Letunic et al. (2017) Nucleic Acids Res doi: 10.1093/nar/gkx922
Letunic et al. (2020) Nucleic Acids Res doi: 10.1093/nar/gkaa937

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SF_P Pulmonary surfactant proteins

SMART accession number:	SM00019
Description:	Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-C, a component of surfactant, is a highly hydrophobic peptide of 35 amino acid residues which is processed from a larger precursor protein. SP-C is post-translationally modified by the covalent attachment of two palmitoyl groups on two adjacent cysteines
Interpro abstract (IPR001729):	Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-C, a component of surfactant, is a highly hydrophobic peptide of 35 amino acid residues which is processed from a larger precursor protein. SP-C is post-translationally modified by the covalent attachment of two palmitoyl groups on two adjacent cysteines [ (PUBMED:2326260) (PUBMED:2015882) ].
GO process:	respiratory gaseous exchange by respiratory system (GO:0007585)
GO component:	extracellular region (GO:0005576)
Family alignment:	View or CHROMA formatHMM/Web logoCLUSTALW formatMSF formatFASTA formatPIR format

There are 68 SF_P domains in 68 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Taxonomic distribution of proteins containing SF_P domain.

  This tree includes only several representative species. The complete taxonomic breakdown of all proteins with SF_P domain is also avaliable.

  Click on the protein counts, or double click on taxonomic names to display all proteins containing SF_P domain in the selected taxonomic class.

• Literature (relevant references for this domain)

• Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.

  • Hayami T et al.
  • Specific loss of chondromodulin-I gene expression in chondrosarcoma and the suppression of tumor angiogenesis and growth by its recombinant protein in vivo.
  • FEBS Lett. 1999; 458: 436-40
  • Display abstract

  • Chondromodulin-I (ChM-I) was previously identified as an angiogenesis inhibitor in cartilage. Here, we demonstrated that the level of ChM-I transcripts was substantially reduced to 100 or even less in the lower-grade chondrosarcomas, in articular cartilage or other benign cartilage tumors. We implanted human chondrosarcoma OUMS-27 cells into nude mice that reproducibly produced tumors with cartilaginous matrix. Tumor-induced angiogenesis was evident when the tumors were excised 30 days after implantation. However, the local administration of recombinant human ChM-I almost completely blocked vascular invasion and tumor growth in vivo. Moreover, ChM-I also inhibited the growth of HT-29 colon adenocarcinoma in vivo, implying its therapeutic potential for solid tumors.

• Disease (disease genes where sequence variants are found in this domain)

• SwissProt sequences and OMIM curated human diseases associated with missense mutations within the SF_P domain.

  Protein	Disease
  Pulmonary surfactant-associated protein C (P11686) (SMART)	OMIM:178620: Pneumonitis, desquamative interstitial OMIM:263000:

• Structure (3D structures containing this domain)

• 3D Structures of SF_P domains in PDB

  PDB code	Main view	Title
  2yad		BRICHOS domain of Surfactant protein C precursor protein

• Links (links to other resources describing this domain)

• INTERPRO	IPR001729

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