SFTPD_RAT
ID SFTPD_RAT Reviewed; 374 AA.
AC P35248;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Pulmonary surfactant-associated protein D;
DE Short=PSP-D;
DE Short=SP-D;
DE AltName: Full=CP4;
DE AltName: Full=Lung surfactant protein D;
DE Flags: Precursor;
GN Name=Sftpd; Synonyms=Sftp4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 20-33.
RC TISSUE=Lung;
RX PubMed=1370483; DOI=10.1016/s0021-9258(18)46025-5;
RA Shimizu H., Fisher J.H., Papst P., Benson B., Lau K., Mason R.J.,
RA Voelker D.R.;
RT "Primary structure of rat pulmonary surfactant protein D. cDNA and deduced
RT amino acid sequence.";
RL J. Biol. Chem. 267:1853-1857(1992).
RN [2]
RP PROTEIN SEQUENCE OF 73-95 AND 153-180, AND HYDROXYLATION AT PRO-77; LYS-86;
RP PRO-95; LYS-98; PRO-170 AND PRO-176.
RC TISSUE=Lung;
RX PubMed=2675969; DOI=10.1021/bi00441a031;
RA Persson A., Chang D., Rust K., Moxley M., Longmore W., Crouch E.;
RT "Purification and biochemical characterization of CP4 (SP-D), a collagenous
RT surfactant-associated protein.";
RL Biochemistry 28:6361-6367(1989).
RN [3]
RP S-NITROSYLATION AT CYS-34 AND CYS-39.
RX PubMed=19007302; DOI=10.1371/journal.pbio.0060266;
RA Guo C.J., Atochina-Vasserman E.N., Abramova E., Foley J.P., Zaman A.,
RA Crouch E., Beers M.F., Savani R.C., Gow A.J.;
RT "S-nitrosylation of surfactant protein-D controls inflammatory function.";
RL PLoS Biol. 6:E266-E266(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Contributes to the lung's defense against inhaled
CC microorganisms, organic antigens and toxins. Interacts with compounds
CC such as bacterial lipopolysaccharides, oligosaccharides and fatty acids
CC and modulates leukocyte action in immune response. May participate in
CC the extracellular reorganization or turnover of pulmonary surfactant.
CC Binds strongly maltose residues and to a lesser extent other alpha-
CC glucosyl moieties.
CC -!- SUBUNIT: Oligomeric complex of 4 set of homotrimers.
CC -!- INTERACTION:
CC P35248; P35248: Sftpd; NbExp=3; IntAct=EBI-11328301, EBI-11328301;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix. Secreted, extracellular space, surface film.
CC -!- PTM: S-nitrosylation at Cys-34 and Cys-39 alters the quaternary
CC structure which results in a pro-inflammatory chemoattractive signaling
CC activity with macrophages. {ECO:0000269|PubMed:19007302}.
CC -!- MISCELLANEOUS: Pulmonary surfactant consists of 90% lipid and 10%
CC protein. There are 4 surfactant-associated proteins: 2 collagenous,
CC carbohydrate-binding glycoproteins (SP-A and SP-D) and 2 small
CC hydrophobic proteins (SP-B and SP-C).
CC -!- SIMILARITY: Belongs to the SFTPD family. {ECO:0000305}.
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DR EMBL; M81231; AAA42170.1; -; mRNA.
DR PIR; A42046; A42046.
DR RefSeq; NP_037010.1; NM_012878.2.
DR AlphaFoldDB; P35248; -.
DR SMR; P35248; -.
DR BioGRID; 247389; 1.
DR DIP; DIP-46337N; -.
DR IntAct; P35248; 1.
DR STRING; 10116.ENSRNOP00000066829; -.
DR GlyGen; P35248; 1 site.
DR iPTMnet; P35248; -.
DR PhosphoSitePlus; P35248; -.
DR Ensembl; ENSRNOT00000084172; ENSRNOP00000074951; ENSRNOG00000056001.
DR GeneID; 25350; -.
DR KEGG; rno:25350; -.
DR CTD; 6441; -.
DR RGD; 3667; Sftpd.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155748; -.
DR InParanoid; P35248; -.
DR OrthoDB; 1341167at2759; -.
DR PhylomeDB; P35248; -.
DR Reactome; R-RNO-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-RNO-391160; Signal regulatory protein family interactions.
DR Reactome; R-RNO-5683826; Surfactant metabolism.
DR Reactome; R-RNO-5686938; Regulation of TLR by endogenous ligand.
DR PRO; PR:P35248; -.
DR Proteomes; UP000002494; Chromosome 16.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005771; C:multivesicular body; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IDA:RGD.
DR GO; GO:0001530; F:lipopolysaccharide binding; IDA:RGD.
DR GO; GO:0048029; F:monosaccharide binding; IDA:RGD.
DR GO; GO:0043152; P:induction of bacterial agglutination; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048286; P:lung alveolus development; ISS:UniProtKB.
DR GO; GO:0052403; P:negative regulation by host of symbiont catalytic activity; ISO:RGD.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:RGD.
DR GO; GO:0050765; P:negative regulation of phagocytosis; IDA:RGD.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:RGD.
DR GO; GO:0008228; P:opsonization; IDA:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:RGD.
DR GO; GO:1905226; P:regulation of adhesion of symbiont to host epithelial cell; ISO:RGD.
DR GO; GO:0050828; P:regulation of liquid surface tension; IDA:RGD.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW.
DR GO; GO:0031960; P:response to corticosteroid; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0070848; P:response to growth factor; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0043129; P:surfactant homeostasis; IMP:RGD.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR015097; Surfac_D-trimer.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF09006; Surfac_D-trimer; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Coiled coil; Collagen; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Gaseous exchange; Glycoprotein; Hydroxylation;
KW Immunity; Innate immunity; Lectin; Phosphoprotein; Reference proteome;
KW Repeat; S-nitrosylation; Secreted; Signal; Surface film.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:1370483"
FT CHAIN 20..374
FT /note="Pulmonary surfactant-associated protein D"
FT /id="PRO_0000017467"
FT DOMAIN 45..221
FT /note="Collagen-like"
FT DOMAIN 259..374
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 40..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 222..253
FT /evidence="ECO:0000255"
FT COMPBIAS 48..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:19007302"
FT MOD_RES 39
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000269|PubMed:19007302"
FT MOD_RES 77
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2675969"
FT MOD_RES 86
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2675969"
FT MOD_RES 95
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2675969"
FT MOD_RES 98
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000269|PubMed:2675969"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 170
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2675969"
FT MOD_RES 176
FT /note="Hydroxyproline"
FT /evidence="ECO:0000269|PubMed:2675969"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 280..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 350..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT CONFLICT 89
FT /note="N -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="K -> C (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
