MUP_RAT
ID MUP_RAT Reviewed; 181 AA.
AC P02761; Q54AE7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Major urinary protein;
DE Short=MUP;
DE AltName: Full=Allergen Rat n I;
DE AltName: Full=Alpha(2)-euglobulin;
DE AltName: Full=Alpha-2u-globulin;
DE AltName: Full=alpha-2u globulin PGCL1;
DE AltName: Allergen=Rat n 1;
DE Contains:
DE RecName: Full=15.5 kDa fatty acid-binding protein;
DE Short=15.5 kDa FABP;
DE Flags: Precursor;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2443176; DOI=10.1016/0167-4781(87)90093-5;
RA Ichiyoshi Y., Endo H., Yamamoto M.;
RT "Length polymorphism in the 3' noncoding region of rat hepatic alpha 2u-
RT globulin mRNAs.";
RL Biochim. Biophys. Acta 910:43-51(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley;
RA Kurtz D.T., Dey M.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Preputial gland;
RX PubMed=10833415; DOI=10.1006/bbrc.2000.2694;
RA Saito K., Nishikawa J., Imagawa M., Nishihara T., Matsuo M.;
RT "Molecular evidence of complex tissue- and sex-specific mRNA expression of
RT the rat alpha(2u)-globulin multigene family.";
RL Biochem. Biophys. Res. Commun. 272:337-344(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Spleen;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-181.
RX PubMed=6167987; DOI=10.1073/pnas.78.6.3478;
RA Unterman R.D., Lynch K.R., Nakhasi H.L., Dolan K.P., Hamilton J.W.,
RA Cohn D.V., Feigelson P.;
RT "Cloning and sequence of several alpha 2u-globulin cDNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:3478-3482(1981).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 34-181.
RX PubMed=6183262; DOI=10.1016/s0021-9258(18)33479-3;
RA Dolan K.P., Unterman R.D., McLaughlin M., Nakhasi H.L., Lynch K.R.,
RA Feigelson P.;
RT "The structure and expression of very closely related members of the alpha
RT 2u globulin gene family.";
RL J. Biol. Chem. 257:13527-13534(1982).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-65.
RX PubMed=6163771; DOI=10.1016/s0021-9258(19)69498-6;
RA Drickamer K., Kwoh T.J., Kurtz D.T.;
RT "Amino acid sequence of the precursor of rat liver alpha 2 micro-
RT globulin.";
RL J. Biol. Chem. 256:3634-3636(1981).
RN [8]
RP PROTEIN SEQUENCE OF 29-48.
RC TISSUE=Kidney;
RX PubMed=2468522; DOI=10.1016/0014-5793(89)80261-3;
RA Kimura H., Odani S., Suzuki J., Arakawa M., Ono T.;
RT "Kidney fatty acid-binding protein: identification as alpha 2U-globulin.";
RL FEBS Lett. 246:101-104(1989).
RN [9]
RP PROTEIN SEQUENCE OF 29-179, AND DISULFIDE BOND.
RC TISSUE=Kidney;
RX PubMed=2005132; DOI=10.1016/s0021-9258(19)67692-1;
RA Kimura H., Odani S., Nishi S., Sato H., Arakawa M., Ono T.;
RT "Primary structure and cellular distribution of two fatty acid-binding
RT proteins in adult rat kidneys.";
RL J. Biol. Chem. 266:5963-5972(1991).
RN [10]
RP PROTEIN SEQUENCE OF 20-44, AND ALLERGEN.
RC TISSUE=Urine;
RX PubMed=8645715; DOI=10.1016/0304-4165(96)00006-2;
RA Bayard C., Holmquist L., Vesterberg O.;
RT "Purification and identification of allergenic alpha (2u)-globulin species
RT of rat urine.";
RL Biochim. Biophys. Acta 1290:129-134(1996).
RN [11]
RP ERRATUM OF PUBMED:8645715.
RA Bayard C., Holmquist L., Vesterberg O.;
RL Biochim. Biophys. Acta 1291:253-255(1996).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=1279439; DOI=10.1038/360186a0;
RA Boecksel Z., Groom C.R., Flower D.R., Wright C.E., Phillips S.E.V.,
RA Cavaggioni A., Findlay J.B.C., North A.C.T.;
RT "Pheromone binding to two rodent urinary proteins revealed by X-ray
RT crystallography.";
RL Nature 360:186-188(1992).
CC -!- FUNCTION: Major urinary proteins (Mups) bind and release pheromones.
CC They may also protect pheromones from oxidation. In this context, they
CC play a role in the regulation of social behaviors, such as aggression,
CC mating, pup-suckling, territory establishment and dominance. Acts as a
CC kairomone, detected by the prey vomeronasal organ and inducing fear
CC reactions in mice.
CC -!- SUBCELLULAR LOCATION: [15.5 kDa fatty acid-binding protein]: Cytoplasm,
CC cytosol. Note=It is probably taken up from the urinary lumen by
CC endocytosis.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Abundant in the urine of adult male rats but absent
CC from that of females.
CC -!- INDUCTION: Synthesis of this protein in the hepatic parenchymal cells
CC is induced in vivo by androgens, glucocorticoids, growth hormone, and
CC insulin, and inhibited by estrogens.
CC -!- ALLERGEN: Causes an allergic reaction in human.
CC {ECO:0000269|PubMed:8645715}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
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DR EMBL; M26835; AAA40643.1; -; mRNA.
DR EMBL; M26837; AAA40641.1; -; mRNA.
DR EMBL; AB039822; BAA96479.1; -; mRNA.
DR EMBL; BC088109; AAH88109.1; -; mRNA.
DR EMBL; BC098654; AAH98654.1; -; mRNA.
DR EMBL; BC105816; AAI05817.1; -; mRNA.
DR EMBL; U31287; AAA75511.1; -; mRNA.
DR EMBL; V01220; CAA24531.1; -; mRNA.
DR EMBL; J00737; AAA41198.1; -; mRNA.
DR PIR; A92317; UART.
DR RefSeq; NP_671747.1; NM_147214.2.
DR PDB; 2A2G; X-ray; 2.90 A; A/B/C/D=1-181.
DR PDB; 2A2U; X-ray; 2.50 A; A/B/C/D=1-181.
DR PDBsum; 2A2G; -.
DR PDBsum; 2A2U; -.
DR AlphaFoldDB; P02761; -.
DR SMR; P02761; -.
DR STRING; 10116.ENSRNOP00000068097; -.
DR Allergome; 3464; Rat n 1.0101.
DR Allergome; 611; Rat n 1.
DR GlyGen; P02761; 1 site.
DR PaxDb; P02761; -.
DR PRIDE; P02761; -.
DR Ensembl; ENSRNOT00000100434; ENSRNOP00000080129; ENSRNOG00000067602.
DR Ensembl; ENSRNOT00000120034; ENSRNOP00000092008; ENSRNOG00000067602.
DR GeneID; 259246; -.
DR UCSC; RGD:708506; rat.
DR RGD; 708506; LOC259246.
DR eggNOG; ENOG502S6GK; Eukaryota.
DR GeneTree; ENSGT01050000244868; -.
DR InParanoid; P02761; -.
DR PhylomeDB; P02761; -.
DR TreeFam; TF338197; -.
DR EvolutionaryTrace; P02761; -.
DR PRO; PR:P02761; -.
DR Proteomes; UP000002494; Chromosome 5.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
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; Allergen; Behavior; Cytoplasm; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Pheromone-binding; Reference proteome;
KW Secreted; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:6163771,
FT ECO:0000269|PubMed:8645715"
FT CHAIN 20..181
FT /note="Major urinary protein"
FT /id="PRO_0000017925"
FT CHAIN 29..179
FT /note="15.5 kDa fatty acid-binding protein"
FT /id="PRO_0000017926"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 83..176
FT /evidence="ECO:0000269|PubMed:2005132"
FT CONFLICT 26
FT /note="R -> S (in Ref. 5; AAA41198)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="G -> D (in Ref. 7; CAA24531)"
FT /evidence="ECO:0000305"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:2A2U"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:2A2U"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:2A2U"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2A2U"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:2A2U"
FT STRAND 70..81
FT /evidence="ECO:0007829|PDB:2A2U"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:2A2U"
FT STRAND 99..114
FT /evidence="ECO:0007829|PDB:2A2U"
FT STRAND 116..128
FT /evidence="ECO:0007829|PDB:2A2U"
FT STRAND 131..144
FT /evidence="ECO:0007829|PDB:2A2U"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:2A2U"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:2A2U"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:2A2U"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2A2U"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:2A2U"
SQ 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
