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P08427 (SFTPA_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pulmonary surfactant-associated protein A

Short name=PSAP
Short name=PSP-A
Short name=SP-A
Gene names
Name:Sftpa1
Synonyms:Sftp-1, Sftp1, Sftpa
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length248 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

Oligomeric complex of 6 set of homotrimers.

Subcellular location

Secretedextracellular spaceextracellular matrix. Secretedextracellular spacesurface film.

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).

Sequence similarities

Belongs to the SFTPA family.

Contains 1 C-type lectin domain.

Contains 1 collagen-like domain.

Sequence caution

The sequence AAA41972.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGaseous exchange
   Cellular componentExtracellular matrix
Secreted
Surface film
   DomainCollagen
Repeat
Signal
   LigandCalcium
Lectin
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to mechanical stimulus

Inferred from expression pattern PubMed 12600831. Source: RGD

cellular response to nitric oxide

Inferred from expression pattern PubMed 15640287. Source: RGD

circadian rhythm

Inferred from expression pattern PubMed 12872443. Source: RGD

positive regulation of phagocytosis

Inferred from direct assay PubMed 15187139. Source: RGD

respiratory gaseous exchange

Inferred from electronic annotation. Source: UniProtKB-KW

response to epidermal growth factor

Inferred from expression pattern PubMed 19781387. Source: RGD

response to glucocorticoid

Inferred from expression pattern PubMed 2015097. Source: RGD

response to hormone

Inferred from expression pattern PubMed 9779374. Source: RGD

response to hyperoxia

Inferred from expression pattern PubMed 11472975. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 14756961. Source: RGD

response to interleukin-6

Inferred from expression pattern PubMed 11000512. Source: RGD

response to lipopolysaccharide

Inferred from expression pattern PubMed 11000512. Source: RGD

response to retinoic acid

Inferred from expression pattern PubMed 9505268. Source: RGD

response to vitamin A

Inferred from expression pattern PubMed 10385596. Source: RGD

   Cellular_componentcollagen trimer

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasmic vesicle

Inferred from direct assay PubMed 16187065. Source: RGD

extracellular space

Inferred from direct assay PubMed 11472975. Source: RGD

multivesicular body

Inferred from direct assay PubMed 16187065. Source: RGD

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

rough endoplasmic reticulum

Inferred from direct assay PubMed 16187065. Source: RGD

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 248228Pulmonary surfactant-associated protein A
PRO_0000017462

Regions

Domain28 – 10073Collagen-like
Domain133 – 248116C-type lectin

Sites

Metal binding2151Calcium
Metal binding2171Calcium; via carbonyl oxygen
Metal binding2341Calcium
Metal binding2351Calcium
Site211Not glycosylated

Amino acid modifications

Modified residue3014-hydroxyproline
Modified residue3314-hydroxyproline
Modified residue3614-hydroxyproline
Modified residue4214-hydroxyproline
Modified residue5414-hydroxyproline
Modified residue5714-hydroxyproline
Modified residue6314-hydroxyproline
Modified residue6714-hydroxyproline
Modified residue7014-hydroxyproline
Modified residue7614-hydroxyproline
Glycosylation2071N-linked (GlcNAc...) Probable
Disulfide bond26Interchain By similarity
Disulfide bond155 ↔ 246 Ref.5
Disulfide bond224 ↔ 238 Ref.5

Experimental info

Sequence conflict781A → G in AAA41973. Ref.1
Sequence conflict781A → G in CAA31573. Ref.1
Sequence conflict781A → G in CAA31574. Ref.1
Sequence conflict841E → G in AAA41973. Ref.1
Sequence conflict841E → G in CAA31573. Ref.1
Sequence conflict841E → G in CAA31574. Ref.1
Sequence conflict1391Missing in AAA41972. Ref.2
Sequence conflict1561T → TF in AAA41972. Ref.2
Sequence conflict1801K → N in CAA31574. Ref.1

Secondary structure

....................... 248
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08427 [UniParc].

Last modified October 1, 1996. Version 3.
Checksum: CAA0203009E682A5

FASTA24826,289
        10         20         30         40         50         60 
MSLCSLAFTL FLTVVAGIKC NVTDVCAGSP GIPGAPGNHG LPGRDGRDGV KGDPGPPGPM 

        70         80         90        100        110        120 
GPPGGMPGLP GRDGLPGAPG APGERGDKGE PGERGLPGFP AYLDEELQTE LYEIKHQILQ 

       130        140        150        160        170        180 
TMGVLSLQGS MLSVGDKVFS TNGQSVNFDT IKEMCTRAGG NIAVPRTPEE NEAIASIAKK 

       190        200        210        220        230        240 
YNNYVYLGMI EDQTPGDFHY LDGASVNYTN WYPGEPRGQG KEKCVEMYTD GTWNDRGCLQ 


YRLAVCEF 

« Hide

References

« Hide 'large scale' references
[1]"Rat pulmonary surfactant protein A is expressed as two differently sized mRNA species which arise from differential polyadenylation of one transcript."
Fisher J.H., Emrie P.A., Shannon J., Sano K., Hattler B., Mason R.J.
Biochim. Biophys. Acta 950:338-345(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
[2]"Isolation and sequence of a cDNA clone for the rat pulmonary surfactant-associated protein (PSP-A)."
Sano K., Fisher J.H., Mason R.J., Kuroki Y., Schilling J., Benson B., Voelker D.
Biochem. Biophys. Res. Commun. 144:367-374(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]"Sequence of rat surfactant protein A gene and functional mapping of its upstream region."
Smith C.I., Rosenberg E., Reisher S.R., Li F., Kefalides P., Fisher A.B., Feinstein S.I.
Am. J. Physiol. 269:L603-L612(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Sprague-Dawley.
Tissue: Lung.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[5]"Crystal structure of trimeric carbohydrate recognition and neck domains of surfactant protein A."
Head J.F., Mealy T.R., McCormack F.X., Seaton B.A.
J. Biol. Chem. 278:43254-43260(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 101-248, CALCIUM-BINDING SITES, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33201 mRNA. Translation: AAA41973.1.
X13176 mRNA. Translation: CAA31573.1.
X13177 mRNA. Translation: CAA31574.1.
M15754 mRNA. Translation: AAA41972.1. Different initiation.
U43092 Genomic DNA. Translation: AAA85516.1.
BC085353 mRNA. Translation: AAH85353.1.
PIRLNRTPS. A29299.
RefSeqNP_001257574.1. NM_001270645.1.
NP_001257576.1. NM_001270647.1.
NP_059025.2. NM_017329.2.
UniGeneRn.11343.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GIEmodel-A101-248[»]
1R13X-ray2.10A101-248[»]
1R14X-ray2.50A101-248[»]
3PAKX-ray1.90A101-248[»]
3PAQX-ray2.10A101-248[»]
3PARX-ray2.30A101-248[»]
3PBFX-ray1.80A101-248[»]
ProteinModelPortalP08427.
SMRP08427. Positions 104-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000039850.

Proteomic databases

PaxDbP08427.
PRIDEP08427.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000047870; ENSRNOP00000039850; ENSRNOG00000011438.
GeneID24773.
KEGGrno:24773.
UCSCRGD:3665. rat.

Organism-specific databases

CTD653509.
RGD3665. Sftpa1.

Phylogenomic databases

eggNOGNOG315755.
GeneTreeENSGT00700000104102.
HOGENOMHOG000085660.
HOVERGENHBG108270.
InParanoidP08427.
KOK10067.
OMAEMYTDGK.
OrthoDBEOG7HXCVB.
PhylomeDBP08427.
TreeFamTF330481.

Gene expression databases

GenevestigatorP08427.

Family and domain databases

Gene3D3.10.100.10. 1 hit.
InterProIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
[Graphical view]
PfamPF01391. Collagen. 2 hits.
PF00059. Lectin_C. 1 hit.
[Graphical view]
SMARTSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMSSF56436. SSF56436. 1 hit.
PROSITEPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08427.
NextBio604356.
PROP08427.

Entry information

Entry nameSFTPA_RAT
AccessionPrimary (citable) accession number: P08427
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 138 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references