MOX12_DROME
ID MOX12_DROME Reviewed; 760 AA.
AC Q6NP60; Q9GTU8; Q9VNV6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=MOXD1 homolog 2;
GN Name=olf413; ORFNames=CG12673;
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 [MRNA].
RA Tickoo S.;
RT "Characterization of olf413 - an olfactory mutation in Drosophila
RT melanogaster.";
RL Thesis (2000), Manipal Academy of Higher Education, India.
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG16682.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF255741; AAG16682.1; ALT_FRAME; mRNA.
DR EMBL; AE014296; AAF51810.4; -; Genomic_DNA.
DR EMBL; BT011070; AAR31141.1; -; mRNA.
DR RefSeq; NP_001262204.1; NM_001275275.1.
DR RefSeq; NP_730711.3; NM_168948.5.
DR AlphaFoldDB; Q6NP60; -.
DR SMR; Q6NP60; -.
DR BioGRID; 65692; 3.
DR IntAct; Q6NP60; 30.
DR STRING; 7227.FBpp0305421; -.
DR GlyGen; Q6NP60; 4 sites.
DR PaxDb; Q6NP60; -.
DR PRIDE; Q6NP60; -.
DR DNASU; 40453; -.
DR EnsemblMetazoa; FBtr0301492; FBpp0290707; FBgn0037153.
DR EnsemblMetazoa; FBtr0333219; FBpp0305421; FBgn0037153.
DR GeneID; 40453; -.
DR KEGG; dme:Dmel_CG12673; -.
DR CTD; 40453; -.
DR FlyBase; FBgn0037153; olf413.
DR VEuPathDB; VectorBase:FBgn0037153; -.
DR eggNOG; KOG3568; Eukaryota.
DR GeneTree; ENSGT00530000063085; -.
DR HOGENOM; CLU_017939_2_0_1; -.
DR InParanoid; Q6NP60; -.
DR OMA; YKKHKRC; -.
DR OrthoDB; 1472750at2759; -.
DR PhylomeDB; Q6NP60; -.
DR SignaLink; Q6NP60; -.
DR BioGRID-ORCS; 40453; 0 hits in 1 CRISPR screen.
DR ChiTaRS; olf413; fly.
DR GenomeRNAi; 40453; -.
DR PRO; PR:Q6NP60; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0037153; Expressed in brain and 15 other tissues.
DR ExpressionAtlas; Q6NP60; baseline and differential.
DR Genevisible; Q6NP60; DM.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005615; C:extracellular space; ISS:FlyBase.
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 Disulfide bond; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..760
FT /note="MOXD1 homolog 2"
FT /id="PRO_0000305222"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 117..233
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 78
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 339..367
FT /evidence="ECO:0000250"
FT DISULFID 467..581
FT /evidence="ECO:0000250"
FT DISULFID 543..565
FT /evidence="ECO:0000250"
FT CONFLICT 598
FT /note="Q -> H (in Ref. 1; AAG16682)"
FT /evidence="ECO:0000305"
FT CONFLICT 656..657
FT /note="VP -> LLFITPQ (in Ref. 1; AAG16682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 760 AA; 84741 MW; CA350B5E07CBED04 CRC64;
MAHPRKAVAT PATLQLGPPA QTAQSPAATL RHSRTASSSR RLSLIRCFIS CHTFNLFLLL
LLLASGVRAA SKLATRSNKT SGSSTASGVG AGTAATSAAA AAASGTPIWD HAIDLNDDFR
ILWQIINQDI TFEIQARTLG YVGFGFSPDG NLAGADMAIG WVDKGQTYFQ DRHVTRNGDP
EPVVDPSQDY MLMLGYENAT HTVLRFRRKL DTCDPSHDIA ITNDTMRLLY MYHAQDPPHG
SVRPGTLPDP ARAFRPYRPM VLMQRAQLPM PSPTHDERVR VLELRNEDVE LPAGDLPLFW
CKMFKLEDIN RKHHLIRYEP IYDSSSSVHY LQHITLHECQ GAHAELEEMA REQGRPCLGA
RSIPLACNAI VASWSRGSEG FTYPHEAGYP IESRQAKYYL METHYNNLKP DFAQLHARQM
ADNSGLKIYF THVLRPNDAG TLSIGMDPNW RHIIPPGQKR VVSEGQCIED CTGYAFPQQG
INIFAVMMRT HQIGKEVKLR QIRQTEELPP IAHDSNIDVA YQDFRRLPQS VHSMPGDRLI
AECIYDSSSR KAITLGGLTM KEESCTVLTL YYPRQKKLTT CHSLPSLPTV LHSLGIEQLA
TDSNPVLISS PPELAGMTLE ARLISYDWEN QFGEFQEATR KGSFKPICWG AKNHVVPGSE
FLEGYSINVT KTYKKHRRCK PKRPLAPPTE RTAPPPASDL SELPVLHELD NNNIIEGAAR
SSRSSATDVH SLSRGSGRHF ISCLLWLGAS SWWLLLMLRT
