SFTPD_MOUSE
ID SFTPD_MOUSE Reviewed; 374 AA.
AC P50404;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Pulmonary surfactant-associated protein D;
DE Short=PSP-D;
DE Short=SP-D;
DE AltName: Full=Lung surfactant protein D;
DE Flags: Precursor;
GN Name=Sftpd; Synonyms=Sftp4;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RX PubMed=7499852;
RA Motwani M., White R.A., Guo N., Dowler L.L., Tauber A.I., Sastry K.N.;
RT "Mouse surfactant protein-D. cDNA cloning, characterization, and gene
RT localization to chromosome 14.";
RL J. Immunol. 155:5671-5677(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10226065; DOI=10.1165/ajrcmb.20.5.3343;
RA Lawson P.R., Perkins V.C., Holmskov U., Reid K.B.;
RT "Genomic organization of the mouse gene for lung surfactant protein D.";
RL Am. J. Respir. Cell Mol. Biol. 20:953-963(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RA Fisher J.H., Sheftelyevich V.V.;
RT "Surfactant protein-D regulates surfactant phospholipid homeostasis in
RT vivo.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 P50404; P50404: Sftpd; NbExp=2; IntAct=EBI-8402361, EBI-8402361;
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:0000250}.
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}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Pulmonary surfactant protein SP-D;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_170";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L40156; AAA92021.1; -; mRNA.
DR EMBL; AF047742; AAD31380.1; -; Genomic_DNA.
DR EMBL; AF047741; AAD31380.1; JOINED; Genomic_DNA.
DR EMBL; AF192134; AAF15277.1; -; Genomic_DNA.
DR EMBL; BC003705; AAH03705.1; -; mRNA.
DR CCDS; CCDS26962.1; -.
DR RefSeq; NP_033186.1; NM_009160.2.
DR AlphaFoldDB; P50404; -.
DR SMR; P50404; -.
DR BioGRID; 203194; 2.
DR DIP; DIP-46338N; -.
DR IntAct; P50404; 1.
DR STRING; 10090.ENSMUSP00000076383; -.
DR GlyGen; P50404; 1 site.
DR PhosphoSitePlus; P50404; -.
DR CPTAC; non-CPTAC-4006; -.
DR MaxQB; P50404; -.
DR PaxDb; P50404; -.
DR PeptideAtlas; P50404; -.
DR PRIDE; P50404; -.
DR ProteomicsDB; 261200; -.
DR Antibodypedia; 3886; 548 antibodies from 38 providers.
DR DNASU; 20390; -.
DR Ensembl; ENSMUST00000077136; ENSMUSP00000076383; ENSMUSG00000021795.
DR GeneID; 20390; -.
DR KEGG; mmu:20390; -.
DR UCSC; uc007tcr.2; mouse.
DR CTD; 6441; -.
DR MGI; MGI:109515; Sftpd.
DR VEuPathDB; HostDB:ENSMUSG00000021795; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155748; -.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; P50404; -.
DR OMA; EMFTNGK; -.
DR OrthoDB; 1341167at2759; -.
DR PhylomeDB; P50404; -.
DR TreeFam; TF330481; -.
DR Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-391160; Signal regulatory protein family interactions.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR BioGRID-ORCS; 20390; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Sftpd; mouse.
DR PRO; PR:P50404; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P50404; protein.
DR Bgee; ENSMUSG00000021795; Expressed in right lung and 44 other tissues.
DR Genevisible; P50404; MM.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0001530; F:lipopolysaccharide binding; ISO:MGI.
DR GO; GO:0048029; F:monosaccharide binding; ISO:MGI.
DR GO; GO:0043152; P:induction of bacterial agglutination; ISO:MGI.
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:MGI.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; ISO:MGI.
DR GO; GO:0050765; P:negative regulation of phagocytosis; ISO:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0008228; P:opsonization; ISO:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR GO; GO:1905226; P:regulation of adhesion of symbiont to host epithelial cell; ISO:MGI.
DR GO; GO:0050828; P:regulation of liquid surface tension; ISO:MGI.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW.
DR GO; GO:0043129; P:surfactant homeostasis; ISS:UniProtKB.
DR CDD; cd03591; CLECT_collectin_like; 1.
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; IPR033990; Collectin_CTLD.
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; Disulfide bond; Extracellular matrix;
KW Gaseous exchange; Glycoprotein; Hydroxylation; Immunity; Innate immunity;
KW Lectin; Reference proteome; Repeat; S-nitrosylation; Secreted; Signal;
KW Surface film.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..374
FT /note="Pulmonary surfactant-associated protein D"
FT /id="PRO_0000017466"
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 38..222
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:0000250|UniProtKB:P35248"
FT MOD_RES 39
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P35248"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 280..372
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 350..364
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 374 AA; 37688 MW; FE034261263F43E4 CRC64;
MLPFLSMLVL LVQPLGNLGA EMKSLSQRSV PNTCTLVMCS PTENGLPGRD GRDGREGPRG
EKGDPGLPGP MGLSGLQGPT GPVGPKGENG SAGEPGPKGE RGLSGPPGLP GIPGPAGKEG
PSGKQGNIGP QGKPGPKGEA GPKGEVGAPG MQGSTGAKGS TGPKGERGAP GVQGAPGNAG
AAGPAGPAGP QGAPGSRGPP GLKGDRGVPG DRGIKGESGL PDSAALRQQM EALKGKLQRL
EVAFSHYQKA ALFPDGRSVG DKIFRTADSE KPFEDAQEMC KQAGGQLASP RSATENAAIQ
QLITAHNKAA FLSMTDVGTE GKFTYPTGEP LVYSNWAPGE PNNNGGAENC VEIFTNGQWN
DKACGEQRLV ICEF
