ID PSPD_HUMAN STANDARD; PRT; 375 AA. AC P35247; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUN-2002 (Rel. 41, Last annotation update) DE Pulmonary surfactant-associated protein D precursor (SP-D) (PSP-D). GN SFTPD OR SFTP4 OR PSPD. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. 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 [2] RP SEQUENCE FROM N.A., AND SEQUENCE OF 214-243. 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 [3] RP SEQUENCE OF 60-375 FROM N.A., AND PARTIAL 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 [4] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX MEDLINE=99197291; PubMed=10368295; 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: Extracellular. 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 A COLLAGENOUS DOMAIN. CC -!- SIMILARITY: CONTAINS 1 C-TYPE LECTIN FAMILY 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; L05485; AAB59450.1; -. DR EMBL; L05483; AAB59450.1; JOINED. DR EMBL; L05484; AAB59450.1; JOINED. DR EMBL; X65018; CAA46152.1; -. DR PIR; A45225; A45225. DR PIR; S18382; S18382. DR PDB; 1B08; 29-NOV-99. DR Genew; HGNC:10803; SFTPD. DR MIM; 178635; -. DR InterPro; IPR000087; Collagen. DR InterPro; IPR001304; Lectin_C. DR Pfam; PF00059; lectin_c; 1. DR Pfam; PF01391; Collagen; 4. DR SMART; SM00034; CLECT; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. KW Glycoprotein; Calcium; Surface film; Gaseous exchange; Hydroxylation; KW Signal; Lectin; Collagen; Repeat; Coiled coil; 3D-structure. FT SIGNAL 1 20 BY SIMILARITY. FT CHAIN 21 375 PULMONARY SURFACTANT-ASSOCIATED PROTEIN FT D. FT DOMAIN 46 222 COLLAGEN-LIKE. FT DOMAIN 223 252 COILED COIL (POTENTIAL). FT DOMAIN 279 375 C-TYPE LECTIN (SHORT FORM). FT DISULFID 281 373 FT DISULFID 351 365 FT CARBOHYD 90 90 N-LINKED (GLCNAC...) (POTENTIAL). FT MOD_RES 78 78 HYDROXYLATION (BY SIMILARITY). FT MOD_RES 87 87 HYDROXYLATION (BY SIMILARITY). FT MOD_RES 96 96 HYDROXYLATION (BY SIMILARITY). FT MOD_RES 99 99 HYDROXYLATION (BY SIMILARITY). FT MOD_RES 171 171 HYDROXYLATION (BY SIMILARITY). FT MOD_RES 177 177 HYDROXYLATION (BY SIMILARITY). FT CONFLICT 31 31 M -> T (IN REF. 2). FT CONFLICT 59 59 P -> F (IN REF. 3). FT CONFLICT 122 122 A -> P (IN REF. 2). FT CONFLICT 180 180 T -> A (IN REF. 2). FT CONFLICT 206 206 D -> P (IN REF. 3). FT CONFLICT 374 374 E -> EH (IN REF. 3). FT HELIX 227 253 FT TURN 254 256 FT STRAND 257 260 FT TURN 261 262 FT STRAND 263 272 FT HELIX 274 283 FT TURN 284 285 FT STRAND 287 288 FT HELIX 294 307 FT TURN 308 308 FT STRAND 311 316 FT TURN 321 322 FT STRAND 325 325 FT TURN 327 328 FT STRAND 331 331 FT STRAND 337 337 FT TURN 339 340 FT HELIX 345 347 FT STRAND 351 354 FT TURN 356 357 FT STRAND 360 363 FT TURN 365 366 FT STRAND 369 375 SQ SEQUENCE 375 AA; 37702 MW; 2986B2699FC01A6A CRC64; MLLFLLSALV LLTQPLGYLE AEMKTYSHRT MPSACTLVMC SSVESGLPGR DGRDGREGPR GEKGDPGLPG AAGQAGMPGQ AGPVGPKGDN GSVGEPGPKG DTGPSGPPGP PGVPGPAGRE GALGKQGNIG PQGKPGPKGE AGPKGEVGAP GMQGSAGARG LAGPKGERGV PGERGVPGNT GAAGSAGAMG PQGSPGARGP PGLKGDKGIP GDKGAKGESG LPDVASLRQQ VEALQGQVQH LQAAFSQYKK VELFPNGQSV GEKIFKTAGF VKPFTEAQLL CTQAGGQLAS PRSAAENAAL QQLVVAKNEA AFLSMTDSKT EGKFTYPTGE SLVYSNWAPG EPNDDGGSED CVEIFTNGKW NDRACGEKRL VVCEF //