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   16-JAN-2019, entry version 72.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA   Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA   Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA   Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA   Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA   Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA   Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA   Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA   Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA   Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA   Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA   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.,
RA   Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA   Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA   Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA   Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA   Waterston R.H., 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
RT   project: 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
CC       gene lacks the last 2 terminal exons, as well as the 3'-UTR and
CC       poly(A) signal found in all other mammalian sequences. This
CC       deletion, which occured after the divergence of humans and
CC       chimpanzees, may interfere with proper mRNA processing and/or
CC       translation. {ECO:0000305}.
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DR   EMBL; U66059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DY655575; -; NOT_ANNOTATED_CDS; mRNA.
DR   UniGene; Hs.641504; -.
DR   ProteinModelPortal; A6NHM9; -.
DR   SMR; A6NHM9; -.
DR   BioMuta; HGNC:33605; -.
DR   PRIDE; A6NHM9; -.
DR   ProteomicsDB; 1208; -.
DR   GeneCards; MOXD2P; -.
DR   HGNC; HGNC:33605; MOXD2P.
DR   neXtProt; NX_A6NHM9; -.
DR   HOVERGEN; HBG099586; -.
DR   InParanoid; A6NHM9; -.
DR   PhylomeDB; A6NHM9; -.
DR   SignaLink; A6NHM9; -.
DR   Proteomes; UP000005640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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:0016715; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen; 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   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; IPR005018; DOMON_domain.
DR   InterPro; IPR028464; Moxd2.
DR   InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR   InterPro; IPR028460; Tbh/DBH.
DR   PANTHER; PTHR10157:SF31; PTHR10157:SF31; 1.
DR   Pfam; PF03712; Cu2_monoox_C; 1.
DR   Pfam; PF01082; Cu2_monooxygen; 1.
DR   Pfam; PF03351; DOMON; 1.
DR   PRINTS; PR00767; DBMONOXGNASE.
DR   SMART; SM00664; DoH; 1.
DR   SUPFAM; SSF49742; SSF49742; 2.
DR   PROSITE; PS50836; DOMON; 1.
PE   5: Uncertain;
KW   Complete proteome; Copper; Disulfide bond; Glycoprotein;
KW   Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW   Signal.
FT   SIGNAL        1     16       {ECO:0000255}.
FT   CHAIN        17    499       Putative DBH-like monooxygenase protein
FT                                2.
FT                                /FTId=PRO_0000305223.
FT   DOMAIN       40    156       DOMON. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00246}.
FT   ACT_SITE    209    209       {ECO:0000255}.
FT   ACT_SITE    389    389       {ECO:0000255}.
FT   METAL       241    241       Copper A. {ECO:0000250}.
FT   METAL       242    242       Copper A. {ECO:0000250}.
FT   METAL       308    308       Copper A. {ECO:0000250}.
FT   METAL       389    389       Copper B. {ECO:0000250}.
FT   METAL       391    391       Copper B. {ECO:0000250}.
FT   METAL       464    464       Copper B. {ECO:0000250}.
FT   CARBOHYD    236    236       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    250    250       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    404    404       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    476    476       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    211    261       {ECO:0000250}.
FT   DISULFID    248    271       {ECO:0000250}.
FT   DISULFID    365    480       {ECO:0000250}.
FT   DISULFID    443    465       {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
//