Surfactant protein D

Protein-coding gene in the species Homo sapiens
SFTPD
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1B08, 1M7L, 1PW9, 1PWB, 2GGU, 2GGX, 2ORJ, 2ORK, 2OS9, 2RIA, 2RIB, 2RIC, 2RID, 2RIE, 3DBZ, 3G81, 3G83, 3G84, 3IKN, 3IKP, 3IKQ, 3IKR, 4E52, 4M17, 4M18

Identifiers
AliasesSFTPD, COLEC7, PSP-D, SFTP4, SP-D, surfactant protein D
External IDsOMIM: 178635; MGI: 109515; HomoloGene: 2272; GeneCards: SFTPD; OMA:SFTPD - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for SFTPD
Genomic location for SFTPD
Band10q22.3Start79,937,467 bp[1]
End79,982,614 bp[1]
Gene location (Mouse)
Chromosome 14 (mouse)
Chr.Chromosome 14 (mouse)[2]
Chromosome 14 (mouse)
Genomic location for SFTPD
Genomic location for SFTPD
Band14 B|14 22.36 cMStart40,894,171 bp[2]
End40,907,106 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • lower lobe of lung

  • visceral pleura

  • upper lobe of lung

  • upper lobe of left lung

  • right lung

  • testicle

  • germinal epithelium

  • body of pancreas

  • skin of leg

  • left lobe of thyroid gland
Top expressed in
  • right lung

  • right lung lobe

  • left lung

  • left lung lobe

  • lacrimal gland

  • trachea

  • olfactory epithelium

  • parotid gland

  • uterus

  • conjunctival fornix
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein binding
  • carbohydrate binding
  • identical protein binding
  • lipopolysaccharide binding
  • monosaccharide binding
Cellular component
  • cytoplasm
  • collagen
  • endoplasmic reticulum membrane
  • clathrin-coated endocytic vesicle
  • endocytic vesicle
  • extracellular region
  • lysosome
  • extracellular space
  • multivesicular body
  • rough endoplasmic reticulum
Biological process
  • surfactant homeostasis
  • positive regulation of phagocytosis
  • immune system process
  • receptor-mediated endocytosis
  • respiratory gaseous exchange by respiratory system
  • reactive oxygen species metabolic process
  • regulation of cytokine production
  • negative regulation of T cell proliferation
  • macrophage chemotaxis
  • defense response to bacterium
  • regulation of immune response
  • lung alveolus development
  • innate immune response
  • toll-like receptor signaling pathway
  • induction of bacterial agglutination
  • regulation of adhesion of symbiont to host epithelial cell
  • developmental process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

6441

20390

Ensembl

ENSG00000133661

ENSMUSG00000021795

UniProt

P35247

P50404

RefSeq (mRNA)

NM_003019

NM_009160

RefSeq (protein)

NP_003010

NP_033186

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

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000133661 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b c 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. ^ a b 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

  • Atochina-Vasserman EN, Beers MF, Kadire H, Tomer Y, Inch A, Scott P, et al. (December 2007). "Selective inhibition of inducible NO synthase activity in vivo reverses inflammatory abnormalities in surfactant protein D-deficient mice". Journal of Immunology. 179 (12): 8090–7. doi:10.4049/jimmunol.179.12.8090. PMC 4009628. PMID 18056350.
  • 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.
  • Hansen S, Holmskov U (August 1998). "Structural aspects of collectins and receptors for collectins". Immunobiology. 199 (2): 165–89. doi:10.1016/s0171-2985(98)80025-9. PMID 9777404.
  • Lu J, Willis AC, Reid KB (June 1992). "Purification, characterization and cDNA cloning of human lung surfactant protein D". The Biochemical Journal. 284. 284 ( Pt 3) (3): 795–802. doi:10.1042/bj2840795. PMC 1132609. PMID 1339284.
  • Persson AV, Gibbons BJ, Shoemaker JD, Moxley MA, Longmore WJ (December 1992). "The major glycolipid recognized by SP-D in surfactant is phosphatidylinositol". Biochemistry. 31 (48): 12183–9. doi:10.1021/bi00163a030. PMID 1457414.
  • Ogasawara Y, Kuroki Y, Akino T (October 1992). "Pulmonary surfactant protein D specifically binds to phosphatidylinositol". The Journal of Biological Chemistry. 267 (29): 21244–9. doi:10.1016/S0021-9258(19)36824-3. PMID 1400434.
  • 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.
  • Kuroki Y, Shiratori M, Ogasawara Y, Tsuzuki A, Akino T (November 1991). "Characterization of pulmonary surfactant protein D: its copurification with lipids". Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1086 (2): 185–90. doi:10.1016/0005-2760(91)90006-4. PMID 1932100.
  • 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.
  • Schaeffer E, Guillou F, Part D, Zakin MM (November 1993). "A different combination of transcription factors modulates the expression of the human transferrin promoter in liver and Sertoli cells". The Journal of Biological Chemistry. 268 (31): 23399–408. doi:10.1016/S0021-9258(19)49476-3. PMID 8226864.
  • Kölble K, Lu J, Mole SE, Kaluz S, Reid KB (August 1993). "Assignment of the human pulmonary surfactant protein D gene (SFTP4) to 10q22-q23 close to the surfactant protein A gene cluster". Genomics. 17 (2): 294–8. doi:10.1006/geno.1993.1324. PMID 8406480.
  • Crouch E, Persson A, Chang D (January 1993). "Accumulation of surfactant protein D in human pulmonary alveolar proteinosis". The American Journal of Pathology. 142 (1): 241–8. PMC 1886847. PMID 8424457.
  • Crouch, E.; Rust, K.; Veile, R.; Donis-Keller, H.; Grosso, L. (February 1993). "Genomic organization of human surfactant protein D (SP-D). SP-D is encoded on chromosome 10q22.2-23.1". Journal of Biological Chemistry. 268 (4): 2976–2983. doi:10.1016/S0021-9258(18)53869-2. PMID 8428971.
  • Rust K, Bingle L, Mariencheck W, Persson A, Crouch EC (February 1996). "Characterization of the human surfactant protein D promoter: transcriptional regulation of SP-D gene expression by glucocorticoids". American Journal of Respiratory Cell and Molecular Biology. 14 (2): 121–30. doi:10.1165/ajrcmb.14.2.8630261. PMID 8630261.
  • Bonaldo MF, Lennon G, Soares MB (September 1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Research. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • 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.
  • Botas C, Poulain F, Akiyama J, Brown C, Allen L, Goerke J, et al. (September 1998). "Altered surfactant homeostasis and alveolar type II cell morphology in mice lacking surfactant protein D". Proceedings of the National Academy of Sciences of the United States of America. 95 (20): 11869–74. Bibcode:1998PNAS...9511869B. doi:10.1073/pnas.95.20.11869. PMC 21732. PMID 9751757.
  • Håkansson K, Lim NK, Hoppe HJ, Reid KB (March 1999). "Crystal structure of the trimeric alpha-helical coiled-coil and the three lectin domains of human lung surfactant protein D". Structure. 7 (3): 255–64. doi:10.1016/S0969-2126(99)80036-7. PMID 10368295.
  • Holmskov U, Mollenhauer J, Madsen J, Vitved L, Gronlund J, Tornoe I, et al. (September 1999). "Cloning of gp-340, a putative opsonin receptor for lung surfactant protein D". Proceedings of the National Academy of Sciences of the United States of America. 96 (19): 10794–9. Bibcode:1999PNAS...9610794H. doi:10.1073/pnas.96.19.10794. PMC 17962. PMID 10485905.
  • Lausen M, Lynch N, Schlosser A, Tornoe I, Saekmose SG, Teisner B, et al. (November 1999). "Microfibril-associated protein 4 is present in lung washings and binds to the collagen region of lung surfactant protein D". The Journal of Biological Chemistry. 274 (45): 32234–40. doi:10.1074/jbc.274.45.32234. PMID 10542261.
  • Madsen J, Kliem A, Tornoe I, Skjodt K, Koch C, Holmskov U (June 2000). "Localization of lung surfactant protein D on mucosal surfaces in human tissues". Journal of Immunology. 164 (11): 5866–70. doi:10.4049/jimmunol.164.11.5866. PMID 10820266.
  • Zhang L, Ikegami M, Crouch EC, Korfhagen TR, Whitsett JA (June 2001). "Activity of pulmonary surfactant protein-D (SP-D) in vivo is dependent on oligomeric structure". The Journal of Biological Chemistry. 276 (22): 19214–9. doi:10.1074/jbc.M010191200. PMID 11278637.

External links

  • v
  • t
  • e
  • 1b08: LUNG SURFACTANT PROTEIN D (SP-D) (FRAGMENT)
    1b08: LUNG SURFACTANT PROTEIN D (SP-D) (FRAGMENT)
  • 1m7l: Solution Structure of the Coiled-Coil Trimerization Domain from Lung Surfactant Protein D
    1m7l: Solution Structure of the Coiled-Coil Trimerization Domain from Lung Surfactant Protein D
  • 1pw9: High resolution crystal structure of an active recombinant fragment of human lung surfactant protein D
    1pw9: High resolution crystal structure of an active recombinant fragment of human lung surfactant protein D
  • 1pwb: High resolution crystal structure of an active recombinant fragment of human lung surfactant protein D with maltose
    1pwb: High resolution crystal structure of an active recombinant fragment of human lung surfactant protein D with maltose
  • 2ggu: crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with maltotriose
    2ggu: crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with maltotriose
  • 2ggx: Crystal structure of the trimer neck and carbohydrate recognition domain of human surfactant protein D in complex with p-nitrophenyl maltoside
    2ggx: Crystal structure of the trimer neck and carbohydrate recognition domain of human surfactant protein D in complex with p-nitrophenyl maltoside
  • 2orj: crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with N-acetyl mannosamine
    2orj: crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with N-acetyl mannosamine
  • 2ork: crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with inositol-1-phosphate
    2ork: crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with inositol-1-phosphate
  • 2os9: crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with myoinositol
    2os9: crystal structure of the trimeric neck and carbohydrate recognition domain of human surfactant protein D in complex with myoinositol


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