CMTD1_HUMAN
ID CMTD1_HUMAN Reviewed; 262 AA.
AC Q86VU5; Q8TE79;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Catechol O-methyltransferase domain-containing protein 1;
DE EC=2.1.1.-;
GN Name=COMTD1; ORFNames=UNQ766/PRO1558;
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].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 44-262 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, AND SUBUNIT.
RG Structural genomics consortium (SGC);
RT "The crystal structure of human catechol-O-methyltransferase domain
RT containing 1 in complex with S-adenosyl-L-methionine.";
RL Submitted (MAR-2006) to the PDB data bank.
CC -!- FUNCTION: Putative O-methyltransferase. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.8}.
CC -!- INTERACTION:
CC Q86VU5; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-2836030, EBI-10173939;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Cation-dependent O-methyltransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU01019}.
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DR EMBL; AY358476; AAQ88840.1; -; mRNA.
DR EMBL; AK074421; BAB85077.1; -; mRNA.
DR EMBL; AL390034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023663; AAH23663.1; -; mRNA.
DR EMBL; BC047774; AAH47774.1; -; mRNA.
DR CCDS; CCDS7349.1; -.
DR RefSeq; NP_653190.2; NM_144589.2.
DR PDB; 2AVD; X-ray; 1.70 A; A/B=36-262.
DR PDBsum; 2AVD; -.
DR AlphaFoldDB; Q86VU5; -.
DR SMR; Q86VU5; -.
DR BioGRID; 125625; 215.
DR IntAct; Q86VU5; 51.
DR MINT; Q86VU5; -.
DR STRING; 9606.ENSP00000361616; -.
DR DrugBank; DB03923; Feruloyl Coenzyme A.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR DrugBank; DB03179; Sinapoyl coenzyme A.
DR GlyGen; Q86VU5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86VU5; -.
DR PhosphoSitePlus; Q86VU5; -.
DR SwissPalm; Q86VU5; -.
DR BioMuta; COMTD1; -.
DR DMDM; 74750472; -.
DR EPD; Q86VU5; -.
DR jPOST; Q86VU5; -.
DR MassIVE; Q86VU5; -.
DR MaxQB; Q86VU5; -.
DR PaxDb; Q86VU5; -.
DR PeptideAtlas; Q86VU5; -.
DR PRIDE; Q86VU5; -.
DR ProteomicsDB; 70070; -.
DR Antibodypedia; 29691; 87 antibodies from 21 providers.
DR DNASU; 118881; -.
DR Ensembl; ENST00000372538.8; ENSP00000361616.3; ENSG00000165644.11.
DR GeneID; 118881; -.
DR KEGG; hsa:118881; -.
DR MANE-Select; ENST00000372538.8; ENSP00000361616.3; NM_144589.4; NP_653190.2.
DR UCSC; uc001jxb.4; human.
DR CTD; 118881; -.
DR DisGeNET; 118881; -.
DR GeneCards; COMTD1; -.
DR HGNC; HGNC:26309; COMTD1.
DR HPA; ENSG00000165644; Tissue enhanced (esophagus, pancreas).
DR neXtProt; NX_Q86VU5; -.
DR OpenTargets; ENSG00000165644; -.
DR PharmGKB; PA134961676; -.
DR VEuPathDB; HostDB:ENSG00000165644; -.
DR eggNOG; KOG1663; Eukaryota.
DR GeneTree; ENSGT00390000004409; -.
DR HOGENOM; CLU_067676_5_3_1; -.
DR InParanoid; Q86VU5; -.
DR OMA; RGMRPDG; -.
DR OrthoDB; 1116724at2759; -.
DR PhylomeDB; Q86VU5; -.
DR TreeFam; TF312986; -.
DR PathwayCommons; Q86VU5; -.
DR SignaLink; Q86VU5; -.
DR BioGRID-ORCS; 118881; 17 hits in 1076 CRISPR screens.
DR ChiTaRS; COMTD1; human.
DR EvolutionaryTrace; Q86VU5; -.
DR GenomeRNAi; 118881; -.
DR Pharos; Q86VU5; Tdark.
DR PRO; PR:Q86VU5; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q86VU5; protein.
DR Bgee; ENSG00000165644; Expressed in lower esophagus mucosa and 145 other tissues.
DR ExpressionAtlas; Q86VU5; baseline and differential.
DR Genevisible; Q86VU5; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002935; SAM_O-MeTrfase.
DR Pfam; PF01596; Methyltransf_3; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51682; SAM_OMT_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..262
FT /note="Catechol O-methyltransferase domain-containing
FT protein 1"
FT /id="PRO_0000233289"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000269|Ref.8"
FT BINDING 110..111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT BINDING 116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000269|Ref.8"
FT BINDING 134
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000269|Ref.8"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 163
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 185
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000269|Ref.8"
FT BINDING 187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000269|Ref.8"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000269|Ref.8"
FT CONFLICT 84
FT /note="S -> Y (in Ref. 2; BAB85077)"
FT /evidence="ECO:0000305"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:2AVD"
FT HELIX 67..77
FT /evidence="ECO:0007829|PDB:2AVD"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2AVD"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:2AVD"
FT STRAND 105..109
FT /evidence="ECO:0007829|PDB:2AVD"
FT HELIX 115..122
FT /evidence="ECO:0007829|PDB:2AVD"
FT STRAND 129..135
FT /evidence="ECO:0007829|PDB:2AVD"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:2AVD"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:2AVD"
FT STRAND 156..161
FT /evidence="ECO:0007829|PDB:2AVD"
FT HELIX 163..172
FT /evidence="ECO:0007829|PDB:2AVD"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:2AVD"
FT HELIX 191..201
FT /evidence="ECO:0007829|PDB:2AVD"
FT STRAND 202..211
FT /evidence="ECO:0007829|PDB:2AVD"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:2AVD"
FT HELIX 227..241
FT /evidence="ECO:0007829|PDB:2AVD"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:2AVD"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:2AVD"
SQ SEQUENCE 262 AA; 28809 MW; 6A422F32D6FBE128 CRC64;
MTQPVPRLSV PAALALGSAA LGAAFATGLF LGRRCPPWRG RREQCLLPPE DSRLWQYLLS
RSMREHPALR SLRLLTLEQP QGDSMMTCEQ AQLLANLARL IQAKKALDLG TFTGYSALAL
ALALPADGRV VTCEVDAQPP ELGRPLWRQA EAEHKIDLRL KPALETLDEL LAAGEAGTFD
VAVVDADKEN CSAYYERCLQ LLRPGGILAV LRVLWRGKVL QPPKGDVAAE CVRNLNERIR
RDVRVYISLL PLGDGLTLAF KI
