MOXD2_HUMAN
ID MOXD2_HUMAN Reviewed; 499 AA.
AC A6NHM9;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Putative DBH-like monooxygenase protein 2;
DE EC=1.14.17.-;
DE AltName: Full=DBH-like monooxygenase protein 2 pseudogene;
DE Flags: Precursor;
GN Name=MOXD2P; Synonyms=MOXD2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 347-487.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP GENE STRUCTURE.
RX PubMed=17642472; DOI=10.1093/molbev/msm146;
RA Hahn Y., Jeong S., Lee B.;
RT "Inactivation of MOXD2 and S100A15A by exon deletion during human
RT evolution.";
RL Mol. Biol. Evol. 24:2203-2212(2007).
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250};
CC Note=Binds 2 copper ions per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the copper type II ascorbate-dependent
CC monooxygenase family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. The human MOXD2 gene
CC lacks the last 2 terminal exons, as well as the 3'-UTR and poly(A)
CC signal found in all other mammalian sequences. This deletion, which
CC occured after the divergence of humans and chimpanzees, may interfere
CC with proper mRNA processing and/or translation. {ECO:0000305}.
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DR EMBL; U66059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DY655575; -; NOT_ANNOTATED_CDS; mRNA.
DR AlphaFoldDB; A6NHM9; -.
DR SMR; A6NHM9; -.
DR GlyGen; A6NHM9; 4 sites.
DR BioMuta; HGNC:33605; -.
DR PRIDE; A6NHM9; -.
DR GeneCards; MOXD2P; -.
DR HGNC; HGNC:33605; MOXD2P.
DR neXtProt; NX_A6NHM9; -.
DR InParanoid; A6NHM9; -.
DR PhylomeDB; A6NHM9; -.
DR Pharos; A6NHM9; Tdark.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; A6NHM9; protein.
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; 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; IPR028464; Moxd2.
DR InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR InterPro; IPR028460; Tbh/DBH.
DR PANTHER; PTHR10157; PTHR10157; 1.
DR PANTHER; PTHR10157:SF31; PTHR10157:SF31; 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 5: Uncertain;
KW Copper; Disulfide bond; Glycoprotein; Metal-binding; Monooxygenase;
KW Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..499
FT /note="Putative DBH-like monooxygenase protein 2"
FT /id="PRO_0000305223"
FT DOMAIN 40..156
FT /note="DOMON"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00246"
FT ACT_SITE 209
FT /evidence="ECO:0000255"
FT ACT_SITE 389
FT /evidence="ECO:0000255"
FT BINDING 241
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250"
FT BINDING 308
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 236
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 476
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 211..261
FT /evidence="ECO:0000250"
FT DISULFID 248..271
FT /evidence="ECO:0000250"
FT DISULFID 365..480
FT /evidence="ECO:0000250"
FT DISULFID 443..465
FT /evidence="ECO:0000250"
SQ SEQUENCE 499 AA; 56320 MW; 73EC5AAEB4BD2867 CRC64;
MAHDLLFRLF PLLALGVPLQ SNRLGPTSRL RYSRFLDPSN VIFLRWDFDL EAEIISFELQ
VRTAGWVGFG VTNRYTNVGS DLVVGGVLPN GNVYFSDQHL VEEDTLKEDG SQDAELLGLT
EDAVYTTMHF SRPFRSCDPH DLDITSNTVR VLAAYGLDDT LKLYRERTFV KSIFLLQVVH
PDDLDVPEDT IIHDLEITNF LIPEDDTTYA CTFLPLPIVS EKHHIYKFEP KLVYHNETTV
HHILVYACGN ASVLPTGISD CYGADPAFSL CSQVIVGSAV GGTSYQFPDD VGVSIGTPLD
PQWILEIHYS NFNNLPGVYD SSGIRVYYTS QLCKYDTDVL QLGFFTFPIH FIPPGAESFM
SYGLCRTEKF EEMNGAPMPD IQVYGYLLHT HLAGRALQAV QYRNGTQLRK ICKDDSYDFN
LQETRDLPSR VEIKPGDELL VECHYQTLDR DSMTFGGPST INEMCLIFLF YYPQNNISSC
MGYPDIIYVA HELGEEASE
