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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
 
 
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