ID SFTPD_BOVIN Reviewed; 369 AA. AC P35246; Q863A1; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 27-JUN-2006, sequence version 2. DT 27-MAR-2024, entry version 163. 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 Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 208-247. RC TISSUE=Lung; RX PubMed=8436402; RA Lim B.L., Lu J., Reid K.B.M.; RT "Structural similarity between bovine conglutinin and bovine lung RT surfactant protein D and demonstration of liver as a site of synthesis of RT conglutinin."; RL Immunology 78:159-165(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Gjerstorff M., Hansen S., Madsen J., Bendixen C., Holmskov U.; RT "Bovine surfactant protein D: genomic characterization, chromosomal RT localization and expression analysis."; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. 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 -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular CC matrix. Secreted, extracellular space, surface film. CC -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG, CC is most likely to be 4-hydroxy as this fits the requirement for 4- CC hydroxylation in vertebrates. {ECO:0000250}. CC -!- PTM: S-nitrosylation at Cys-35 and Cys-40 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 --------------------------------------------------------------------------- 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; X75911; CAA53510.1; -; mRNA. DR EMBL; AJ548848; CAD69922.1; -; Genomic_DNA. DR EMBL; AJ548849; CAD69922.1; JOINED; Genomic_DNA. DR EMBL; AJ548850; CAD69922.1; JOINED; Genomic_DNA. DR PIR; S33603; S33603. DR RefSeq; NP_851369.1; NM_181026.2. DR AlphaFoldDB; P35246; -. DR SMR; P35246; -. DR BioGRID; 159354; 2. DR STRING; 9913.ENSBTAP00000008579; -. DR GlyCosmos; P35246; 1 site, No reported glycans. DR PaxDb; 9913-ENSBTAP00000008579; -. DR Ensembl; ENSBTAT00000008579.6; ENSBTAP00000008579.5; ENSBTAG00000046421.2. DR GeneID; 282072; -. DR KEGG; bta:282072; -. DR CTD; 6441; -. DR VEuPathDB; HostDB:ENSBTAG00000046421; -. DR eggNOG; KOG4297; Eukaryota. DR GeneTree; ENSGT00940000155748; -. DR HOGENOM; CLU_049894_3_0_1; -. DR InParanoid; P35246; -. DR OMA; EMFTNGK; -. DR OrthoDB; 4641030at2759; -. DR TreeFam; TF330481; -. DR Reactome; R-BTA-166016; Toll Like Receptor 4 (TLR4) Cascade. DR Reactome; R-BTA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell. DR Reactome; R-BTA-391160; Signal regulatory protein family interactions. DR Reactome; R-BTA-5683826; Surfactant metabolism. DR Reactome; R-BTA-5686938; Regulation of TLR by endogenous ligand. DR Proteomes; UP000009136; Chromosome 28. DR Bgee; ENSBTAG00000046421; Expressed in lung and 35 other cell types or tissues. DR ExpressionAtlas; P35246; baseline. DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0048286; P:lung alveolus development; ISS:UniProtKB. DR GO; GO:0050778; P:positive regulation of immune response; IEA:UniProt. DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central. DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW. DR GO; GO:0043129; P:surfactant homeostasis; ISS:UniProtKB. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1. DR Gene3D; 1.20.5.360; SFTPD helical domain; 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 PANTHER; PTHR24023; COLLAGEN ALPHA; 1. DR PANTHER; PTHR24023:SF958; ZGC:113232; 1. 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; C-type lectin-like; 1. DR SUPFAM; SSF57944; Triple coiled coil domain of C-type lectins; 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; Reference proteome; Repeat; KW S-nitrosylation; Secreted; Signal; Surface film. FT SIGNAL 1..20 FT /evidence="ECO:0000250" FT CHAIN 21..369 FT /note="Pulmonary surfactant-associated protein D" FT /id="PRO_0000017464" FT DOMAIN 46..216 FT /note="Collagen-like" FT DOMAIN 254..369 FT /note="C-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT REGION 41..215 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 217..248 FT /evidence="ECO:0000255" FT COMPBIAS 47..63 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 100..114 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 35 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:P35248" FT MOD_RES 40 FT /note="S-nitrosocysteine" FT /evidence="ECO:0000250|UniProtKB:P35248" FT MOD_RES 78 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 87 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250" FT MOD_RES 96 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 99 FT /note="5-hydroxylysine" FT /evidence="ECO:0000250" FT MOD_RES 165 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 171 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT CARBOHYD 90 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 275..367 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DISULFID 345..359 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT CONFLICT 262 FT /note="E -> V (in Ref. 1; CAA53510)" FT /evidence="ECO:0000305" FT CONFLICT 288 FT /note="A -> G (in Ref. 1; CAA53510)" FT /evidence="ECO:0000305" SQ SEQUENCE 369 AA; 37405 MW; 4A74B7593508AE5D CRC64; MLLLPLSVLL LLTQPWRSLG AEMKIYSQKT MANACTLVMC SPPEDGLPGR DGRDGREGPR GEKGDPGSPG PAGRAGMPGP AGPIGLKGDN GSAGEPGPKG DTGPPGPPGM PGPAGREGPS GKQGSMGPPG TPGPKGDTGP KGGVGAPGIQ GSPGPAGLKG ERGAPGEPGA PGRAGAPGPA GAIGPQGPSG ARGPPGLKGD RGTPGERGAK GESGLAEVNA LRQRVGILEG QLQRLQNAFS QYKKAMLFPN GRSVGEKIFK TEGSEKTFQD AQQICTQAGG QLPSPRSAAE NEALTQLATA QNKAAFLSMS DTRKEGTFIY PTGEPLVYSN WAPQEPNNDG GSENCVEIFP NGKWNDKVCG EQRLVICEF //