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P02761

- MUP_RAT

UniProt

P02761 - MUP_RAT

Protein

Major urinary protein

Gene
N/A
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Major urinary proteins (Mups) bind and release pheromones. They may also protect pheromones from oxidation. In this context, they play a role in the regulation of social behaviors, such as aggression, mating, pup-suckling, territory establishment and dominance. Acts as a kairomone, detected by the prey vomeronasal organ and inducing fear reactions in mice.

    GO - Molecular functioni

    1. insulin-activated receptor activity Source: UniProtKB
    2. pheromone binding Source: UniProtKB
    3. small molecule binding Source: InterPro
    4. transporter activity Source: InterPro

    GO - Biological processi

    1. aerobic respiration Source: UniProtKB
    2. cellular response to lipid Source: UniProtKB
    3. energy reserve metabolic process Source: UniProtKB
    4. glucose homeostasis Source: UniProtKB
    5. heat generation Source: UniProtKB
    6. insulin receptor signaling pathway Source: GOC
    7. locomotor rhythm Source: UniProtKB
    8. mitochondrion morphogenesis Source: UniProtKB
    9. negative regulation of gluconeogenesis Source: UniProtKB
    10. negative regulation of insulin secretion involved in cellular response to glucose stimulus Source: UniProtKB
    11. negative regulation of lipid biosynthetic process Source: UniProtKB
    12. negative regulation of lipid storage Source: UniProtKB
    13. negative regulation of transcription, DNA-templated Source: UniProtKB
    14. positive regulation of gene expression Source: UniProtKB
    15. positive regulation of glucose metabolic process Source: UniProtKB
    16. positive regulation of lipid metabolic process Source: UniProtKB
    17. positive regulation of protein kinase B signaling Source: UniProtKB

    Keywords - Biological processi

    Behavior, Transport

    Keywords - Ligandi

    Pheromone-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Major urinary protein
    Short name:
    MUP
    Alternative name(s):
    Allergen Rat n I
    Alpha(2)-euglobulin
    Alpha-2u-globulin
    alpha-2u globulin PGCL1
    Allergen: Rat n 1
    Cleaved into the following chain:
    15.5 kDa fatty acid-binding protein
    Short name:
    15.5 kDa FABP
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi708506. LOC259246.

    Subcellular locationi

    Chain 15.5 kDa fatty acid-binding protein : Cytoplasmcytosol
    Note: It is probably taken up from the urinary lumen by endocytosis.

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular space Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Secreted

    Pathology & Biotechi

    Allergenic propertiesi

    Causes an allergic reaction in human.1 Publication

    Keywords - Diseasei

    Allergen

    Protein family/group databases

    Allergomei3464. Rat n 1.0101.
    611. Rat n 1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19192 PublicationsAdd
    BLAST
    Chaini20 – 181162Major urinary proteinPRO_0000017925Add
    BLAST
    Chaini29 – 17915115.5 kDa fatty acid-binding proteinPRO_0000017926Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi54 – 541N-linked (GlcNAc...)Curated
    Disulfide bondi83 ↔ 1761 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP02761.
    PRIDEiP02761.

    Expressioni

    Tissue specificityi

    Abundant in the urine of adult male rats but absent from that of females.

    Inductioni

    Synthesis of this protein in the hepatic parenchymal cells is induced in vivo by androgens, glucocorticoids, growth hormone, and insulin, and inhibited by estrogens.

    Gene expression databases

    GenevestigatoriP02761.

    Structurei

    Secondary structure

    1
    181
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni24 – 274
    Helixi31 – 344
    Beta strandi39 – 446
    Helixi48 – 503
    Beta strandi60 – 678
    Beta strandi70 – 8112
    Beta strandi83 – 9210
    Beta strandi99 – 11416
    Beta strandi116 – 12813
    Beta strandi131 – 14414
    Helixi147 – 15812
    Turni159 – 1613
    Helixi164 – 1663
    Beta strandi167 – 1693
    Helixi170 – 1723

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A2GX-ray2.90A/B/C/D1-181[»]
    2A2UX-ray2.50A/B/C/D1-181[»]
    ProteinModelPortaliP02761.
    SMRiP02761. Positions 20-177.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02761.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the calycin superfamily. Lipocalin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG45000.
    HOGENOMiHOG000231458.
    HOVERGENiHBG000215.
    InParanoidiP02761.
    PhylomeDBiP02761.
    TreeFamiTF338197.

    Family and domain databases

    Gene3Di2.40.128.20. 1 hit.
    InterProiIPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    IPR002971. Maj_urinary.
    [Graphical view]
    PfamiPF00061. Lipocalin. 1 hit.
    [Graphical view]
    PRINTSiPR00179. LIPOCALIN.
    PR01221. MAJORURINARY.
    SUPFAMiSSF50814. SSF50814. 1 hit.
    PROSITEiPS00213. LIPOCALIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P02761-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLLLLLLCL GLTLVCGHAE EASSTRGNLD VAKLNGDWFS IVVASNKREK    50
    IEENGSMRVF MQHIDVLENS LGFKFRIKEN GECRELYLVA YKTPEDGEYF 100
    VEYDGGNTFT ILKTDYDRYV MFHLINFKNG ETFQLMVLYG RTKDLSSDIK 150
    EKFAKLCEAH GITRDNIIDL TKTDRCLQAR G 181
    Length:181
    Mass (Da):20,737
    Last modified:July 21, 1986 - v1
    Checksum:i6A01309DC55032DC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261R → S in AAA41198. (PubMed:6167987)Curated
    Sequence conflicti55 – 551G → D in CAA24531. (PubMed:6163771)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26835 mRNA. Translation: AAA40643.1.
    M26837 mRNA. Translation: AAA40641.1.
    AB039822 mRNA. Translation: BAA96479.1.
    BC088109 mRNA. Translation: AAH88109.1.
    BC098654 mRNA. Translation: AAH98654.1.
    BC105816 mRNA. Translation: AAI05817.1.
    U31287 mRNA. Translation: AAA75511.1.
    V01220 mRNA. Translation: CAA24531.1.
    J00737 mRNA. Translation: AAA41198.1.
    PIRiA92317. UART.
    RefSeqiNP_671747.1. NM_147214.2.
    UniGeneiRn.224459.

    Genome annotation databases

    GeneIDi259246.
    KEGGirno:259246.
    UCSCiRGD:708506. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26835 mRNA. Translation: AAA40643.1 .
    M26837 mRNA. Translation: AAA40641.1 .
    AB039822 mRNA. Translation: BAA96479.1 .
    BC088109 mRNA. Translation: AAH88109.1 .
    BC098654 mRNA. Translation: AAH98654.1 .
    BC105816 mRNA. Translation: AAI05817.1 .
    U31287 mRNA. Translation: AAA75511.1 .
    V01220 mRNA. Translation: CAA24531.1 .
    J00737 mRNA. Translation: AAA41198.1 .
    PIRi A92317. UART.
    RefSeqi NP_671747.1. NM_147214.2.
    UniGenei Rn.224459.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2A2G X-ray 2.90 A/B/C/D 1-181 [» ]
    2A2U X-ray 2.50 A/B/C/D 1-181 [» ]
    ProteinModelPortali P02761.
    SMRi P02761. Positions 20-177.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    Allergomei 3464. Rat n 1.0101.
    611. Rat n 1.

    Proteomic databases

    PaxDbi P02761.
    PRIDEi P02761.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 259246.
    KEGGi rno:259246.
    UCSCi RGD:708506. rat.

    Organism-specific databases

    RGDi 708506. LOC259246.

    Phylogenomic databases

    eggNOGi NOG45000.
    HOGENOMi HOG000231458.
    HOVERGENi HBG000215.
    InParanoidi P02761.
    PhylomeDBi P02761.
    TreeFami TF338197.

    Miscellaneous databases

    EvolutionaryTracei P02761.
    NextBioi 624294.

    Gene expression databases

    Genevestigatori P02761.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    IPR002971. Maj_urinary.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR00179. LIPOCALIN.
    PR01221. MAJORURINARY.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00213. LIPOCALIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Length polymorphism in the 3' noncoding region of rat hepatic alpha 2u-globulin mRNAs."
      Ichiyoshi Y., Endo H., Yamamoto M.
      Biochim. Biophys. Acta 910:43-51(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Kurtz D.T., Dey M.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
    3. "Molecular evidence of complex tissue- and sex-specific mRNA expression of the rat alpha(2u)-globulin multigene family."
      Saito K., Nishikawa J., Imagawa M., Nishihara T., Matsuo M.
      Biochem. Biophys. Res. Commun. 272:337-344(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Preputial gland.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver and Spleen.
    5. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-181.
    6. "The structure and expression of very closely related members of the alpha 2u globulin gene family."
      Dolan K.P., Unterman R.D., McLaughlin M., Nakhasi H.L., Lynch K.R., Feigelson P.
      J. Biol. Chem. 257:13527-13534(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 34-181.
    7. "Amino acid sequence of the precursor of rat liver alpha 2 micro-globulin."
      Drickamer K., Kwoh T.J., Kurtz D.T.
      J. Biol. Chem. 256:3634-3636(1981) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-65.
    8. "Kidney fatty acid-binding protein: identification as alpha 2U-globulin."
      Kimura H., Odani S., Suzuki J., Arakawa M., Ono T.
      FEBS Lett. 246:101-104(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-48.
      Tissue: Kidney.
    9. "Primary structure and cellular distribution of two fatty acid-binding proteins in adult rat kidneys."
      Kimura H., Odani S., Nishi S., Sato H., Arakawa M., Ono T.
      J. Biol. Chem. 266:5963-5972(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-179, DISULFIDE BOND.
      Tissue: Kidney.
    10. "Purification and identification of allergenic alpha (2u)-globulin species of rat urine."
      Bayard C., Holmquist L., Vesterberg O.
      Biochim. Biophys. Acta 1290:129-134(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-44, ALLERGEN.
      Tissue: Urine.
    11. Erratum
      Bayard C., Holmquist L., Vesterberg O.
      Biochim. Biophys. Acta 1291:253-255(1996)
    12. "Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography."
      Boecksel Z., Groom C.R., Flower D.R., Wright C.E., Phillips S.E.V., Cavaggioni A., Findlay J.B.C., North A.C.T.
      Nature 360:186-188(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

    Entry informationi

    Entry nameiMUP_RAT
    AccessioniPrimary (citable) accession number: P02761
    Secondary accession number(s): Q54AE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Allergens
      Nomenclature of allergens and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3