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Uteroglobin (Blastokinin) (Secretoglobin family 1A member 1)

 UTER_RABIT              Reviewed;          91 AA.
P02779;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
12-SEP-2018, entry version 130.
RecName: Full=Uteroglobin;
AltName: Full=Blastokinin;
AltName: Full=Secretoglobin family 1A member 1;
Flags: Precursor;
Name=SCGB1A1; Synonyms=UGB, UGL;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE.
PubMed=6309802;
Bailly A., Atger M., Atger P., Cerbon M.-A., Alizon M., Vu Hai M.T.,
Logeat F., Milgrom E.;
"The rabbit uteroglobin gene. Structure and interaction with the
progesterone receptor.";
J. Biol. Chem. 258:10384-10389(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6304644; DOI=10.1093/nar/11.8.2257;
Suske G., Wenz M., Cato A.C.B., Beato M.;
"The uteroglobin gene region: hormonal regulation, repetitive elements
and complete nucleotide sequence of the gene.";
Nucleic Acids Res. 11:2257-2271(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6956897; DOI=10.1073/pnas.79.16.4853;
Menne C., Suske G., Arnemann J., Wenz M., Cato A.C.B., Beato M.;
"Isolation and structure of the gene for the progesterone-inducible
protein uteroglobin.";
Proc. Natl. Acad. Sci. U.S.A. 79:4853-4857(1982).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6299663; DOI=10.1089/dna.1.1981.1.19;
Chandra T., Bullock D.W., Woo S.L.C.;
"Hormonally regulated mammalian gene expression: steady-state level
and nucleotide sequence of rabbit uteroglobin mRNA.";
DNA 1:19-26(1981).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6287481;
Suske G., Menne C., Cato A., Wenz M., Beato M.;
"Characterization and sequence analysis of interspersed repetitive DNA
sequences transcribed in X.laevis embryos.";
Prog. Clin. Biol. Res. 85:139-146(1982).
[6]
PROTEIN SEQUENCE OF 1-73 (PRECURSOR PROTEIN).
PubMed=571719; DOI=10.1042/bj1770985;
Atger M., Mercier J.-C., Haze G., Fridlansky F., Milgrom E.;
"N-terminal sequences of uteroglobin and its precursor.";
Biochem. J. 177:985-988(1979).
[7]
PROTEIN SEQUENCE OF 22-91.
PubMed=568483; DOI=10.1021/bi00612a003;
Ponstingl H., Nieto A., Beato M.;
"Amino acid sequence of progesterone-induced rabbit uteroglobin.";
Biochemistry 17:3908-3912(1978).
[8]
PROTEIN SEQUENCE OF 22-91.
PubMed=281700; DOI=10.1073/pnas.75.11.5516;
Popp R.A., Foresman K.R., Wise L.D., Daniel J.C. Jr.;
"Amino acid sequence of a progesterone-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 75:5516-5519(1978).
[9]
SEQUENCE REVISION TO 50-62 AND 67-71.
Popp R.A., Foresman K.R., Wise L.D., Daniel J.C. Jr.;
Submitted (OCT-1982) to the PIR data bank.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 22-91.
PubMed=2415398; DOI=10.1016/0014-5793(85)80162-9;
de Haro M.S., Nieto A.;
"Primary structure of rabbit lung uteroglobin as deduced from the
nucleotide sequence of a cDNA.";
FEBS Lett. 193:247-249(1985).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-77.
PubMed=7417250; DOI=10.1016/0006-291X(80)90724-X;
Chandra T., Woo S.L.C., Bullock D.W.;
"Cloning of the rabbit uteroglobin structural gene.";
Biochem. Biophys. Res. Commun. 95:197-204(1980).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 53-72.
PubMed=6156676; DOI=10.1016/0006-291X(80)90599-9;
Atger M., Perricaudet M., Tiollais P., Milgrom E.;
"Bacterial cloning of the rabbit uteroglobin structural gene.";
Biochem. Biophys. Res. Commun. 93:1082-1088(1980).
[13]
X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS).
PubMed=2704039; DOI=10.1016/0022-2836(89)90530-5;
Bally R., Delettre J.;
"Structure and refinement of the oxidized P21 form of uteroglobin at
1.64-A resolution.";
J. Mol. Biol. 206:153-170(1989).
[14]
X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS).
PubMed=3656405; DOI=10.1016/0022-2836(87)90250-6;
Morize I., Surcouf E., Vaney M.C., Epelboin Y., Buehner M.,
Fridlansky F., Milgrom E., Mornon J.-P.;
"Refinement of the C222(1) crystal form of oxidized uteroglobin at
1.34-A resolution.";
J. Mol. Biol. 194:725-739(1987).
[15]
STRUCTURE BY NMR OF 39-68.
PubMed=8025221; DOI=10.1002/bip.360340609;
Improta S., Pastore A., Mammi S., Peggion E.;
"Conformation and molecular dynamics calculations on uteroglobin
fragment 18-47.";
Biopolymers 34:773-782(1994).
-!- FUNCTION: Uteroglobin binds progesterone specifically and with
high affinity. It may regulate progesterone concentrations
reaching the blastocyst. It is also a potent inhibitor of
phospholipase A2.
-!- SUBUNIT: Homodimer; antiparallel disulfide-linked.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Synthesized in the uterus and lung.
-!- INDUCTION: By progesterone.
-!- SIMILARITY: Belongs to the secretoglobin family. {ECO:0000305}.
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EMBL; K01657; AAA31497.1; -; mRNA.
EMBL; J00689; AAA31495.1; -; Genomic_DNA.
EMBL; J00688; AAA31495.1; JOINED; Genomic_DNA.
EMBL; X01423; CAA25669.1; -; Genomic_DNA.
EMBL; M32012; AAA31500.1; -; Genomic_DNA.
EMBL; M25090; AAA31500.1; JOINED; Genomic_DNA.
EMBL; M27564; AAA31496.1; -; mRNA.
EMBL; M25057; AAA31498.1; -; Genomic_DNA.
EMBL; M25038; AAA31499.1; -; mRNA.
PIR; A92391; UGRB.
RefSeq; NP_001075706.1; NM_001082237.1.
UniGene; Ocu.1976; -.
PDB; 1UTG; X-ray; 1.34 A; A=22-91.
PDB; 2UTG; X-ray; 1.64 A; A/B=22-91.
PDBsum; 1UTG; -.
PDBsum; 2UTG; -.
ProteinModelPortal; P02779; -.
SMR; P02779; -.
STRING; 9986.ENSOCUP00000012245; -.
PRIDE; P02779; -.
Ensembl; ENSOCUT00000014246; ENSOCUP00000012245; ENSOCUG00000014249.
GeneID; 100009053; -.
KEGG; ocu:100009053; -.
CTD; 7356; -.
eggNOG; ENOG410J459; Eukaryota.
eggNOG; ENOG4111966; LUCA.
GeneTree; ENSGT00530000064300; -.
HOGENOM; HOG000220914; -.
HOVERGEN; HBG018062; -.
InParanoid; P02779; -.
OMA; ASAEICP; -.
OrthoDB; EOG091G15B2; -.
TreeFam; TF338407; -.
EvolutionaryTrace; P02779; -.
Proteomes; UP000001811; Unplaced.
Bgee; ENSOCUG00000014249; Expressed in 2 organ(s), highest expression level in prefrontal cortex.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032696; P:negative regulation of interleukin-13 production; IEA:Ensembl.
GO; GO:0032713; P:negative regulation of interleukin-4 production; IEA:Ensembl.
GO; GO:0032714; P:negative regulation of interleukin-5 production; IEA:Ensembl.
GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
GO; GO:0043488; P:regulation of mRNA stability; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
CDD; cd00633; Secretoglobin; 1.
InterPro; IPR016126; Secretoglobin.
InterPro; IPR035960; Secretoglobin_sf.
InterPro; IPR000329; Uteroglobin.
Pfam; PF01099; Uteroglobin; 1.
PRINTS; PR00486; UTEROGLOBIN.
SUPFAM; SSF48201; SSF48201; 1.
PROSITE; PS51311; SCGB; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Disulfide bond; Lipid-binding; Phospholipase A2 inhibitor;
Reference proteome; Secreted; Signal; Steroid-binding.
SIGNAL 1 21 {ECO:0000269|PubMed:281700,
ECO:0000269|PubMed:568483,
ECO:0000269|PubMed:571719}.
CHAIN 22 91 Uteroglobin. {ECO:0000269|PubMed:568483}.
/FTId=PRO_0000036369.
DISULFID 24 24 Interchain (with C-90).
{ECO:0000269|PubMed:281700}.
DISULFID 90 90 Interchain (with C-24).
{ECO:0000269|PubMed:281700}.
CONFLICT 6 6 T -> F (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 16 16 C -> G (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 46 46 L -> V (in Ref. 5; AAA31500).
{ECO:0000305}.
CONFLICT 67 68 DS -> NT (in Ref. 12; AAA31499).
{ECO:0000305}.
CONFLICT 82 82 E -> Q (in Ref. 7; AA sequence).
{ECO:0000305}.
HELIX 25 36 {ECO:0000244|PDB:1UTG}.
HELIX 39 47 {ECO:0000244|PDB:1UTG}.
HELIX 53 66 {ECO:0000244|PDB:1UTG}.
HELIX 71 85 {ECO:0000244|PDB:1UTG}.
HELIX 88 90 {ECO:0000244|PDB:1UTG}.
SEQUENCE 91 AA; 9983 MW; 0C1978AAE5D550CA CRC64;
MKLAITLALV TLALLCSPAS AGICPRFAHV IENLLLGTPS SYETSLKEFE PDDTMKDAGM
QMKKVLDSLP QTTRENIMKL TEKIVKSPLC M


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