MUP3_MOUSE
ID MUP3_MOUSE Reviewed; 184 AA.
AC P04939; P97897; Q8VCG6;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Major urinary protein 3;
DE Short=MUP 3;
DE AltName: Full=Non-group 1/group 2 MUP15;
DE Flags: Precursor;
GN Name=Mup3;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=3004936; DOI=10.1002/j.1460-2075.1985.tb04060.x;
RA Clark A.J., Chave-Cox A., Ma X., Bishop J.O.;
RT "Analysis of mouse major urinary protein genes: variation between the
RT exonic sequences of group 1 genes and a comparison with an active gene out
RT with group 1 both suggest that gene conversion has occurred between MUP
RT genes.";
RL EMBO J. 4:3167-3171(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 72-184.
RX PubMed=3600652; DOI=10.1128/mcb.7.5.1938-1946.1987;
RA Shahan K., Gilmartin M., Derman E.;
RT "Nucleotide sequences of liver, lachrymal, and submaxillary gland mouse
RT major urinary protein mRNAs: mosaic structure and construction of panels of
RT gene-specific synthetic oligonucleotide probes.";
RL Mol. Cell. Biol. 7:1938-1946(1987).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-66.
RC STRAIN=C57BL/6J; TISSUE=Plasma;
RX PubMed=16944957; DOI=10.1021/pr060186m;
RA Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.;
RT "Proteome-wide characterization of N-glycosylation events by diagonal
RT chromatography.";
RL J. Proteome Res. 5:2438-2447(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
CC -!- FUNCTION: Binds pheromones that are released from drying urine of
CC males. These pheromones affect the sexual behavior of females.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Abundant in the urine of adult male mice but absent
CC from that of females.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:16944957}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; X03525; CAA27228.1; -; mRNA.
DR EMBL; M27608; AAA39766.1; -; mRNA.
DR EMBL; BC019965; AAH19965.1; -; mRNA.
DR EMBL; M16359; AAA39762.1; -; mRNA.
DR EMBL; M16357; AAA39761.1; -; mRNA.
DR CCDS; CCDS18234.1; -.
DR PIR; S10125; S10125.
DR RefSeq; NP_001034633.1; NM_001039544.1.
DR AlphaFoldDB; P04939; -.
DR SMR; P04939; -.
DR STRING; 10090.ENSMUSP00000081579; -.
DR Allergome; 478; Mus m 1.
DR GlyGen; P04939; 1 site.
DR iPTMnet; P04939; -.
DR PhosphoSitePlus; P04939; -.
DR SwissPalm; P04939; -.
DR jPOST; P04939; -.
DR MaxQB; P04939; -.
DR PaxDb; P04939; -.
DR PeptideAtlas; P04939; -.
DR PRIDE; P04939; -.
DR ProteomicsDB; 287641; -.
DR DNASU; 17842; -.
DR GeneID; 17842; -.
DR KEGG; mmu:17842; -.
DR CTD; 17842; -.
DR MGI; MGI:97235; Mup3.
DR eggNOG; ENOG502S6GK; Eukaryota.
DR InParanoid; P04939; -.
DR OrthoDB; 1475169at2759; -.
DR PhylomeDB; P04939; -.
DR BioGRID-ORCS; 17842; 1 hit in 51 CRISPR screens.
DR ChiTaRS; Mup3; mouse.
DR PRO; PR:P04939; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P04939; protein.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005009; F:insulin receptor activity; ISS:UniProtKB.
DR GO; GO:0005549; F:odorant binding; IBA:GO_Central.
DR GO; GO:0005550; F:pheromone binding; ISS:UniProtKB.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; ISS:UniProtKB.
DR GO; GO:0071396; P:cellular response to lipid; ISS:UniProtKB.
DR GO; GO:0006112; P:energy reserve metabolic process; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0031649; P:heat generation; ISS:UniProtKB.
DR GO; GO:0045475; P:locomotor rhythm; ISS:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; ISS:UniProtKB.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0051055; P:negative regulation of lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0010888; P:negative regulation of lipid storage; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0010907; P:positive regulation of glucose metabolic process; ISS:UniProtKB.
DR GO; GO:0045834; P:positive regulation of lipid metabolic process; ISS:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR002345; Lipocalin.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR InterPro; IPR002971; Maj_urinary.
DR PANTHER; PTHR11430; PTHR11430; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR01221; MAJORURINARY.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Pheromone-binding; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..22
FT CHAIN 23..184
FT /note="Major urinary protein 3"
FT /id="PRO_0000017929"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16944957"
FT DISULFID 86..179
FT /evidence="ECO:0000250"
FT CONFLICT 49
FT /note="Y -> D (in Ref. 2; AAH19965)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 184 AA; 21465 MW; EA731827BC3972B6 CRC64;
MKLLLPLLLL LCLELTLVCI HAEESSSMER NFNVEQISGY WFSIAEASYE REKIEEHGSM
RAFVENITVL ENSLVFKFHL IVNEECTEMT AIGEQTEKAG IYYMNYDGFN TFSILKTDYD
NYIMIHLINK KDGKTFQLME LYGREPDLSL DIKEKFAKLC EEHGIIRENI IDLTNVNRCL
EARE
