MOXD2_MOUSE
ID MOXD2_MOUSE Reviewed; 619 AA.
AC Q7TT41; Q91XT2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=DBH-like monooxygenase protein 2;
DE EC=1.14.17.-;
DE AltName: Full=Dopamine-beta-hydroxylase-like protein;
DE Flags: Precursor;
GN Name=Moxd2; Synonyms=Dbhl, Dbhl1;
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 [GENOMIC DNA].
RX PubMed=11160223; DOI=10.4049/jimmunol.166.3.1771;
RA Chen F., Rowen L., Hood L., Rothenberg E.V.;
RT "Differential transcriptional regulation of individual TCR V beta segments
RT before gene rearrangement.";
RL J. Immunol. 166:1771-1780(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RA Matsuda M., Horseman N.D.;
RT "Thymus-specific expression of dopamine beta-hydroxylase-like gene mRNA in
RT mice.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION.
RC TISSUE=Embryo;
RX PubMed=11397006; DOI=10.1006/dbio.2001.0275;
RA Knecht A.K., Bronner-Fraser M.;
RT "DBHR, a gene with homology to dopamine beta-hydroxylase, is expressed in
RT the neural crest throughout early development.";
RL Dev. Biol. 234:365-375(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=15337741; DOI=10.1074/jbc.m407486200;
RA Xin X., Mains R.E., Eipper B.A.;
RT "Monooxygenase X, a member of the copper-dependent monooxygenase family
RT localized to the endoplasmic reticulum.";
RL J. Biol. Chem. 279:48159-48167(2004).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed at low levels in thymus and testis.
CC {ECO:0000269|PubMed:15337741}.
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
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DR EMBL; AE000663; AAB69054.1; -; Genomic_DNA.
DR EMBL; AB065134; BAB62024.1; -; mRNA.
DR CCDS; CCDS20039.1; -.
DR RefSeq; NP_647457.2; NM_139296.2.
DR AlphaFoldDB; Q7TT41; -.
DR SMR; Q7TT41; -.
DR STRING; 10090.ENSMUSP00000031937; -.
DR GlyGen; Q7TT41; 3 sites.
DR PaxDb; Q7TT41; -.
DR PRIDE; Q7TT41; -.
DR ProteomicsDB; 291389; -.
DR TopDownProteomics; Q7TT41; -.
DR DNASU; 194357; -.
DR Ensembl; ENSMUST00000031937; ENSMUSP00000031937; ENSMUSG00000029885.
DR GeneID; 194357; -.
DR KEGG; mmu:194357; -.
DR UCSC; uc009bnh.1; mouse.
DR CTD; 194357; -.
DR MGI; MGI:2388042; Moxd2.
DR VEuPathDB; HostDB:ENSMUSG00000029885; -.
DR eggNOG; KOG3568; Eukaryota.
DR GeneTree; ENSGT00530000063085; -.
DR HOGENOM; CLU_017939_1_0_1; -.
DR InParanoid; Q7TT41; -.
DR OMA; NEMCLVF; -.
DR OrthoDB; 1472750at2759; -.
DR PhylomeDB; Q7TT41; -.
DR TreeFam; TF320698; -.
DR BioGRID-ORCS; 194357; 1 hit in 71 CRISPR screens.
DR PRO; PR:Q7TT41; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q7TT41; protein.
DR Bgee; ENSMUSG00000029885; Expressed in olfactory epithelium and 21 other tissues.
DR Genevisible; Q7TT41; MM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030667; C:secretory granule membrane; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
DR GO; GO:0004500; F:dopamine beta-monooxygenase activity; IBA:GO_Central.
DR GO; GO:0042420; P:dopamine catabolic process; IBA:GO_Central.
DR GO; GO:0042421; P:norepinephrine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006589; P:octopamine biosynthetic process; IBA:GO_Central.
DR CDD; cd09631; DOMON_DOH; 1.
DR Gene3D; 2.60.120.230; -; 1.
DR Gene3D; 2.60.120.310; -; 1.
DR InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR InterPro; IPR000323; Cu2_ascorb_mOase_N.
DR InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
DR InterPro; IPR024548; Cu2_monoox_C.
DR InterPro; IPR000945; DBH-like.
DR InterPro; IPR045266; DOH_DOMON.
DR InterPro; IPR005018; DOMON_domain.
DR InterPro; IPR028464; Moxd2.
DR InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR InterPro; IPR028460; Tbh/DBH.
DR PANTHER; PTHR10157; PTHR10157; 1.
DR PANTHER; PTHR10157:SF31; PTHR10157:SF31; 1.
DR Pfam; PF03712; Cu2_monoox_C; 1.
DR Pfam; PF01082; Cu2_monooxygen; 1.
DR PRINTS; PR00767; DBMONOXGNASE.
DR SMART; SM00664; DoH; 1.
DR SUPFAM; SSF49742; SSF49742; 2.
DR PROSITE; PS50836; DOMON; 1.
PE 2: Evidence at transcript level;
KW Copper; Disulfide bond; Glycoprotein; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..619
FT /note="DBH-like monooxygenase protein 2"
FT /id="PRO_0000305224"
FT TOPO_DOM 22..594
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 40..156
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT ACT_SITE 209
FT /evidence="ECO:0000255"
FT ACT_SITE 390
FT /evidence="ECO:0000255"
FT BINDING 241
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 390
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 465
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 211..261
FT /evidence="ECO:0000250"
FT DISULFID 248..271
FT /evidence="ECO:0000250"
FT DISULFID 366..481
FT /evidence="ECO:0000250"
FT DISULFID 444..466
FT /evidence="ECO:0000250"
FT CONFLICT 289
FT /note="D -> G (in Ref. 2; BAB62024)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="L -> V (in Ref. 2; BAB62024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 619 AA; 69397 MW; 74518832AD5E1A63 CRC64;
MACVLLFRLF LLLVLAAFSQ GKRLGPTSPL RYSRFLDPSR AVFLRWDFDY EAEIITFELQ
VQTTGWVGLG ITDRYTFVGS DLVVGGVLPN GNVYFSDQHL LDEDTLEQDG SQDAELLRLT
EDAVSTTMRF SRPFRTCDPH DRDITSDTMR VLAAYGPDDI PKMSREHTFV KSIFLLQMLQ
YDDQDAPEDT IIHDLKISNF IIPEDDTTYA CTFLPLPIVS KKHHIYKFEP ILVERNETMV
HHVLVYACGN SSVLPTGIGE CYGSDPAFSL CSHVIAGWAV GGLSYQFPDD VGISIGTPFD
PQWIRLEIHY SNFQNLPGIR DTSGMRLFYT SHLRKYDMGV LQLGISVFPI HFIPPGAEAF
LSYGLCKTDK FEELNGAPVS DIYISACLLH THLAGRSLQA LQYRNGTQLQ VVCKDFSYDF
NLQESRDLPH PVVIKPGDEL LIECHYQTLD RDFMTFGGAS TINEMCLIFF FYYPRINISS
CMGYPDIIYV TNELGEEASE NPMENLMVLD NVEWTPENIK KAEKACKESQ QTVLIKTIDE
EVENTTGWIP DIIPTPRGPC LESTGGKVEP QDNTPAGFRA VPLALSGSNT ATLRPLPMIA
VLFLQGSLSC LLAMLQTGV
