GenomeNet

Database: UniProt
Entry: D3Z9R2_RAT
LinkDB: D3Z9R2_RAT
Original site: D3Z9R2_RAT 
ID   D3Z9R2_RAT              Unreviewed;       393 AA.
AC   D3Z9R2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Methyltransferase 22, Kin17 lysine {ECO:0000313|Ensembl:ENSRNOP00000003700.4};
GN   Name=Mettl22 {ECO:0000313|Ensembl:ENSRNOP00000003700.4,
GN   ECO:0000313|RGD:1311433};
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 {ECO:0000313|Ensembl:ENSRNOP00000003700.4, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000003700.4, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000003700.4,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000003700.4}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000003700.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_213210.4; XM_213210.9.
DR   AlphaFoldDB; D3Z9R2; -.
DR   SMR; D3Z9R2; -.
DR   STRING; 10116.ENSRNOP00000003700; -.
DR   iPTMnet; D3Z9R2; -.
DR   PhosphoSitePlus; D3Z9R2; -.
DR   PaxDb; 10116-ENSRNOP00000003700; -.
DR   PeptideAtlas; D3Z9R2; -.
DR   Ensembl; ENSRNOT00000003700.8; ENSRNOP00000003700.4; ENSRNOG00000002714.8.
DR   KEGG; rno:287054; -.
DR   UCSC; RGD:1311433; rat.
DR   AGR; RGD:1311433; -.
DR   CTD; 79091; -.
DR   RGD; 1311433; Mettl22.
DR   eggNOG; KOG2497; Eukaryota.
DR   GeneTree; ENSGT00510000048539; -.
DR   HOGENOM; CLU_048361_0_0_1; -.
DR   InParanoid; D3Z9R2; -.
DR   OMA; AYERIQQ; -.
DR   OrthoDB; 450395at2759; -.
DR   PhylomeDB; D3Z9R2; -.
DR   TreeFam; TF324844; -.
DR   Reactome; R-RNO-8876725; Protein methylation.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000002714; Expressed in skeletal muscle tissue and 19 other cell types or tissues.
DR   Genevisible; D3Z9R2; RN.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR   GO; GO:0008276; F:protein methyltransferase activity; ISO:RGD.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR038899; METTL22.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR23108:SF0; METHYLTRANSFERASE-LIKE PROTEIN 22; 1.
DR   PANTHER; PTHR23108; METHYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022603}.
FT   REGION          54..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   393 AA;  43738 MW;  0E3CFCC531F94270 CRC64;
     MGPAMDEVTF KSDTVLSDVH LYTPNQRHLM VRLNGMGQPV FLSQFKLLWS QDSWTDSGAE
     DNGPRAVSTE ETPPAGSGSG HSHEDLSLQA EDDNTIQEGL SVPLDEDGDL DVVRRPRAAS
     DPNPAEPARD KVHPMILEQE EDDLVGDQAR ESCPYSIIKI EHTMATPLED VGKQVWRGAL
     LLADYILFRR DLFQGCTVLE LGAGTGLASI VAATMAHTVY CTDVGTDLLA MCQRNVALNR
     HLAATGGGVV KVKELDWMKD DLCTDPKVPF SWSEEEIADL YDHTTVLLAA EVFYDDDLTN
     ALFHTFSRLV HRLKNACTAI LSVEKRFNFT LRHLDVTCEA YDHFRASLDS LEKLADGRLR
     FLVEPVETSF PQLLGYERIQ QLELWKIVVE PAA
//
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