SFTPD_MACMU
ID SFTPD_MACMU Reviewed; 375 AA.
AC Q1PBC5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=16988005; DOI=10.1128/cvi.00198-06;
RA Stone G.W., Barzee S., Snarsky V., Spina C.A., Lifson J.D., Pillai V.K.,
RA Amara R.R., Villinger F., Kornbluth R.S.;
RT "Macaque multimeric soluble CD40 ligand and GITR ligand constructs are
RT immunostimulatory molecules in vitro.";
RL Clin. Vaccine Immunol. 13:1223-1230(2006).
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}.
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; DQ457096; ABE68875.1; -; mRNA.
DR RefSeq; NP_001035283.1; NM_001040193.1.
DR RefSeq; XP_015002617.1; XM_015147131.1.
DR AlphaFoldDB; Q1PBC5; -.
DR SMR; Q1PBC5; -.
DR STRING; 9544.ENSMMUP00000003737; -.
DR Ensembl; ENSMMUT00000003955; ENSMMUP00000003737; ENSMMUG00000002787.
DR GeneID; 678657; -.
DR KEGG; mcc:678657; -.
DR CTD; 6441; -.
DR VEuPathDB; HostDB:ENSMMUG00000002787; -.
DR VGNC; VGNC:77190; SFTPD.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155748; -.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; Q1PBC5; -.
DR OMA; EMFTNGK; -.
DR OrthoDB; 1341167at2759; -.
DR TreeFam; TF330481; -.
DR Proteomes; UP000006718; Chromosome 9.
DR Bgee; ENSMMUG00000002787; Expressed in lung and 2 other tissues.
DR ExpressionAtlas; Q1PBC5; 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:0005791; C:rough endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0043152; P:induction of bacterial agglutination; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR GO; GO:0052403; P:negative regulation by host of symbiont catalytic activity; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central.
DR GO; GO:1905226; P:regulation of adhesion of symbiont to host epithelial cell; IEA:Ensembl.
DR GO; GO:0002682; P:regulation of immune system process; IEA:UniProt.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW.
DR GO; GO:0043129; P:surfactant homeostasis; IBA:GO_Central.
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; 3.
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 2: Evidence at transcript 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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..375
FT /note="Pulmonary surfactant-associated protein D"
FT /id="PRO_0000269560"
FT DOMAIN 46..222
FT /note="Collagen-like"
FT DOMAIN 260..374
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..251
FT /evidence="ECO:0000255"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..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 DISULFID 281..373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 351..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 375 AA; 37677 MW; CFBC515EFEEED9BD CRC64;
MLLFLLSALV LLTQSLGYLE ADMKTYSQRT APSACTLVMC SSVESGLPGR DGRDGREGPR
GEKGDPGLPG AAGKAGMPGE AGPVGPKGDN GSIGEPGPKG DTGPSGPPGP PGVPGPAGRE
GPLGKQGNIG PQGKPGPKGE AGPKGEVGAP GMQGSAGARG PAGPKGDRGV PGERGAPGNA
GAAGSAGVMG PQGSPGARGP PGLKGDKGVP GDKGAKGESG LPDVASLRQQ VEALQKQVQH
LQAAFSQYKK VELFPNGQSV GEKIFKTAGF VKPFTEAQLV CTQAGGQLAS PRSAAENAAL
QQLVIAQNEA AFLSMTDSKM EGKFTYPTGE SLVYSNWAPG EPNDDGGSED CVEIFTNGKW
NDRACGEKRL VVCEF
