SMART: Pfam domain Uteroglobin

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.

VDKLPVPLDDIIPSFDPLKMLLKTLGISVEHLVTGLKKCVDELGPEASEAVKKLLVIIIC
SYFPGRSLC

Uteroglobin

PFAM accession number:	PF01099
Interpro abstract (IPR016126):	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. 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 17kDa 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.

PFAM accession number:

PF01099

Interpro abstract (IPR016126):

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.

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 17kDa 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.

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