UTER_RABIT
ID UTER_RABIT Reviewed; 91 AA.
AC P02779;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Uteroglobin;
DE AltName: Full=Blastokinin;
DE AltName: Full=Secretoglobin family 1A member 1;
DE Flags: Precursor;
GN Name=SCGB1A1; Synonyms=UGB, UGL;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=6309802; DOI=10.1016/s0021-9258(17)44468-1;
RA Bailly A., Atger M., Atger P., Cerbon M.-A., Alizon M., Vu Hai M.T.,
RA Logeat F., Milgrom E.;
RT "The rabbit uteroglobin gene. Structure and interaction with the
RT progesterone receptor.";
RL J. Biol. Chem. 258:10384-10389(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6304644; DOI=10.1093/nar/11.8.2257;
RA Suske G., Wenz M., Cato A.C.B., Beato M.;
RT "The uteroglobin gene region: hormonal regulation, repetitive elements and
RT complete nucleotide sequence of the gene.";
RL Nucleic Acids Res. 11:2257-2271(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6956897; DOI=10.1073/pnas.79.16.4853;
RA Menne C., Suske G., Arnemann J., Wenz M., Cato A.C.B., Beato M.;
RT "Isolation and structure of the gene for the progesterone-inducible protein
RT uteroglobin.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:4853-4857(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6299663; DOI=10.1089/dna.1.1981.1.19;
RA Chandra T., Bullock D.W., Woo S.L.C.;
RT "Hormonally regulated mammalian gene expression: steady-state level and
RT nucleotide sequence of rabbit uteroglobin mRNA.";
RL DNA 1:19-26(1981).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6287481;
RA Suske G., Menne C., Cato A., Wenz M., Beato M.;
RT "Characterization and sequence analysis of interspersed repetitive DNA
RT sequences transcribed in X.laevis embryos.";
RL Prog. Clin. Biol. Res. 85:139-146(1982).
RN [6]
RP PROTEIN SEQUENCE OF 1-73 (PRECURSOR PROTEIN).
RX PubMed=571719; DOI=10.1042/bj1770985;
RA Atger M., Mercier J.-C., Haze G., Fridlansky F., Milgrom E.;
RT "N-terminal sequences of uteroglobin and its precursor.";
RL Biochem. J. 177:985-988(1979).
RN [7]
RP PROTEIN SEQUENCE OF 22-91.
RX PubMed=568483; DOI=10.1021/bi00612a003;
RA Ponstingl H., Nieto A., Beato M.;
RT "Amino acid sequence of progesterone-induced rabbit uteroglobin.";
RL Biochemistry 17:3908-3912(1978).
RN [8]
RP PROTEIN SEQUENCE OF 22-91.
RX PubMed=281700; DOI=10.1073/pnas.75.11.5516;
RA Popp R.A., Foresman K.R., Wise L.D., Daniel J.C. Jr.;
RT "Amino acid sequence of a progesterone-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:5516-5519(1978).
RN [9]
RP SEQUENCE REVISION TO 50-62 AND 67-71.
RA Popp R.A., Foresman K.R., Wise L.D., Daniel J.C. Jr.;
RL Submitted (OCT-1982) to the PIR data bank.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-91.
RX PubMed=2415398; DOI=10.1016/0014-5793(85)80162-9;
RA de Haro M.S., Nieto A.;
RT "Primary structure of rabbit lung uteroglobin as deduced from the
RT nucleotide sequence of a cDNA.";
RL FEBS Lett. 193:247-249(1985).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 39-77.
RX PubMed=7417250; DOI=10.1016/0006-291x(80)90724-x;
RA Chandra T., Woo S.L.C., Bullock D.W.;
RT "Cloning of the rabbit uteroglobin structural gene.";
RL Biochem. Biophys. Res. Commun. 95:197-204(1980).
RN [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-72.
RX PubMed=6156676; DOI=10.1016/0006-291x(80)90599-9;
RA Atger M., Perricaudet M., Tiollais P., Milgrom E.;
RT "Bacterial cloning of the rabbit uteroglobin structural gene.";
RL Biochem. Biophys. Res. Commun. 93:1082-1088(1980).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), AND SUBUNIT.
RX PubMed=2704039; DOI=10.1016/0022-2836(89)90530-5;
RA Bally R., Delettre J.;
RT "Structure and refinement of the oxidized P21 form of uteroglobin at 1.64-A
RT resolution.";
RL J. Mol. Biol. 206:153-170(1989).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.34 ANGSTROMS), AND SUBUNIT.
RX PubMed=3656405; DOI=10.1016/0022-2836(87)90250-6;
RA Morize I., Surcouf E., Vaney M.C., Epelboin Y., Buehner M., Fridlansky F.,
RA Milgrom E., Mornon J.-P.;
RT "Refinement of the C222(1) crystal form of oxidized uteroglobin at 1.34-A
RT resolution.";
RL J. Mol. Biol. 194:725-739(1987).
RN [15]
RP STRUCTURE BY NMR OF 39-68.
RX PubMed=8025221; DOI=10.1002/bip.360340609;
RA Improta S., Pastore A., Mammi S., Peggion E.;
RT "Conformation and molecular dynamics calculations on uteroglobin fragment
RT 18-47.";
RL Biopolymers 34:773-782(1994).
CC -!- FUNCTION: Uteroglobin binds progesterone specifically and with high
CC affinity. It may regulate progesterone concentrations reaching the
CC blastocyst. It is also a potent inhibitor of phospholipase A2.
CC -!- SUBUNIT: Antiparallel homodimer; disulfide-linked (PubMed:2704039,
CC PubMed:3656405). Interaction with LMBR1L is controversial.
CC {ECO:0000250|UniProtKB:P11684, ECO:0000269|PubMed:2704039,
CC ECO:0000269|PubMed:3656405}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Synthesized in the uterus and lung.
CC -!- INDUCTION: By progesterone.
CC -!- SIMILARITY: Belongs to the secretoglobin family. {ECO:0000305}.
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DR EMBL; K01657; AAA31497.1; -; mRNA.
DR EMBL; J00689; AAA31495.1; -; Genomic_DNA.
DR EMBL; J00688; AAA31495.1; JOINED; Genomic_DNA.
DR EMBL; X01423; CAA25669.1; -; Genomic_DNA.
DR EMBL; M32012; AAA31500.1; -; Genomic_DNA.
DR EMBL; M25090; AAA31500.1; JOINED; Genomic_DNA.
DR EMBL; M27564; AAA31496.1; -; mRNA.
DR EMBL; M25057; AAA31498.1; -; Genomic_DNA.
DR EMBL; M25038; AAA31499.1; -; mRNA.
DR PIR; A92391; UGRB.
DR RefSeq; NP_001075706.1; NM_001082237.1.
DR PDB; 1UTG; X-ray; 1.34 A; A=22-91.
DR PDB; 2UTG; X-ray; 1.64 A; A/B=22-91.
DR PDBsum; 1UTG; -.
DR PDBsum; 2UTG; -.
DR AlphaFoldDB; P02779; -.
DR SMR; P02779; -.
DR STRING; 9986.ENSOCUP00000012245; -.
DR Ensembl; ENSOCUT00000014246; ENSOCUP00000012245; ENSOCUG00000005922.
DR GeneID; 100009053; -.
DR KEGG; ocu:100009053; -.
DR CTD; 7356; -.
DR eggNOG; ENOG502SXFT; Eukaryota.
DR GeneTree; ENSGT00950000183045; -.
DR HOGENOM; CLU_166234_1_0_1; -.
DR InParanoid; P02779; -.
DR OMA; MKIAITI; -.
DR OrthoDB; 1608982at2759; -.
DR TreeFam; TF338407; -.
DR EvolutionaryTrace; P02779; -.
DR Proteomes; UP000001811; Unplaced.
DR Bgee; ENSOCUG00000005922; Expressed in upper lobe of left lung and 18 other tissues.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0019834; F:phospholipase A2 inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00633; Secretoglobin; 1.
DR InterPro; IPR016126; Secretoglobin.
DR InterPro; IPR043215; Secretoglobin_1C-like.
DR InterPro; IPR035960; Secretoglobin_sf.
DR InterPro; IPR000329; Uteroglobin.
DR PANTHER; PTHR10136; PTHR10136; 1.
DR Pfam; PF01099; Uteroglobin; 1.
DR PRINTS; PR00486; UTEROGLOBIN.
DR SUPFAM; SSF48201; SSF48201; 1.
DR PROSITE; PS51311; SCGB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Lipid-binding;
KW Phospholipase A2 inhibitor; Reference proteome; Secreted; Signal;
KW Steroid-binding.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:281700,
FT ECO:0000269|PubMed:568483, ECO:0000269|PubMed:571719"
FT CHAIN 22..91
FT /note="Uteroglobin"
FT /evidence="ECO:0000269|PubMed:568483"
FT /id="PRO_0000036369"
FT DISULFID 24
FT /note="Interchain (with C-90)"
FT /evidence="ECO:0000269|PubMed:281700"
FT DISULFID 90
FT /note="Interchain (with C-24)"
FT /evidence="ECO:0000269|PubMed:281700"
FT CONFLICT 6
FT /note="T -> F (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 16
FT /note="C -> G (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 46
FT /note="L -> V (in Ref. 5; AAA31500)"
FT /evidence="ECO:0000305"
FT CONFLICT 67..68
FT /note="DS -> NT (in Ref. 12; AAA31499)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="E -> Q (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:1UTG"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:1UTG"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:1UTG"
FT HELIX 71..85
FT /evidence="ECO:0007829|PDB:1UTG"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:1UTG"
SQ SEQUENCE 91 AA; 9983 MW; 0C1978AAE5D550CA CRC64;
MKLAITLALV TLALLCSPAS AGICPRFAHV IENLLLGTPS SYETSLKEFE PDDTMKDAGM
QMKKVLDSLP QTTRENIMKL TEKIVKSPLC M
