ID P33MX_RAT Reviewed; 304 AA. AC Q5U2R6; Q7TP81; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 1. DT 27-MAR-2024, entry version 94. DE RecName: Full=Putative monooxygenase p33MONOX; DE EC=1.-.-.-; DE AltName: Full=liver regeneration-related protein LRRG011; GN Name=P33monox; ORFNames=Aa2-141; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Liver; RA Xu C.S., Li W.Q., Li Y.C., Ma H., Wang L., Wang S.F., Han H.P., Wang G.P., RA Chai L.Q., Yuan J.Y., Yang K.J., Yan H.M., Chang C.F., Zhao L.F., Shi J.B., RA Rahman S., Wang Q.N., Zhang J.B.; RT "Liver regeneration after PH."; RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Heart; 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 SUBCELLULAR LOCATION. RX PubMed=21153684; DOI=10.1007/s11010-010-0690-4; RA Mishra M., Inoue N., Heese K.; RT "Characterizing the novel protein p33MONOX."; RL Mol. Cell. Biochem. 350:127-134(2011). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). 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:0000269|PubMed:21153684}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q5U2R6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q5U2R6-2; Sequence=VSP_028806, VSP_028807; CC -!- SIMILARITY: Belongs to the P33MONOX family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY325163; AAP92564.1; -; mRNA. DR EMBL; BC085893; AAH85893.1; -; mRNA. DR RefSeq; NP_001014029.1; NM_001014007.1. [Q5U2R6-1] DR AlphaFoldDB; Q5U2R6; -. DR SMR; Q5U2R6; -. DR STRING; 10116.ENSRNOP00000023125; -. DR iPTMnet; Q5U2R6; -. DR PhosphoSitePlus; Q5U2R6; -. DR PaxDb; 10116-ENSRNOP00000023125; -. DR Ensembl; ENSRNOT00000098242.1; ENSRNOP00000085391.1; ENSRNOG00000017133.8. [Q5U2R6-1] DR Ensembl; ENSRNOT00055025704; ENSRNOP00055020972; ENSRNOG00055015016. [Q5U2R6-1] DR Ensembl; ENSRNOT00060031492; ENSRNOP00060025561; ENSRNOG00060018277. [Q5U2R6-1] DR Ensembl; ENSRNOT00065016903; ENSRNOP00065012943; ENSRNOG00065010427. [Q5U2R6-1] DR GeneID; 306766; -. DR KEGG; rno:306766; -. DR UCSC; RGD:1359256; rat. [Q5U2R6-1] DR AGR; RGD:1359256; -. DR CTD; 57179; -. DR RGD; 1359256; LOC306766. DR eggNOG; ENOG502QRB0; Eukaryota. DR GeneTree; ENSGT00390000000537; -. DR HOGENOM; CLU_079377_0_0_1; -. DR InParanoid; Q5U2R6; -. DR OMA; KQNSSAQ; -. DR OrthoDB; 5311228at2759; -. DR PhylomeDB; Q5U2R6; -. DR TreeFam; TF332226; -. DR PRO; PR:Q5U2R6; -. DR Proteomes; UP000002494; Chromosome 17. DR Bgee; ENSRNOG00000017133; Expressed in adult mammalian kidney and 19 other cell types or tissues. 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; MONOOXYGENASE P33MONOX-RELATED; 1. DR PANTHER; PTHR28342:SF1; MONOOXYGENASE P33MONOX-RELATED; 1. DR Pfam; PF15302; P33MONOX; 1. DR Genevisible; Q5U2R6; RN. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; NADP; Oxidoreductase; Phosphoprotein; KW Reference proteome. FT CHAIN 1..304 FT /note="Putative monooxygenase p33MONOX" FT /id="PRO_0000307733" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 38..57 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 69..96 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 159..231 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 262..304 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 68..78 FT /note="Flavin-containing monooxygenase motif" FT COMPBIAS 77..93 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 170..204 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 276..290 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 45 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9DBN4" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q96A73" FT MOD_RES 184 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT VAR_SEQ 1..39 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_028806" FT VAR_SEQ 40..54 FT /note="DPAPMTPPPSDMGSI -> MEPVTKTPELTWAAS (in isoform 2)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_028807" SQ SEQUENCE 304 AA; 32797 MW; FD2D14A5894D266F CRC64; MASRQPEVPP ALAPSGPLSK MSLPIGMCRR AFSYDDALED PAPMTPPPSD MGSIPWKPVI PERKYQHLDK TEEGAASVSS LAVTPSTATD SSDKAPVVKA KATHIIMNSL ITKQTQESIQ RFEQQAGLRD AGYTPHKGLT TEETKYLRVA EALHKLKLQS GETTREEKHP ASAQSSPSST PHSSPKQKSR GWFPSGSSTA LPAPNPHSMD PGGGNDRNSA DKWSLFGPRP LQKSDSGFAI QAYKGAPKPS PMEVMRAQAT RAGEDPAVFK PPKMDVPVVE GKKQPPRTHN LKPRDLNVLT PTGF //