位置:首页 > 蛋白库 > MUP4_MOUSE
MUP4_MOUSE
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   03-AUG-2022, entry version 172.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; P11590; -.
DR   PRIDE; P11590; -.
DR   ProteomicsDB; 287642; -.
DR   DNASU; 17843; -.
DR   Ensembl; ENSMUST00000075973; ENSMUSP00000075356; ENSMUSG00000041333.
DR   GeneID; 17843; -.
DR   KEGG; mmu:17843; -.
DR   UCSC; uc008tag.1; mouse.
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; 1475169at2759; -.
DR   PhylomeDB; P11590; -.
DR   TreeFam; TF338197; -.
DR   BioGRID-ORCS; 17843; 0 hits in 52 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 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: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; 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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025