MUP6_MOUSE
ID MUP6_MOUSE Reviewed; 180 AA.
AC P02762; P70119; Q78EF5; Q91V46;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Major urinary protein 6;
DE Short=MUP 6;
DE AltName: Full=Alpha-2U-globulin;
DE AltName: Full=Group 1, BS6;
DE AltName: Allergen=Mus m 1;
DE Flags: Precursor;
GN Name=Mup6;
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 [GENOMIC DNA].
RX PubMed=3004935; DOI=10.1002/j.1460-2075.1985.tb04059.x;
RA Clark A.J., Ghazal P., Bingham R.W., Barrett D., Bishop J.O.;
RT "Sequence structures of a mouse major urinary protein gene and pseudogene
RT compared.";
RL EMBO J. 4:3159-3165(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6329733; DOI=10.1002/j.1460-2075.1984.tb01925.x;
RA Clark A.J., Clissold P.M., Shawi R.A., Beattie P., Bishop J.O.;
RT "Structure of mouse major urinary protein genes: different splicing
RT configurations in the 3'-non-coding region.";
RL EMBO J. 3:1045-1052(1984).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
RX PubMed=3858875; DOI=10.1073/pnas.82.12.4182;
RA Ghazal P., Clark J.A., Bishop J.;
RT "Evolutionary amplification of a pseudogene.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4182-4185(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE OF 1-32.
RX PubMed=7937138; DOI=10.1093/nar/22.20.4132;
RA Caubin J., Iglesias T., Bernal J., Munoz A., Marquez G., Barbero J.L.,
RA Zaballos A.;
RT "Isolation of genomic DNA fragments corresponding to genes modulated in
RT vivo by a transcription factor.";
RL Nucleic Acids Res. 22:4132-4138(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
RX PubMed=2824995; DOI=10.1128/mcb.7.10.3705-3712.1987;
RA Held W.A., Gallagher J.F., Hohman C.M., Kuhn N.J., Sampsell B.M.,
RA Hughes R.G. Jr.;
RT "Identification and characterization of functional genes encoding the mouse
RT major urinary proteins.";
RL Mol. Cell. Biol. 7:3705-3712(1987).
RN [8]
RP NUCLEOTIDE SEQUENCE OF 20-41.
RX PubMed=7107707; DOI=10.1083/jcb.94.2.414;
RA Krauter K., Leinwand L., D'Eustachio P., Ruddle F., Darnell J.E. Jr.;
RT "Structural genes of the mouse major urinary protein are on chromosome 4.";
RL J. Cell Biol. 94:414-417(1982).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-180.
RX PubMed=8065364; DOI=10.1128/mcb.14.9.6326-6336.1994;
RA Belgrader P., Maquat L.E.;
RT "Nonsense but not missense mutations can decrease the abundance of nuclear
RT mRNA for the mouse major urinary protein, while both types of mutations can
RT facilitate exon skipping.";
RL Mol. Cell. Biol. 14:6326-6336(1994).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=1279439; DOI=10.1038/360186a0;
RA Boecksel Z., Groom C.R., Flower D.R., Wright C.E., Phillips S.E.V.,
RA Cavaggioni A., Findlay J.B.C., North A.C.T.;
RT "Pheromone binding to two rodent urinary proteins revealed by X-ray
RT crystallography.";
RL Nature 360:186-188(1992).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=11316880; DOI=10.1110/ps.52201;
RA Timm D.E., Baker L.-J., Mueller H., Zidek L., Novotny M.V.;
RT "Structural basis of pheromone binding to mouse major urinary protein (MUP-
RT I).";
RL Protein Sci. 10:997-1004(2001).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=14871097; DOI=10.1021/ja038461i;
RA Bingham R.J., Findlay J.B., Hsieh S.-Y., Kalverda A.P., Kjellberg A.,
RA Perazzolo C., Phillips S.E., Seshadri K., Trinh C.H., Turnbull W.B.,
RA Bodenhausen G., Homans S.W.;
RT "Thermodynamics of binding of 2-methoxy-3-isopropylpyrazine and 2-methoxy-
RT 3-isobutylpyrazine to the major urinary protein.";
RL J. Am. Chem. Soc. 126:1675-1681(2004).
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 -!- ALLERGEN: Causes an allergic reaction in human.
CC -!- MISCELLANEOUS: There are about 15 group 1 MUP genes and their
CC transcripts make up about 5% of male mouse liver RNA.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; X03208; CAA26953.1; -; Genomic_DNA.
DR EMBL; AK013259; BAB28753.1; -; mRNA.
DR EMBL; BC013649; AAH13649.1; -; mRNA.
DR EMBL; M17759; AAA39763.1; -; Genomic_DNA.
DR EMBL; Z32546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; M17818; AAA40543.1; -; Genomic_DNA.
DR EMBL; M17814; AAA40540.1; -; Genomic_DNA.
DR EMBL; M17817; AAA40544.1; -; Genomic_DNA.
DR EMBL; U12201; AAA99109.1; -; Genomic_DNA.
DR CCDS; CCDS51187.2; -.
DR CCDS; CCDS57278.1; -.
DR PIR; A03216; UAMS.
DR RefSeq; NP_001128599.1; NM_001135127.2.
DR RefSeq; NP_001186865.1; NM_001199936.1.
DR RefSeq; NP_001268908.1; NM_001281979.1.
DR RefSeq; XP_006537551.1; XM_006537488.2.
DR PDB; 1I04; X-ray; 2.00 A; A=1-180.
DR PDB; 1I05; X-ray; 2.00 A; A=1-180.
DR PDB; 1I06; X-ray; 1.90 A; A=1-180.
DR PDB; 1MUP; X-ray; 2.40 A; A=15-180.
DR PDB; 2LB6; NMR; -; A=19-180.
DR PDB; 2NND; X-ray; 1.60 A; A=19-75, A=82-180.
DR PDB; 2NNE; X-ray; 1.60 A; A=19-75, A=82-180.
DR PDBsum; 1I04; -.
DR PDBsum; 1I05; -.
DR PDBsum; 1I06; -.
DR PDBsum; 1MUP; -.
DR PDBsum; 2LB6; -.
DR PDBsum; 2NND; -.
DR PDBsum; 2NNE; -.
DR AlphaFoldDB; P02762; -.
DR BMRB; P02762; -.
DR SMR; P02762; -.
DR STRING; 10090.ENSMUSP00000079442; -.
DR Allergome; 3378; Mus m 1.0101.
DR Allergome; 478; Mus m 1.
DR Allergome; 8430; Mus m 1.0102.
DR iPTMnet; P02762; -.
DR PhosphoSitePlus; P02762; -.
DR SwissPalm; P02762; -.
DR SWISS-2DPAGE; P02762; -.
DR jPOST; P02762; -.
DR MaxQB; P02762; -.
DR PaxDb; P02762; -.
DR PRIDE; P02762; -.
DR Ensembl; ENSMUST00000080606; ENSMUSP00000079442; ENSMUSG00000078673.
DR Ensembl; ENSMUST00000095051; ENSMUSP00000092661; ENSMUSG00000078675.
DR Ensembl; ENSMUST00000107483; ENSMUSP00000103107; ENSMUSG00000078675.
DR Ensembl; ENSMUST00000107506; ENSMUSP00000103130; ENSMUSG00000078686.
DR Ensembl; ENSMUST00000122381; ENSMUSP00000113741; ENSMUSG00000078686.
DR GeneID; 100038948; -.
DR GeneID; 100039177; -.
DR GeneID; 100189605; -.
DR KEGG; mmu:100038948; -.
DR KEGG; mmu:100039177; -.
DR KEGG; mmu:100189605; -.
DR UCSC; uc008tak.3; mouse.
DR CTD; 100038948; -.
DR CTD; 100039177; -.
DR CTD; 100189605; -.
DR VEuPathDB; HostDB:ENSMUSG00000078673; -.
DR VEuPathDB; HostDB:ENSMUSG00000078675; -.
DR VEuPathDB; HostDB:ENSMUSG00000078686; -.
DR eggNOG; ENOG502S6GK; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR HOGENOM; CLU_094061_4_0_1; -.
DR InParanoid; P02762; -.
DR OMA; VPGKFRH; -.
DR OrthoDB; 1107052at2759; -.
DR PhylomeDB; P02762; -.
DR TreeFam; TF338197; -.
DR BioGRID-ORCS; 100038948; 3 hits in 24 CRISPR screens.
DR BioGRID-ORCS; 100039177; 3 hits in 25 CRISPR screens.
DR BioGRID-ORCS; 100189605; 4 hits in 29 CRISPR screens.
DR EvolutionaryTrace; P02762; -.
DR PRO; PR:P02762; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P02762; protein.
DR Bgee; ENSMUSG00000078673; Expressed in quadriceps femoris and 25 other tissues.
DR ExpressionAtlas; P02762; baseline and differential.
DR Genevisible; P02762; MM.
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 1: Evidence at protein level;
KW 3D-structure; Allergen; Disulfide bond; Pheromone-binding;
KW Reference proteome; Secreted; Signal; Transport.
FT SIGNAL 1..18
FT CHAIN 19..180
FT /note="Major urinary protein 6"
FT /id="PRO_0000017932"
FT DISULFID 82..175
FT CONFLICT 145
FT /note="S -> M (in Ref. 1; CAA26953)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="E -> K (in Ref. 9; AAA99109)"
FT /evidence="ECO:0000305"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1I04"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:2NND"
FT STRAND 38..46
FT /evidence="ECO:0007829|PDB:2NND"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:2NND"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:2NND"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:2NND"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:2NND"
FT STRAND 98..113
FT /evidence="ECO:0007829|PDB:2NND"
FT STRAND 115..127
FT /evidence="ECO:0007829|PDB:2NND"
FT STRAND 130..142
FT /evidence="ECO:0007829|PDB:2NND"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:2NND"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:2NND"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2NND"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1I06"
SQ SEQUENCE 180 AA; 20649 MW; B4A429BDA0700947 CRC64;
MKMLLLLCLG LTLVCVHAEE ASSTGRNFNV EKINGEWHTI ILASDKREKI EDNGNFRLFL
EQIHVLENSL VLKFHTVRDE ECSELSMVAD KTEKAGEYSV TYDGFNTFTI PKTDYDNFLM
AHLINEKDGE TFQLMGLYGR EPDLSSDIKE RFAQLCEEHG ILRENIIDLS NANRCLQARE
