ID SFTPD_HUMAN Reviewed; 375 AA. AC P35247; Q5T0M3; Q6FH08; Q86YK9; Q8TCD8; Q9UCJ2; Q9UCJ3; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 2. DT 10-JUN-2008, entry version 99. DE Pulmonary surfactant-associated protein D precursor (SP-D) (PSP-D) DE (Lung surfactant protein D). GN Name=SFTPD; Synonyms=PSPD, SFTP4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 214-243, AND VARIANT RP THR-31. RC TISSUE=Amniotic fluid, and Lung; RX MEDLINE=92322003; PubMed=1339284; RA Lu J., Willis A.C., Reid K.B.M.; RT "Purification, characterization and cDNA cloning of human lung RT surfactant protein D."; RL Biochem. J. 284:795-802(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT THR-180. RC TISSUE=Placenta; RX MEDLINE=93155122; PubMed=8428971; RA Crouch E., Rust K., Veile R., Donis-Keller H., Grosso L.; RT "Genomic organization of human surfactant protein D (SP-D). SP-D is RT encoded on chromosome 10q22.2-23.1."; RL J. Biol. Chem. 268:2976-2983(1993). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-31. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., RA Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., RA Korn B., Zuo D., Hu Y., LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-31; VAL-123; RP THR-180; THR-290 AND LYS-309. RG SeattleSNPs program for genomic applications; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-180. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-180. RC TISSUE=Lung; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 46-72 AND 223-260. RX PubMed=8424457; RA Crouch E., Persson A., Chang D.; RT "Accumulation of surfactant protein D in human pulmonary alveolar RT proteinosis."; RL Am. J. Pathol. 142:241-248(1993). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-375, AND PARTIAL PROTEIN RP SEQUENCE. RC TISSUE=Lung; RX MEDLINE=91378578; PubMed=1898081; DOI=10.1016/0003-9861(91)90597-C; RA Rust K., Grosso L., Zhang V., Chang D., Persson A., Longmore W., RA Cai G.-Z., Crouch E.; RT "Human surfactant protein D: SP-D contains a C-type lectin RT carbohydrate recognition domain."; RL Arch. Biochem. Biophys. 290:116-126(1991). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX MEDLINE=99197291; PubMed=10368295; DOI=10.1016/S0969-2126(99)80036-7; RA Hakansson K., Lim N.K., Hoppe H.-J., Reid K.B.M.; RT "Crystal structure of the trimeric alpha-helical coiled-coil and the RT three lectin domains of human lung surfactant protein D."; RL Structure 7:255-264(1999). CC -!- FUNCTION: Contributes to the lung's defense against inhaled CC microorganisms. May participate in the extracellular CC reorganization or turnover of pulmonary surfactant. Binds strongly CC maltose residues and to a lesser extent other alpha-glucosyl CC 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: The N-terminus is blocked. CC -!- PTM: Hydroxylation on proline residues within the sequence motif, CC GXPG, is most likely to be 4-hydroxy as this fits the requirement CC for 4-hydroxylation in vertebrates (By similarity). CC -!- MISCELLANEOUS: Pulmonary surfactant consists of 90% lipid and 10% CC protein. There are 4 surfactant-associated proteins: 2 CC collagenous, carbohydrate-binding glycoproteins (SP-A and SP-D) CC and 2 small hydrophobic proteins (SP-B and SP-C). CC -!- SIMILARITY: Belongs to the SFTPD family. CC -!- SIMILARITY: Contains 1 C-type lectin domain. CC -!- SIMILARITY: Contains 1 collagen-like domain. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/sftpd/"; 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; X65018; CAA46152.1; -; mRNA. DR EMBL; L05485; AAB59450.1; -; Genomic_DNA. DR EMBL; L05483; AAB59450.1; JOINED; Genomic_DNA. DR EMBL; L05484; AAB59450.1; JOINED; Genomic_DNA. DR EMBL; CR541948; CAG46746.1; -; mRNA. DR EMBL; AY216721; AAO22991.1; -; Genomic_DNA. DR EMBL; AL512662; CAI14436.1; -; Genomic_DNA. DR EMBL; BC022318; AAH22318.1; -; mRNA. DR PIR; A45225; A45225. DR RefSeq; NP_003010.4; -. DR UniGene; Hs.253495; -. DR PDB; 1B08; X-ray; 2.30 A; A/B/C=224-375. DR PDB; 1M7L; NMR; -; A/B/C=220-257. DR PDB; 1PW9; X-ray; 1.60 A; A/B/C=199-375. DR PDB; 1PWB; X-ray; 1.40 A; A/B/C=199-375. DR PDB; 2GGU; X-ray; 1.90 A; A/B/C=223-375. DR PDB; 2GGX; X-ray; 1.90 A; A/B/C=223-375. DR PDB; 2ORJ; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 2ORK; X-ray; 1.89 A; A/B/C=223-375. DR PDB; 2OS9; X-ray; 1.70 A; A/B/C=223-375. DR PDB; 2RIA; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 2RIB; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 2RIC; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 2RID; X-ray; 1.80 A; A/B/C=223-375. DR PDB; 2RIE; X-ray; 1.60 A; A/B/C=223-375. DR PDBsum; 1B08; -. DR PDBsum; 1M7L; -. DR PDBsum; 1PW9; -. DR PDBsum; 1PWB; -. DR PDBsum; 2GGU; -. DR PDBsum; 2GGX; -. DR PDBsum; 2ORJ; -. DR PDBsum; 2ORK; -. DR PDBsum; 2OS9; -. DR PDBsum; 2RIA; -. DR PDBsum; 2RIB; -. DR PDBsum; 2RIC; -. DR PDBsum; 2RID; -. DR PDBsum; 2RIE; -. DR Ensembl; ENSG00000133661; Homo sapiens. DR GeneID; 6441; -. DR KEGG; hsa:6441; -. DR HGNC; HGNC:10803; SFTPD. DR HPA; CAB004578; -. DR MIM; 178635; gene. DR PharmGKB; PA35715; -. DR HOVERGEN; P35247; -. DR ArrayExpress; P35247; -. DR CleanEx; HS_SFTPD; -. DR GermOnline; ENSG00000133661; Homo sapiens. DR GO; GO:0030139; C:endocytic vesicle; TAS:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB. DR GO; GO:0005764; C:lysosome; TAS:UniProtKB. DR GO; GO:0008367; F:bacterial binding; TAS:UniProtKB. DR GO; GO:0005529; F:sugar binding; TAS:UniProtKB. DR GO; GO:0048286; P:alveolus development; IMP:UniProtKB. DR GO; GO:0045087; P:innate immune response; TAS:UniProtKB. DR GO; GO:0048246; P:macrophage chemotaxis; TAS:UniProtKB. DR GO; GO:0045085; P:negative regulation of interleukin-2 biosyn...; TAS:UniProtKB. DR GO; GO:0042130; P:negative regulation of T cell proliferation; TAS:UniProtKB. DR GO; GO:0006800; P:oxygen and reactive oxygen species metaboli...; TAS:UniProtKB. DR GO; GO:0050766; P:positive regulation of phagocytosis; TAS:UniProtKB. DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:UniProtKB. DR GO; GO:0001817; P:regulation of cytokine production; NAS:UniProtKB. DR GO; GO:0043129; P:surfactant homeostasis; IMP:UniProtKB. DR InterPro; IPR001304; C-type_lectin. DR InterPro; IPR016186; C-type_lectin-like. DR InterPro; IPR008161; Clg_helix. DR InterPro; IPR008160; Collagen. DR InterPro; IPR015097; Surfac_D-trimer. DR Gene3D; G3DSA:3.10.100.10; C-type_lectin-like; 1. DR Pfam; PF01391; Collagen; 4. DR Pfam; PF00059; Lectin_C; 1. DR Pfam; PF09006; Surfac_D-trimer; 1. DR ProDom; PD000007; Clg_helix; 1. DR SMART; SM00034; CLECT; 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; KW Direct protein sequencing; Extracellular matrix; Gaseous exchange; KW Glycoprotein; Hydroxylation; Lectin; Polymorphism; Repeat; Secreted; KW Signal; Surface film. FT SIGNAL 1 20 By similarity. FT CHAIN 21 375 Pulmonary surfactant-associated protein FT D. FT /FTId=PRO_0000017465. FT DOMAIN 46 222 Collagen-like. FT DOMAIN 260 375 C-type lectin. FT COILED 223 252 Potential. FT MOD_RES 78 78 4-hydroxyproline (By similarity). FT MOD_RES 87 87 5-hydroxylysine (By similarity). FT MOD_RES 96 96 4-hydroxyproline (By similarity). FT MOD_RES 99 99 5-hydroxylysine (By similarity). FT MOD_RES 171 171 4-hydroxyproline (By similarity). FT MOD_RES 177 177 4-hydroxyproline (By similarity). FT CARBOHYD 90 90 N-linked (GlcNAc...) (Potential). FT DISULFID 281 373 FT DISULFID 351 365 FT VARIANT 31 31 M -> T. FT /FTId=VAR_020937. FT VARIANT 123 123 L -> V. FT /FTId=VAR_020938. FT VARIANT 180 180 A -> T (in dbSNP:rs2243639). FT /FTId=VAR_020939. FT VARIANT 290 290 S -> T. FT /FTId=VAR_020940. FT VARIANT 309 309 E -> K. FT /FTId=VAR_020941. FT CONFLICT 22 22 E -> G (in Ref. 6; AAH22318). FT CONFLICT 59 59 P -> F (in Ref. 7; AA sequence). FT CONFLICT 122 122 P -> A (in Ref. 2; AAB59450). FT CONFLICT 240 240 H -> P (in Ref. 7; AA sequence). FT CONFLICT 341 341 E -> K (in Ref. 6; AAH22318). FT CONFLICT 369 369 R -> S (in Ref. 3; CAG46746). FT HELIX 226 253 FT TURN 254 256 FT STRAND 257 260 FT STRAND 263 273 FT HELIX 274 283 FT STRAND 286 288 FT HELIX 294 307 FT STRAND 318 320 FT HELIX 345 347 FT STRAND 351 354 FT STRAND 360 363 SQ SEQUENCE 375 AA; 37698 MW; 79380764F2B86E67 CRC64; MLLFLLSALV LLTQPLGYLE AEMKTYSHRT MPSACTLVMC SSVESGLPGR DGRDGREGPR GEKGDPGLPG AAGQAGMPGQ AGPVGPKGDN GSVGEPGPKG DTGPSGPPGP PGVPGPAGRE GPLGKQGNIG PQGKPGPKGE AGPKGEVGAP GMQGSAGARG LAGPKGERGV PGERGVPGNA GAAGSAGAMG PQGSPGARGP PGLKGDKGIP GDKGAKGESG LPDVASLRQQ VEALQGQVQH LQAAFSQYKK VELFPNGQSV GEKIFKTAGF VKPFTEAQLL CTQAGGQLAS PRSAAENAAL QQLVVAKNEA AFLSMTDSKT EGKFTYPTGE SLVYSNWAPG EPNDDGGSED CVEIFTNGKW NDRACGEKRL VVCEF //