ID   MET22_MOUSE             Reviewed;         393 AA.
AC   Q8R1C6; Q3UW48;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Methyltransferase-like protein 22;
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q9BUU2};
GN   Name=Mettl22;
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=Epididymis;
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].
RC   TISSUE=Eye;
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).
CC   -!- FUNCTION: Protein N-lysine methyltransferase. Trimethylates KIN at Lys-
CC       135 (in vitro). {ECO:0000250|UniProtKB:Q9BUU2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC         Evidence={ECO:0000250|UniProtKB:Q9BUU2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC         Evidence={ECO:0000250|UniProtKB:Q9BUU2};
CC   -!- SUBUNIT: Interacts with members of the heat shock protein 90 and 70
CC       families; these proteins probably are methylation substrates.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL22
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE23071.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK136614; BAE23071.1; ALT_FRAME; mRNA.
DR   EMBL; BC024814; AAH24814.1; -; mRNA.
DR   CCDS; CCDS27938.1; -.
DR   RefSeq; NP_666359.1; NM_146247.1.
DR   AlphaFoldDB; Q8R1C6; -.
DR   SMR; Q8R1C6; -.
DR   STRING; 10090.ENSMUSP00000044108; -.
DR   iPTMnet; Q8R1C6; -.
DR   PhosphoSitePlus; Q8R1C6; -.
DR   EPD; Q8R1C6; -.
DR   PaxDb; Q8R1C6; -.
DR   PRIDE; Q8R1C6; -.
DR   ProteomicsDB; 252539; -.
DR   Antibodypedia; 51872; 32 antibodies from 11 providers.
DR   DNASU; 239706; -.
DR   Ensembl; ENSMUST00000046470; ENSMUSP00000044108; ENSMUSG00000039345.
DR   GeneID; 239706; -.
DR   KEGG; mmu:239706; -.
DR   UCSC; uc007ycl.1; mouse.
DR   CTD; 79091; -.
DR   MGI; MGI:2384301; Mettl22.
DR   VEuPathDB; HostDB:ENSMUSG00000039345; -.
DR   eggNOG; KOG2793; Eukaryota.
DR   GeneTree; ENSGT00510000048539; -.
DR   HOGENOM; CLU_048361_0_0_1; -.
DR   InParanoid; Q8R1C6; -.
DR   OMA; ITCEAYS; -.
DR   OrthoDB; 1612133at2759; -.
DR   PhylomeDB; Q8R1C6; -.
DR   TreeFam; TF324844; -.
DR   Reactome; R-MMU-8876725; Protein methylation.
DR   BioGRID-ORCS; 239706; 3 hits in 72 CRISPR screens.
DR   PRO; PR:Q8R1C6; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q8R1C6; protein.
DR   Bgee; ENSMUSG00000039345; Expressed in interventricular septum and 265 other tissues.
DR   ExpressionAtlas; Q8R1C6; baseline and differential.
DR   Genevisible; Q8R1C6; MM.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR   GO; GO:0008276; F:protein methyltransferase activity; ISO:MGI.
DR   GO; GO:0006479; P:protein methylation; ISO:MGI.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR038899; METTL22.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR23108; PTHR23108; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   2: Evidence at transcript level;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..393
FT                   /note="Methyltransferase-like protein 22"
FT                   /id="PRO_0000286592"
FT   REGION          54..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUU2"
SQ   SEQUENCE   393 AA;  43586 MW;  344DD0EF85E961CC CRC64;
     MGPAMDEVTF KSDTVLSDVH LYTPNQRHLM VRLNGMGQPV FLSQFKLLWS RDSWTDSGAE
     DSGPTDVSTE EMPPAGSGSG HSHEDLSLQA GDDNTIQEGL SVPLDEDGDL DVVRRPRAAS
     DPNPAEPARD KVHPTILAQE EDDLVGDQEY ESCPHSIIKI EHTMATPLED VGKQVWRGAL
     LLADYILFRR DLFQGCTVLE LGAGTGLASI VAATMAHTVY CTDVGTDLLA MCQRNVALNS
     HLTATGGGVV KVKELDWLKD NLCTDPKAPF SWSEEEIADL YDHTTVLLAA EVFYDDDLTN
     ALFNTLSRLV HRLKNACTAI FSVEKRFNFT LRHLDVTCEA YDHFRASLDS LEKLADGRLR
     FMVEPVEASF PQLLVYERIR QLELWKIVVE PAA