MOXD1_MOUSE
ID MOXD1_MOUSE Reviewed; 613 AA.
AC Q9CXI3; Q6PFA8; Q8BUZ7; Q8R394; Q9JJA6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=DBH-like monooxygenase protein 1;
DE EC=1.14.17.-;
DE AltName: Full=DBH-related protein;
DE AltName: Full=Monooxygenase X;
DE Flags: Precursor;
GN Name=Moxd1; Synonyms=Dbhr, Mox;
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=Head, Ovary, and Uterus;
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 STRAIN=Czech II; TISSUE=Mammary tumor;
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 [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 IDENTIFICATION, TISSUE SPECIFICITY, GLYCOSYLATION, AND SUBCELLULAR
RP LOCATION.
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: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15337741}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:15337741}.
CC -!- TISSUE SPECIFICITY: Broadly exprressed, with highest levels in salivary
CC gland and ovary. {ECO:0000269|PubMed:15337741}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:15337741}.
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38265.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB041606; BAA95089.1; -; mRNA.
DR EMBL; AK014340; BAB29283.1; -; mRNA.
DR EMBL; AK030274; BAC26871.1; -; mRNA.
DR EMBL; AK081586; BAC38265.1; ALT_FRAME; mRNA.
DR EMBL; BC025892; AAH25892.1; -; mRNA.
DR EMBL; BC057652; AAH57652.1; -; mRNA.
DR CCDS; CCDS23750.1; -.
DR RefSeq; NP_067484.2; NM_021509.5.
DR AlphaFoldDB; Q9CXI3; -.
DR SMR; Q9CXI3; -.
DR STRING; 10090.ENSMUSP00000093460; -.
DR GlyGen; Q9CXI3; 4 sites.
DR PhosphoSitePlus; Q9CXI3; -.
DR EPD; Q9CXI3; -.
DR MaxQB; Q9CXI3; -.
DR PaxDb; Q9CXI3; -.
DR PeptideAtlas; Q9CXI3; -.
DR PRIDE; Q9CXI3; -.
DR ProteomicsDB; 295653; -.
DR Antibodypedia; 32922; 144 antibodies from 22 providers.
DR DNASU; 59012; -.
DR Ensembl; ENSMUST00000095784; ENSMUSP00000093460; ENSMUSG00000020000.
DR GeneID; 59012; -.
DR KEGG; mmu:59012; -.
DR UCSC; uc007equ.1; mouse.
DR CTD; 26002; -.
DR MGI; MGI:1921582; Moxd1.
DR VEuPathDB; HostDB:ENSMUSG00000020000; -.
DR eggNOG; KOG3568; Eukaryota.
DR GeneTree; ENSGT00530000063085; -.
DR HOGENOM; CLU_017939_4_1_1; -.
DR InParanoid; Q9CXI3; -.
DR OMA; SMDTLYW; -.
DR OrthoDB; 1472750at2759; -.
DR PhylomeDB; Q9CXI3; -.
DR TreeFam; TF320698; -.
DR BioGRID-ORCS; 59012; 4 hits in 74 CRISPR screens.
DR PRO; PR:Q9CXI3; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CXI3; protein.
DR Bgee; ENSMUSG00000020000; Expressed in vas deferens and 151 other tissues.
DR Genevisible; Q9CXI3; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
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; IPR028463; MOXD1.
DR InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR InterPro; IPR028460; Tbh/DBH.
DR PANTHER; PTHR10157; PTHR10157; 1.
DR PANTHER; PTHR10157:SF28; PTHR10157:SF28; 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 1: Evidence at protein level;
KW Copper; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..613
FT /note="DBH-like monooxygenase protein 1"
FT /id="PRO_0000305218"
FT TOPO_DOM 20..587
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 588..608
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 35..148
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT ACT_SITE 203
FT /evidence="ECO:0000255"
FT ACT_SITE 389
FT /evidence="ECO:0000255"
FT BINDING 235
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 307
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 391
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 464
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 247
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 517
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 205..257
FT /evidence="ECO:0000250"
FT DISULFID 242..269
FT /evidence="ECO:0000250"
FT DISULFID 364..480
FT /evidence="ECO:0000250"
FT DISULFID 368..550
FT /evidence="ECO:0000250"
FT DISULFID 443..465
FT /evidence="ECO:0000250"
FT CONFLICT 11
FT /note="A -> V (in Ref. 2; AAH57652)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="V -> A (in Ref. 2; AAH25892/AAH57652)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="D -> V (in Ref. 1; BAA95089)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="P -> L (in Ref. 2; AAH25892/AAH57652)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="K -> R (in Ref. 1; BAC38265)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="S -> N (in Ref. 2; AAH25892/AAH57652)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="G -> D (in Ref. 2; AAH25892/AAH57652)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 613 AA; 69678 MW; 4A202563373AC927 CRC64;
MCGWPLLVLW ALLPATAAGS PGRSYPHRVV LDPEGKYWLH WGRQGERLAF RLEVRTNGYV
GFGFSPTGSM AAADIVVGGV AHGRPYLQDY FTNADRELEK DAQQDYHLDY AMENSTHTVI
EFSRELHTCD VNDKSLTDST VRVIWAYHHD DPGESGPKYH DLNRGTRSLR LLNPEKANVV
STVLPYFDLV NQNVPIPNKG TTYWCQMFKI PTFQEKHHVI KVEPIIERGH ENLVHHILVY
QCSSNFNDSV LDFGHECYHP NMPDAFLTCE TVILAWGIGG EGFTYPPHVG LSLGMPLDPR
YVLLEVHYDN PARRKGLIDS SGLRVFHTTD IRRYDAGVIE AGLWVSLFHT IPPGMPEFHS
EGHCTLECLE EALGAEKPSG IHVFAVLLHA HLAGKGIRLR HFRKGEEMKL LAYDDDYDFN
FQEFQYLREE QTILPGDNLI TECRYNTKDR AVMTWGGLST RNEMCLSYLL YYPRVNLTRC
SSIPDIMEQL QFIGVKEIYR PVTTWPFIIK SPKQYRNLSF MDAMNKFKWT KKEGLSFNKL
VLSLPVNVRC SKTDNAEWSI QGMTAIPPDI KRPYEAEPLV CEKAASPPLH GIFSLRLLTC
ALLLGSMLSS QGL
