Surfactant protein D

Last updated
SFTPD
Protein SFTPD PDB 1b08.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases SFTPD , COLEC7, PSP-D, SFTP4, SP-D, surfactant protein D
External IDs OMIM: 178635; MGI: 109515; HomoloGene: 2272; GeneCards: SFTPD; OMA:SFTPD - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003019

NM_009160

RefSeq (protein)

NP_003010

NP_033186

Location (UCSC) Chr 10: 79.94 – 79.98 Mb Chr 14: 40.89 – 40.91 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Surfactant protein D, also known as SP-D, is a lung surfactant protein part of the collagenous family of lectins called collectin. [5] In humans, SP-D is encoded by the SFTPD gene [6] [7] and is part of the innate immune system. [8] [9] Each SP-D subunit is composed of an N-terminal domain, a collagenous region, a nucleating neck region, and a C-terminal lectin domain. [5] [10] Three of these subunits assemble to form a homotrimer, which further assemble into a tetrameric complex. [5] [10]

Interactions

Surfactant protein D has been shown to interact with DMBT1, [11] [12] and hemagglutinin of influenza A virus. [13] Post-translational modification of SP-D i.e. S-nitrosylation switches its function. [14] [15] [16]

See also

Related Research Articles

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Erika Crouch is a professor of pathology and the Carol B. and Jerome T. Loeb Professor of Medical Education at Washington University in St. Louis.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000133661 Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000021795 Ensembl, 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. 1 2 3 Hoppe HJ, Barlow PN, Reid KB (May 1994). "A parallel three stranded alpha-helical bundle at the nucleation site of collagen triple-helix formation". FEBS Letters. 344 (2–3): 191–5. Bibcode:1994FEBSL.344..191H. doi: 10.1016/0014-5793(94)00383-1 . PMID   8187882. S2CID   2920539.
  6. Rust K, Grosso L, Zhang V, Chang D, Persson A, Longmore W, et al. (October 1991). "Human surfactant protein D: SP-D contains a C-type lectin carbohydrate recognition domain". Archives of Biochemistry and Biophysics. 290 (1): 116–26. doi:10.1016/0003-9861(91)90597-C. PMID   1898081.
  7. Lu J, Willis AC, Reid KB (June 1992). "Purification, characterization and cDNA cloning of human lung surfactant protein D". The Biochemical Journal. 284. 284 (3): 795–802. doi:10.1042/bj2840795. PMC   1132609 . PMID   1339284.
  8. "Entrez Gene: SFTPD surfactant, pulmonary-associated protein D".
  9. Brandt EB, Mingler MK, Stevenson MD, Wang N, Khurana Hershey GK, Whitsett JA, Rothenberg ME (May 2008). "Surfactant protein D alters allergic lung responses in mice and human subjects". The Journal of Allergy and Clinical Immunology. 121 (5): 1140–1147.e2. doi:10.1016/j.jaci.2008.02.011. PMC   4145593 . PMID   18355911.
  10. 1 2 Crouch E, Persson A, Chang D, Heuser J (June 1994). "Molecular structure of pulmonary surfactant protein D (SP-D)". The Journal of Biological Chemistry. 269 (25): 17311–9. doi: 10.1016/S0021-9258(17)32556-5 . PMID   8006040.
  11. Tino MJ, Wright JR (April 1999). "Glycoprotein-340 binds surfactant protein-A (SP-A) and stimulates alveolar macrophage migration in an SP-A-independent manner". American Journal of Respiratory Cell and Molecular Biology. 20 (4): 759–68. doi:10.1165/ajrcmb.20.4.3439. PMID   10101009. S2CID   29437779.
  12. Holmskov U, Lawson P, Teisner B, Tornoe I, Willis AC, Morgan C, et al. (May 1997). "Isolation and characterization of a new member of the scavenger receptor superfamily, glycoprotein-340 (gp-340), as a lung surfactant protein-D binding molecule". The Journal of Biological Chemistry. 272 (21): 13743–9. doi: 10.1074/jbc.272.21.13743 . PMID   9153228.
  13. Goh BC, Rynkiewicz MJ, Cafarella TR, White MR, Hartshorn KL, Allen K, et al. (November 2013). "Molecular mechanisms of inhibition of influenza by surfactant protein D revealed by large-scale molecular dynamics simulation". Biochemistry. 52 (47): 8527–38. doi:10.1021/bi4010683. PMC   3927399 . PMID   24224757.
  14. Guo CJ, Atochina-Vasserman EN, Abramova E, Foley JP, Zaman A, Crouch E, et al. (November 2008). "S-nitrosylation of surfactant protein-D controls inflammatory function". PLOS Biology. 6 (11): e266. doi: 10.1371/journal.pbio.0060266 . PMC   2581630 . PMID   19007302.
  15. Atochina-Vasserman EN, Guo CJ, Abramova E, Golden TN, Sims M, James ML, et al. (July 2015). "Surfactant dysfunction and lung inflammation in the female mouse model of lymphangioleiomyomatosis". American Journal of Respiratory Cell and Molecular Biology. 53 (1): 96–104. doi:10.1165/rcmb.2014-0224OC. PMC   4566108 . PMID   25474372.
  16. Atochina-Vasserman EN, Winkler C, Abramova H, Schaumann F, Krug N, Gow AJ, et al. (April 2011). "Segmental allergen challenge alters multimeric structure and function of surfactant protein D in humans". American Journal of Respiratory and Critical Care Medicine. 183 (7): 856–64. doi:10.1164/rccm.201004-0654OC. PMC   3086753 . PMID   21131470.

Further reading