MUP11_MOUSE
ID MUP11_MOUSE Reviewed; 181 AA.
AC P04938;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Major urinary protein 11 {ECO:0000305};
DE Flags: Precursor;
GN Name=Mup11 {ECO:0000312|MGI:MGI:3709617};
GN Synonyms=Mup9 {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 [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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-181.
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 [3]
RP IDENTIFICATION.
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 [4]
RP STRUCTURE BY NMR OF 20-181, FUNCTION, AND DISULFIDE BOND.
RX PubMed=25279835; DOI=10.1371/journal.pone.0108415;
RA Phelan M.M., McLean L., Armstrong S.D., Hurst J.L., Beynon R.J., Lian L.Y.;
RT "The structure, stability and pheromone binding of the male mouse protein
RT sex pheromone darcin.";
RL PLoS ONE 9:E108415-E108415(2014).
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 (Probable). Binds the pheromone analog 2-
CC sec-butyl-4,5-dihydrothiazole (SBT) in vitro (PubMed:25279835).
CC {ECO:0000269|PubMed:25279835, 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; BX950196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X03524; CAA27227.1; -; mRNA.
DR EMBL; X04115; CAA27729.1; -; mRNA.
DR EMBL; M27609; AAA39765.1; -; mRNA.
DR EMBL; BK006652; DAA06305.1; -; Genomic_DNA.
DR PIR; S10124; S10124.
DR RefSeq; NP_001157998.1; NM_001164526.1.
DR RefSeq; NP_001186262.1; NM_001199333.1.
DR PDB; 2LB6; NMR; -; A=20-181.
DR PDBsum; 2LB6; -.
DR AlphaFoldDB; P04938; -.
DR BMRB; P04938; -.
DR SMR; P04938; -.
DR STRING; 10090.ENSMUSP00000095648; -.
DR Allergome; 478; Mus m 1.
DR PhosphoSitePlus; P04938; -.
DR SwissPalm; P04938; -.
DR SWISS-2DPAGE; P04938; -.
DR jPOST; P04938; -.
DR MaxQB; P04938; -.
DR PaxDb; P04938; -.
DR PeptideAtlas; P04938; -.
DR PRIDE; P04938; -.
DR DNASU; 100048884; -.
DR Ensembl; ENSMUST00000098040; ENSMUSP00000095648; ENSMUSG00000078674.
DR Ensembl; ENSMUST00000098046; ENSMUSP00000095654; ENSMUSG00000073834.
DR GeneID; 100039028; -.
DR GeneID; 100048884; -.
DR KEGG; mmu:100039028; -.
DR KEGG; mmu:100048884; -.
DR CTD; 100039028; -.
DR CTD; 100048884; -.
DR MGI; MGI:3709617; Mup11.
DR VEuPathDB; HostDB:ENSMUSG00000073834; -.
DR VEuPathDB; HostDB:ENSMUSG00000078674; -.
DR eggNOG; ENOG502S6GK; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR InParanoid; P04938; -.
DR OMA; HASGECK; -.
DR OrthoDB; 1475169at2759; -.
DR PhylomeDB; P04938; -.
DR BioGRID-ORCS; 100039028; 2 hits in 10 CRISPR screens.
DR BioGRID-ORCS; 100048884; 4 hits in 23 CRISPR screens.
DR ChiTaRS; Mup11; mouse.
DR PRO; PR:P04938; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P04938; protein.
DR Bgee; ENSMUSG00000073834; Expressed in liver and 35 other tissues.
DR ExpressionAtlas; P04938; baseline and differential.
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; IDA: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:0071394; P:cellular response to testosterone stimulus; IEP: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; Behavior; Disulfide bond; Pheromone-binding;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..181
FT /note="Major urinary protein 11"
FT /evidence="ECO:0000255"
FT /id="PRO_0000201023"
FT DISULFID 83..176
FT /evidence="ECO:0000269|PubMed:25279835"
FT CONFLICT 31
FT /note="V -> R (in Ref. 2; AAA39765/CAA27227)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="N -> K (in Ref. 2; CAA27729)"
FT /evidence="ECO:0000305"
FT CONFLICT 155
FT /note="Q -> K (in Ref. 2; CAA27729)"
FT /evidence="ECO:0000305"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2LB6"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:2LB6"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:2LB6"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:2LB6"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2LB6"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:2LB6"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2LB6"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:2LB6"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:2LB6"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:2LB6"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2LB6"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2LB6"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:2LB6"
FT STRAND 131..144
FT /evidence="ECO:0007829|PDB:2LB6"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:2LB6"
FT HELIX 150..157
FT /evidence="ECO:0007829|PDB:2LB6"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:2LB6"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2LB6"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:2LB6"
SQ SEQUENCE 181 AA; 20763 MW; D81FEBBF70A7E310 CRC64;
MKMLLLLLCL GLTLVCVHAE EASSTGRNFN VEKINGEWHT IILASDKREK IEDNGNFRLF
LEQIHVLENS LVLKFHTVRD EECSELSMVA DKTEKAGEYS VTYDGFNTFT IPKTDYDNFL
MAHLINEKDG ETFQLMGLYG REPDLSSDIK ERFAQLCEEH GILRENIIDL SNANRCLQAR
E
