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P33MX_MOUSE
ID   P33MX_MOUSE             Reviewed;         303 AA.
AC   Q9DBN4; Q3TJ26; Q3UMA7; Q69ZP2; Q8C1J8; Q9D4T9;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Putative monooxygenase p33MONOX;
DE            EC=1.-.-.-;
GN   Name=P33monox; Synonyms=Kiaa1191;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Amnion, Head, Liver, Mammary gland, Placenta, Skin, and Testis;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Kidney, and Mammary tumor;
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   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44; THR-175 AND SER-183, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   TISSUE SPECIFICITY, AND 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).
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=3;
CC       Name=1;
CC         IsoId=Q9DBN4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9DBN4-2; Sequence=VSP_028802, VSP_028803;
CC       Name=3;
CC         IsoId=Q9DBN4-3; Sequence=VSP_028804, VSP_028805;
CC   -!- TISSUE SPECIFICITY: Expressed in neuronal pyramidal cells of the
CC       hippocampus and in the neurons of the cortex.
CC       {ECO:0000269|PubMed:21153684}.
CC   -!- SIMILARITY: Belongs to the P33MONOX family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32404.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   -!- SEQUENCE CAUTION: [Isoform 2]:
CC       Sequence=BAC25449.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK173126; BAD32404.1; ALT_INIT; mRNA.
DR   EMBL; AK004845; BAB23611.1; -; mRNA.
DR   EMBL; AK014792; BAC25449.1; ALT_FRAME; mRNA.
DR   EMBL; AK016176; BAB30137.1; -; mRNA.
DR   EMBL; AK028697; BAC26072.1; -; mRNA.
DR   EMBL; AK145025; BAE26191.1; -; mRNA.
DR   EMBL; AK159945; BAE35501.1; -; mRNA.
DR   EMBL; AK167616; BAE39669.1; -; mRNA.
DR   EMBL; AK169399; BAE41145.1; -; mRNA.
DR   EMBL; BC033445; AAH33445.1; -; mRNA.
DR   EMBL; BC039775; AAH39775.1; -; mRNA.
DR   EMBL; BC043040; AAH43040.1; -; mRNA.
DR   EMBL; BC054417; AAH54417.1; -; mRNA.
DR   CCDS; CCDS26529.1; -. [Q9DBN4-1]
DR   RefSeq; NP_001239574.1; NM_001252645.1.
DR   RefSeq; NP_001239575.1; NM_001252646.1.
DR   RefSeq; NP_001239576.1; NM_001252647.1.
DR   RefSeq; NP_001239577.1; NM_001252648.1.
DR   RefSeq; NP_598558.1; NM_133797.4. [Q9DBN4-1]
DR   RefSeq; XP_006517541.1; XM_006517478.3. [Q9DBN4-1]
DR   AlphaFoldDB; Q9DBN4; -.
DR   SMR; Q9DBN4; -.
DR   BioGRID; 220877; 3.
DR   STRING; 10090.ENSMUSP00000026989; -.
DR   iPTMnet; Q9DBN4; -.
DR   PhosphoSitePlus; Q9DBN4; -.
DR   EPD; Q9DBN4; -.
DR   MaxQB; Q9DBN4; -.
DR   PaxDb; Q9DBN4; -.
DR   PeptideAtlas; Q9DBN4; -.
DR   PRIDE; Q9DBN4; -.
DR   ProteomicsDB; 294091; -. [Q9DBN4-2]
DR   ProteomicsDB; 294092; -. [Q9DBN4-3]
DR   Antibodypedia; 45989; 99 antibodies from 20 providers.
DR   DNASU; 97820; -.
DR   Ensembl; ENSMUST00000026989; ENSMUSP00000026989; ENSMUSG00000025871. [Q9DBN4-1]
DR   GeneID; 97820; -.
DR   KEGG; mmu:97820; -.
DR   UCSC; uc007qof.3; mouse. [Q9DBN4-1]
DR   MGI; MGI:1921162; 4833439L19Rik.
DR   VEuPathDB; HostDB:ENSMUSG00000025871; -.
DR   eggNOG; ENOG502QRB0; Eukaryota.
DR   GeneTree; ENSGT00390000000537; -.
DR   InParanoid; Q9DBN4; -.
DR   OMA; SPRSHNI; -.
DR   OrthoDB; 1021703at2759; -.
DR   PhylomeDB; Q9DBN4; -.
DR   TreeFam; TF332226; -.
DR   BioGRID-ORCS; 97820; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; 4833439L19Rik; mouse.
DR   PRO; PR:Q9DBN4; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q9DBN4; protein.
DR   Bgee; ENSMUSG00000025871; Expressed in right kidney and 268 other tissues.
DR   ExpressionAtlas; Q9DBN4; baseline and differential.
DR   Genevisible; Q9DBN4; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA: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   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; NADP; Oxidoreductase; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..303
FT                   /note="Putative monooxygenase p33MONOX"
FT                   /id="PRO_0000307731"
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          66..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          260..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           67..77
FT                   /note="Flavin-containing monooxygenase motif"
FT   COMPBIAS        76..90
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         44
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         175
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         183
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..70
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_028802"
FT   VAR_SEQ         71..112
FT                   /note="EEGAASVSSLAVTPSPATDSSDKAPVVKAKATHVIMSSLITK -> MGAFVA
FT                   LSRWLCSVQPSSLLGHLEPRSLFSAGSRAAGGGRAE (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_028803"
FT   VAR_SEQ         152..164
FT                   /note="LHKLKLQSGETAK -> PHFPFKTASVIPF (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_028804"
FT   VAR_SEQ         165..303
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_028805"
FT   CONFLICT        13
FT                   /note="P -> H (in Ref. 2; BAE26191)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127..139
FT                   /note="LRDAGYTPHKGLT -> RRDSCITPQWGLS (in Ref. 2;
FT                   BAB30137)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="T -> A (in Ref. 2; BAE39669)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145
FT                   /note="Y -> L (in Ref. 2; BAB30137)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   303 AA;  32715 MW;  2203ADB0AC7EB153 CRC64;
     MASRQPEVPA LAPSGPLGKM SLPIGMCRRA FSYDDALEDP APMTPPPSDM GSIPWKPVIP
     ERKYQHLDKT EEGAASVSSL AVTPSPATDS SDKAPVVKAK ATHVIMSSLI TKQTQESIQR
     FEQQAGLRDA GYTPHKGLTT EETKYLRVAE ALHKLKLQSG ETAKEEKHPA SAQSTPSSTP
     HASPKQKSRG WFPSGSSTAL PAPNPHTMDP GSGNDRNSAD KWSLFGPRPL QKSDSGFAIQ
     AYKGAPRPSP MEVMRAQATR VGEDPATFKP PKMDVPMVEG KKQPLRTHNL KPRDLNVLTP
     TGF
 
 
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