Jump to content

Uteroglobin

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Monkbot (talk | contribs) at 21:43, 8 December 2020 (Task 18 (cosmetic): eval 25 templates: del empty params (5×);). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

SCGB1A1
Identifiers
AliasesSCGB1A1, CC10, CC16, CCPBP, CCSP, UGB, UP-1, UP1, secretoglobin family 1A member 1
External IDsOMIM: 192020; MGI: 98919; HomoloGene: 2518; GeneCards: SCGB1A1; OMA:SCGB1A1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003357

NM_011681

RefSeq (protein)

NP_003348

NP_035811

Location (UCSC)Chr 11: 62.41 – 62.42 MbChr 19: 9.06 – 9.07 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Uteroglobin, also known as secretoglobin family 1A member 1 (SCGB1A1), is a protein that in humans is encoded by the SCGB1A1 gene.[5]

SCGB1A1 is the founding member of the secretoglobin family of small, secreted, disulfide-bridged dimeric proteins found only in mammals.[6] This antiparallel disulfide linked homodimeric protein is multifunctional and found in various tissues in various names such as: uteroglobin (UG, UGB), uteroglobin-like antigen (UGL), blastokinin, club-cell secretory protein (CCSP), Clara-cell 16 kD protein (17 in rat/mice), club-cell-specific 10 kD protein (CC10), human protein 1, urine protein 1 (UP-1), polychlorinated biphenyl-binding protein (PCB-BP), human club cell phospholipid-binding protein (hCCPBP), secretoglobin 1A member 1 (SCGB1A1).[7]

This protein is specifically expressed in club cells in the lungs.[8]

Function

The precise physiological role of uteroglobin is not yet known. Putative functions are:

  1. Immunomodulation
  2. Progesterone binding: weak in some animals, especially weak in humans. (Note: UGB is itself progesterone induced gene in the endometrium in Lagomorphs)
  3. Inhibits phospholipase A2 in vitro
  4. Binds phosphatidylcholine, phosphatidylinositol
  5. Binds to fibronectin: The uteroglobulin knockout mice on the inbred C57Bl6 strain develop Goodpasture's syndrome like glomerulopathy due to fibronectin binding of IgA which might potentially be prevented by uteroglobin replacement. However contrary to the animal model claims, human genetic data might suggest that the effect may be indirect[9]
  6. Uteroglobin knockout mice on the inbred 129 strain appear to have healthy phenotype (no glomerulopathy development), but show physiological differences in their responses to respiratory challenges. The phenotype exhibited by these mice are; decreased bioaccumulation of biphenyls, susceptibility and increased IL-13, and IL-6 following hyperoxic challenge, and changes in the club cell morphology. [10]
  7. Target of polychlorinated biphenyl (pcb) binding

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000149021Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000024653Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Wolf M, Klug J, Hackenberg R, Gessler M, Grzeschik KH, Beato M, Suske G (September 1992). "Human CC10, the homologue of rabbit uteroglobin: genomic cloning, chromosomal localization and expression in endometrial cell lines" (PDF). Hum. Mol. Genet. 1 (6): 371–8. doi:10.1093/hmg/1.6.371. PMID 1284526.
  6. ^ Laukaitis CM, Karn RC (2005). "Evolution of the secretoglobins: a genomic and proteomic view". Biological Journal of the Linnean Society. 84 (3): 493–501. doi:10.1111/j.1095-8312.2005.00450.x.
  7. ^ Klug J, Beier HM, Bernard A, Chilton BS, Fleming TP, Lehrer RI, Miele L, Pattabiraman N, Singh G (2000). "Uteroglobin/Clara cell 10-kDa family of proteins: nomenclature committee report". Ann. N. Y. Acad. Sci. 923 (1): 348–54. Bibcode:2000NYASA.923..348K. doi:10.1111/j.1749-6632.2000.tb05549.x. PMID 11193777. S2CID 38862724.
  8. ^ Zhang, Liqian; Whitsett, Jeffrey A.; Stripp, Barry R. (1997). "Regulation of Clara cell secretory protein gene transcription by thyroid transcription factor-1". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1350 (3): 359–367. doi:10.1016/S0167-4781(96)00180-7. PMID 9061032.
  9. ^ Vollmer M, Krapf R, Hildebrandt F (1998). "Exclusion of the uteroglobin gene as a candidate for fibronectin glomerulopathy (GFND)". Nephrol. Dial. Transplant. 13 (9): 2417–8. doi:10.1093/ndt/13.9.2417. PMID 9761542.
  10. ^ Stripp BR, Reynolds SD, Boe IM, Lund J, Power JH, Coppens JT, Wong V, Reynolds PR, Plopper CG (August 2002). "Clara cell secretory protein deficiency alters clara cell secretory apparatus and the protein composition of airway lining fluid". Am. J. Respir. Cell Mol. Biol. 27 (2): 170–8. doi:10.1165/ajrcmb.27.2.200200270c. PMID 12151308.

Further reading