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 01-NOV-1997 (REL. 35, 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; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RX MEDLINE; 93155122. RA CROUCH E., RUST K., VEILE R., DONIS-KELLER H., GROSSO L.; RL J. BIOL. CHEM. 268:2976-2983(1993). RN [2] RP SEQUENCE FROM N.A., AND SEQUENCE OF 214-243. RC TISSUE=LUNG, AND AMNIOTIC FLUID; RX MEDLINE; 92322003. RA LU J., WILLIS A.C., REID K.B.M.; 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. RA RUST K., GROSSO L., ZHANG V., CHANG D., PERSSON A., LONGMORE W., RA CAI G.-Z., CROUCH E.; RL ARCH. BIOCHEM. BIOPHYS. 290:116-126(1991). 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 -!- PULMONARY SURFACTANT CONSISTS OF 90% LIPID AND 10% PROTEIN. THERE CC ARE 4 SURFACTANT ASSOCIATED PROTEIN: 2 COLLAGENOUS, CARBOHYDRATE- CC BINDING GLYCOPROTEINS (SP-A AND SP-D) AND 2 SMALL HYDROPHOBIC CC 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; G292507; -. DR EMBL; L05483; G292507; JOINED. DR EMBL; L05484; G292507; JOINED. DR EMBL; X65018; G34767; -. DR PIR; A45225; A45225. DR PIR; S18382; S18382. DR HSSP; P02462; 1BBE. DR MIM; 178635; -. 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. FT SIGNAL 1 20 BY SIMILARITY. FT CHAIN 21 375 PULMONARY SURFACTANT PROTEIN D. FT DOMAIN 46 222 COLLAGEN-LIKE. FT DOMAIN 279 375 C-TYPE LECTIN (SHORT FORM). FT DISULFID 281 373 BY SIMILARITY. FT DISULFID 351 365 BY SIMILARITY. FT MOD_RES ?21 ?21 BLOCKED. FT CARBOHYD 90 90 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). SQ SEQUENCE 375 AA; 37702 MW; D63C1352 CRC32; 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 //