SYHM_HUMAN
ID SYHM_HUMAN Reviewed; 506 AA.
AC P49590; B4DDY8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Histidine--tRNA ligase, mitochondrial;
DE EC=6.1.1.21 {ECO:0000269|PubMed:21464306};
DE AltName: Full=Histidine--tRNA ligase-like;
DE AltName: Full=Histidyl-tRNA synthetase;
DE Short=HisRS;
DE Flags: Precursor;
GN Name=HARS2; Synonyms=HARSL, HARSR, HO3;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=7755634; DOI=10.1006/bbrc.1995.1696;
RA O'Hanlon T.P., Raben N., Miller F.W.;
RT "A novel gene oriented in a head-to-head configuration with the human
RT histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a
RT polypeptide homologous to HRS.";
RL Biochem. Biophys. Res. Commun. 210:556-566(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Skin;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-444, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [13]
RP VARIANTS PRLTS2 VAL-200 AND LEU-368, CHARACTERIZATION OF VARIANTS PRLTS2
RP VAL-200 AND LEU-368, SUBUNIT, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND
RP FUNCTION.
RX PubMed=21464306; DOI=10.1073/pnas.1103471108;
RA Pierce S.B., Chisholm K.M., Lynch E.D., Lee M.K., Walsh T., Opitz J.M.,
RA Li W., Klevit R.E., King M.C.;
RT "Mutations in mitochondrial histidyl tRNA synthetase HARS2 cause ovarian
RT dysgenesis and sensorineural hearing loss of Perrault syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:6543-6548(2011).
RN [14]
RP VARIANTS PRLTS2 GLN-46; GLU-58; LYS-87; CYS-150 AND GLN-327.
RX PubMed=31449985; DOI=10.1016/j.ejmg.2019.103733;
RA Karstensen H.G., Rendtorff N.D., Hindbaek L.S., Colombo R., Stein A.,
RA Birkebaek N.H., Hartmann-Petersen R., Lindorff-Larsen K., Hoejland A.T.,
RA Petersen M.B., Tranebjaerg L.;
RT "Novel HARS2 missense variants identified in individuals with sensorineural
RT hearing impairment and Perrault syndrome.";
RL Eur. J. Med. Genet. 2019:103733-103733(2019).
CC -!- FUNCTION: Mitochondrial aminoacyl-tRNA synthetase that catalyzes the
CC ATP-dependent ligation of histidine to the 3'-end of its cognate tRNA,
CC via the formation of an aminoacyl-adenylate intermediate (His-AMP).
CC {ECO:0000269|PubMed:21464306}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC Evidence={ECO:0000269|PubMed:21464306};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21464306}.
CC -!- INTERACTION:
CC P49590; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-3909030, EBI-741181;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:21464306}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49590-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49590-2; Sequence=VSP_055133;
CC -!- TISSUE SPECIFICITY: A high level expression is seen in the heart,
CC kidney and skeletal muscle while a lower level expression is seen in
CC the brain and liver.
CC -!- DISEASE: Perrault syndrome 2 (PRLTS2) [MIM:614926]: A sex-influenced
CC disorder characterized by sensorineural deafness in both males and
CC females and ovarian dysgenesis in females. Affected females have
CC primary amenorrhea, streak gonads, and infertility, whereas affected
CC males show normal pubertal development and are fertile.
CC {ECO:0000269|PubMed:21464306, ECO:0000269|PubMed:31449985}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U18936; AAA73972.1; -; Genomic_DNA.
DR EMBL; U18937; AAA73974.1; -; mRNA.
DR EMBL; AK293390; BAG56899.1; -; mRNA.
DR EMBL; AC116353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62019.1; -; Genomic_DNA.
DR EMBL; BC007680; AAH07680.1; -; mRNA.
DR EMBL; BC014982; AAH14982.1; -; mRNA.
DR CCDS; CCDS4238.1; -. [P49590-1]
DR CCDS; CCDS64267.1; -. [P49590-2]
DR PIR; I38913; I38913.
DR PIR; I38915; I38915.
DR RefSeq; NP_001265660.1; NM_001278731.1. [P49590-2]
DR RefSeq; NP_001265661.1; NM_001278732.1.
DR RefSeq; NP_036340.1; NM_012208.3. [P49590-1]
DR AlphaFoldDB; P49590; -.
DR SMR; P49590; -.
DR BioGRID; 117006; 223.
DR DIP; DIP-59626N; -.
DR IntAct; P49590; 37.
DR MINT; P49590; -.
DR STRING; 9606.ENSP00000230771; -.
DR iPTMnet; P49590; -.
DR MetOSite; P49590; -.
DR PhosphoSitePlus; P49590; -.
DR BioMuta; HARS2; -.
DR EPD; P49590; -.
DR jPOST; P49590; -.
DR MassIVE; P49590; -.
DR MaxQB; P49590; -.
DR PaxDb; P49590; -.
DR PeptideAtlas; P49590; -.
DR PRIDE; P49590; -.
DR ProteomicsDB; 3907; -.
DR ProteomicsDB; 56026; -. [P49590-1]
DR Antibodypedia; 27080; 218 antibodies from 23 providers.
DR DNASU; 23438; -.
DR Ensembl; ENST00000230771.9; ENSP00000230771.3; ENSG00000112855.17. [P49590-1]
DR Ensembl; ENST00000508522.5; ENSP00000423616.1; ENSG00000112855.17. [P49590-2]
DR Ensembl; ENST00000645749.1; ENSP00000494296.1; ENSG00000112855.17. [P49590-1]
DR GeneID; 23438; -.
DR KEGG; hsa:23438; -.
DR MANE-Select; ENST00000230771.9; ENSP00000230771.3; NM_012208.4; NP_036340.1.
DR UCSC; uc003lgx.5; human. [P49590-1]
DR CTD; 23438; -.
DR DisGeNET; 23438; -.
DR GeneCards; HARS2; -.
DR GeneReviews; HARS2; -.
DR HGNC; HGNC:4817; HARS2.
DR HPA; ENSG00000112855; Low tissue specificity.
DR MalaCards; HARS2; -.
DR MIM; 600783; gene.
DR MIM; 614926; phenotype.
DR neXtProt; NX_P49590; -.
DR OpenTargets; ENSG00000112855; -.
DR Orphanet; 2855; Perrault syndrome.
DR PharmGKB; PA29192; -.
DR VEuPathDB; HostDB:ENSG00000112855; -.
DR eggNOG; KOG1936; Eukaryota.
DR GeneTree; ENSGT00390000005922; -.
DR HOGENOM; CLU_025113_4_2_1; -.
DR InParanoid; P49590; -.
DR OMA; YQIQKVW; -.
DR OrthoDB; 1065556at2759; -.
DR PhylomeDB; P49590; -.
DR TreeFam; TF300652; -.
DR BRENDA; 6.1.1.21; 2681.
DR PathwayCommons; P49590; -.
DR Reactome; R-HSA-379726; Mitochondrial tRNA aminoacylation.
DR SignaLink; P49590; -.
DR BioGRID-ORCS; 23438; 353 hits in 1085 CRISPR screens.
DR GeneWiki; HARS2; -.
DR GenomeRNAi; 23438; -.
DR Pharos; P49590; Tbio.
DR PRO; PR:P49590; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; P49590; protein.
DR Bgee; ENSG00000112855; Expressed in cerebellar hemisphere and 186 other tissues.
DR ExpressionAtlas; P49590; baseline and differential.
DR Genevisible; P49590; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IDA:WormBase.
DR GO; GO:0042802; F:identical protein binding; IPI:WormBase.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IDA:WormBase.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR GO; GO:0006418; P:tRNA aminoacylation for protein translation; TAS:Reactome.
DR CDD; cd00773; HisRS-like_core; 1.
DR CDD; cd00859; HisRS_anticodon; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR InterPro; IPR033656; HisRS_anticodon.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00442; hisS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Aminoacyl-tRNA synthetase; ATP-binding;
KW Deafness; Disease variant; Ligase; Mitochondrion; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..506
FT /note="Histidine--tRNA ligase, mitochondrial"
FT /id="PRO_0000136336"
FT BINDING 131..133
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 158
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 174
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 178
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 327
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT BINDING 331..332
FT /ligand="L-histidine"
FT /ligand_id="ChEBI:CHEBI:57595"
FT /evidence="ECO:0000250|UniProtKB:P12081"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 444
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 37..61
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055133"
FT VARIANT 46
FT /note="L -> Q (in PRLTS2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31449985"
FT /id="VAR_083046"
FT VARIANT 58
FT /note="K -> E (in PRLTS2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31449985"
FT /id="VAR_083047"
FT VARIANT 87
FT /note="R -> K (in PRLTS2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31449985"
FT /id="VAR_083048"
FT VARIANT 150
FT /note="R -> C (in PRLTS2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31449985"
FT /id="VAR_083049"
FT VARIANT 200
FT /note="L -> V (in PRLTS2; the mutant protein is expressed,
FT can dimerize and localizes to the mitochondria; has
FT significantly decreased enzymatic activity compared to
FT wild-type; dbSNP:rs397515410)"
FT /evidence="ECO:0000269|PubMed:21464306"
FT /id="VAR_069532"
FT VARIANT 327
FT /note="R -> Q (in PRLTS2; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:31449985"
FT /id="VAR_083050"
FT VARIANT 368
FT /note="V -> L (in PRLTS2; the mutant protein is expressed,
FT can dimerize and localizes to the mitochondria; has
FT significantly decreased enzymatic activity compared to
FT wild-type; dbSNP:rs376177973)"
FT /evidence="ECO:0000269|PubMed:21464306"
FT /id="VAR_069533"
SQ SEQUENCE 506 AA; 56888 MW; E1CE879837AE26E7 CRC64;
MPLLGLLPRR AWASLLSQLL RPPCASCTGA VRCQSQVAEA VLTSQLKAHQ EKPNFIIKTP
KGTRDLSPQH MVVREKILDL VISCFKRHGA KGMDTPAFEL KETLTEKYGE DSGLMYDLKD
QGGELLSLRY DLTVPFARYL AMNKVKKMKR YHVGKVWRRE SPTIVQGRYR EFCQCDFDIA
GQFDPMIPDA ECLKIMCEIL SGLQLGDFLI KVNDRRIVDG MFAVCGVPES KFRAICSSID
KLDKMAWKDV RHEMVVKKGL APEVADRIGD YVQCHGGVSL VEQMFQDPRL SQNKQALEGL
GDLKLLFEYL TLFGIADKIS FDLSLARGLD YYTGVIYEAV LLQTPTQAGE EPLNVGSVAA
GGRYDGLVGM FDPKGHKVPC VGLSIGVERI FYIVEQRMKT KGEKVRTTET QVFVATPQKN
FLQERLKLIA ELWDSGIKAE MLYKNNPKLL TQLHYCESTG IPLVVIIGEQ ELKEGVIKIR
SVASREEVAI KRENFVAEIQ KRLSES
