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Pulmonary surfactant-associated protein D (PSP-D) (SP-D) (CP4) (Lung surfactant protein D)

 SFTPD_RAT               Reviewed;         374 AA.
P35248;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
01-FEB-1994, sequence version 1.
20-JUN-2018, entry version 130.
RecName: Full=Pulmonary surfactant-associated protein D;
Short=PSP-D;
Short=SP-D;
AltName: Full=CP4;
AltName: Full=Lung surfactant protein D;
Flags: Precursor;
Name=Sftpd; Synonyms=Sftp4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-33.
TISSUE=Lung;
PubMed=1370483;
Shimizu H., Fisher J.H., Papst P., Benson B., Lau K., Mason R.J.,
Voelker D.R.;
"Primary structure of rat pulmonary surfactant protein D. cDNA and
deduced amino acid sequence.";
J. Biol. Chem. 267:1853-1857(1992).
[2]
PROTEIN SEQUENCE OF 73-95 AND 153-180, AND HYDROXYLATION AT PRO-77;
LYS-86; PRO-95; LYS-98; PRO-170 AND PRO-176.
TISSUE=Lung;
PubMed=2675969; DOI=10.1021/bi00441a031;
Persson A., Chang D., Rust K., Moxley M., Longmore W., Crouch E.;
"Purification and biochemical characterization of CP4 (SP-D), a
collagenous surfactant-associated protein.";
Biochemistry 28:6361-6367(1989).
[3]
S-NITROSYLATION AT CYS-34 AND CYS-39.
PubMed=19007302; DOI=10.1371/journal.pbio.0060266;
Guo C.J., Atochina-Vasserman E.N., Abramova E., Foley J.P., Zaman A.,
Crouch E., Beers M.F., Savani R.C., Gow A.J.;
"S-nitrosylation of surfactant protein-D controls inflammatory
function.";
PLoS Biol. 6:E266-E266(2008).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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.
-!- SUBUNIT: Oligomeric complex of 4 set of homotrimers.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-11328301, EBI-11328301;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix. Secreted, extracellular space, surface film.
-!- PTM: S-nitrosylation at Cys-34 and Cys-39 alters the quaternary
structure which results in a pro-inflammatory chemoattractive
signaling activity with macrophages.
{ECO:0000269|PubMed:19007302}.
-!- 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}.
-----------------------------------------------------------------------
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EMBL; M81231; AAA42170.1; -; mRNA.
PIR; A42046; A42046.
RefSeq; NP_037010.1; NM_012878.2.
UniGene; Rn.11348; -.
ProteinModelPortal; P35248; -.
SMR; P35248; -.
BioGrid; 247389; 1.
DIP; DIP-46337N; -.
IntAct; P35248; 1.
iPTMnet; P35248; -.
PhosphoSitePlus; P35248; -.
PRIDE; P35248; -.
GeneID; 25350; -.
KEGG; rno:25350; -.
CTD; 6441; -.
RGD; 3667; Sftpd.
HOVERGEN; HBG108270; -.
InParanoid; P35248; -.
KO; K10068; -.
PhylomeDB; P35248; -.
PRO; PR:P35248; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0005771; C:multivesicular body; IDA:RGD.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0042802; F:identical protein binding; IDA:RGD.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:RGD.
GO; GO:0048029; F:monosaccharide binding; IDA:RGD.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0048286; P:lung alveolus development; ISS:UniProtKB.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:RGD.
GO; GO:0050765; P:negative regulation of phagocytosis; IDA:RGD.
GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:RGD.
GO; GO:0008228; P:opsonization; IDA:RGD.
GO; GO:0050766; P:positive regulation of phagocytosis; IDA:RGD.
GO; GO:0050828; P:regulation of liquid surface tension; IDA:RGD.
GO; GO:0007585; P:respiratory gaseous exchange; IEA:UniProtKB-KW.
GO; GO:0031960; P:response to corticosteroid; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0070848; P:response to growth factor; IEP:RGD.
GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
GO; GO:0043129; P:surfactant homeostasis; IMP:RGD.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR008160; Collagen.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR015097; Surfac_D-trimer.
Pfam; PF01391; Collagen; 2.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF09006; Surfac_D-trimer; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
Calcium; Coiled coil; Collagen; Complete proteome;
Direct protein sequencing; Disulfide bond; Extracellular matrix;
Gaseous exchange; Glycoprotein; Hydroxylation; Immunity;
Innate immunity; Lectin; Phosphoprotein; Reference proteome; Repeat;
S-nitrosylation; Secreted; Signal; Surface film.
SIGNAL 1 19 {ECO:0000269|PubMed:1370483}.
CHAIN 20 374 Pulmonary surfactant-associated protein
D.
/FTId=PRO_0000017467.
DOMAIN 45 221 Collagen-like.
DOMAIN 259 374 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
COILED 222 253 {ECO:0000255}.
MOD_RES 34 34 S-nitrosocysteine.
{ECO:0000269|PubMed:19007302}.
MOD_RES 39 39 S-nitrosocysteine.
{ECO:0000269|PubMed:19007302}.
MOD_RES 77 77 Hydroxyproline.
{ECO:0000269|PubMed:2675969}.
MOD_RES 86 86 5-hydroxylysine.
{ECO:0000269|PubMed:2675969}.
MOD_RES 95 95 Hydroxyproline.
{ECO:0000269|PubMed:2675969}.
MOD_RES 98 98 5-hydroxylysine.
{ECO:0000269|PubMed:2675969}.
MOD_RES 109 109 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 170 170 Hydroxyproline.
{ECO:0000269|PubMed:2675969}.
MOD_RES 176 176 Hydroxyproline.
{ECO:0000269|PubMed:2675969}.
CARBOHYD 89 89 N-linked (GlcNAc...) asparagine.
DISULFID 280 372 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 350 364 {ECO:0000255|PROSITE-ProRule:PRU00040}.
CONFLICT 89 89 N -> E (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 164 164 K -> C (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 374 AA; 37561 MW; DB2BB5E399DB4A3C CRC64;
MLHFLSMLVL LVQPLGDLGA EMKTLSQRSI TNTCTLVLCS PTENGLPGRD GRDGREGPRG
EKGDPGLPGP MGLSGLPGPR GPVGPKGENG SAGEPGPKGE RGLVGPPGSP GISGPAGKEG
PSGKQGNIGP QGKPGPKGEA GPKGEVGAPG MQGSAGAKGP AGPKGERGAP GEQGAPGNAG
AAGPAGPAGP QGAPGSRGPP GLKGDRGAPG DRGIKGESGL PDSAALRQQM EALNGKLQRL
EAAFSRYKKA ALFPDGQSVG DKIFRAANSE EPFEDAKEMC RQAGGQLASP RSATENAAVQ
QLVTAHSKAA FLSMTDVGTE GKFTYPTGEA LVYSNWAPGE PNNNGGAENC VEIFTNGQWN
DKACGEQRLV ICEF


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