ID SFTPA_MOUSE Reviewed; 248 AA.
AC P35242;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 27-MAR-2024, entry version 166.
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=Sftp-1, Sftp1, Sftpa;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DBA/2J;
RX PubMed=1443158; DOI=10.1152/ajplung.1992.263.5.l546;
RA Korfhagen T.R., Bruno M.D., Glasser S.W., Ciraolo P.J., Whitsett J.A.,
RA Lattier D.L., Wikenheiser K.A., Clark J.C.;
RT "Murine pulmonary surfactant SP-A gene: cloning, sequence, and
RT transcriptional activity.";
RL Am. J. Physiol. 263:L546-L554(1992).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION.
RX PubMed=25965346; DOI=10.1371/journal.pone.0126576;
RA Yang L., Carrillo M., Wu Y.M., DiAngelo S.L., Silveyra P., Umstead T.M.,
RA Halstead E.S., Davies M.L., Hu S., Floros J., McCormack F.X.,
RA Christensen N.D., Chroneos Z.C.;
RT "SP-R210 (Myo18A) isoforms as intrinsic modulators of macrophage priming
RT and activation.";
RL PLoS ONE 10:E0126576-E0126576(2015).
RN [4]
RP MUTAGENESIS OF TYR-208, AND SUBCELLULAR LOCATION.
RX PubMed=31601679; DOI=10.1084/jem.20182351;
RA Takezaki A., Tsukumo S.I., Setoguchi Y., Ledford J.G., Goto H.,
RA Hosomichi K., Uehara H., Nishioka Y., Yasutomo K.;
RT "A homozygous SFTPA1 mutation drives necroptosis of type II alveolar
RT epithelial cells in patients with idiopathic pulmonary fibrosis.";
RL J. Exp. Med. 216:2724-2735(2019).
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 (PubMed:25965346). {ECO:0000269|PubMed:25965346}.
CC -!- SUBUNIT: Oligomeric complex of 6 set of homotrimers.
CC {ECO:0000250|UniProtKB:Q8IWL2}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:31601679}. Secreted,
CC extracellular space, extracellular matrix {ECO:0000305}. Secreted,
CC extracellular space, surface film {ECO:0000305}.
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 -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Pulmonary surfactant protein SP-A;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_355";
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DR EMBL; S48768; AAB24274.1; -; Genomic_DNA.
DR CCDS; CCDS26960.1; -.
DR PIR; A48853; A48853.
DR AlphaFoldDB; P35242; -.
DR SMR; P35242; -.
DR IntAct; P35242; 7.
DR MINT; P35242; -.
DR STRING; 10090.ENSMUSP00000129696; -.
DR GlyCosmos; P35242; 2 sites, No reported glycans.
DR GlyGen; P35242; 2 sites.
DR iPTMnet; P35242; -.
DR PhosphoSitePlus; P35242; -.
DR MaxQB; P35242; -.
DR PaxDb; 10090-ENSMUSP00000129696; -.
DR PeptideAtlas; P35242; -.
DR ProteomicsDB; 257211; -.
DR AGR; MGI:109518; -.
DR MGI; MGI:109518; Sftpa1.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; P35242; -.
DR PhylomeDB; P35242; -.
DR Reactome; R-MMU-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-MMU-391160; Signal regulatory protein family interactions.
DR Reactome; R-MMU-5683826; Surfactant metabolism.
DR Reactome; R-MMU-5686938; Regulation of TLR by endogenous ligand.
DR PRO; PR:P35242; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P35242; Protein.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050766; P:positive regulation of phagocytosis; ISO:MGI.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW.
DR CDD; cd03591; CLECT_collectin_like; 1.
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; IPR033990; Collectin_CTLD.
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.
PE 1: Evidence at protein 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:0000250"
FT CHAIN 21..248
FT /note="Pulmonary surfactant-associated protein A"
FT /id="PRO_0000017459"
FT DOMAIN 28..100
FT /note="Collagen-like"
FT DOMAIN 132..248
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 28..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 234
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 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 67
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 70
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 76
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT CARBOHYD 21
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 26
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 155..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 224..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT MUTAGEN 208
FT /note="Y->H: Knockin homozygous mice develop progressive
FT pulmonary fibrosis. The mutant protein is not secreted in
FT bronchoalveolar fluid from mutant mice."
FT /evidence="ECO:0000269|PubMed:31601679"
SQ SEQUENCE 248 AA; 26157 MW; 6688BF070E3EB9AE CRC64;
MSLGSLAFTL FLTVVAGIKC NGTEVCAGSP GIPGTPGNHG LPGRDGRDGI KGDPGPPGPM
GPPGGMPGLP GRDGLPGAPG APGEHGDKGE PGERGLPGFP AYLDEELQTA SYEIKHQILQ
TMGVLSLQGS MLSVGDKVFS TNGQSVNFDT IREMCTRAGG HIAAPRNPEE NEAIASITKK
YNTYPYLGVI EGQTPGDFHY LDGASVNYTN WYPGEPRGRG KEKCVEMYTD GKWNDKGCLQ
YRLAICEF
//
