SFTPA_PIG
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 03-AUG-2022, entry version 127.
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}.
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DR EMBL; L41350; AAA88403.1; -; mRNA.
DR RefSeq; NP_999430.1; NM_214265.1.
DR AlphaFoldDB; P49874; -.
DR SMR; P49874; -.
DR STRING; 9823.ENSSSCP00000011022; -.
DR PaxDb; P49874; -.
DR PeptideAtlas; P49874; -.
DR GeneID; 397503; -.
DR CTD; 653509; -.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P49874; -.
DR OrthoDB; 1172460at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P49874; SS.
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:0005791; C:rough endoplasmic reticulum; 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; -; 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 Pfam; PF00059; Lectin_C; 1.
DR SMART; SM00034; CLECT; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
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
