MOX11_DROME
ID MOX11_DROME Reviewed; 698 AA.
AC Q9VUY0; Q8SYE9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=MOXD1 homolog 1;
DE EC=1.14.17.-;
DE Flags: Precursor;
GN ORFNames=CG5235;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=11900973; DOI=10.1016/s0925-4773(02)00010-2;
RA Brody T., Stivers C., Nagle J., Odenwald W.F.;
RT "Identification of novel Drosophila neural precursor genes using a
RT differential embryonic head cDNA screen.";
RL Mech. Dev. 113:41-59(2002).
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: Secreted {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Maternally transcribed. During neurogenesis,
CC expression is reactivated in neuroblasts and ganglion mother cells, and
CC disappears as neurons differentiate. {ECO:0000269|PubMed:11900973}.
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
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DR EMBL; AE014296; AAF49543.2; -; Genomic_DNA.
DR EMBL; AY071594; AAL49216.1; -; mRNA.
DR RefSeq; NP_001261921.1; NM_001274992.2.
DR RefSeq; NP_648833.1; NM_140576.4.
DR AlphaFoldDB; Q9VUY0; -.
DR SMR; Q9VUY0; -.
DR BioGRID; 65067; 1.
DR STRING; 7227.FBpp0075252; -.
DR GlyGen; Q9VUY0; 6 sites.
DR PaxDb; Q9VUY0; -.
DR PRIDE; Q9VUY0; -.
DR DNASU; 39758; -.
DR EnsemblMetazoa; FBtr0075497; FBpp0075252; FBgn0036565.
DR EnsemblMetazoa; FBtr0333599; FBpp0305776; FBgn0036565.
DR GeneID; 39758; -.
DR KEGG; dme:Dmel_CG5235; -.
DR UCSC; CG5235-RA; d. melanogaster.
DR FlyBase; FBgn0036565; CG5235.
DR VEuPathDB; VectorBase:FBgn0036565; -.
DR eggNOG; KOG3568; Eukaryota.
DR GeneTree; ENSGT00530000063085; -.
DR HOGENOM; CLU_017939_0_0_1; -.
DR InParanoid; Q9VUY0; -.
DR OMA; SMDTLYW; -.
DR OrthoDB; 1472750at2759; -.
DR PhylomeDB; Q9VUY0; -.
DR BioGRID-ORCS; 39758; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39758; -.
DR PRO; PR:Q9VUY0; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0036565; Expressed in cleaving embryo and 32 other tissues.
DR ExpressionAtlas; Q9VUY0; baseline and differential.
DR Genevisible; Q9VUY0; DM.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
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; IPR020611; Cu2_ascorb_mOase_CS-1.
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; PS00084; CU2_MONOOXYGENASE_1; 1.
DR PROSITE; PS50836; DOMON; 1.
PE 2: Evidence at transcript level;
KW Copper; Disulfide bond; Glycoprotein; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..698
FT /note="MOXD1 homolog 1"
FT /id="PRO_0000305221"
FT DOMAIN 54..174
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT ACT_SITE 232
FT /evidence="ECO:0000255"
FT ACT_SITE 425
FT /evidence="ECO:0000255"
FT BINDING 265
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 427
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT BINDING 500
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 140
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 465
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 538
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 272..309
FT /evidence="ECO:0000250"
FT DISULFID 403..516
FT /evidence="ECO:0000250"
FT DISULFID 479..501
FT /evidence="ECO:0000250"
SQ SEQUENCE 698 AA; 79456 MW; 4677729C4580A53A CRC64;
MSVQDVLWIV LTVQLSFGLA YFENNQRTQD YDVDKNGSVH HKNWVRNEMM DSLGLYWLKW
WINANENSIY FEVTVHTRGF AGLGFSKDGR LARADMVLMW VDDATGHPNV LDCHGALHPS
SGPPLQDDTQ NYDVLDGKQN GTHTILKFKR KIETCDPFDI PLSADTFKVL WSIGENDPIH
GNLDWQGQSR GVKALQLFSP MFTKNSHSIE GIQKWDITVN NVTIDRSMDT LYWCKIVRLP
ELTGKQHIIG YEPLLSGKYE RNVVHHMTLF ECQSKIYSGS DPSSWDLWVR SAGTVCNSNL
LTPRDWDSCS TPVAVWSLGS DGQFLPPHAG IPMGGASGVS YYMLEIHYDN PDGKESVDHS
GFRIHYTPNL RTYDSGILIS GVSISETQLI PPGQKKYRSV GICGPSCSSV MFPKDGIKII
SGTLHSHQAG RTISLRHVRS GKELNPIIVD ENYDYRHQKV HQLANETVVL PGDYLITDCS
YETKYRKRPT FGGYSTKEEM CLTFITYYPK IEMSGCYSMT PVREFFEMFR VYQFYSLNMT
DVENMFLYNS DYTDYSKQAK NATNKPNSGK TSKEDVIYQE SLLNKLVISD PAEFHDRTFL
SHLNQLPWHD PLFTKRVEQA FITGTHMTFC RVSKDSLSIP SEIIRYPEFT AYVKPPAACL
NYLFTDNEEL RSGSSQFFTD FTLSLLLLIQ LGLQTTLL