ID MUP4_MOUSE Reviewed; 178 AA.
AC P11590;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 27-MAR-2024, entry version 180.
DE RecName: Full=Major urinary protein 4;
DE Short=MUP 4;
DE Flags: Precursor;
GN Name=Mup4;
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=Lacrimal gland;
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 [LARGE SCALE MRNA].
RC TISSUE=Salivary gland;
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 PROTEIN SEQUENCE OF 17-25, LIGAND AFFINITY ASSAY, AND FUNCTION.
RC TISSUE=Nasal mucus;
RX PubMed=12192080; DOI=10.1110/ps.0204202;
RA Sharrow S.D., Vaughn J.L., Zidek L., Novotny M.V., Stone M.J.;
RT "Pheromone binding by polymorphic mouse major urinary proteins.";
RL Protein Sci. 11:2247-2256(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=3600653; DOI=10.1128/mcb.7.5.1947-1954.1987;
RA Shahan K., Denaro M., Gilmartin M., Shi Y., Derman E.;
RT "Expression of six mouse major urinary protein genes in the mammary,
RT parotid, sublingual, submaxillary, and lachrymal glands and in the liver.";
RL Mol. Cell. Biol. 7:1947-1954(1987).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (0.96 ANGSTROMS) OF 17-178 IN COMPLEX WITH
RP PHEROMONES, FUNCTION, AND DISULFIDE BOND.
RX PubMed=20509168; DOI=10.1002/pro.426;
RA Perez-Miller S., Zou Q., Novotny M.V., Hurley T.D.;
RT "High resolution X-ray structures of mouse major urinary protein nasal
RT isoform in complex with pheromones.";
RL Protein Sci. 19:1469-1479(2010).
CC -!- FUNCTION: Binds pheromones, likely to displace pheromones complexed to
CC urinary MUPs and transport them to the vomeronasal organ (VNO) where
CC they associate with their neuronal receptor(s). MUP4 is highly specific
CC for the male mouse pheromone 2-sec-butyl-4,5-dihydrothiazole (SBT).
CC {ECO:0000269|PubMed:12192080, ECO:0000269|PubMed:20509168}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in lacrimal gland, parotid gland,
CC sublingual gland, nasal mucus, and vomeronasal organ.
CC {ECO:0000269|PubMed:3600653}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; M16358; AAA39769.1; -; mRNA.
DR EMBL; BC012227; AAH12227.1; -; mRNA.
DR CCDS; CCDS18228.1; -.
DR PIR; C26890; C26890.
DR RefSeq; NP_032674.1; NM_008648.1.
DR PDB; 3KFF; X-ray; 0.96 A; A=17-178.
DR PDB; 3KFG; X-ray; 1.43 A; A=17-178.
DR PDB; 3KFH; X-ray; 1.02 A; A=17-178.
DR PDB; 3KFI; X-ray; 1.42 A; A=17-178.
DR PDBsum; 3KFF; -.
DR PDBsum; 3KFG; -.
DR PDBsum; 3KFH; -.
DR PDBsum; 3KFI; -.
DR AlphaFoldDB; P11590; -.
DR SMR; P11590; -.
DR STRING; 10090.ENSMUSP00000075356; -.
DR Allergome; 478; Mus m 1.
DR iPTMnet; P11590; -.
DR PhosphoSitePlus; P11590; -.
DR jPOST; P11590; -.
DR MaxQB; P11590; -.
DR PaxDb; 10090-ENSMUSP00000075356; -.
DR ProteomicsDB; 287642; -.
DR DNASU; 17843; -.
DR Ensembl; ENSMUST00000075973.3; ENSMUSP00000075356.3; ENSMUSG00000041333.7.
DR GeneID; 17843; -.
DR KEGG; mmu:17843; -.
DR UCSC; uc008tag.1; mouse.
DR AGR; MGI:97236; -.
DR CTD; 17843; -.
DR MGI; MGI:97236; Mup4.
DR VEuPathDB; HostDB:ENSMUSG00000041333; -.
DR eggNOG; ENOG502S6GK; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR HOGENOM; CLU_094061_4_0_1; -.
DR InParanoid; P11590; -.
DR OMA; FHTKVNG; -.
DR OrthoDB; 4635611at2759; -.
DR PhylomeDB; P11590; -.
DR TreeFam; TF338197; -.
DR BioGRID-ORCS; 17843; 1 hit in 57 CRISPR screens.
DR ChiTaRS; Mup4; mouse.
DR EvolutionaryTrace; P11590; -.
DR PRO; PR:P11590; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P11590; Protein.
DR Bgee; ENSMUSG00000041333; Expressed in parotid gland and 27 other cell types or tissues.
DR ExpressionAtlas; P11590; baseline and differential.
DR Genevisible; P11590; MM.
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:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; 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: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 phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISS:UniProtKB.
DR CDD; cd19428; lipocalin_MUP-like; 1.
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; LIPOCALIN; 1.
DR PANTHER; PTHR11430:SF76; MAJOR URINARY PROTEIN 1-RELATED; 1.
DR Pfam; PF00061; Lipocalin; 1.
DR PRINTS; PR00179; LIPOCALIN.
DR PRINTS; PR01221; MAJORURINARY.
DR SUPFAM; SSF50814; Lipocalins; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Pheromone-binding;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..16
FT /evidence="ECO:0000269|PubMed:12192080"
FT CHAIN 17..178
FT /note="Major urinary protein 4"
FT /id="PRO_0000017930"
FT DISULFID 80..173
FT /evidence="ECO:0000269|PubMed:20509168"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:3KFF"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:3KFF"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:3KFF"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:3KFF"
FT STRAND 65..76
FT /evidence="ECO:0007829|PDB:3KFF"
FT STRAND 79..89
FT /evidence="ECO:0007829|PDB:3KFF"
FT STRAND 96..111
FT /evidence="ECO:0007829|PDB:3KFF"
FT STRAND 113..125
FT /evidence="ECO:0007829|PDB:3KFF"
FT STRAND 128..140
FT /evidence="ECO:0007829|PDB:3KFF"
FT HELIX 144..156
FT /evidence="ECO:0007829|PDB:3KFF"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:3KFF"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3KFF"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3KFF"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3KFF"
SQ SEQUENCE 178 AA; 20542 MW; F0ACF73F17D5A57C CRC64;
MKLLLCLGLT LVCIHAEEAT SKGQNLNVEK INGEWFSILL ASDKREKIEE HGSMRVFVEH
IHVLENSLAF KFHTVIDGEC SEIFLVADKT EKAGEYSVMY DGFNTFTILK TDYDNYIMFH
LINEKDGKTF QLMELYGRKA DLNSDIKEKF VKLCEEHGII KENIIDLTKT NRCLKARE
//
