NP81; -.
BioGrid; 120278; 35.
IntAct; Q9NP81; 24.
MINT; Q9NP81; -.
STRING; 9606.ENSP00000472847; -.
iPTMnet; Q9NP81; -.
PhosphoSitePlus; Q9NP81; -.
BioMuta; SARS2; -.
DMDM; 23822219; -.
EPD; Q9NP81; -.
MaxQB; Q9NP81; -.
PaxDb; Q9NP81; -.
PeptideAtlas; Q9NP81; -.
PRIDE; Q9NP81; -.
ProteomicsDB; 81925; -.
ProteomicsDB; 81926; -. [Q9NP81-2]
Ensembl; ENST00000221431; ENSP00000221431; ENSG00000104835. [Q9NP81-1]
Ensembl; ENST00000600042; ENSP00000472847; ENSG00000104835. [Q9NP81-2]
Ensembl; ENST00000634687; ENSP00000489539; ENSG00000283104. [Q9NP81-1]
Ensembl; ENST00000635245; ENSP00000489453; ENSG00000283104. [Q9NP81-2]
GeneID; 54938; -.
KEGG; hsa:54938; -.
UCSC; uc002oka.3; human. [Q9NP81-1]
CTD; 54938; -.
DisGeNET; 54938; -.
EuPathDB; HostDB:ENSG00000104835.14; -.
GeneCards; SARS2; -.
HGNC; HGNC:17697; SARS2.
HPA; HPA052730; -.
HPA; HPA056957; -.
MalaCards; SARS2; -.
MIM; 612804; gene.
MIM; 613845; phenotype.
neXtProt; NX_Q9NP81; -.
OpenTargets; ENSG00000104835; -.
Orphanet; 363694; Hyperuricemia-pulmonary hypertension-renal failure-alkalosis syndrome.
PharmGKB; PA134899753; -.
eggNOG; KOG2509; Eukaryota.
eggNOG; COG0172; LUCA.
GeneTree; ENSGT00940000153792; -.
HOGENOM; HOG000035937; -.
HOVERGEN; HBG023869; -.
InParanoid; Q9NP81; -.
KO; K01875; -.
OMA; KHIRQNP; -.
OrthoDB; EOG091G05BT; -.
PhylomeDB; Q9NP81; -.
BRENDA; 6.1.1.11; 2681.
Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
UniPathway; UPA00906; UER00895.
ChiTaRS; SARS2; human.
GeneWiki; SARS2; -.
GenomeRNAi; 54938; -.
PRO; PR:Q9NP81; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000104835; Expressed in 88 organ(s), highest expression level in adult mammalian kidney.
CleanEx; HS_SARS2; -.
ExpressionAtlas; Q9NP81; baseline and differential.
Genevisible; Q9NP81; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0004828; F:serine-tRNA ligase activity; ISS:UniProtKB.
GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006434; P:seryl-tRNA aminoacylation; ISS:UniProtKB.
GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
CDD; cd00770; SerRS_core; 1.
InterPro; IPR002314; aa-tRNA-synt_IIb.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR002317; Ser-tRNA-ligase_type_1.
InterPro; IPR033729; SerRS_core.
InterPro; IPR010978; tRNA-bd_arm.
PANTHER; PTHR11778; PTHR11778; 1.
Pfam; PF00587; tRNA-synt_2b; 1.
PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
PRINTS; PR00981; TRNASYNTHSER.
SUPFAM; SSF46589; SSF46589; 1.
TIGRFAMs; TIGR00414; serS; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase;
ATP-binding; Complete proteome; Ligase; Mitochondrion;
Nucleotide-binding; Polymorphism; Protein biosynthesis;
Reference proteome; Transit peptide.
TRANSIT 1 34 Mitochondrion.
{ECO:0000250|UniProtKB:Q9N0F3}.
CHAIN 35 518 Serine--tRNA ligase, mitochondrial.
/FTId=PRO_0000035822.
NP_BIND 330 332 ATP. {ECO:0000250|UniProtKB:Q9N0F3}.
NP_BIND 418 421 ATP. {ECO:0000250|UniProtKB:Q9N0F3}.
REGION 299 301 L-serine binding.
{ECO:0000250|UniProtKB:Q9N0F3}.
BINDING 345 345 ATP; via amide nitrogen and carbonyl
oxygen. {ECO:0000250|UniProtKB:Q9N0F3}.
BINDING 352 352 L-serine. {ECO:0000250|UniProtKB:Q9N0F3}.
BINDING 453 453 L-serine. {ECO:0000250|UniProtKB:Q9N0F3}.
MOD_RES 110 110 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9JJL8}.
MOD_RES 195 195 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q9JJL8}.
VAR_SEQ 132 155 DPKYQGLRARGREIRKELVHLYPR -> VRLDPGAGSIFGP
TFLPFPGQLSLLV (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043020.
VARIANT 35 35 T -> A (in dbSNP:rs34264048).
/FTId=VAR_052645.
VARIANT 83 83 S -> L (in dbSNP:rs34050897).
/FTId=VAR_052646.
VARIANT 390 390 D -> G (in HUPRAS; dbSNP:rs727502784).
{ECO:0000269|PubMed:21255763}.
/FTId=VAR_065820.
SEQUENCE 518 AA; 58283 MW; C6516A9527B34EB7 CRC64;
MAASMARRLW PLLTRRGFRP RGGCISNDSP RRSFTTEKRN RNLLYEYARE GYSALPQLDI
ERFCACPEEA AHALELRKGE LRSADLPAII STWQELRQLQ EQIRSLEEEK AAVTEAVRAL
LANQDSGEVQ QDPKYQGLRA RGREIRKELV HLYPREAQLE EQFYLQALKL PNQTHPDVPV
GDESQARVLH MVGDKPVFSF QPRGHLEIGE KLDIIRQKRL SHVSGHRSYY LRGAGALLQH
GLVNFTFNKL LRRGFTPMTV PDLLRGAVFE GCGMTPNANP SQIYNIDPAR FKDLNLAGTA
EVGLAGYFMD HTVAFRDLPV RMVCSSTCYR AETNTGQEPR GLYRVHHFTK VEMFGVTGPG
LEQSSQLLEE FLSLQMEILT ELGLHFRVLD MPTQELGLPA YRKFDIEAWM PGRGRFGEVT
SASNCTDFQS RRLHIMFQTE AGELQFAHTV NATACAVPRL LIALLESNQQ KDGSVLVPPA
LQSYLGTDRI TAPTHVPLQY IGPNQPRKPG LPGQPAVS


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