MOXD1_DANRE
ID MOXD1_DANRE Reviewed; 614 AA.
AC Q5TZ24; A3KQJ8; A4IGE3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=DBH-like monooxygenase protein 1 homolog;
DE EC=1.14.17.-;
DE Flags: Precursor;
GN Name=moxd1; ORFNames=si:ch211-193l17.1, si:dkey-266k12.5, si:dkeyp-119b4.5;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=3;
CC IsoId=Q5TZ24-3; Sequence=Displayed;
CC Name=1;
CC IsoId=Q5TZ24-1; Sequence=VSP_031643;
CC Name=2;
CC IsoId=Q5TZ24-2; Sequence=VSP_028290, VSP_028291;
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAM46906.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX530723; CAH69122.1; -; Genomic_DNA.
DR EMBL; BX323010; CAH69122.1; JOINED; Genomic_DNA.
DR EMBL; BX323010; CAI21101.1; -; Genomic_DNA.
DR EMBL; BX530723; CAI21101.1; JOINED; Genomic_DNA.
DR EMBL; BX682549; CAM46906.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC135059; AAI35060.1; -; mRNA.
DR RefSeq; NP_001038671.1; NM_001045206.2. [Q5TZ24-1]
DR RefSeq; XP_005160648.1; XM_005160591.3. [Q5TZ24-3]
DR AlphaFoldDB; Q5TZ24; -.
DR SMR; Q5TZ24; -.
DR STRING; 7955.ENSDARP00000105872; -.
DR PaxDb; Q5TZ24; -.
DR Ensembl; ENSDART00000127291; ENSDARP00000111612; ENSDARG00000031136. [Q5TZ24-1]
DR Ensembl; ENSDART00000130494; ENSDARP00000105872; ENSDARG00000031136. [Q5TZ24-3]
DR Ensembl; ENSDART00000153088; ENSDARP00000127316; ENSDARG00000031136. [Q5TZ24-2]
DR GeneID; 570584; -.
DR KEGG; dre:570584; -.
DR CTD; 26002; -.
DR ZFIN; ZDB-GENE-030131-9320; moxd1.
DR eggNOG; KOG3568; Eukaryota.
DR GeneTree; ENSGT00530000063085; -.
DR HOGENOM; CLU_1660104_0_0_1; -.
DR InParanoid; Q5TZ24; -.
DR OMA; SMDTLYW; -.
DR OrthoDB; 1472750at2759; -.
DR PhylomeDB; Q5TZ24; -.
DR TreeFam; TF320698; -.
DR PRO; PR:Q5TZ24; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 20.
DR Bgee; ENSDARG00000031136; Expressed in granulocyte and 16 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:SF42; PTHR10157:SF42; 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 Alternative splicing; Copper; Disulfide bond; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..614
FT /note="DBH-like monooxygenase protein 1 homolog"
FT /id="PRO_0000305220"
FT TOPO_DOM 23..593
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 594..612
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 37..150
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT ACT_SITE 205
FT /evidence="ECO:0000255"
FT ACT_SITE 391
FT /evidence="ECO:0000255"
FT BINDING 237
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 238
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 391
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 393
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 207..259
FT /evidence="ECO:0000250"
FT DISULFID 244..271
FT /evidence="ECO:0000250"
FT DISULFID 366..482
FT /evidence="ECO:0000250"
FT DISULFID 370..552
FT /evidence="ECO:0000250"
FT DISULFID 445..467
FT /evidence="ECO:0000250"
FT VAR_SEQ 140..159
FT /note="GSTVRVIWAFHAEDVGESGL -> VGLTRCIILWLQNSERNSFR (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_028290"
FT VAR_SEQ 160..614
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_028291"
FT VAR_SEQ 374..378
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_031643"
FT CONFLICT 39
FT /note="Y -> H (in Ref. 2; AAI35060)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="I -> V (in Ref. 1; CAM46906 and 2; AAI35060)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="A -> T (in Ref. 1; CAM46906)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="P -> S (in Ref. 1; CAM46906)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="T -> S (in Ref. 1; CAM46906)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="Q -> K (in Ref. 1; CAM46906)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 614 AA; 69345 MW; B80BBD26A3B31388 CRC64;
MSENKLFCAI VFLTSLFCST CSQGTRFVHS AALDAERRYN IKWGFDESTI TFEIEVETRG
YVGFGLSPTG AMSSSDIVIG GVLNGSPYLL DYFTDSNRKV HRDPLQNYEL LYGRENDTHT
VLAFSRNLQT CDDNDKIITG STVRVIWAFH AEDVGESGLV YHGMNRGRKS LRLLNPGTGP
SIPAGTAFFD LQNKEVPVPH KDTTYWCQIF RFPEMKKKHH VIRIEPLIQK GHENLVHHIL
LYQCDSNLNK SEVNRGHECY HPNMPDSFLT CETVLFAWAI GGEGFTYPPH VGMSIGTSID
PVYVQLEIHF DNPSLQGGIV DSSGLRLYYS PSLRRYDAGV IETGVWVSLY HMLPPGMTDY
ITEGHCTQEC LQESLDSEMP SGVHVFAVLL HAHLAGRAIT ARHFRQQLEL QPLASDDQFD
FNFQEFQPLS QERLILPGDS LITECRYNTK GRMNMTWGGL STREEMCLSF LLYYPRVNLA
KCESLPEIAG QLKFIGVTEI QEPVTTWPFV IKSPKKYSNL SFTEAMDKYK WTMKKGKSFN
DIVRKLPMNV RCSKTGQDEW SIQGMIVSPP EVRSEQTSTA VVACRKDSAI QCEHSLALLL
TACLLLILQT CLHL
