ID SFTPA_PIG Reviewed; 249 AA. AC P49874; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 133. DE RecName: Full=Pulmonary surfactant-associated protein A; DE Short=PSAP; DE Short=PSP-A; DE Short=SP-A; DE Flags: Precursor; GN Name=SFTPA1; Synonyms=SFTP1, SFTPA; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lung; RA Adamou J.E., Elshourbagy N.A.; RT "A cDNA clone for the porcine pulmonary surfactant - associated protein RT (PSP-A)."; RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: In presence of calcium ions, it binds to surfactant CC phospholipids and contributes to lower the surface tension at the air- CC liquid interface in the alveoli of the mammalian lung and is essential CC for normal respiration. Enhances the expression of MYO18A/SP-R210 on CC alveolar macrophages. {ECO:0000250|UniProtKB:P35242}. CC -!- SUBUNIT: Oligomeric complex of 6 set of homotrimers. CC {ECO:0000250|UniProtKB:Q8IWL2}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q8IWL2}. CC Secreted, extracellular space, extracellular matrix CC {ECO:0000250|UniProtKB:Q8IWL2}. Secreted, extracellular space, surface CC film {ECO:0000250|UniProtKB:Q8IWL2}. 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 SFTPA 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; L41350; AAA88403.1; -; mRNA. DR RefSeq; NP_999430.1; NM_214265.1. DR AlphaFoldDB; P49874; -. DR SMR; P49874; -. DR STRING; 9823.ENSSSCP00000067056; -. DR GlyCosmos; P49874; 1 site, No reported glycans. DR PaxDb; 9823-ENSSSCP00000011022; -. DR PeptideAtlas; P49874; -. DR GeneID; 397503; -. DR CTD; 653509; -. DR eggNOG; KOG4297; Eukaryota. DR InParanoid; P49874; -. DR OrthoDB; 4641030at2759; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. 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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW. DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 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; IPR016187; CTDL_fold. DR PANTHER; PTHR22803:SF155; C-TYPE LECTIN DOMAIN CONTAINING 10A; 1. DR PANTHER; PTHR22803; MANNOSE, PHOSPHOLIPASE, LECTIN RECEPTOR RELATED; 1. DR Pfam; PF00059; Lectin_C; 1. DR SMART; SM00034; CLECT; 1. DR SUPFAM; SSF56436; C-type lectin-like; 1. DR SUPFAM; SSF57944; Triple coiled coil domain of C-type lectins; 1. DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1. DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1. DR Genevisible; P49874; SS. PE 2: Evidence at transcript level; KW Calcium; Collagen; Disulfide bond; Extracellular matrix; Gaseous exchange; KW Glycoprotein; Hydroxylation; Lectin; Metal-binding; Reference proteome; KW Repeat; Secreted; Signal; Surface film. FT SIGNAL 1..20 FT /evidence="ECO:0000255" FT CHAIN 21..249 FT /note="Pulmonary surfactant-associated protein A" FT /id="PRO_0000017460" FT DOMAIN 28..100 FT /note="Collagen-like" FT DOMAIN 133..249 FT /note="C-type lectin" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT REGION 29..102 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 216 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 218 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 235 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT BINDING 236 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250" FT MOD_RES 30 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 33 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 36 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 42 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 54 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 57 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 63 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT MOD_RES 70 FT /note="4-hydroxyproline" FT /evidence="ECO:0000250" FT CARBOHYD 208 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000250" FT DISULFID 26 FT /note="Interchain" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DISULFID 155..247 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" FT DISULFID 225..239 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040" SQ SEQUENCE 249 AA; 26702 MW; 3C4E05AD07F2A7CD CRC64; MLRWPLALTF LLLAVSGLEC DVKEVCLASP GIPGTPGSHG LPGRDGRDGI KGDPGPPGPM GPPGGMAGPP GQDGMIGAPG LPGERGEKGE PGERGPPGLP AHLDEELQSA LHEIRHQILQ SMGVLSFQEF MLAVGEKVFS TNGQSVAFWM SLESCVPEQV GRIAAPRSPE ENEAIASIVK KHNTYAYLGL VEGPTAGDFF YLDGTPVNYT NWYPGEPRGR GKEKCVEMYT DGQWNDRNCQ QYRLAICEF //