MET7B_RAT
ID MET7B_RAT Reviewed; 244 AA.
AC Q562C4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Thiol S-methyltransferase METTL7B;
DE AltName: Full=Associated with lipid droplet protein 1;
DE Short=ALDI;
DE AltName: Full=Methyltransferase-like protein 7B;
DE EC=2.1.1.9 {ECO:0000250|UniProtKB:Q6UX53};
DE Flags: Precursor;
GN Name=Mettl7b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Spleen;
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 [2]
RP PROTEIN SEQUENCE OF 33-46; 56-63; 93-105; 115-131; 154-162; 189-206 AND
RP 214-241, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=17004324; DOI=10.1111/j.1600-0854.2006.00465.x;
RA Turro S., Ingelmo-Torres M., Estanyol J.M., Tebar F., Fernandez M.A.,
RA Albor C.V., Gaus K., Grewal T., Enrich C., Pol A.;
RT "Identification and characterization of associated with lipid droplet
RT protein 1: a novel membrane-associated protein that resides on hepatic
RT lipid droplets.";
RL Traffic 7:1254-1269(2006).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY.
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: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:0000269|PubMed:17004324}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17004324}. Lipid droplet
CC {ECO:0000269|PubMed:17004324}. 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.
CC -!- TISSUE SPECIFICITY: Highly expressed in liver and kidney. No expression
CC in testis, heart, lung, brain, spleen or cultured fibroblasts.
CC {ECO:0000269|PubMed:17004324}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; BC092587; AAH92587.1; -; mRNA.
DR EMBL; BC092590; AAH92590.1; -; mRNA.
DR RefSeq; NP_001019447.1; NM_001024276.1.
DR AlphaFoldDB; Q562C4; -.
DR SMR; Q562C4; -.
DR STRING; 10116.ENSRNOP00000010760; -.
DR iPTMnet; Q562C4; -.
DR PhosphoSitePlus; Q562C4; -.
DR PaxDb; Q562C4; -.
DR PRIDE; Q562C4; -.
DR Ensembl; ENSRNOT00000010760; ENSRNOP00000010760; ENSRNOG00000007927.
DR GeneID; 366792; -.
DR KEGG; rno:366792; -.
DR UCSC; RGD:1305205; rat.
DR CTD; 196410; -.
DR RGD; 1305205; Mettl7b.
DR eggNOG; KOG4300; Eukaryota.
DR GeneTree; ENSGT00940000162340; -.
DR HOGENOM; CLU_037990_7_2_1; -.
DR InParanoid; Q562C4; -.
DR OMA; TWTLCSI; -.
DR OrthoDB; 1178802at2759; -.
DR PhylomeDB; Q562C4; -.
DR TreeFam; TF331790; -.
DR PRO; PR:Q562C4; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000007927; Expressed in liver and 15 other tissues.
DR Genevisible; Q562C4; RN.
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 Direct protein sequencing; Endoplasmic reticulum; Lipid droplet; Membrane;
KW Methyltransferase; 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_0000251924"
FT CONFLICT 39
FT /note="L -> F (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 42
FT /note="T -> M (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="K -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 244 AA; 27904 MW; BAE46C09986456CB CRC64;
MDVLVPLLQL LVLLLTLPLH LLALLGCWQP ICKTYFPYLM ATLTARSYKK MESKKRELFS
QIKDLKGTSN EVTLLELGCG TGANFQFYPP GCKVTCVDPN PNFEKFLTKS MAENRHLQYE
RFIVAYGENM KQLADSSMDV VVCTLVLCSV QSPRKVLQEV QRVLKPGGLL FFWEHVSEPQ
GSQALLWQRV LEPTWKHIGD GCHLTRETWK DIEKAQFSEV QLEWQPPPFK WLPVGPHIMG
KAVK
