UniProt functional annotation for P35247



	UniProt functional annotation for P35247

UniProt code: P35247.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

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. {ECO:0000269|PubMed:23478426}.

Subunit: Oligomeric complex of 4 set of homotrimers.

Subcellular location: Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film.

Tissue specificity: Expressed in lung, brain, pancreas and adipose tissue (mainly mature adipocytes). {ECO:0000269|PubMed:23478426}.

Ptm: The N-terminus is blocked.

Ptm: 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. {ECO:0000250}.

Ptm: S-nitrosylation at Cys-35 and Cys-40 alters the quaternary structure which results in a pro-inflammatory chemoattractive signaling activity with macrophages. {ECO:0000250}.

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).

Similarity: Belongs to the SFTPD family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



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. {ECO:0000269\|PubMed:23478426}.


Subunit:		Oligomeric complex of 4 set of homotrimers.
Subcellular location:		Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film.
Tissue specificity:		Expressed in lung, brain, pancreas and adipose tissue (mainly mature adipocytes). {ECO:0000269\|PubMed:23478426}.
Ptm:		The N-terminus is blocked.
Ptm:		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. {ECO:0000250}.
Ptm:		S-nitrosylation at Cys-35 and Cys-40 alters the quaternary structure which results in a pro-inflammatory chemoattractive signaling activity with macrophages. {ECO:0000250}.
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).
Similarity:		Belongs to the SFTPD family. {ECO:0000305}.