mammaglobin-A precursor [Homo sapiens]
Protein Classification
Secretoglobin domain-containing protein( domain architecture ID 10471268)
Secretoglobin domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Uteroglobin | pfam01099 | Uteroglobin family; Uteroglobin is a homodimer of two identical 70 amino acid polypeptides ... |
15-90 | 2.59e-23 | ||
Uteroglobin family; Uteroglobin is a homodimer of two identical 70 amino acid polypeptides linked by two disulphide bridges. The precise role of uteroglobin has still to be elucidated. : Pssm-ID: 460063 Cd Length: 90 Bit Score: 84.96 E-value: 2.59e-23
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| Name | Accession | Description | Interval | E-value | ||
| Uteroglobin | pfam01099 | Uteroglobin family; Uteroglobin is a homodimer of two identical 70 amino acid polypeptides ... |
15-90 | 2.59e-23 | ||
Uteroglobin family; Uteroglobin is a homodimer of two identical 70 amino acid polypeptides linked by two disulphide bridges. The precise role of uteroglobin has still to be elucidated. Pssm-ID: 460063 Cd Length: 90 Bit Score: 84.96 E-value: 2.59e-23
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| Secretoglobin | cd00633 | Secretoglobins are relatively small, secreted, disulphide-bridged dimeric proteins with ... |
22-90 | 2.46e-18 | ||
Secretoglobins are relatively small, secreted, disulphide-bridged dimeric proteins with encoding genes sharing substantial sequence similarity. Their family subunits may be grouped into five subfamilies, A-E. Uteroglobin (subfamily A), which is identical to Clara cell protein (CC10), forms a globular shaped homodimer with a large hydrophobic pocket located between the two dimers. The uteroglobin monomer structure is composed of four alpha 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. The hydrophobic pocket binds steroids, particularly progesterone, with high specificity. However, the true biological function of uteroglobin is poorly understood. In mammals, uteroglobin has immunosuppressive and anti-inflammatory properties through the inhibition of phospholipase A2. The other four main subfamilies of secretoglobins are found in heterodimeric combinations, with B and C subfamilies disulphide-bridged to the E and D subfamilies, respectively. [See review by Laukaitis C.M. _ Karn R.C. (2005). Biological Journal of the Linnean Society 84, 493]. These include rat prostatic steroid-binding protein (PBP or prostatein), human mammaglobin (or heteroglobin), lipophilins, major cat allergen Fel dI, the hamster Harderian gland proteins and mouse salivary androgen-binding protein (ABP). Example of such a heterodimer: ABPalpha-like sequences are closely related to cat Fel dI chain 1, whereas ABPbeta-gamma-like sequences are closely related to Fel dI chain 2. Thus, the heterodimeric structure of ABPalpha-beta and ABPalpha-gamma is recapitulated by the sequence-similar Fel dI chains 1 and 2. This conservation of primary and quaternary structure indicates that the genome of the eutherian common ancestor of cats, rodents, and primates contained a similar gene pair. Pssm-ID: 238346 Cd Length: 67 Bit Score: 71.56 E-value: 2.46e-18
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| Name | Accession | Description | Interval | E-value | ||
| Uteroglobin | pfam01099 | Uteroglobin family; Uteroglobin is a homodimer of two identical 70 amino acid polypeptides ... |
15-90 | 2.59e-23 | ||
Uteroglobin family; Uteroglobin is a homodimer of two identical 70 amino acid polypeptides linked by two disulphide bridges. The precise role of uteroglobin has still to be elucidated. Pssm-ID: 460063 Cd Length: 90 Bit Score: 84.96 E-value: 2.59e-23
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| Secretoglobin | cd00633 | Secretoglobins are relatively small, secreted, disulphide-bridged dimeric proteins with ... |
22-90 | 2.46e-18 | ||
Secretoglobins are relatively small, secreted, disulphide-bridged dimeric proteins with encoding genes sharing substantial sequence similarity. Their family subunits may be grouped into five subfamilies, A-E. Uteroglobin (subfamily A), which is identical to Clara cell protein (CC10), forms a globular shaped homodimer with a large hydrophobic pocket located between the two dimers. The uteroglobin monomer structure is composed of four alpha 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. The hydrophobic pocket binds steroids, particularly progesterone, with high specificity. However, the true biological function of uteroglobin is poorly understood. In mammals, uteroglobin has immunosuppressive and anti-inflammatory properties through the inhibition of phospholipase A2. The other four main subfamilies of secretoglobins are found in heterodimeric combinations, with B and C subfamilies disulphide-bridged to the E and D subfamilies, respectively. [See review by Laukaitis C.M. _ Karn R.C. (2005). Biological Journal of the Linnean Society 84, 493]. These include rat prostatic steroid-binding protein (PBP or prostatein), human mammaglobin (or heteroglobin), lipophilins, major cat allergen Fel dI, the hamster Harderian gland proteins and mouse salivary androgen-binding protein (ABP). Example of such a heterodimer: ABPalpha-like sequences are closely related to cat Fel dI chain 1, whereas ABPbeta-gamma-like sequences are closely related to Fel dI chain 2. Thus, the heterodimeric structure of ABPalpha-beta and ABPalpha-gamma is recapitulated by the sequence-similar Fel dI chains 1 and 2. This conservation of primary and quaternary structure indicates that the genome of the eutherian common ancestor of cats, rodents, and primates contained a similar gene pair. Pssm-ID: 238346 Cd Length: 67 Bit Score: 71.56 E-value: 2.46e-18
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| OTU_VCIP135 | cd22769 | OTU (ovarian tumor) domain of deubiquitinating protein VCIP135; Deubiquitinating protein ... |
42-80 | 6.21e-03 | ||
OTU (ovarian tumor) domain of deubiquitinating protein VCIP135; Deubiquitinating protein VCIP135 is also called valosin-containing protein p97/p47 complex-interacting protein 1, valosin-containing protein p97/p47 complex-interacting protein p135, or VCP/p47 complex-interacting 135-kDa protein. It is a deubiquitinase (DUB)/ubiquitin thioesterase (EC 3.4.19.12) that hydrolyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitin chains. It is necessary for VCP-mediated reassembly of Golgi stacks after mitosis, and may play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER). VCIP135 controls Golgi membrane dynamics in the cell cycle and is required for Golgi and ER assembly. It belongs to the OTU family of cysteine proteases that use a conserved cysteine and histidine, and in most cases an aspartate, as the catalytic triad. Not all members of this subfamily contain the active site. It is closely related to proteins classified as family C64 cysteine protease by MEROPS, such as TNFAIP3, ZRANB1, and OTUD7A/B. Pssm-ID: 438606 Cd Length: 197 Bit Score: 33.81 E-value: 6.21e-03
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