MOXD2_DANRE
ID MOXD2_DANRE Reviewed; 572 AA.
AC Q08CS6; A4QP47; Q501Y1; Q5SPP6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=DBH-like monooxygenase protein 2 homolog;
DE EC=1.14.17.-;
DE Flags: Precursor;
GN Name=moxd2; Synonyms=moxd1l; ORFNames=si:ch211-203k16.5;
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].
RC TISSUE=Olfactory epithelium;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (SEP-2006) 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: Membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH95821.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH95821.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAI24116.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI39650.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAI11757.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL845420; CAI11757.2; ALT_INIT; Genomic_DNA.
DR EMBL; BX784041; CAI11757.2; JOINED; Genomic_DNA.
DR EMBL; BX784041; CAM16827.1; -; Genomic_DNA.
DR EMBL; AL845420; CAM16827.1; JOINED; Genomic_DNA.
DR EMBL; BC095821; AAH95821.1; ALT_SEQ; mRNA.
DR EMBL; BC124115; AAI24116.1; ALT_INIT; mRNA.
DR EMBL; BC139649; AAI39650.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q08CS6; -.
DR SMR; Q08CS6; -.
DR STRING; 7955.ENSDARP00000113999; -.
DR PaxDb; Q08CS6; -.
DR ZFIN; ZDB-GENE-060126-3; moxd1l.
DR eggNOG; KOG3568; Eukaryota.
DR InParanoid; Q08CS6; -.
DR PhylomeDB; Q08CS6; -.
DR TreeFam; TF320698; -.
DR PRO; PR:Q08CS6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
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; IPR008977; PHM/PNGase_F_dom_sf.
DR InterPro; IPR028460; Tbh/DBH.
DR PANTHER; PTHR10157; PTHR10157; 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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..572
FT /note="DBH-like monooxygenase protein 2 homolog"
FT /id="PRO_0000305225"
FT TOPO_DOM 27..552
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 42..157
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT ACT_SITE 207
FT /evidence="ECO:0000255"
FT ACT_SITE 381
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 301
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 456
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 468
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 503
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 518
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 209..256
FT /evidence="ECO:0000250"
FT DISULFID 244..263
FT /evidence="ECO:0000250"
FT DISULFID 358..472
FT /evidence="ECO:0000250"
FT DISULFID 435..457
FT /evidence="ECO:0000250"
FT CONFLICT 34
FT /note="F -> S (in Ref. 2; AAI24116)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="I -> L (in Ref. 2; AAH95821)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="S -> L (in Ref. 2; AAH95821/AAI39650)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="T -> A (in Ref. 2; AAI39650)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="M -> V (in Ref. 2; AAH95821)"
FT /evidence="ECO:0000305"
FT CONFLICT 213
FT /note="R -> K (in Ref. 2; AAH95821)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="E -> K (in Ref. 2; AAH95821)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="T -> I (in Ref. 2; AAH95821/AAI24116/AAI39650)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="H -> Q (in Ref. 2; AAH95821)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="K -> N (in Ref. 2; AAH95821)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="Missing (in Ref. 2; AAH95821)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="Y -> H (in Ref. 2; AAI39650)"
FT /evidence="ECO:0000305"
FT CONFLICT 571
FT /note="A -> V (in Ref. 2; AAI24116)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 64050 MW; 78338EACDD384DE0 CRC64;
MGTCLKGNMS VLSLVLFLLS VQQFWAQEDP LLPFSEHLDL EHNVQLKWGF DKIQGTILFQ
LSVNTSGWIS FGLSPNGGMT GADIVIGGVD NKGTYFTDRH ALGNSMPVVD QKQNYKLLSL
SESDGKTVMK FQRSIESCDE NDLPVTILPM KLIYAYGETD DISYHKAQRG TKEVNLLKYM
PRASLSNATY FDITMENFML PANQTYYHCK TARAPTFDSK QHIYRIEPVI TNYDLVHHLL
LYRCPPTVTE PLELECYTKT ERCMETIAVW GVGGGDFEFP EVAGLPIGGN VGDFFYRLEV
HYNNVNKTAG RVDSSGLRFY YTSKLRQHDA GILMTGLAVI PSYAIPPKAK SFLTYGMCDT
TYIPKVLETA NDLQVFSVMM HTHLAGRKVR VGHFREGKQI DLLAVDENYN FEFQQVTNLG
KTKTVKLGDK LLVECTYNTE NRNTLTQGGL STSDEMCLAF LFYYPAMNLS GCESLPHFSS
LVSEMGAGDT GTWLYMMNTM AWNDSSINEY QQTLKKINQT VIVVNSFNKA SITNGTIPDL
KVSPPEPCVR ACATKNLAFM SLFLCLAGMW AS
