MUP1_MOUSE
ID MUP1_MOUSE Reviewed; 180 AA.
AC P11588; Q61921;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Major urinary protein 1;
DE Short=MUP 1;
DE Flags: Precursor;
GN Name=Mup1;
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 TISSUE=Liver;
RX PubMed=2888770; DOI=10.1083/jcb.105.3.1073;
RA Bennett A.L., Paulson K.E., Miller R.E., Darnell J.E. Jr.;
RT "Acquisition of antigens characteristic of adult pericentral hepatocytes by
RT differentiating fetal hepatoblasts in vitro.";
RL J. Cell Biol. 105:1073-1085(1987).
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 X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-180.
RX PubMed=16104761; DOI=10.1021/ja0527525;
RA Barratt E., Bingham R.J., Warner D.J., Laughton C.A., Phillips S.E.,
RA Homans S.W.;
RT "Van der Waals interactions dominate ligand-protein association in a
RT protein binding site occluded from solvent water.";
RL J. Am. Chem. Soc. 127:11827-11834(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA39764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M16355; AAA39767.1; -; mRNA.
DR EMBL; M28649; AAA39764.1; ALT_INIT; mRNA.
DR EMBL; BC012221; AAH12221.1; -; mRNA.
DR CCDS; CCDS18231.1; -.
DR RefSeq; NP_001186924.1; NM_001199995.1.
DR PDB; 1QY0; X-ray; 1.80 A; A=23-180.
DR PDB; 1QY1; X-ray; 1.70 A; A=19-180.
DR PDB; 1QY2; X-ray; 1.75 A; A=19-180.
DR PDB; 1YP6; X-ray; 1.80 A; A=19-180.
DR PDB; 1YP7; X-ray; 2.00 A; A=19-180.
DR PDB; 2DM5; X-ray; 1.70 A; A=20-180.
DR PDBsum; 1QY0; -.
DR PDBsum; 1QY1; -.
DR PDBsum; 1QY2; -.
DR PDBsum; 1YP6; -.
DR PDBsum; 1YP7; -.
DR PDBsum; 2DM5; -.
DR AlphaFoldDB; P11588; -.
DR BMRB; P11588; -.
DR SMR; P11588; -.
DR STRING; 10090.ENSMUSP00000112787; -.
DR Allergome; 478; Mus m 1.
DR iPTMnet; P11588; -.
DR PhosphoSitePlus; P11588; -.
DR SwissPalm; P11588; -.
DR jPOST; P11588; -.
DR PaxDb; P11588; -.
DR PRIDE; P11588; -.
DR Ensembl; ENSMUST00000117932; ENSMUSP00000112787; ENSMUSG00000094793.
DR GeneID; 100039054; -.
DR KEGG; mmu:100039054; -.
DR UCSC; uc008tay.3; mouse.
DR CTD; 100039054; -.
DR MGI; MGI:97233; Mup1.
DR VEuPathDB; HostDB:ENSMUSG00000094793; -.
DR eggNOG; ENOG502S6GK; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR HOGENOM; CLU_094061_4_0_1; -.
DR InParanoid; P11588; -.
DR OrthoDB; 1475169at2759; -.
DR PhylomeDB; P11588; -.
DR TreeFam; TF338197; -.
DR BioGRID-ORCS; 100039054; 4 hits in 15 CRISPR screens.
DR ChiTaRS; Mup1; mouse.
DR EvolutionaryTrace; P11588; -.
DR PRO; PR:P11588; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P11588; protein.
DR Bgee; ENSMUSG00000094793; Expressed in liver and 17 other tissues.
DR ExpressionAtlas; P11588; baseline and differential.
DR Genevisible; P11588; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005009; F:insulin receptor activity; IDA:UniProtKB.
DR GO; GO:0005549; F:odorant binding; IBA:GO_Central.
DR GO; GO:0005186; F:pheromone activity; IDA:MGI.
DR GO; GO:0005550; F:pheromone binding; IDA:UniProtKB.
DR GO; GO:0036094; F:small molecule binding; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IDA:UniProtKB.
DR GO; GO:0071240; P:cellular response to food; IEP:UniProtKB.
DR GO; GO:0071396; P:cellular response to lipid; IDA:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IEP:UniProtKB.
DR GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:UniProtKB.
DR GO; GO:0006112; P:energy reserve metabolic process; IDA:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
DR GO; GO:0031649; P:heat generation; IDA:UniProtKB.
DR GO; GO:0045475; P:locomotor rhythm; IDA:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IDA:UniProtKB.
DR GO; GO:0045721; P:negative regulation of gluconeogenesis; IDA:UniProtKB.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
DR GO; GO:0051055; P:negative regulation of lipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0010888; P:negative regulation of lipid storage; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0010907; P:positive regulation of glucose metabolic process; IDA:UniProtKB.
DR GO; GO:0045834; P:positive regulation of lipid metabolic process; IDA:UniProtKB.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA: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 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 1"
FT /id="PRO_0000017927"
FT DISULFID 82..175
FT CONFLICT 44
FT /note="S -> F (in Ref. 2; AAA39764)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="K -> N (in Ref. 2; AAA39764)"
FT /evidence="ECO:0000305"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:1QY1"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:1QY1"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:1QY1"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:1QY1"
FT STRAND 67..78
FT /evidence="ECO:0007829|PDB:1QY1"
FT STRAND 81..91
FT /evidence="ECO:0007829|PDB:1QY1"
FT STRAND 98..113
FT /evidence="ECO:0007829|PDB:1QY1"
FT STRAND 115..127
FT /evidence="ECO:0007829|PDB:1QY1"
FT STRAND 130..142
FT /evidence="ECO:0007829|PDB:1QY1"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:1QY1"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1QY1"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:1QY1"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:1QY1"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1YP7"
SQ SEQUENCE 180 AA; 20648 MW; 5AA429BDA0700347 CRC64;
MKMLLLLCLG LTLVCVHAEE ASSTGRNFNV EKINGEWHTI ILASDKREKI EDNGNFRLFL
EQIHVLENSL VLKFHTVRDE ECSELSMVAD KTEKAGEYSV TYDGFNTFTI PKTDYDNFLM
AHLINEKDGE TFQLMGLYGR EPDLSSDIKE RFAQLCEKHG ILRENIIDLS NANRCLQARE
