MUP2_MOUSE
ID MUP2_MOUSE Reviewed; 180 AA.
AC P11589; Q99JF6;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Major urinary protein 2;
DE Short=MUP 2;
DE Flags: Precursor;
GN Name=Mup2;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=SWR/J; TISSUE=Liver;
RA Spisni A.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [4]
RP STRUCTURE BY NMR.
RX PubMed=10583419; DOI=10.1046/j.1432-1327.1999.00984.x;
RA Luecke C., Franzoni L., Abbate F., Lohr F., Ferrari E., Sorbi R.T.,
RA Rueterjans H., Spisni A.;
RT "Solution structure of a recombinant mouse major urinary protein.";
RL Eur. J. Biochem. 266:1210-1218(1999).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=10605093; DOI=10.1023/a:1008328813017;
RA Abbate F., Franzoni L., Lohr F., Luecke C., Ferrari E., Sorbi R.T.,
RA Rueterjans H., Spisni A.;
RT "Complete 1H, 15N and 13C assignment of a recombinant mouse major urinary
RT protein.";
RL J. Biomol. NMR 15:187-188(1999).
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 -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; M16356; AAA39768.1; -; mRNA.
DR EMBL; AJ309921; CAC34259.1; -; mRNA.
DR EMBL; BC012259; AAH12259.1; -; mRNA.
DR EMBL; BC059097; AAH59097.1; -; mRNA.
DR PDB; 1DF3; NMR; -; A=19-180.
DR PDB; 1JV4; X-ray; 1.75 A; A=19-180.
DR PDB; 1ZND; X-ray; 1.60 A; A=19-180.
DR PDB; 1ZNE; X-ray; 2.00 A; A=19-180.
DR PDB; 1ZNG; X-ray; 1.60 A; A=19-180.
DR PDB; 1ZNH; X-ray; 2.10 A; A=19-180.
DR PDB; 1ZNK; X-ray; 1.60 A; A=19-180.
DR PDB; 1ZNL; X-ray; 1.70 A; A=19-180.
DR PDB; 2DM5; X-ray; 1.70 A; A=19-180.
DR PDB; 2NND; X-ray; 1.60 A; A=19-180.
DR PDB; 2NNE; X-ray; 1.60 A; A=19-180.
DR PDB; 2OZQ; X-ray; 1.80 A; A=19-180.
DR PDBsum; 1DF3; -.
DR PDBsum; 1JV4; -.
DR PDBsum; 1ZND; -.
DR PDBsum; 1ZNE; -.
DR PDBsum; 1ZNG; -.
DR PDBsum; 1ZNH; -.
DR PDBsum; 1ZNK; -.
DR PDBsum; 1ZNL; -.
DR PDBsum; 2DM5; -.
DR PDBsum; 2NND; -.
DR PDBsum; 2NNE; -.
DR PDBsum; 2OZQ; -.
DR AlphaFoldDB; P11589; -.
DR BMRB; P11589; -.
DR SMR; P11589; -.
DR STRING; 10090.ENSMUSP00000095655; -.
DR Allergome; 478; Mus m 1.
DR Allergome; 8430; Mus m 1.0102.
DR iPTMnet; P11589; -.
DR PhosphoSitePlus; P11589; -.
DR SwissPalm; P11589; -.
DR SWISS-2DPAGE; P11589; -.
DR jPOST; P11589; -.
DR MaxQB; P11589; -.
DR PaxDb; P11589; -.
DR PeptideAtlas; P11589; -.
DR PRIDE; P11589; -.
DR ProteomicsDB; 286086; -.
DR MGI; MGI:97234; Mup2.
DR eggNOG; ENOG502S6GK; Eukaryota.
DR InParanoid; P11589; -.
DR ChiTaRS; Mup2; mouse.
DR EvolutionaryTrace; P11589; -.
DR PRO; PR:P11589; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P11589; 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 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 3D-structure; Disulfide bond; Pheromone-binding; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..18
FT CHAIN 19..180
FT /note="Major urinary protein 2"
FT /id="PRO_0000017928"
FT DISULFID 82..175
FT /evidence="ECO:0000250"
FT CONFLICT 154
FT /note="K -> Q (in Ref. 2; CAC34259)"
FT /evidence="ECO:0000305"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1JV4"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1ZND"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:1ZND"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1ZND"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1ZND"
FT STRAND 67..78
FT /evidence="ECO:0007829|PDB:1ZND"
FT STRAND 81..91
FT /evidence="ECO:0007829|PDB:1ZND"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:1DF3"
FT STRAND 98..113
FT /evidence="ECO:0007829|PDB:1ZND"
FT STRAND 115..127
FT /evidence="ECO:0007829|PDB:1ZND"
FT STRAND 130..142
FT /evidence="ECO:0007829|PDB:1ZND"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:1ZND"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1ZND"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1ZND"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1JV4"
SQ SEQUENCE 180 AA; 20664 MW; 477F5971ACAB622A CRC64;
MKMLLLLCLG LTLVCVHAEE ASSTGRNFNV EKINGEWHTI ILASDKREKI EDNGNFRLFL
EQIHVLEKSL VLKFHTVRDE ECSELSMVAD KTEKAGEYSV TYDGFNTFTI PKTDYDNFLM
AHLINEKDGE TFQLMGLYGR EPDLSSDIKE RFAKLCEEHG ILRENIIDLS NANRCLQARE
