ID   UTER_LEPCA              Reviewed;          91 AA.
AC   P06913;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-MAY-2022, entry version 87.
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   Lepus capensis (Brown hare).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Lepus.
OX   NCBI_TaxID=9981;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=3019311; DOI=10.1042/bj2350895;
RA   Lopez de Haro M.S., Nieto A.;
RT   "Nucleotide and derived amino acid sequences of a cDNA coding for pre-
RT   uteroglobin from the lung of the hare (Lepus capensis).";
RL   Biochem. J. 235:895-898(1986).
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 (By similarity).
CC       Interaction with LMBR1L is controversial (By similarity).
CC       {ECO:0000250|UniProtKB:P11684}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the secretoglobin family. {ECO:0000305}.
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DR   EMBL; M25609; AAA30960.1; -; mRNA.
DR   PIR; A23825; UGRBL.
DR   AlphaFoldDB; P06913; -.
DR   SMR; P06913; -.
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   3: Inferred from homology;
KW   Disulfide bond; Lipid-binding; Phospholipase A2 inhibitor; Secreted;
KW   Signal; Steroid-binding.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000250"
FT   CHAIN           22..91
FT                   /note="Uteroglobin"
FT                   /id="PRO_0000036368"
FT   DISULFID        24
FT                   /note="Interchain (with C-90)"
FT                   /evidence="ECO:0000250"
FT   DISULFID        90
FT                   /note="Interchain (with C-24)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   91 AA;  9879 MW;  587614DAE9E4820F CRC64;
     MKLTITLALV TLALLCSPAS AGICPGFAHV IENLLLGTPS SYETSLKEFQ PDDAMKDAGM
     QMKKVLDTLP QTTRENIIKL TEKIVKSPLC M