The domain within your query sequence starts at position 30 and ends at position 98; the E-value for the Uteroglobin domain shown below is 1.3e-16.



PFAM accession number:PF01099
Interpro abstract (IPR016126):

Secretoglobins are relatively small, secreted, disulphide-bridged dimeric proteins with encoding genes sharing substantial sequence similarity [(PUBMED:7868811),(PUBMED:11193777)]. Members of this family include:

  • Uteroglobin, a mammalian, steroid-inducible, secreted anti-inflammatory/immunomodulatory protein [(PUBMED:17916741)].
  • Mammaglobin, expressed in ovarian cancer cells [(PUBMED:18021217)].
  • Lipophilin B, which exists as a complex with mammary-specific mammaglobin A [(PUBMED:17163411)].
  • Clara cell 17 kDa protein, which inhibits phospholipase A2 and papain, and also binds to progesterone [(PUBMED:1560460),(PUBMED:11193778)].
  • Allergen Fel d 1 (Felis silvestris catus (Cat) allergen 1) chains 1 and 2, a tetrameric glycoprotein formed by two heterodimers that elicit IgE responses in people with allergy to cats [(PUBMED:17543334),(PUBMED:12851385)].

Secretoglobin proteins have a four-helical structure, and in the case of uteroglobin, form homodimers, whereas allergen Fel d 1 forms a tetramer of two heterodimers (chains 1 and 2). The conservation of this primary and quaternary structure indicates that the genome of the eutherian common ancestor of cats, rodents, and primates contained a similar gene pair.

Uteroglobin (blastokinin or Clara cell protein CC10) is a mammalian steroid-inducible secreted protein originally isolated from the uterus of rabbits during early pregnancy [(PUBMED:2378892)]. The mucosal epithelia of several organs that communicate with the external environment express uteroglobin. Its tissue-specific expression is regulated by steroid hormones, and is augmented in the uterus by non-steroidal prolactin. Uteroglobin may be a multi-functional protein with anti-inflammatory/immunomodulatory properties, acting to inhibit phospholipase A2 activity [(PUBMED:3319534),(PUBMED:11193767)], and binding to (and possibly sequestering) several hydrophobic ligands such as progesterone, retinols, polychlorinated biphenyls, phospholipids and prostaglandins [(PUBMED:11193782),(PUBMED:11193750)]. In addition, uteroglobin has anti-chemotactic, anti-allergic, anti-tumourigenic and embryo growth-stimulatory properties. Uteroglobin may have a homeostatic role against oxidative damage, inflammation, autoimmunity and cancer [(PUBMED:17916741), (PUBMED:17928103), (PUBMED:11193760), (PUBMED:7770456)]. However, the true biological function of uteroglobin is poorly understood. Uteroglobin consists of a disulphide-linked homodimer with a large hydrophobic pocket located between the two dimers [(PUBMED:3656405)]. Each monomer being composed of four helices that do not form a canonical four helix-bundle motif but rather a boomerang-shaped structure in which helices H1, H3, and H4 are able to bind a homodimeric partner [(PUBMED:11193783)]. The hydrophobic pocket binds steroids, particularly progesterone, with high specificity. It is a member of the secretoglobin superfamily.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Uteroglobin