SFTPD_BOVIN
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 03-AUG-2022, entry version 156.
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}.
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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 PaxDb; P35246; -.
DR Ensembl; ENSBTAT00000008579; ENSBTAP00000008579; ENSBTAG00000046421.
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; 1341167at2759; -.
DR TreeFam; TF330481; -.
DR Reactome; R-BTA-391160; Signal regulatory protein family interactions.
DR Reactome; R-BTA-5683826; Surfactant metabolism.
DR Proteomes; UP000009136; Chromosome 28.
DR Bgee; ENSBTAG00000046421; Expressed in lung and 35 other tissues.
DR ExpressionAtlas; P35246; baseline and differential.
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:0005791; C:rough endoplasmic reticulum; 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: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; -; 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; 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
