ID SFTPD_HUMAN STANDARD; PRT; 375 AA. AC P35247; Q86YK9; Q9UCJ2; Q9UCJ3; DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 2. DT 05-SEP-2006, entry version 72. DE Pulmonary surfactant-associated protein D precursor (SP-D) (PSP-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 [GENOMIC DNA], AND VARIANTS THR-31; VAL-123; RP THR-180; THR-290 AND LYS-309. RA Rieder M.J., Carrington D.P., da Ponte S.H., Hastings N.C., RA Ahearn M.O., Kuldanek S.A., Rajkumar N., Toth E.J., Yi Q., RA Nickerson D.A.; RT "SeattleSNPs. NHLBI HL66682 program for genomic applications, UW- RT FHCRC, Seattle, WA (URL: http://pga.gs.washington.edu)."; RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases. RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-375, AND PARTIAL PROTEIN RP SEQUENCE. RC TISSUE=Lung; RX MEDLINE=91378578; PubMed=1898081; 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 [6] 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. Binds strongly maltose residues and to a lesser CC extent other alpha-glucosyl moieties. It could participate in the CC extracellular reorganization or turnover of pulmonary surfactant. CC -!- SUBUNIT: Oligomeric complex of 4 set of homotrimers. CC -!- SUBCELLULAR LOCATION: Secreted protein; extracellular space. CC -!- PTM: The N-terminus is blocked. CC -!- MISCELLANEOUS: Pulmonary surfactant consists of 90% lipid and 10% CC protein. There are 4 surfactant-associated protein: 2 collagenous, CC carbohydrate-binding glycoproteins (SP-A and SP-D) and 2 small CC hydrophobic proteins (SP-B and SP-C). CC -!- SIMILARITY: Contains 1 C-type lectin domain. CC -!- SIMILARITY: Contains 1 collagen-like domain. 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; AY216721; AAO22991.1; -; Genomic_DNA. DR PIR; A45225; A45225. DR PDB; 1B08; X-ray; A/B/C=224-375. DR PDB; 1M7L; NMR; A/B/C=220-257. DR PDB; 1PW9; X-ray; A/B/C=199-375. DR PDB; 1PWB; X-ray; A/B/C=199-375. DR Ensembl; ENSG00000133661; Homo sapiens. DR H-InvDB; HIX0008974; -. DR HGNC; HGNC:10803; SFTPD. DR MIM; 178635; gene. DR ArrayExpress; P35247; -. DR RZPD-ProtExp; IOH13776; -. DR RZPD-ProtExp; RZPDo834B1234; -. DR GO; GO:0030139; C:endocytic vesicle; TAS. DR GO; GO:0005576; C:extracellular region; TAS. DR GO; GO:0005764; C:lysosome; TAS. DR GO; GO:0008367; F:bacterial binding; TAS. DR GO; GO:0005529; F:sugar binding; TAS. DR GO; GO:0048286; P:alveolus development; IMP. DR GO; GO:0045087; P:innate immune response; TAS. DR GO; GO:0048246; P:macrophage chemotaxis; TAS. DR GO; GO:0045085; P:negative regulation of interleukin-2 biosyn...; TAS. DR GO; GO:0042130; P:negative regulation of T cell proliferation; TAS. DR GO; GO:0006800; P:oxygen and reactive oxygen species metabolism; TAS. DR GO; GO:0050766; P:positive regulation of phagocytosis; TAS. DR GO; GO:0006898; P:receptor mediated endocytosis; TAS. DR GO; GO:0001817; P:regulation of cytokine production; NAS. DR GO; GO:0043129; P:surfactant homeostasis; IMP. DR InterPro; IPR008161; Clg_helix. DR InterPro; IPR008160; Collagen. DR InterPro; IPR001304; Lectin_C. DR Pfam; PF01391; Collagen; 4. DR Pfam; PF00059; Lectin_C; 1. DR ProDom; PD000007; Clg_helix; 2. DR SMART; SM00034; CLECT; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. KW 3D-structure; Calcium; Coiled coil; Collagen; KW Direct protein sequencing; Gaseous exchange; Glycoprotein; KW Hydroxylation; Lectin; Polymorphism; Repeat; 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 Hydroxyproline (By similarity). FT MOD_RES 87 87 5-hydroxylysine (By similarity). FT MOD_RES 96 96 Hydroxyproline (By similarity). FT MOD_RES 99 99 5-hydroxylysine (By similarity). FT MOD_RES 171 171 Hydroxyproline (By similarity). FT MOD_RES 177 177 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:17885900 and FT dbSNP:2243639). 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 59 59 P -> F (in Ref. 3 and 4). FT CONFLICT 63 63 K -> E (in Ref. 4). FT CONFLICT 122 122 P -> A (in Ref. 2 and 3). FT CONFLICT 206 206 D -> P (in Ref. 3). FT CONFLICT 240 240 H -> P (in Ref. 4). FT CONFLICT 374 374 E -> EH (in Ref. 3). FT HELIX 226 253 FT TURN 254 256 FT STRAND 257 260 FT TURN 261 262 FT STRAND 263 273 FT HELIX 274 283 FT TURN 284 285 FT STRAND 286 288 FT STRAND 293 293 FT HELIX 294 307 FT TURN 308 308 FT STRAND 311 312 FT STRAND 314 314 FT STRAND 316 316 FT STRAND 318 320 FT TURN 321 322 FT STRAND 325 325 FT TURN 327 328 FT STRAND 329 329 FT STRAND 331 331 FT STRAND 333 333 FT STRAND 337 337 FT TURN 339 340 FT HELIX 345 347 FT STRAND 351 354 FT TURN 356 357 FT STRAND 358 358 FT STRAND 360 363 FT TURN 365 366 FT STRAND 367 375 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 //