SFTPA_RAT
ID SFTPA_RAT Reviewed; 248 AA.
AC P08427;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 3.
DT 03-AUG-2022, entry version 186.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=2901856; DOI=10.1016/0167-4781(88)90130-3;
RA Fisher J.H., Emrie P.A., Shannon J., Sano K., Hattler B., Mason R.J.;
RT "Rat pulmonary surfactant protein A is expressed as two differently sized
RT mRNA species which arise from differential polyadenylation of one
RT transcript.";
RL Biochim. Biophys. Acta 950:338-345(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND HYDROXYLATION AT
RP PRO-30; PRO-33; PRO-36; PRO-42; PRO-54; PRO-57; PRO-63; PRO-67; PRO-70 AND
RP PRO-76.
RX PubMed=3579914; DOI=10.1016/s0006-291x(87)80519-3;
RA Sano K., Fisher J.H., Mason R.J., Kuroki Y., Schilling J., Benson B.,
RA Voelker D.;
RT "Isolation and sequence of a cDNA clone for the rat pulmonary surfactant-
RT associated protein (PSP-A).";
RL Biochem. Biophys. Res. Commun. 144:367-374(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=7491978; DOI=10.1152/ajplung.1995.269.5.l603;
RA Smith C.I., Rosenberg E., Reisher S.R., Li F., Kefalides P., Fisher A.B.,
RA Feinstein S.I.;
RT "Sequence of rat surfactant protein A gene and functional mapping of its
RT upstream region.";
RL Am. J. Physiol. 269:L603-L612(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 101-248, CALCIUM-BINDING SITES,
RP DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=12913002; DOI=10.1074/jbc.m305628200;
RA Head J.F., Mealy T.R., McCormack F.X., Seaton B.A.;
RT "Crystal structure of trimeric carbohydrate recognition and neck domains of
RT surfactant protein A.";
RL J. Biol. Chem. 278:43254-43260(2003).
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:0000269|PubMed:12913002}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA41972.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M33201; AAA41973.1; -; mRNA.
DR EMBL; X13176; CAA31573.1; -; mRNA.
DR EMBL; X13177; CAA31574.1; -; mRNA.
DR EMBL; M15754; AAA41972.1; ALT_INIT; mRNA.
DR EMBL; U43092; AAA85516.1; -; Genomic_DNA.
DR EMBL; BC085353; AAH85353.1; -; mRNA.
DR PIR; A29299; LNRTPS.
DR RefSeq; NP_001257574.1; NM_001270645.1.
DR RefSeq; NP_001257576.1; NM_001270647.1.
DR RefSeq; NP_059025.2; NM_017329.2.
DR PDB; 1R13; X-ray; 2.10 A; A=101-248.
DR PDB; 1R14; X-ray; 2.50 A; A=101-248.
DR PDB; 3PAK; X-ray; 1.90 A; A=101-248.
DR PDB; 3PAQ; X-ray; 2.10 A; A=101-248.
DR PDB; 3PAR; X-ray; 2.30 A; A=101-248.
DR PDB; 3PBF; X-ray; 1.80 A; A=101-248.
DR PDB; 4WR9; X-ray; 2.30 A; A=101-248.
DR PDB; 4WRC; X-ray; 1.80 A; A=101-248.
DR PDB; 4WRE; X-ray; 1.75 A; A=101-248.
DR PDB; 4WRF; X-ray; 1.90 A; A=101-248.
DR PDB; 4WUW; X-ray; 2.40 A; A=101-248.
DR PDB; 4WUX; X-ray; 1.90 A; A=101-248.
DR PDB; 5FFR; X-ray; 2.20 A; A=101-248.
DR PDB; 5FFS; X-ray; 1.80 A; A=101-248.
DR PDB; 5FFT; X-ray; 2.20 A; A=101-248.
DR PDBsum; 1R13; -.
DR PDBsum; 1R14; -.
DR PDBsum; 3PAK; -.
DR PDBsum; 3PAQ; -.
DR PDBsum; 3PAR; -.
DR PDBsum; 3PBF; -.
DR PDBsum; 4WR9; -.
DR PDBsum; 4WRC; -.
DR PDBsum; 4WRE; -.
DR PDBsum; 4WRF; -.
DR PDBsum; 4WUW; -.
DR PDBsum; 4WUX; -.
DR PDBsum; 5FFR; -.
DR PDBsum; 5FFS; -.
DR PDBsum; 5FFT; -.
DR AlphaFoldDB; P08427; -.
DR SMR; P08427; -.
DR BioGRID; 246897; 1.
DR STRING; 10116.ENSRNOP00000039850; -.
DR UniLectin; P08427; -.
DR GlyGen; P08427; 1 site.
DR PaxDb; P08427; -.
DR ABCD; P08427; 21 sequenced antibodies.
DR Ensembl; ENSRNOT00000047870; ENSRNOP00000039850; ENSRNOG00000011438.
DR GeneID; 24773; -.
DR KEGG; rno:24773; -.
DR UCSC; RGD:3665; rat.
DR CTD; 653509; -.
DR RGD; 3665; Sftpa1.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000156653; -.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; P08427; -.
DR OMA; KCNQNRL; -.
DR OrthoDB; 1172460at2759; -.
DR PhylomeDB; P08427; -.
DR TreeFam; TF330481; -.
DR Reactome; R-RNO-391160; Signal regulatory protein family interactions.
DR Reactome; R-RNO-5683826; Surfactant metabolism.
DR Reactome; R-RNO-5686938; Regulation of TLR by endogenous ligand.
DR EvolutionaryTrace; P08427; -.
DR PRO; PR:P08427; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000011438; Expressed in lung and 2 other tissues.
DR Genevisible; P08427; RN.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005771; C:multivesicular body; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEP:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0008228; P:opsonization; ISO:RGD.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IDA:RGD.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW.
DR GO; GO:0070849; P:response to epidermal growth factor; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0055093; P:response to hyperoxia; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0070741; P:response to interleukin-6; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR CDD; cd03591; CLECT_collectin_like; 1.
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; IPR033990; Collectin_CTLD.
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 1: Evidence at protein level;
KW 3D-structure; Calcium; Collagen; Direct protein sequencing; Disulfide bond;
KW Extracellular matrix; Gaseous exchange; Glycoprotein; Hydroxylation;
KW Lectin; Metal-binding; Reference proteome; Repeat; Secreted; Signal;
KW Surface film.
FT SIGNAL 1..20
FT CHAIN 21..248
FT /note="Pulmonary surfactant-associated protein A"
FT /id="PRO_0000017462"
FT DOMAIN 28..100
FT /note="Collagen-like"
FT DOMAIN 133..248
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 31..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 215
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 217
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 234
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT SITE 21
FT /note="Not glycosylated"
FT MOD_RES 30
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3579914"
FT MOD_RES 33
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3579914"
FT MOD_RES 36
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3579914"
FT MOD_RES 42
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3579914"
FT MOD_RES 54
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3579914"
FT MOD_RES 57
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3579914"
FT MOD_RES 63
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3579914"
FT MOD_RES 67
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3579914"
FT MOD_RES 70
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3579914"
FT MOD_RES 76
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000269|PubMed:3579914"
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 ECO:0000269|PubMed:12913002"
FT DISULFID 224..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:12913002"
FT CONFLICT 78
FT /note="A -> G (in Ref. 1; AAA41973/CAA31573/CAA31574)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="E -> G (in Ref. 1; AAA41973/CAA31573/CAA31574)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="Missing (in Ref. 2; AAA41972)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="T -> TF (in Ref. 2; AAA41972)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="K -> N (in Ref. 1; CAA31574)"
FT /evidence="ECO:0000305"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:4WRE"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:4WRE"
FT STRAND 137..146
FT /evidence="ECO:0007829|PDB:4WRE"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:4WRE"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4WRC"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:4WRE"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4WRE"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:4WRC"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:3PBF"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:3PAR"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:4WRE"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:4WRE"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:4WRE"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:4WRE"
SQ SEQUENCE 248 AA; 26289 MW; CAA0203009E682A5 CRC64;
MSLCSLAFTL FLTVVAGIKC NVTDVCAGSP GIPGAPGNHG LPGRDGRDGV KGDPGPPGPM
GPPGGMPGLP GRDGLPGAPG APGERGDKGE PGERGLPGFP AYLDEELQTE LYEIKHQILQ
TMGVLSLQGS MLSVGDKVFS TNGQSVNFDT IKEMCTRAGG NIAVPRTPEE NEAIASIAKK
YNNYVYLGMI EDQTPGDFHY LDGASVNYTN WYPGEPRGQG KEKCVEMYTD GTWNDRGCLQ
YRLAVCEF
