P35247 · SFTPD_HUMAN
- ProteinPulmonary surfactant-associated protein D
- GeneSFTPD
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids375 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
Miscellaneous
Pulmonary surfactant consists of 90% lipid and 10% protein. There are 4 surfactant-associated proteins: 2 collagenous, carbohydrate-binding glycoproteins (SP-A and SP-D) and 2 small hydrophobic proteins (SP-B and SP-C).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePulmonary surfactant-associated protein D
- Short namesPSP-D; SP-D
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP35247
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_020937 | 31 | in dbSNP:rs721917 | |||
Sequence: M → T | ||||||
Natural variant | VAR_020938 | 123 | in dbSNP:rs17878336 | |||
Sequence: L → V | ||||||
Natural variant | VAR_020939 | 180 | in dbSNP:rs2243639 | |||
Sequence: T → A | ||||||
Natural variant | VAR_020940 | 290 | in dbSNP:rs3088308 | |||
Sequence: S → T | ||||||
Natural variant | VAR_020941 | 309 | in dbSNP:rs4469829 | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 415 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, modified residue, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MLLFLLSALVLLTQPLGYLE | ||||||
Chain | PRO_0000017465 | 21-375 | Pulmonary surfactant-associated protein D | |||
Sequence: AEMKTYSHRTMPSACTLVMCSSVESGLPGRDGRDGREGPRGEKGDPGLPGAAGQAGMPGQAGPVGPKGDNGSVGEPGPKGDTGPSGPPGPPGVPGPAGREGPLGKQGNIGPQGKPGPKGEAGPKGEVGAPGMQGSAGARGLAGPKGERGVPGERGVPGNTGAAGSAGAMGPQGSPGARGPPGLKGDKGIPGDKGAKGESGLPDVASLRQQVEALQGQVQHLQAAFSQYKKVELFPNGQSVGEKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIFTNGKWNDRACGEKRLVVCEF | ||||||
Modified residue | 35 | S-nitrosocysteine | ||||
Sequence: C | ||||||
Modified residue | 40 | S-nitrosocysteine | ||||
Sequence: C | ||||||
Modified residue | 78 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 87 | 5-hydroxylysine | ||||
Sequence: K | ||||||
Glycosylation | 90 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 96 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 99 | 5-hydroxylysine | ||||
Sequence: K | ||||||
Modified residue | 171 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 177 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Disulfide bond | 281↔373 | |||||
Sequence: CTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIFTNGKWNDRACGEKRLVVC | ||||||
Disulfide bond | 351↔365 | |||||
Sequence: CVEIFTNGKWNDRAC |
Post-translational modification
The N-terminus is blocked.
Hydroxylation on proline residues within the sequence motif, GXPG, is most likely to be 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.
S-nitrosylation at Cys-35 and Cys-40 alters the quaternary structure which results in a pro-inflammatory chemoattractive signaling activity with macrophages.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in lung, brain, pancreas and adipose tissue (mainly mature adipocytes).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Oligomeric complex of 4 set of homotrimers.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P35247 | ACE2 Q9BYF1 | 2 | EBI-11316157, EBI-7730807 | |
XENO | P35247 | S P0DTC2 | 3 | EBI-11316157, EBI-25474821 | |
BINARY | P35247 | UPK1A O00322 | 3 | EBI-11316157, EBI-14031976 | |
XENO | PRO_0000017465 | S P0DTC2 | 11 | EBI-27021977, EBI-25474821 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 45-221 | Disordered | ||||
Sequence: SGLPGRDGRDGREGPRGEKGDPGLPGAAGQAGMPGQAGPVGPKGDNGSVGEPGPKGDTGPSGPPGPPGVPGPAGREGPLGKQGNIGPQGKPGPKGEAGPKGEVGAPGMQGSAGARGLAGPKGERGVPGERGVPGNTGAAGSAGAMGPQGSPGARGPPGLKGDKGIPGDKGAKGESGL | ||||||
Domain | 46-222 | Collagen-like | ||||
Sequence: GLPGRDGRDGREGPRGEKGDPGLPGAAGQAGMPGQAGPVGPKGDNGSVGEPGPKGDTGPSGPPGPPGVPGPAGREGPLGKQGNIGPQGKPGPKGEAGPKGEVGAPGMQGSAGARGLAGPKGERGVPGERGVPGNTGAAGSAGAMGPQGSPGARGPPGLKGDKGIPGDKGAKGESGLP | ||||||
Compositional bias | 49-63 | Basic and acidic residues | ||||
Sequence: GRDGRDGREGPRGEK | ||||||
Compositional bias | 101-117 | Pro residues | ||||
Sequence: DTGPSGPPGPPGVPGPA | ||||||
Coiled coil | 223-252 | |||||
Sequence: DVASLRQQVEALQGQVQHLQAAFSQYKKVE | ||||||
Domain | 260-375 | C-type lectin | ||||
Sequence: VGEKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIFTNGKWNDRACGEKRLVVCEF |
Sequence similarities
Belongs to the SFTPD family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length375
- Mass (Da)37,728
- Last updated2011-01-11 v3
- Checksum298917699FC40F6A
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5T0M2 | Q5T0M2_HUMAN | SFTPD | 218 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 22 | in Ref. 6; AAH22318 | ||||
Sequence: E → G | ||||||
Compositional bias | 49-63 | Basic and acidic residues | ||||
Sequence: GRDGRDGREGPRGEK | ||||||
Sequence conflict | 59 | in Ref. 7; AA sequence | ||||
Sequence: P → F | ||||||
Compositional bias | 101-117 | Pro residues | ||||
Sequence: DTGPSGPPGPPGVPGPA | ||||||
Sequence conflict | 122 | in Ref. 2; AAB59450 | ||||
Sequence: P → A | ||||||
Sequence conflict | 240 | in Ref. 7; AA sequence | ||||
Sequence: H → P | ||||||
Sequence conflict | 341 | in Ref. 6; AAH22318 | ||||
Sequence: E → K | ||||||
Sequence conflict | 369 | in Ref. 3; CAG46746 | ||||
Sequence: R → S |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X65018 EMBL· GenBank· DDBJ | CAA46152.1 EMBL· GenBank· DDBJ | mRNA | ||
L05485 EMBL· GenBank· DDBJ | AAB59450.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L05483 EMBL· GenBank· DDBJ | AAB59450.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
L05484 EMBL· GenBank· DDBJ | AAB59450.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CR541948 EMBL· GenBank· DDBJ | CAG46746.1 EMBL· GenBank· DDBJ | mRNA | ||
AY216721 EMBL· GenBank· DDBJ | AAO22991.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL512662 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC022318 EMBL· GenBank· DDBJ | AAH22318.1 EMBL· GenBank· DDBJ | mRNA |