MET7B_MOUSE
ID MET7B_MOUSE Reviewed; 244 AA.
AC Q9DD20; Q78ID2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Thiol S-methyltransferase METTL7B;
DE AltName: Full=Methyltransferase-like protein 7B;
DE EC=2.1.1.9 {ECO:0000250|UniProtKB:Q6UX53};
DE Flags: Precursor;
GN Name=Mettl7b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-244.
RC STRAIN=FVB/N; TISSUE=Colon;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000250|UniProtKB:Q6UX53}.
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:0000250|UniProtKB:Q6UX53};
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=AAH24898.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK002239; BAB21956.2; -; mRNA.
DR EMBL; BC024898; AAH24898.1; ALT_INIT; mRNA.
DR CCDS; CCDS24301.1; -.
DR RefSeq; NP_082129.2; NM_027853.2.
DR AlphaFoldDB; Q9DD20; -.
DR SMR; Q9DD20; -.
DR BioGRID; 214841; 1.
DR IntAct; Q9DD20; 1.
DR STRING; 10090.ENSMUSP00000026398; -.
DR iPTMnet; Q9DD20; -.
DR PhosphoSitePlus; Q9DD20; -.
DR SwissPalm; Q9DD20; -.
DR jPOST; Q9DD20; -.
DR MaxQB; Q9DD20; -.
DR PaxDb; Q9DD20; -.
DR PeptideAtlas; Q9DD20; -.
DR PRIDE; Q9DD20; -.
DR ProteomicsDB; 295544; -.
DR Antibodypedia; 27618; 197 antibodies from 30 providers.
DR DNASU; 71664; -.
DR Ensembl; ENSMUST00000026398; ENSMUSP00000026398; ENSMUSG00000025347.
DR GeneID; 71664; -.
DR KEGG; mmu:71664; -.
DR UCSC; uc007hpd.1; mouse.
DR CTD; 196410; -.
DR MGI; MGI:1918914; Mettl7b.
DR VEuPathDB; HostDB:ENSMUSG00000025347; -.
DR eggNOG; KOG4300; Eukaryota.
DR GeneTree; ENSGT00940000162340; -.
DR HOGENOM; CLU_037990_7_2_1; -.
DR InParanoid; Q9DD20; -.
DR OMA; TWTLCSI; -.
DR OrthoDB; 1178802at2759; -.
DR PhylomeDB; Q9DD20; -.
DR TreeFam; TF331790; -.
DR BioGRID-ORCS; 71664; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q9DD20; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9DD20; protein.
DR Bgee; ENSMUSG00000025347; Expressed in left lobe of liver and 55 other tissues.
DR Genevisible; Q9DD20; MM.
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; ISS:UniProtKB.
DR GO; GO:0018708; F:thiol S-methyltransferase activity; ISS: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; Signal; Transferase.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..244
FT /note="Thiol S-methyltransferase METTL7B"
FT /id="PRO_0000251923"
SQ SEQUENCE 244 AA; 28049 MW; 1E760F4BB0004637 CRC64;
MDALVLFLQL LVLLLTLPLH LLALLGCWQP ICKTYFPYFM AMLTARSYKK MESKKRELFS
QIKDLKGTSG NVALLELGCG TGANFQFYPQ GCKVTCVDPN PNFEKFLTKS MAENRHLQYE
RFIVAYGENM KQLADSSMDV VVCTLVLCSV QSPRKVLQEV QRVLRPGGLL FFWEHVAEPQ
GSRAFLWQRV LEPTWKHIGD GCHLTRETWK DIERAQFSEV QLEWQPPPFR WLPVGPHIMG
KAVK
