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Major urinary protein (MUP) (Allergen Rat n I) (Alpha(2)-euglobulin) (Alpha-2u-globulin) (alpha-2u globulin PGCL1) (allergen Rat n 1) [Cleaved into: 15.5 kDa fatty acid-binding protein (15.5 kDa FABP)]

 MUP_RAT                 Reviewed;         181 AA.
P02761; Q54AE7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
10-MAY-2017, entry version 148.
RecName: Full=Major urinary protein;
Short=MUP;
AltName: Full=Allergen Rat n I;
AltName: Full=Alpha(2)-euglobulin;
AltName: Full=Alpha-2u-globulin;
AltName: Full=alpha-2u globulin PGCL1;
AltName: Allergen=Rat n 1;
Contains:
RecName: Full=15.5 kDa fatty acid-binding protein;
Short=15.5 kDa FABP;
Flags: Precursor;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2443176; DOI=10.1016/0167-4781(87)90093-5;
Ichiyoshi Y., Endo H., Yamamoto M.;
"Length polymorphism in the 3' noncoding region of rat hepatic alpha
2u-globulin mRNAs.";
Biochim. Biophys. Acta 910:43-51(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Kurtz D.T., Dey M.;
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Preputial gland;
PubMed=10833415; DOI=10.1006/bbrc.2000.2694;
Saito K., Nishikawa J., Imagawa M., Nishihara T., Matsuo M.;
"Molecular evidence of complex tissue- and sex-specific mRNA
expression of the rat alpha(2u)-globulin multigene family.";
Biochem. Biophys. Res. Commun. 272:337-344(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver, and Spleen;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-181.
PubMed=6167987; DOI=10.1073/pnas.78.6.3478;
Unterman R.D., Lynch K.R., Nakhasi H.L., Dolan K.P., Hamilton J.W.,
Cohn D.V., Feigelson P.;
"Cloning and sequence of several alpha 2u-globulin cDNAs.";
Proc. Natl. Acad. Sci. U.S.A. 78:3478-3482(1981).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 34-181.
PubMed=6183262;
Dolan K.P., Unterman R.D., McLaughlin M., Nakhasi H.L., Lynch K.R.,
Feigelson P.;
"The structure and expression of very closely related members of the
alpha 2u globulin gene family.";
J. Biol. Chem. 257:13527-13534(1982).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-65.
PubMed=6163771;
Drickamer K., Kwoh T.J., Kurtz D.T.;
"Amino acid sequence of the precursor of rat liver alpha 2 micro-
globulin.";
J. Biol. Chem. 256:3634-3636(1981).
[8]
PROTEIN SEQUENCE OF 29-48.
TISSUE=Kidney;
PubMed=2468522; DOI=10.1016/0014-5793(89)80261-3;
Kimura H., Odani S., Suzuki J., Arakawa M., Ono T.;
"Kidney fatty acid-binding protein: identification as alpha 2U-
globulin.";
FEBS Lett. 246:101-104(1989).
[9]
PROTEIN SEQUENCE OF 29-179, AND DISULFIDE BOND.
TISSUE=Kidney;
PubMed=2005132;
Kimura H., Odani S., Nishi S., Sato H., Arakawa M., Ono T.;
"Primary structure and cellular distribution of two fatty acid-binding
proteins in adult rat kidneys.";
J. Biol. Chem. 266:5963-5972(1991).
[10]
PROTEIN SEQUENCE OF 20-44, AND ALLERGEN.
TISSUE=Urine;
PubMed=8645715; DOI=10.1016/0304-4165(96)00006-2;
Bayard C., Holmquist L., Vesterberg O.;
"Purification and identification of allergenic alpha (2u)-globulin
species of rat urine.";
Biochim. Biophys. Acta 1290:129-134(1996).
[11]
ERRATUM.
Bayard C., Holmquist L., Vesterberg O.;
Biochim. Biophys. Acta 1291:253-255(1996).
[12]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=1279439; DOI=10.1038/360186a0;
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.;
"Pheromone binding to two rodent urinary proteins revealed by X-ray
crystallography.";
Nature 360:186-188(1992).
-!- 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.
-!- SUBCELLULAR LOCATION: 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.
-!- ALLERGEN: Causes an allergic reaction in human.
{ECO:0000269|PubMed:8645715}.
-!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
{ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M26835; AAA40643.1; -; mRNA.
EMBL; M26837; AAA40641.1; -; mRNA.
EMBL; AB039822; BAA96479.1; -; mRNA.
EMBL; BC088109; AAH88109.1; -; mRNA.
EMBL; BC098654; AAH98654.1; -; mRNA.
EMBL; BC105816; AAI05817.1; -; mRNA.
EMBL; U31287; AAA75511.1; -; mRNA.
EMBL; V01220; CAA24531.1; -; mRNA.
EMBL; J00737; AAA41198.1; -; mRNA.
PIR; A92317; UART.
RefSeq; NP_671747.1; NM_147214.2.
UniGene; Rn.224459; -.
PDB; 2A2G; X-ray; 2.90 A; A/B/C/D=1-181.
PDB; 2A2U; X-ray; 2.50 A; A/B/C/D=1-181.
PDBsum; 2A2G; -.
PDBsum; 2A2U; -.
ProteinModelPortal; P02761; -.
SMR; P02761; -.
STRING; 10116.ENSRNOP00000047327; -.
Allergome; 3464; Rat n 1.0101.
Allergome; 611; Rat n 1.
PaxDb; P02761; -.
PRIDE; P02761; -.
GeneID; 259246; -.
KEGG; rno:259246; -.
UCSC; RGD:708506; rat.
RGD; 708506; LOC259246.
eggNOG; ENOG410J5XW; Eukaryota.
eggNOG; ENOG411154J; LUCA.
HOGENOM; HOG000231458; -.
HOVERGEN; HBG000215; -.
InParanoid; P02761; -.
PhylomeDB; P02761; -.
TreeFam; TF338197; -.
EvolutionaryTrace; P02761; -.
PRO; PR:P02761; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005009; F:insulin-activated receptor activity; ISS:UniProtKB.
GO; GO:0005550; F:pheromone binding; ISS:UniProtKB.
GO; GO:0036094; F:small molecule binding; IEA:InterPro.
GO; GO:0005215; F:transporter activity; IEA:InterPro.
GO; GO:0009060; P:aerobic respiration; ISS:UniProtKB.
GO; GO:0071396; P:cellular response to lipid; ISS:UniProtKB.
GO; GO:0006112; P:energy reserve metabolic process; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0031649; P:heat generation; ISS:UniProtKB.
GO; GO:0045475; P:locomotor rhythm; ISS:UniProtKB.
GO; GO:0070584; P:mitochondrion morphogenesis; ISS:UniProtKB.
GO; GO:0045721; P:negative regulation of gluconeogenesis; ISS:UniProtKB.
GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
GO; GO:0051055; P:negative regulation of lipid biosynthetic process; ISS:UniProtKB.
GO; GO:0010888; P:negative regulation of lipid storage; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
GO; GO:0010907; P:positive regulation of glucose metabolic process; ISS:UniProtKB.
GO; GO:0045834; P:positive regulation of lipid metabolic process; ISS:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS: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.
Pfam; PF00061; Lipocalin; 1.
PRINTS; PR00179; LIPOCALIN.
PRINTS; PR01221; MAJORURINARY.
SUPFAM; SSF50814; SSF50814; 1.
PROSITE; PS00213; LIPOCALIN; 1.
1: Evidence at protein level;
3D-structure; Allergen; Behavior; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Pheromone-binding; Reference proteome; Secreted; Signal; Transport.
SIGNAL 1 19 {ECO:0000269|PubMed:6163771,
ECO:0000269|PubMed:8645715}.
CHAIN 20 181 Major urinary protein.
/FTId=PRO_0000017925.
CHAIN 29 179 15.5 kDa fatty acid-binding protein.
/FTId=PRO_0000017926.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 83 176 {ECO:0000269|PubMed:2005132}.
CONFLICT 26 26 R -> S (in Ref. 5; AAA41198).
{ECO:0000305}.
CONFLICT 55 55 G -> D (in Ref. 7; CAA24531).
{ECO:0000305}.
TURN 24 27 {ECO:0000244|PDB:2A2U}.
HELIX 31 34 {ECO:0000244|PDB:2A2U}.
STRAND 39 44 {ECO:0000244|PDB:2A2U}.
HELIX 48 50 {ECO:0000244|PDB:2A2U}.
STRAND 60 67 {ECO:0000244|PDB:2A2U}.
STRAND 70 81 {ECO:0000244|PDB:2A2U}.
STRAND 83 92 {ECO:0000244|PDB:2A2U}.
STRAND 99 114 {ECO:0000244|PDB:2A2U}.
STRAND 116 128 {ECO:0000244|PDB:2A2U}.
STRAND 131 144 {ECO:0000244|PDB:2A2U}.
HELIX 147 158 {ECO:0000244|PDB:2A2U}.
TURN 159 161 {ECO:0000244|PDB:2A2U}.
HELIX 164 166 {ECO:0000244|PDB:2A2U}.
STRAND 167 169 {ECO:0000244|PDB:2A2U}.
HELIX 170 172 {ECO:0000244|PDB:2A2U}.
SEQUENCE 181 AA; 20737 MW; 6A01309DC55032DC CRC64;
MKLLLLLLCL GLTLVCGHAE EASSTRGNLD VAKLNGDWFS IVVASNKREK IEENGSMRVF
MQHIDVLENS LGFKFRIKEN GECRELYLVA YKTPEDGEYF VEYDGGNTFT ILKTDYDRYV
MFHLINFKNG ETFQLMVLYG RTKDLSSDIK EKFAKLCEAH GITRDNIIDL TKTDRCLQAR
G


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