ID   P33MX_PONAB             Reviewed;         305 AA.
AC   Q5R8Q8;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Putative monooxygenase p33MONOX;
DE            EC=1.-.-.-;
GN   Name=P33MONOX;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Potential NADPH-dependent oxidoreductase. May be involved in
CC       the regulation of neuronal survival, differentiation and axonal
CC       outgrowth (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NELFB, NOL12 and PRNP.
CC       {ECO:0000250|UniProtKB:Q96A73}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the P33MONOX family. {ECO:0000305}.
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DR   EMBL; CR859693; CAH91852.1; -; mRNA.
DR   AlphaFoldDB; Q5R8Q8; -.
DR   SMR; Q5R8Q8; -.
DR   STRING; 9601.ENSPPYP00000024248; -.
DR   eggNOG; ENOG502QRB0; Eukaryota.
DR   InParanoid; Q5R8Q8; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR026759; P33MONOX.
DR   PANTHER; PTHR28342; PTHR28342; 1.
DR   Pfam; PF15302; P33MONOX; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; NADP; Oxidoreductase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..305
FT                   /note="Putative monooxygenase p33MONOX"
FT                   /id="PRO_0000307732"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           67..77
FT                   /note="Flavin-containing monooxygenase motif"
FT   COMPBIAS        164..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..291
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         44
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBN4"
FT   MOD_RES         175
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9DBN4"
FT   MOD_RES         182
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A73"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96A73"
SQ   SEQUENCE   305 AA;  33249 MW;  02027F4E834C9421 CRC64;
     MASRQPEVPA LEASGPLGKM SLPIGIYRRA LSYDDTLEDP APMTPPPSDM GSVPWKPVIP
     ERKYQHLAKV EEGEASLPSP AMTLSSAIDS VDKVPVVKAK ATHVIMNSLI TKQTQESIQH
     FERQAGLRDA GYTPHKGLTT EETKYLRVAE ALHKLKLQSG EITKEERQPA SAQSTPSTTP
     HSSPKQRSRG WFTSGSSTAL PGPNPSTMDS GSGDKDRNLS DKWSLFGPRS LQKYDSGSST
     TQAYRGVQKP SPLELIRAQA NRMAEDPAAL KPPKMDIPVM EGKKQPPRAH NLKPRDLNVL
     TPTGF