MOXD1_CHICK
ID MOXD1_CHICK Reviewed; 614 AA.
AC Q98ST7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
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 [2]
RP IDENTIFICATION.
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 {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neural crest at all developmental
CC stages, and in developing somite and myotome.
CC {ECO:0000269|PubMed:11397006}.
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
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DR EMBL; AF327450; AAK37507.1; -; mRNA.
DR RefSeq; NP_989955.1; NM_204624.1.
DR AlphaFoldDB; Q98ST7; -.
DR SMR; Q98ST7; -.
DR STRING; 9031.ENSGALP00000004587; -.
DR PaxDb; Q98ST7; -.
DR GeneID; 395333; -.
DR KEGG; gga:395333; -.
DR CTD; 26002; -.
DR VEuPathDB; HostDB:geneid_395333; -.
DR eggNOG; KOG3568; Eukaryota.
DR InParanoid; Q98ST7; -.
DR OrthoDB; 1472750at2759; -.
DR PhylomeDB; Q98ST7; -.
DR PRO; PR:Q98ST7; -.
DR Proteomes; UP000000539; Unplaced.
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: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 2: Evidence at transcript level;
KW Copper; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..614
FT /note="DBH-like monooxygenase protein 1"
FT /id="PRO_0000305219"
FT TOPO_DOM 23..592
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..613
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"
SQ SEQUENCE 614 AA; 69503 MW; A5DBD8A45C5FA899 CRC64;
MRPLRPWALL LGALLGAAAA AARRYPHVAV LDGAAAYRLL WGRRGSALAF RLEVRTRGYV
GFGLSAGGGM ASADIVVGGV EGGRPYLQDY HTDENRVLKK DPQQDYHLEY AMENSTHTIL
AFSRELYTCD PNDKSITEST VRVIWAYHHK DLGEAGQNYH GSTRGTKSLR LLNPEKAEVS
PASLSYFDLT NKDVPVPDKD TTYWCQMFKI PVQHEKHHVT KVEPLIQKDH ENLVHHILLY
QCSSNLNDSV LDYGHECYHP NMPDSFFTCE TVIFAWAIGG EGFTYPPHVG LSIGTAADPQ
FVLMEVHYDN PTYTEGLIDN SGLRLFYTPV LRKYDAGVIE AGLWVSLFHN IPPGMPEFVS
EGHCTLECLE EALGAERPSG IHVFAVLLHA HLAGRAIRMR HFRNGEEQKL LAYDEEFDFN
FQEFQYLEEE RTIMPGDNLI TECHYSTTDR IRMTWGGLST RNEMCLSYLL YYPRINLTRC
ASIPDIMEQL QFIGVKEIYR PVRTWPFIIK SPKQYKNLSF MDAMNKFKWS KSEGLSYNEL
VLKLPMNVRC SKTDNAEWSF QGMTAFPPEV ERPYKTEPVI CSSSSCLPCS LSLTLLFVVY
VASSTIGNFG PVVQ
