Major urinary protein precursor - Rattus norvegicus (Rat)

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P02761 (MUP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 127. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names	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
Organism	Rattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier	10116 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	181 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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: Cytoplasm › cytosol. 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 process	Behavior Transport
Cellular component	Cytoplasm Secreted
Disease	Allergen
Domain	Signal
Ligand	Pheromone-binding
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	aerobic 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 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-dependent 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 cascade Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytosol 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_function	insulin-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Ref.7 Ref.10

Chain

20 – 181

162

Major urinary protein

PRO_0000017925

Chain

29 – 179

151

15.5 kDa fatty acid-binding protein

PRO_0000017926

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Probable

Disulfide bond

83 ↔ 176

Ref.9

Experimental info

Sequence conflict

R → S in AAA41198. Ref.5

Sequence conflict

G → D in CAA24531. Ref.7

Secondary structure

181

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P02761 [UniParc].

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

181

20,737

        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' referencesShow '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.

IPI

IPI00191711.

PIR

UART. A92317.

RefSeq

NP_671747.1. NM_147214.2.

UniGene

Rn.224459.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P02761.

SMR

P02761. Positions 20-177.

ModBase

Search...

Protein family/group databases

Allergome

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

Proteomic databases

PaxDb

P02761.

PRIDE

P02761.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

259246.

KEGG

rno:259246.

UCSC

RGD:708506. rat.

Organism-specific databases

RGD

708506. LOC259246.

Phylogenomic databases

eggNOG

NOG45000.

HOGENOM

HOG000231458.

HOVERGEN

HBG000215.

InParanoid

P02761.

OMA

HANGECK.

OrthoDB

EOG4GMTZB.

Gene expression databases

Genevestigator

P02761.

GermOnline

ENSRNOG00000024745. Rattus norvegicus.

Family and domain databases

Gene3D

2.40.128.20. 1 hit.

InterPro

IPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002971. Maj_urinary.
[Graphical view]

PANTHER

PTHR11430:SF29. PTHR11430:SF29. 1 hit.

Pfam

PF00061. Lipocalin. 1 hit.
[Graphical view]

PRINTS

PR00179. LIPOCALIN.
PR01221. MAJORURINARY.

SUPFAM

SSF50814. Calycin. 1 hit.

PROSITE

PS00213. LIPOCALIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P02761.

NextBio

624294.

Entry information

Entry name

MUP_RAT

Accession

Primary (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:	April 3, 2013
This is version 127 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Allergens

Nomenclature of allergens and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following chain:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents