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 24-JAN-2024, entry version 191. 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; 234. DR DIP; DIP-59626N; -. DR IntAct; P49590; 38. DR MINT; P49590; -. DR STRING; 9606.ENSP00000494965; -. DR iPTMnet; P49590; -. DR MetOSite; P49590; -. DR PhosphoSitePlus; P49590; -. DR SwissPalm; P49590; -. DR BioMuta; HARS2; -. DR EPD; P49590; -. DR jPOST; P49590; -. DR MassIVE; P49590; -. DR MaxQB; P49590; -. DR PaxDb; 9606-ENSP00000230771; -. DR PeptideAtlas; P49590; -. DR ProteomicsDB; 3907; -. DR ProteomicsDB; 56026; -. [P49590-1] DR Pumba; P49590; -. DR Antibodypedia; 27080; 245 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 AGR; HGNC:4817; -. 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; 642945; Perrault syndrome type 1. DR Orphanet; 642976; Perrault syndrome type 2. 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; 5476704at2759; -. 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; 384 hits in 1165 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 188 other cell types or tissues. DR ExpressionAtlas; P49590; baseline and differential. 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; 3.40.50.800; Anticodon-binding domain; 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 NCBIfam; TIGR00442; hisS; 1. DR PANTHER; PTHR11476:SF6; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11476; HISTIDYL-TRNA SYNTHETASE; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF13393; tRNA-synt_His; 1. DR PIRSF; PIRSF001549; His-tRNA_synth; 1. DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1. DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. DR Genevisible; P49590; HS. 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; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31449985" FT /id="VAR_083046" FT VARIANT 58 FT /note="K -> E (in PRLTS2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31449985" FT /id="VAR_083047" FT VARIANT 87 FT /note="R -> K (in PRLTS2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31449985" FT /id="VAR_083048" FT VARIANT 150 FT /note="R -> C (in PRLTS2; uncertain 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; uncertain 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 //