MUP5_MOUSE
ID MUP5_MOUSE Reviewed; 180 AA.
AC P11591; A2RSZ7; B5TE77;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Major urinary protein 5 {ECO:0000312|MGI:MGI:104974};
DE Flags: Precursor;
GN Name=Mup5 {ECO:0000312|MGI:MGI:104974};
GN Synonyms=Mup18 {ECO:0000303|PubMed:18815613};
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=C57BL/6J {ECO:0000312|EMBL:ACF70717.1};
RC TISSUE=Submandibular gland {ECO:0000312|EMBL:ACF70717.1};
RX PubMed=18815613; DOI=10.1371/journal.pone.0003280;
RA Logan D.W., Marton T.F., Stowers L.;
RT "Species specificity in major urinary proteins by parallel evolution.";
RL PLoS ONE 3:E3280-E3280(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI32311.1};
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).
CC -!- FUNCTION: Major urinary proteins (Mups) bind pheromones, and thus
CC stabilize them to allow slow release into the air from urine marks. May
CC protect pheromones from oxidation. May also act as pheromones
CC themselves. In this context, they play a role in the regulation of
CC social behaviors, such as aggression, mating, pup-suckling, territory
CC establishment and dominance. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q5FW60}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; M16360; AAA39770.1; -; mRNA.
DR EMBL; EU882233; ACF70717.1; -; mRNA.
DR EMBL; CT990634; CAQ12473.1; -; Genomic_DNA.
DR EMBL; AL772344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466527; EDL31167.1; -; Genomic_DNA.
DR EMBL; BC132310; AAI32311.1; -; mRNA.
DR EMBL; BC132312; AAI32313.1; -; mRNA.
DR EMBL; BK006671; DAA06314.1; -; Genomic_DNA.
DR CCDS; CCDS18232.1; -.
DR PIR; D26890; D26890.
DR RefSeq; NP_032675.2; NM_008649.2.
DR AlphaFoldDB; P11591; -.
DR SMR; P11591; -.
DR STRING; 10090.ENSMUSP00000080908; -.
DR Allergome; 478; Mus m 1.
DR PhosphoSitePlus; P11591; -.
DR jPOST; P11591; -.
DR MaxQB; P11591; -.
DR PaxDb; P11591; -.
DR PRIDE; P11591; -.
DR ProteomicsDB; 286087; -.
DR DNASU; 17844; -.
DR Ensembl; ENSMUST00000082287; ENSMUSP00000080908; ENSMUSG00000058523.
DR GeneID; 17844; -.
DR KEGG; mmu:17844; -.
DR UCSC; uc008tbq.1; mouse.
DR CTD; 17844; -.
DR MGI; MGI:104974; Mup5.
DR VEuPathDB; HostDB:ENSMUSG00000058523; -.
DR eggNOG; ENOG502S6GK; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR InParanoid; P11591; -.
DR OMA; QLYAREP; -.
DR OrthoDB; 1475169at2759; -.
DR PhylomeDB; P11591; -.
DR TreeFam; TF338197; -.
DR BioGRID-ORCS; 17844; 4 hits in 40 CRISPR screens.
DR ChiTaRS; Mup5; mouse.
DR PRO; PR:P11591; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P11591; protein.
DR Bgee; ENSMUSG00000058523; Expressed in olfactory epithelium and 39 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Behavior; Disulfide bond; Pheromone-binding; Reference proteome; Secreted;
KW Signal; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..180
FT /note="Major urinary protein 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000017931"
FT DISULFID 82..175
FT /evidence="ECO:0000250|UniProtKB:P11590"
FT CONFLICT 15
FT /note="Y -> C (in Ref. 1; AAA39770, 4; EDL31167 and 5;
FT AAI32311/AAI32313)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="G -> R (in Ref. 1; AAA39770, 4; EDL31167 and 5;
FT AAI32311/AAI32313)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="L -> F (in Ref. 1; AAA39770, 4; EDL31167 and 5;
FT AAI32311/AAI32313)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20933 MW; A9F8F621D858F45A CRC64;
MKLLLLLCLE LTLVYVHAEE ASSEGQNLNV EKINGKWFSI LLASDKREKI EEHGTMRVFV
EHIDVLENSL AFKFHTVIDE ECTEIYLVAD KTEKAGEYSV TYDGFNTFTI LKTDYDNYIM
FHLINKKDEE NFQLMELFGR EPDLSSDIKE KFAKLCEEHG IVRENIIDLS NANRCLQARE
