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Protein

Pulmonary surfactant-associated protein D

Gene

Sftpd

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • identical protein binding Source: RGD
  • lipopolysaccharide binding Source: RGD
  • monosaccharide binding Source: RGD

GO - Biological processi

  • innate immune response Source: UniProtKB-KW
  • lung alveolus development Source: UniProtKB
  • negative regulation of interleukin-2 production Source: RGD
  • negative regulation of phagocytosis Source: RGD
  • negative regulation of T cell proliferation Source: RGD
  • opsonization Source: RGD
  • positive regulation of phagocytosis Source: RGD
  • regulation of liquid surface tension Source: RGD
  • respiratory gaseous exchange Source: UniProtKB-KW
  • response to corticosteroid Source: RGD
  • response to glucocorticoid Source: RGD
  • response to growth factor Source: RGD
  • response to hyperoxia Source: RGD
  • surfactant homeostasis Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Gaseous exchange, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Pulmonary surfactant-associated protein D
Short name:
PSP-D
Short name:
SP-D
Alternative name(s):
CP4
Lung surfactant protein D
Gene namesi
Name:Sftpd
Synonyms:Sftp4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3667. Sftpd.

Subcellular locationi

GO - Cellular componenti

  • collagen trimer Source: UniProtKB-KW
  • cytoplasmic vesicle Source: RGD
  • extracellular space Source: RGD
  • multivesicular body Source: RGD
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
  • rough endoplasmic reticulum Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted, Surface film

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 374355Pulmonary surfactant-associated protein DPRO_0000017467Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei34 – 341S-nitrosocysteine1 Publication
Modified residuei39 – 391S-nitrosocysteine1 Publication
Modified residuei77 – 771Hydroxyproline1 Publication
Modified residuei86 – 8615-hydroxylysine1 Publication
Glycosylationi89 – 891N-linked (GlcNAc...)
Modified residuei95 – 951Hydroxyproline1 Publication
Modified residuei98 – 9815-hydroxylysine1 Publication
Modified residuei109 – 1091PhosphoserineCombined sources
Modified residuei170 – 1701Hydroxyproline1 Publication
Modified residuei176 – 1761Hydroxyproline1 Publication
Disulfide bondi280 ↔ 372PROSITE-ProRule annotation
Disulfide bondi350 ↔ 364PROSITE-ProRule annotation

Post-translational modificationi

S-nitrosylation at Cys-34 and Cys-39 alters the quaternary structure which results in a pro-inflammatory chemoattractive signaling activity with macrophages.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Phosphoprotein, S-nitrosylation

Proteomic databases

PRIDEiP35248.

PTM databases

iPTMnetiP35248.

Interactioni

Subunit structurei

Oligomeric complex of 4 set of homotrimers.

GO - Molecular functioni

  • identical protein binding Source: RGD

Protein-protein interaction databases

BioGridi247389. 1 interaction.
DIPiDIP-46337N.
IntActiP35248. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP35248.
SMRiP35248. Positions 222-374.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 221177Collagen-likeAdd
BLAST
Domaini259 – 374116C-type lectinPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili222 – 25332Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the SFTPD family.Curated
Contains 1 C-type lectin domain.PROSITE-ProRule annotation
Contains 1 collagen-like domain.Curated

Keywords - Domaini

Coiled coil, Collagen, Repeat, Signal

Phylogenomic databases

HOVERGENiHBG108270.
InParanoidiP35248.
KOiK10068.
PhylomeDBiP35248.

Family and domain databases

Gene3Di1.20.5.360. 1 hit.
3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR015097. Surfac_D-trimer.
[Graphical view]
PfamiPF01391. Collagen. 2 hits.
PF00059. Lectin_C. 1 hit.
PF09006. Surfac_D-trimer. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P35248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLHFLSMLVL LVQPLGDLGA EMKTLSQRSI TNTCTLVLCS PTENGLPGRD
60 70 80 90 100
GRDGREGPRG EKGDPGLPGP MGLSGLPGPR GPVGPKGENG SAGEPGPKGE
110 120 130 140 150
RGLVGPPGSP GISGPAGKEG PSGKQGNIGP QGKPGPKGEA GPKGEVGAPG
160 170 180 190 200
MQGSAGAKGP AGPKGERGAP GEQGAPGNAG AAGPAGPAGP QGAPGSRGPP
210 220 230 240 250
GLKGDRGAPG DRGIKGESGL PDSAALRQQM EALNGKLQRL EAAFSRYKKA
260 270 280 290 300
ALFPDGQSVG DKIFRAANSE EPFEDAKEMC RQAGGQLASP RSATENAAVQ
310 320 330 340 350
QLVTAHSKAA FLSMTDVGTE GKFTYPTGEA LVYSNWAPGE PNNNGGAENC
360 370
VEIFTNGQWN DKACGEQRLV ICEF
Length:374
Mass (Da):37,561
Last modified:February 1, 1994 - v1
Checksum:iDB2BB5E399DB4A3C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891N → E AA sequence (PubMed:2675969).Curated
Sequence conflicti164 – 1641K → C AA sequence (PubMed:2675969).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81231 mRNA. Translation: AAA42170.1.
PIRiA42046.
RefSeqiNP_037010.1. NM_012878.2.
XP_008769287.1. XM_008771065.1.
UniGeneiRn.11348.

Genome annotation databases

GeneIDi25350.
KEGGirno:25350.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M81231 mRNA. Translation: AAA42170.1.
PIRiA42046.
RefSeqiNP_037010.1. NM_012878.2.
XP_008769287.1. XM_008771065.1.
UniGeneiRn.11348.

3D structure databases

ProteinModelPortaliP35248.
SMRiP35248. Positions 222-374.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247389. 1 interaction.
DIPiDIP-46337N.
IntActiP35248. 1 interaction.

PTM databases

iPTMnetiP35248.

Proteomic databases

PRIDEiP35248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25350.
KEGGirno:25350.

Organism-specific databases

CTDi6441.
RGDi3667. Sftpd.

Phylogenomic databases

HOVERGENiHBG108270.
InParanoidiP35248.
KOiK10068.
PhylomeDBiP35248.

Miscellaneous databases

PROiP35248.

Family and domain databases

Gene3Di1.20.5.360. 1 hit.
3.10.100.10. 1 hit.
InterProiIPR001304. C-type_lectin.
IPR016186. C-type_lectin-like.
IPR018378. C-type_lectin_CS.
IPR016187. C-type_lectin_fold.
IPR008160. Collagen.
IPR015097. Surfac_D-trimer.
[Graphical view]
PfamiPF01391. Collagen. 2 hits.
PF00059. Lectin_C. 1 hit.
PF09006. Surfac_D-trimer. 1 hit.
[Graphical view]
SMARTiSM00034. CLECT. 1 hit.
[Graphical view]
SUPFAMiSSF56436. SSF56436. 1 hit.
PROSITEiPS00615. C_TYPE_LECTIN_1. 1 hit.
PS50041. C_TYPE_LECTIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Primary structure of rat pulmonary surfactant protein D. cDNA and deduced amino acid sequence."
    Shimizu H., Fisher J.H., Papst P., Benson B., Lau K., Mason R.J., Voelker D.R.
    J. Biol. Chem. 267:1853-1857(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-33.
    Tissue: Lung.
  2. "Purification and biochemical characterization of CP4 (SP-D), a collagenous surfactant-associated protein."
    Persson A., Chang D., Rust K., Moxley M., Longmore W., Crouch E.
    Biochemistry 28:6361-6367(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 73-95 AND 153-180, HYDROXYLATION AT PRO-77; LYS-86; PRO-95; LYS-98; PRO-170 AND PRO-176.
    Tissue: Lung.
  3. Cited for: S-NITROSYLATION AT CYS-34 AND CYS-39.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSFTPD_RAT
AccessioniPrimary (citable) accession number: P35248
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: July 6, 2016
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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).

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.