SFTPD_PIG
ID SFTPD_PIG Reviewed; 378 AA.
AC Q9N1X4;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
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;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10640760; DOI=10.4049/jimmunol.164.3.1442;
RA van Eijk M., Haagsman H.P., Skinner T., Archibald A.L., Reid K.B.M.,
RA Lawson P.R.;
RT "Porcine lung surfactant protein D: complementary DNA cloning, chromosomal
RT localization, and tissue distribution.";
RL J. Immunol. 164:1442-1450(2000).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Oligomeric complex of 4 set of homotrimers. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Secreted, extracellular space, surface film
CC {ECO:0000250}.
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; AF132496; AAF22145.2; -; mRNA.
DR RefSeq; NP_999275.1; NM_214110.1.
DR RefSeq; XP_013838830.1; XM_013983376.1.
DR PDB; 4DN8; X-ray; 2.20 A; A=223-378.
DR PDB; 6BBD; X-ray; 1.90 A; A=225-378.
DR PDB; 6BBE; X-ray; 1.90 A; A=223-378.
DR PDBsum; 4DN8; -.
DR PDBsum; 6BBD; -.
DR PDBsum; 6BBE; -.
DR AlphaFoldDB; Q9N1X4; -.
DR SMR; Q9N1X4; -.
DR STRING; 9823.ENSSSCP00000011020; -.
DR UniLectin; Q9N1X4; -.
DR PaxDb; Q9N1X4; -.
DR PeptideAtlas; Q9N1X4; -.
DR PRIDE; Q9N1X4; -.
DR Ensembl; ENSSSCT00005050684; ENSSSCP00005031332; ENSSSCG00005031583.
DR Ensembl; ENSSSCT00030028687; ENSSSCP00030012809; ENSSSCG00030020739.
DR Ensembl; ENSSSCT00040049871; ENSSSCP00040020708; ENSSSCG00040037098.
DR Ensembl; ENSSSCT00050068407; ENSSSCP00050029347; ENSSSCG00050050252.
DR Ensembl; ENSSSCT00065023689; ENSSSCP00065009643; ENSSSCG00065017815.
DR Ensembl; ENSSSCT00070002361; ENSSSCP00070001974; ENSSSCG00070001221.
DR GeneID; 397198; -.
DR KEGG; ssc:397198; -.
DR CTD; 6441; -.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; Q9N1X4; -.
DR OMA; EMFTNGK; -.
DR TreeFam; TF330481; -.
DR Reactome; R-SSC-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-SSC-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-SSC-391160; Signal regulatory protein family interactions.
DR Reactome; R-SSC-5683826; Surfactant metabolism.
DR Reactome; R-SSC-5686938; Regulation of TLR by endogenous ligand.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 14.
DR Genevisible; Q9N1X4; SS.
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; 1.
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 3D-structure; Calcium; Coiled coil; Collagen; 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:0000255"
FT CHAIN 21..378
FT /note="Pulmonary surfactant-associated protein D"
FT /id="PRO_5000056060"
FT DOMAIN 46..222
FT /note="Collagen-like"
FT DOMAIN 260..378
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 43..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..254
FT /evidence="ECO:0000255"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
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 171
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 177
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 323
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 281..376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 354..368
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT HELIX 226..253
FT /evidence="ECO:0007829|PDB:6BBD"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:6BBD"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:6BBD"
FT STRAND 263..272
FT /evidence="ECO:0007829|PDB:6BBD"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:6BBD"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:6BBD"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:6BBD"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:4DN8"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6BBD"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:6BBD"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:6BBD"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:6BBD"
FT STRAND 372..378
FT /evidence="ECO:0007829|PDB:6BBD"
SQ SEQUENCE 378 AA; 37986 MW; 3504E8C1E56C341D CRC64;
MLLLPLSVLI LLTQPPRSLG AEMKTYSQRA VANACALVMC SPMENGLPGR DGRDGREGPR
GEKGDPGLPG AVGRAGMPGL AGPVGPKGDN GSTGEPGAKG DIGPCGPPGP PGIPGPAGKE
GPSGQQGNIG PPGTPGPKGE TGPKGEVGAL GMQGSTGARG PAGLKGERGA PGERGAPGSA
GAAGPAGATG PQGPSGARGP PGLKGDRGPP GERGAKGESG LPGITALRQQ VETLQGQVQR
LQKAFSQYKK VELFPNGRGV GEKIFKTGGF EKTFQDAQQV CTQAGGQMAS PRSETENEAL
SQLVTAQNKA AFLSMTDIKT EGNFTYPTGE PLVYANWAPG EPNNNGGSSG AENCVEIFPN
GKWNDKACGE LRLVICEF
