Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00362
Entry Name
UniProt Accession
Theoretical PI
6.19
Molecular Weight
21052.79
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Pulmonary surfactant-associated protein C
Protein Synonyms/Alias
SP-C; Pulmonary surfactant-associated proteolipid SPL(Val); SP5;
Gene Name
SFTPC
Gene Synonyms/Alias
SFTP2;
Created Date
01-OCT-1989
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
28
Canonical
RGRFGIPCCPVHLKR
[1][2]
S-Palmitoylation
29
Canonical
GRFGIPCCPVHLKRL
[1][2]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Curstedt T, Johansson J, Persson P, Eklund A, Robertson B, Löwenadler B,Jörnvall H. Hydrophobic surfactant-associated polypeptides: SP-C is a lipopeptidewith two palmitoylated cysteine residues, whereas SP-B lacks covalently linkedfatty acyl groups. Proc Natl Acad Sci U S A. 1990 Apr;87(8):2985-9.[PMID:2326260]
[2] Mulugeta S, Beers MF. Processing of surfactant protein C requires a type IItransmembrane topology directed by juxtamembrane positively charged residues. JBiol Chem. 2003 Nov 28;278(48):47979-86. Epub 2003 Aug 21.[PMID:12933801]
Functional Description
Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air- liquid interface in the peripheral air spaces.
Sequence Annotation
Domain: 94 197 BRICHOS.
Protein Length
197 AA.
Protein Sequence
(Canonical)
MDVGSKEVLM ESPPDYSAAP RGRFGIPCCP VHLKRLLIVV VVVVLIVVVI VGALLMGLHM  60
SQKHTEMVLE MSIGAPEAQQ RLALSEHLVT TATFSIGSTG LVVYDYQQLL IAYKPAPGTC  120
CYIMKIAPES IPSLEALNRK VHNFQMECSL QAKPAVPTSK LGQAEGRDAG SAPSGGDPAF  180
LGMAVNTLCG EVPLYYI                                                 197
FASTA
(Canonical)
>LipidDB-9606-00362|P11686
MDVGSKEVLMESPPDYSAAPRGRFGIPCCPVHLKRLLIVVVVVVLIVVVIVGALLMGLHM
SQKHTEMVLEMSIGAPEAQQRLALSEHLVTTATFSIGSTGLVVYDYQQLLIAYKPAPGTC
CYIMKIAPESIPSLEALNRKVHNFQMECSLQAKPAVPTSKLGQAEGRDAGSAPSGGDPAF
LGMAVNTLCGEVPLYYI
Gene Ontology
GO:0097208; C:alveolar lamellar body; IEA:Ensembl
GO:0005615; C:extracellular space; IEA:Ensembl
GO:0005771; C:multivesicular body; IEA:Ensembl
GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl
GO:0071732; P:cellular response to nitric oxide; IEA:Ensembl
GO:0007623; P:circadian rhythm; IEA:Ensembl
GO:0051260; P:protein homooligomerization; IEA:Ensembl
GO:0007585; P:respiratory gaseous exchange; IEA:UniProtKB-KW
GO:0051591; P:response to cAMP; IEA:Ensembl
GO:0051384; P:response to glucocorticoid; IEA:Ensembl
GO:0009749; P:response to glucose; IEA:Ensembl
GO:0070848; P:response to growth factor; IEA:Ensembl
GO:0055093; P:response to hyperoxia; IEA:Ensembl
GO:0070741; P:response to interleukin-6; IEA:Ensembl
GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl
GO:0032526; P:response to retinoic acid; IEA:Ensembl
GO:0033189; P:response to vitamin A; IEA:Ensembl
Interpro
InterPro; IPR007084; BRICHOS_dom
InterPro; IPR001729; Pulm_surfact_AP
InterPro; IPR018051; SP-C_palmitoylation_site
InterPro; IPR015091; Surfactant_protein_propep
Pfam
Pfam; PF04089; BRICHOS;
Pfam; PF08999; SP_C-Propep;
SMART
SMART; SM01039; BRICHOS;
SMART; SM00019; SF_P;
PROSITE
PROSITE; PS50869; BRICHOS;
PROSITE; PS00341; SURFACT_PALMITOYL;
PRINTS