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P02761 (MUP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. 15.5 kDa fatty acid-binding protein
    Short name=15.5 kDa FABP
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subcellular location

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

Secreted.

Tissue specificity

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

Induction

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

Allergenic properties

Causes an allergic reaction in human. Ref.10

Sequence similarities

Belongs to the calycin superfamily. Lipocalin family.

Ontologies

Keywords
   Biological processBehavior
Transport
   Cellular componentCytoplasm
Secreted
   DiseaseAllergen
   DomainSignal
   LigandPheromone-binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaerobic respiration

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to lipid

Inferred from sequence or structural similarity. Source: UniProtKB

energy reserve metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glucose homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

heat generation

Inferred from sequence or structural similarity. Source: UniProtKB

insulin receptor signaling pathway

Inferred from sequence or structural similarity. Source: GOC

locomotor rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of gluconeogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of insulin secretion involved in cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of lipid biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of lipid storage

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of glucose metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of lipid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein kinase B signaling

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 6886376. Source: UniProtKB

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functioninsulin-activated receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

pheromone binding

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule binding

Inferred from electronic annotation. Source: InterPro

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.7 Ref.10
Chain20 – 181162Major urinary protein
PRO_0000017925
Chain29 – 17915115.5 kDa fatty acid-binding protein
PRO_0000017926

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Probable
Disulfide bond83 ↔ 176 Ref.9

Experimental info

Sequence conflict261R → S in AAA41198. Ref.5
Sequence conflict551G → D in CAA24531. Ref.7

Secondary structure

............................ 181
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02761 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 6A01309DC55032DC

FASTA18120,737
        10         20         30         40         50         60 
MKLLLLLLCL GLTLVCGHAE EASSTRGNLD VAKLNGDWFS IVVASNKREK IEENGSMRVF 

        70         80         90        100        110        120 
MQHIDVLENS LGFKFRIKEN GECRELYLVA YKTPEDGEYF VEYDGGNTFT ILKTDYDRYV 

       130        140        150        160        170        180 
MFHLINFKNG ETFQLMVLYG RTKDLSSDIK EKFAKLCEAH GITRDNIIDL TKTDRCLQAR 


G 

« Hide

References

« Hide 'large scale' references
[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]"Cloning and sequence of several alpha 2u-globulin cDNAs."
Unterman R.D., Lynch K.R., Nakhasi H.L., Dolan K.P., Hamilton J.W., Cohn D.V., Feigelson P.
Proc. Natl. Acad. Sci. U.S.A. 78:3478-3482(1981) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRUART. A92317.
RefSeqNP_671747.1. NM_147214.2.
UniGeneRn.224459.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A2GX-ray2.90A/B/C/D1-181[»]
2A2UX-ray2.50A/B/C/D1-181[»]
ProteinModelPortalP02761.
SMRP02761. Positions 20-177.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome3464. Rat n 1.0101.
611. Rat n 1.

Proteomic databases

PaxDbP02761.
PRIDEP02761.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID259246.
KEGGrno:259246.
UCSCRGD:708506. rat.

Organism-specific databases

RGD708506. LOC259246.

Phylogenomic databases

eggNOGNOG45000.
HOGENOMHOG000231458.
HOVERGENHBG000215.
InParanoidP02761.
PhylomeDBP02761.
TreeFamTF338197.

Gene expression databases

GenevestigatorP02761.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002971. Maj_urinary.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00179. LIPOCALIN.
PR01221. MAJORURINARY.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02761.
NextBio624294.

Entry information

Entry nameMUP_RAT
AccessionPrimary (citable) accession number: P02761
Secondary accession number(s): Q54AE7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 11, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Allergens

Nomenclature of allergens and list of entries