MET7B_HUMAN
ID MET7B_HUMAN Reviewed; 244 AA.
AC Q6UX53; A8K247; Q8WUI1;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Thiol S-methyltransferase METTL7B;
DE AltName: Full=Methyltransferase-like protein 7B;
DE EC=2.1.1.9 {ECO:0000269|PubMed:33649426};
DE Flags: Precursor;
GN Name=METTL7B; ORFNames=UNQ594/PRO1180;
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 [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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 IDENTIFICATION BY 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-98.
RX PubMed=33649426; DOI=10.1038/s41598-021-84218-5;
RA Maldonato B.J., Russell D.A., Totah R.A.;
RT "Human METTL7B is an alkyl thiol methyltransferase that metabolizes
RT hydrogen sulfide and captopril.";
RL Sci. Rep. 11:4857-4857(2021).
CC -!- FUNCTION: Thiol S-methyltransferase that catalyzes the transfer of a
CC methyl group from S-adenosyl-l-methionine to hydrogen sulfide and other
CC thiol compounds including dithiothreitol, 7alpha-thiospironolactone, L-
CC penicillamine, and captopril. {ECO:0000269|PubMed:33649426}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a thiol + S-adenosyl-L-methionine = a methyl thioether + H(+)
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:18277, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29256, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:86315; EC=2.1.1.9;
CC Evidence={ECO:0000269|PubMed:33649426};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=146.2 uM for hydrogen sulfide {ECO:0000269|PubMed:33649426};
CC KM=89.8 uM for captopril {ECO:0000269|PubMed:33649426};
CC KM=25.5 uM for dithiothreitol {ECO:0000269|PubMed:33649426};
CC KM=48.9 uM for 7alpha-thiospironolactone
CC {ECO:0000269|PubMed:33649426};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q562C4}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q562C4}. Lipid droplet
CC {ECO:0000250|UniProtKB:Q562C4}. Note=Highly concentrated in the
CC perinuclear area of the endoplasmic reticulum (ER) and surrounding
CC lipid droplets. May be associated with the specific regions of the LR
CC that form lipid droplets and targeted to the initial deposits of lipids
CC where the lipid droplets form. {ECO:0000250|UniProtKB:Q562C4}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ88872.1; Type=Erroneous termination; Note=Extended C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAF82801.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY358508; AAQ88872.1; ALT_TERM; mRNA.
DR EMBL; AK290112; BAF82801.1; ALT_INIT; mRNA.
DR CCDS; CCDS8887.2; -.
DR RefSeq; NP_689850.2; NM_152637.2.
DR AlphaFoldDB; Q6UX53; -.
DR SMR; Q6UX53; -.
DR BioGRID; 128204; 16.
DR IntAct; Q6UX53; 6.
DR STRING; 9606.ENSP00000377796; -.
DR iPTMnet; Q6UX53; -.
DR PhosphoSitePlus; Q6UX53; -.
DR SwissPalm; Q6UX53; -.
DR BioMuta; METTL7B; -.
DR DMDM; 115502257; -.
DR EPD; Q6UX53; -.
DR jPOST; Q6UX53; -.
DR MassIVE; Q6UX53; -.
DR MaxQB; Q6UX53; -.
DR PaxDb; Q6UX53; -.
DR PeptideAtlas; Q6UX53; -.
DR PRIDE; Q6UX53; -.
DR ProteomicsDB; 67567; -.
DR Antibodypedia; 27618; 197 antibodies from 30 providers.
DR DNASU; 196410; -.
DR Ensembl; ENST00000394252.4; ENSP00000377796.3; ENSG00000170439.8.
DR GeneID; 196410; -.
DR KEGG; hsa:196410; -.
DR MANE-Select; ENST00000394252.4; ENSP00000377796.3; NM_152637.3; NP_689850.2.
DR UCSC; uc010spr.3; human.
DR CTD; 196410; -.
DR DisGeNET; 196410; -.
DR GeneCards; METTL7B; -.
DR HGNC; HGNC:28276; METTL7B.
DR HPA; ENSG00000170439; Tissue enhanced (epididymis, liver).
DR neXtProt; NX_Q6UX53; -.
DR OpenTargets; ENSG00000170439; -.
DR PharmGKB; PA143485533; -.
DR VEuPathDB; HostDB:ENSG00000170439; -.
DR eggNOG; KOG4300; Eukaryota.
DR GeneTree; ENSGT00940000162340; -.
DR HOGENOM; CLU_037990_7_2_1; -.
DR InParanoid; Q6UX53; -.
DR OMA; TWTLCSI; -.
DR OrthoDB; 1178802at2759; -.
DR PhylomeDB; Q6UX53; -.
DR TreeFam; TF331790; -.
DR PathwayCommons; Q6UX53; -.
DR SignaLink; Q6UX53; -.
DR BioGRID-ORCS; 196410; 10 hits in 1068 CRISPR screens.
DR GenomeRNAi; 196410; -.
DR Pharos; Q6UX53; Tbio.
DR PRO; PR:Q6UX53; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6UX53; protein.
DR Bgee; ENSG00000170439; Expressed in ileal mucosa and 106 other tissues.
DR ExpressionAtlas; Q6UX53; baseline and differential.
DR Genevisible; Q6UX53; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0018708; F:thiol S-methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR013216; Methyltransf_11.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF08241; Methyltransf_11; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid droplet; Membrane; Methyltransferase;
KW Reference proteome; S-adenosyl-L-methionine; Signal; Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..244
FT /note="Thiol S-methyltransferase METTL7B"
FT /id="PRO_0000251922"
FT MUTAGEN 98
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:33649426"
SQ SEQUENCE 244 AA; 27775 MW; EB43D3787C7AFA8B CRC64;
MDILVPLLQL LVLLLTLPLH LMALLGCWQP LCKSYFPYLM AVLTPKSNRK MESKKRELFS
QIKGLTGASG KVALLELGCG TGANFQFYPP GCRVTCLDPN PHFEKFLTKS MAENRHLQYE
RFVVAPGEDM RQLADGSMDV VVCTLVLCSV QSPRKVLQEV RRVLRPGGVL FFWEHVAEPY
GSWAFMWQQV FEPTWKHIGD GCCLTRETWK DLENAQFSEI QMERQPPPLK WLPVGPHIMG
KAVK
