LTO1_HUMAN
ID LTO1_HUMAN Reviewed; 137 AA.
AC Q8WV07; B2R4R2; Q8NFK0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Protein LTO1 homolog {ECO:0000303|PubMed:23318452, ECO:0000305};
DE AltName: Full=Oral cancer-overexpressed protein 1;
DE AltName: Full=Tumor-amplified and overexpressed sequence 1;
GN Name=LTO1 {ECO:0000303|PubMed:23318452, ECO:0000312|HGNC:HGNC:17589};
GN Synonyms=ORAOV1 {ECO:0000312|HGNC:HGNC:17589},
GN TAOS1 {ECO:0000303|PubMed:12172009};
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12172009; DOI=10.1073/pnas.172285799;
RA Huang X., Gollin S.M., Raja S., Godfrey T.E.;
RT "High-resolution mapping of the 11q13 amplicon and identification of a
RT gene, TAOS1, that is amplified and overexpressed in oral cancer cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11369-11374(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Melanoma, and Pancreatic carcinoma;
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-4, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP FUNCTION, AND INTERACTION WITH YAE1.
RX PubMed=23318452; DOI=10.1038/onc.2012.604;
RA Zhai C., Li Y., Mascarenhas C., Lin Q., Li K., Vyrides I., Grant C.M.,
RA Panaretou B.;
RT "The function of ORAOV1/LTO1, a gene that is overexpressed frequently in
RT cancer: essential roles in the function and biogenesis of the ribosome.";
RL Oncogene 33:484-494(2014).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH PYCR1 AND PYCR2.
RX PubMed=24930674; DOI=10.18632/oncotarget.1561;
RA Togashi Y., Arao T., Kato H., Matsumoto K., Terashima M., Hayashi H.,
RA de Velasco M.A., Fujita Y., Kimura H., Yasuda T., Shiozaki H., Nishio K.;
RT "Frequent amplification of ORAOV1 gene in esophageal squamous cell cancer
RT promotes an aggressive phenotype via proline metabolism and ROS
RT production.";
RL Oncotarget 5:2962-2973(2014).
RN [9]
RP FUNCTION.
RX PubMed=26182403; DOI=10.7554/elife.08231;
RA Paul V.D., Muehlenhoff U., Stuempfig M., Seebacher J., Kugler K.G.,
RA Renicke C., Taxis C., Gavin A.C., Pierik A.J., Lill R.;
RT "The deca-GX3 proteins Yae1-Lto1 function as adaptors recruiting the ABC
RT protein Rli1 for iron-sulfur cluster insertion.";
RL Elife 4:E08231-E08231(2015).
CC -!- FUNCTION: The complex LTO1:YAE1 functions as a target specific adapter
CC that probably recruits apo-ABCE1 to the cytosolic iron-sulfur protein
CC assembly (CIA) complex machinery (PubMed:26182403). May be required for
CC biogenesis of the large ribosomal subunit and initiation of translation
CC (PubMed:23318452). May play a role in the regulation of proline
CC metabolism and ROS production (PubMed:24930674).
CC {ECO:0000269|PubMed:23318452, ECO:0000269|PubMed:24930674,
CC ECO:0000269|PubMed:26182403}.
CC -!- SUBUNIT: Forms a complex with YAE1 (PubMed:23318452). Interacts with
CC PYCR1 and PYCR2 (PubMed:24930674). {ECO:0000269|PubMed:23318452,
CC ECO:0000269|PubMed:24930674}.
CC -!- INTERACTION:
CC Q8WV07; O15499: GSC2; NbExp=3; IntAct=EBI-12249832, EBI-19954058;
CC Q8WV07; Q9NRH1: YAE1; NbExp=8; IntAct=EBI-12249832, EBI-712905;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P53846}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in placenta,
CC kidney and skeletal muscle. {ECO:0000269|PubMed:12172009,
CC ECO:0000269|PubMed:24930674}.
CC -!- MISCELLANEOUS: Amplified and overexpressed in oral cancer cells.
CC -!- SIMILARITY: Belongs to the LTO1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ORAOV1ID41611ch11q13.html";
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DR EMBL; AF503940; AAM97902.1; -; mRNA.
DR EMBL; AK311918; BAG34859.1; -; mRNA.
DR EMBL; CH471076; EAW74749.1; -; Genomic_DNA.
DR EMBL; BC019024; AAH19024.4; -; mRNA.
DR EMBL; BC065542; AAH65542.1; -; mRNA.
DR CCDS; CCDS8192.1; -.
DR RefSeq; NP_703152.1; NM_153451.2.
DR RefSeq; XP_006718533.1; XM_006718470.2.
DR AlphaFoldDB; Q8WV07; -.
DR SMR; Q8WV07; -.
DR BioGRID; 128622; 20.
DR IntAct; Q8WV07; 3.
DR STRING; 9606.ENSP00000279147; -.
DR iPTMnet; Q8WV07; -.
DR PhosphoSitePlus; Q8WV07; -.
DR BioMuta; ORAOV1; -.
DR DMDM; 85701377; -.
DR EPD; Q8WV07; -.
DR jPOST; Q8WV07; -.
DR MassIVE; Q8WV07; -.
DR MaxQB; Q8WV07; -.
DR PaxDb; Q8WV07; -.
DR PeptideAtlas; Q8WV07; -.
DR PRIDE; Q8WV07; -.
DR ProteomicsDB; 74732; -.
DR Antibodypedia; 58325; 67 antibodies from 20 providers.
DR DNASU; 220064; -.
DR Ensembl; ENST00000279147.9; ENSP00000279147.5; ENSG00000149716.13.
DR Ensembl; ENST00000535657.5; ENSP00000446129.1; ENSG00000149716.13.
DR GeneID; 220064; -.
DR KEGG; hsa:220064; -.
DR MANE-Select; ENST00000279147.9; ENSP00000279147.5; NM_153451.3; NP_703152.1.
DR UCSC; uc001opc.4; human.
DR CTD; 220064; -.
DR DisGeNET; 220064; -.
DR GeneCards; LTO1; -.
DR HGNC; HGNC:17589; LTO1.
DR HPA; ENSG00000149716; Low tissue specificity.
DR MIM; 607224; gene.
DR neXtProt; NX_Q8WV07; -.
DR OpenTargets; ENSG00000149716; -.
DR PharmGKB; PA38242; -.
DR VEuPathDB; HostDB:ENSG00000149716; -.
DR eggNOG; KOG4595; Eukaryota.
DR GeneTree; ENSGT00390000009426; -.
DR HOGENOM; CLU_093191_0_1_1; -.
DR InParanoid; Q8WV07; -.
DR OMA; CYQGFAL; -.
DR OrthoDB; 1584299at2759; -.
DR PhylomeDB; Q8WV07; -.
DR TreeFam; TF332075; -.
DR PathwayCommons; Q8WV07; -.
DR SignaLink; Q8WV07; -.
DR BioGRID-ORCS; 220064; 768 hits in 1083 CRISPR screens.
DR ChiTaRS; ORAOV1; human.
DR GenomeRNAi; 220064; -.
DR Pharos; Q8WV07; Tbio.
DR PRO; PR:Q8WV07; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8WV07; protein.
DR Bgee; ENSG00000149716; Expressed in right hemisphere of cerebellum and 109 other tissues.
DR ExpressionAtlas; Q8WV07; baseline and differential.
DR Genevisible; Q8WV07; HS.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IDA:UniProtKB.
DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IMP:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IMP:UniProtKB.
DR InterPro; IPR019191; Essential_protein_Yae1_N.
DR Pfam; PF09811; Yae1_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..137
FT /note="Protein LTO1 homolog"
FT /id="PRO_0000058075"
FT REGION 22..58
FT /note="deca-GX3 motif; required for interaction with YAE1
FT and the CIA complex"
FT /evidence="ECO:0000250|UniProtKB:P53846"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VARIANT 3
FT /note="G -> S (in dbSNP:rs56107468)"
FT /id="VAR_062231"
SQ SEQUENCE 137 AA; 15354 MW; 7FD11DF1C08DD37A CRC64;
MAGSQDIFDA IVMADERFHG EGYREGYEEG SSLGVMEGRQ HGTLHGAKIG SEIGCYQGFA
FAWKCLLHSC TTEKDSRKMK VLESLIGMIQ KFPYDDPTYD KLHEDLDKIR GKFKQFCSLL
NVQPDFKISA EGSGLSF
