Q8IWL1 · SFPA2_HUMAN
- ProteinPulmonary surfactant-associated protein A2
- GeneSFTPA2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids248 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration.
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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Aspect | Term | |
---|---|---|
Cellular Component | clathrin-coated endocytic vesicle | |
Cellular Component | collagen trimer | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | lamellar body | |
Cellular Component | multivesicular body | |
Molecular Function | carbohydrate binding | |
Biological Process | respiratory gaseous exchange by respiratory system |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePulmonary surfactant-associated protein A2
- Short namesPSP-A; PSPA; SP-A; SP-A2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8IWL1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Interstitial lung disease 2 (ILD2)
- Note
- DescriptionA form of interstitial lung disease, a heterogeneous group of diseases affecting the distal part of the lung and characterized by a progressive remodeling of the alveolar interstitium. The disease spectrum ranges from idiopathic interstitial pneumonia or pneumonitis to idiopathic pulmonary fibrosis, that is associated with an increased risk of developing lung cancer. Clinical features of interstitial lung disease include dyspnea, clubbing of the fingers, and restrictive lung capacity. ILD2 inheritance is autosomal dominant.
- See alsoMIM:178500
Natural variants in ILD2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086122 | 171 | N>I | in ILD2; uncertain significance; impaired secretion | |
VAR_086123 | 178 | V>M | in ILD2; impaired secretion | |
VAR_086124 | 181 | Y>C | in ILD2; uncertain significance; impaired secretion | |
VAR_063519 | 198 | F>S | in ILD2; the mutant protein is retained in the endoplasmic reticulum and is not secreted; dbSNP:rs121917738 | |
VAR_063520 | 231 | G>V | in ILD2; the mutant protein is retained in the endoplasmic reticulum and is not secreted; dbSNP:rs121917737 | |
VAR_086125 | 233 | W>C | in ILD2; impaired secretion | |
VAR_086126 | 233 | W>L | in ILD2; impaired secretion | |
VAR_086127 | 233 | W>R | in ILD2; impaired secretion | |
VAR_086128 | 238 | C>S | in ILD2; impaired secretion | |
VAR_086129 | 242 | R>Q | in ILD2; uncertain significance; impaired secretion |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_021293 | 9 | in allele 1A0; dbSNP:rs1059046 | |||
Sequence: T → N | ||||||
Natural variant | VAR_063518 | 12 | in dbSNP:rs72659394 | |||
Sequence: L → W | ||||||
Natural variant | VAR_021294 | 50 | in dbSNP:rs192907309 | |||
Sequence: V → L | ||||||
Natural variant | VAR_021295 | 91 | in allele 1A; dbSNP:rs17886395 | |||
Sequence: A → P | ||||||
Natural variant | VAR_086122 | 171 | in ILD2; uncertain significance; impaired secretion | |||
Sequence: N → I | ||||||
Natural variant | VAR_086123 | 178 | in ILD2; impaired secretion | |||
Sequence: V → M | ||||||
Natural variant | VAR_086124 | 181 | in ILD2; uncertain significance; impaired secretion | |||
Sequence: Y → C | ||||||
Natural variant | VAR_063519 | 198 | in ILD2; the mutant protein is retained in the endoplasmic reticulum and is not secreted; dbSNP:rs121917738 | |||
Sequence: F → S | ||||||
Natural variant | VAR_021296 | 223 | in allele 1A1, allele 1A3 and allele 1A4; dbSNP:rs1965708 | |||
Sequence: Q → K | ||||||
Natural variant | VAR_063520 | 231 | in ILD2; the mutant protein is retained in the endoplasmic reticulum and is not secreted; dbSNP:rs121917737 | |||
Sequence: G → V | ||||||
Natural variant | VAR_086125 | 233 | in ILD2; impaired secretion | |||
Sequence: W → C | ||||||
Natural variant | VAR_086126 | 233 | in ILD2; impaired secretion | |||
Sequence: W → L | ||||||
Natural variant | VAR_086127 | 233 | in ILD2; impaired secretion | |||
Sequence: W → R | ||||||
Natural variant | VAR_086128 | 238 | in ILD2; impaired secretion | |||
Sequence: C → S | ||||||
Natural variant | VAR_086129 | 242 | in ILD2; uncertain significance; impaired secretion | |||
Sequence: R → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 409 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MWLCPLALTLILMAASGAAC | ||||||
Chain | PRO_0000017458 | 21-248 | Pulmonary surfactant-associated protein A2 | |||
Sequence: EVKDVCVGSPGIPGTPGSHGLPGRDGRDGVKGDPGPPGPMGPPGETPCPPGNNGLPGAPGVPGERGEKGEAGERGPPGLPAHLDEELQATLHDFRHQILQTRGALSLQGSIMTVGEKVFSSNGQSITFDAIQEACARAGGRIAVPRNPEENEAIASFVKKYNTYAYVGLTEGPSPGDFRYSDGTPVNYTNWYRGEPAGRGKEQCVEMYTDGQWNDRNCLYSRLTICEF | ||||||
Disulfide bond | 26 | Interchain | ||||
Sequence: C | ||||||
Modified residue | 30 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 33 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 36 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 42 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 54 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 57 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 63 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 67 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Modified residue | 70 | 4-hydroxyproline | ||||
Sequence: P | ||||||
Disulfide bond | 155↔246 | |||||
Sequence: CARAGGRIAVPRNPEENEAIASFVKKYNTYAYVGLTEGPSPGDFRYSDGTPVNYTNWYRGEPAGRGKEQCVEMYTDGQWNDRNCLYSRLTIC | ||||||
Glycosylation | 207 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 224↔238 | |||||
Sequence: CVEMYTDGQWNDRNC |
Post-translational modification
N-acetylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Oligomeric complex of 6 set of homotrimers.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q8IWL1 | NCS1 P62166 | 3 | EBI-12350685, EBI-746987 | |
BINARY | Q8IWL1 | UBQLN2 Q9UHD9 | 6 | EBI-12350685, EBI-947187 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 28-100 | Collagen-like | ||||
Sequence: GSPGIPGTPGSHGLPGRDGRDGVKGDPGPPGPMGPPGETPCPPGNNGLPGAPGVPGERGEKGEAGERGPPGLP | ||||||
Region | 33-101 | Disordered | ||||
Sequence: PGTPGSHGLPGRDGRDGVKGDPGPPGPMGPPGETPCPPGNNGLPGAPGVPGERGEKGEAGERGPPGLPA | ||||||
Compositional bias | 55-76 | Pro residues | ||||
Sequence: GPPGPMGPPGETPCPPGNNGLP | ||||||
Domain | 132-248 | C-type lectin | ||||
Sequence: MTVGEKVFSSNGQSITFDAIQEACARAGGRIAVPRNPEENEAIASFVKKYNTYAYVGLTEGPSPGDFRYSDGTPVNYTNWYRGEPAGRGKEQCVEMYTDGQWNDRNCLYSRLTICEF |
Sequence similarities
Belongs to the SFTPA family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length248
- Mass (Da)26,169
- Last updated2022-02-23 v2
- Checksum5E5510F0E9A7B6A4
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A1W2PR89 | A0A1W2PR89_HUMAN | SFTPA2 | 38 | ||
R4GMN3 | R4GMN3_HUMAN | SFTPA2 | 97 | ||
X6REF7 | X6REF7_HUMAN | SFTPA2 | 158 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 55-76 | Pro residues | ||||
Sequence: GPPGPMGPPGETPCPPGNNGLP | ||||||
Sequence conflict | 247 | in Ref. 2; AAA60319 | ||||
Sequence: E → D |
Polymorphism
At least 6 alleles of SFTPA2 are known: 1A, 1A0, 1A1, 1A2, 1A3 and 1A4. The sequence shown is that of allele 1A2.
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
K03475 EMBL· GenBank· DDBJ | AAA36520.1 EMBL· GenBank· DDBJ | mRNA | ||
M68519 EMBL· GenBank· DDBJ | AAA60319.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
HQ021421 EMBL· GenBank· DDBJ | ADO27664.1 EMBL· GenBank· DDBJ | mRNA | ||
HQ021422 EMBL· GenBank· DDBJ | ADO27665.1 EMBL· GenBank· DDBJ | mRNA | ||
HQ021423 EMBL· GenBank· DDBJ | ADO27666.1 EMBL· GenBank· DDBJ | mRNA | ||
HQ021424 EMBL· GenBank· DDBJ | ADO27667.1 EMBL· GenBank· DDBJ | mRNA | ||
HQ021427 EMBL· GenBank· DDBJ | ADO27670.1 EMBL· GenBank· DDBJ | mRNA | ||
HQ021428 EMBL· GenBank· DDBJ | ADO27671.1 EMBL· GenBank· DDBJ | mRNA | ||
HQ021429 EMBL· GenBank· DDBJ | ADO27672.1 EMBL· GenBank· DDBJ | mRNA | ||
HQ021430 EMBL· GenBank· DDBJ | ADO27673.1 EMBL· GenBank· DDBJ | mRNA | ||
AY206682 EMBL· GenBank· DDBJ | AAO13490.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX248123 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC111571 EMBL· GenBank· DDBJ | AAI11572.1 EMBL· GenBank· DDBJ | mRNA | ||
BC139727 EMBL· GenBank· DDBJ | AAI39728.1 EMBL· GenBank· DDBJ | mRNA | ||
BC157866 EMBL· GenBank· DDBJ | AAI57867.1 EMBL· GenBank· DDBJ | mRNA | ||
BC157890 EMBL· GenBank· DDBJ | AAI57891.1 EMBL· GenBank· DDBJ | mRNA |