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Major urinary protein 1 (MUP 1)

 MUP1_MOUSE              Reviewed;         180 AA.
P11588; Q61921;
01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
01-OCT-1989, sequence version 1.
31-JAN-2018, entry version 169.
RecName: Full=Major urinary protein 1;
Short=MUP 1;
Flags: Precursor;
Name=Mup1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=3600652; DOI=10.1128/MCB.7.5.1938;
Shahan K., Gilmartin M., Derman E.;
"Nucleotide sequences of liver, lachrymal, and submaxillary gland
mouse major urinary protein mRNAs: mosaic structure and construction
of panels of gene-specific synthetic oligonucleotide probes.";
Mol. Cell. Biol. 7:1938-1946(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=2888770; DOI=10.1083/jcb.105.3.1073;
Bennett A.L., Paulson K.E., Miller R.E., Darnell J.E. Jr.;
"Acquisition of antigens characteristic of adult pericentral
hepatocytes by differentiating fetal hepatoblasts in vitro.";
J. Cell Biol. 105:1073-1085(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 19-180.
PubMed=16104761; DOI=10.1021/ja0527525;
Barratt E., Bingham R.J., Warner D.J., Laughton C.A., Phillips S.E.,
Homans S.W.;
"Van der Waals interactions dominate ligand-protein association in a
protein binding site occluded from solvent water.";
J. Am. Chem. Soc. 127:11827-11834(2005).
-!- FUNCTION: Binds pheromones that are released from drying urine of
males. These pheromones affect the sexual behavior of females.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Abundant in the urine of adult male mice but
absent from that of females.
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA39764.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; M16355; AAA39767.1; -; mRNA.
EMBL; M28649; AAA39764.1; ALT_INIT; mRNA.
EMBL; BC012221; AAH12221.1; -; mRNA.
CCDS; CCDS18231.1; -.
RefSeq; NP_001186924.1; NM_001199995.1.
UniGene; Mm.335875; -.
UniGene; Mm.422695; -.
UniGene; Mm.457982; -.
UniGene; Mm.482072; -.
UniGene; Mm.482236; -.
PDB; 1QY0; X-ray; 1.80 A; A=23-180.
PDB; 1QY1; X-ray; 1.70 A; A=19-180.
PDB; 1QY2; X-ray; 1.75 A; A=19-180.
PDB; 1YP6; X-ray; 1.80 A; A=19-180.
PDB; 1YP7; X-ray; 2.00 A; A=19-180.
PDB; 2DM5; X-ray; 1.70 A; A=20-180.
PDBsum; 1QY0; -.
PDBsum; 1QY1; -.
PDBsum; 1QY2; -.
PDBsum; 1YP6; -.
PDBsum; 1YP7; -.
PDBsum; 2DM5; -.
ProteinModelPortal; P11588; -.
SMR; P11588; -.
IntAct; P11588; 4.
MINT; MINT-1865367; -.
Allergome; 478; Mus m 1.
iPTMnet; P11588; -.
PhosphoSitePlus; P11588; -.
PaxDb; P11588; -.
PRIDE; P11588; -.
Ensembl; ENSMUST00000117932; ENSMUSP00000112787; ENSMUSG00000094793.
GeneID; 100039054; -.
KEGG; mmu:100039054; -.
UCSC; uc008tay.3; mouse.
CTD; 100039054; -.
MGI; MGI:97233; Mup1.
eggNOG; ENOG410J5XW; Eukaryota.
eggNOG; ENOG411154J; LUCA.
GeneTree; ENSGT00530000063356; -.
HOGENOM; HOG000231458; -.
HOVERGEN; HBG000215; -.
InParanoid; P11588; -.
PhylomeDB; P11588; -.
TreeFam; TF338197; -.
EvolutionaryTrace; P11588; -.
PRO; PR:P11588; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000094793; -.
ExpressionAtlas; P11588; baseline and differential.
Genevisible; P11588; MM.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005009; F:insulin-activated receptor activity; IDA:UniProtKB.
GO; GO:0005186; F:pheromone activity; IDA:MGI.
GO; GO:0005550; F:pheromone binding; IDA:UniProtKB.
GO; GO:0036094; F:small molecule binding; IEA:InterPro.
GO; GO:0009060; P:aerobic respiration; IDA:UniProtKB.
GO; GO:0071240; P:cellular response to food; IEP:UniProtKB.
GO; GO:0071396; P:cellular response to lipid; IDA:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IEP:UniProtKB.
GO; GO:0071394; P:cellular response to testosterone stimulus; IEP:UniProtKB.
GO; GO:0006112; P:energy reserve metabolic process; IDA:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0031649; P:heat generation; IDA:UniProtKB.
GO; GO:0045475; P:locomotor rhythm; IDA:UniProtKB.
GO; GO:0070584; P:mitochondrion morphogenesis; IDA:UniProtKB.
GO; GO:0045721; P:negative regulation of gluconeogenesis; IDA:UniProtKB.
GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:UniProtKB.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; IDA:UniProtKB.
GO; GO:0010888; P:negative regulation of lipid storage; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0010907; P:positive regulation of glucose metabolic process; IDA:UniProtKB.
GO; GO:0045834; P:positive regulation of lipid metabolic process; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0035634; P:response to stilbenoid; IEP:UniProtKB.
Gene3D; 2.40.128.20; -; 1.
InterPro; IPR012674; Calycin.
InterPro; IPR002345; Lipocalin.
InterPro; IPR022272; Lipocalin_CS.
InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
InterPro; IPR002971; Maj_urinary.
PANTHER; PTHR11430; PTHR11430; 1.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR01221; MAJORURINARY.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Pheromone-binding;
Reference proteome; Secreted; Signal; Transport.
SIGNAL 1 18
CHAIN 19 180 Major urinary protein 1.
/FTId=PRO_0000017927.
DISULFID 82 175
CONFLICT 44 44 S -> F (in Ref. 2; AAA39764).
{ECO:0000305}.
CONFLICT 127 127 K -> N (in Ref. 2; AAA39764).
{ECO:0000305}.
HELIX 30 33 {ECO:0000244|PDB:1QY1}.
STRAND 38 46 {ECO:0000244|PDB:1QY1}.
HELIX 47 50 {ECO:0000244|PDB:1QY1}.
STRAND 59 65 {ECO:0000244|PDB:1QY1}.
STRAND 67 78 {ECO:0000244|PDB:1QY1}.
STRAND 81 91 {ECO:0000244|PDB:1QY1}.
STRAND 98 113 {ECO:0000244|PDB:1QY1}.
STRAND 115 127 {ECO:0000244|PDB:1QY1}.
STRAND 130 142 {ECO:0000244|PDB:1QY1}.
HELIX 146 157 {ECO:0000244|PDB:1QY1}.
TURN 158 160 {ECO:0000244|PDB:1QY1}.
HELIX 163 165 {ECO:0000244|PDB:1QY1}.
STRAND 166 168 {ECO:0000244|PDB:1QY1}.
TURN 170 172 {ECO:0000244|PDB:1YP7}.
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


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