SFTPA_CANLF
ID SFTPA_CANLF Reviewed; 248 AA.
AC P06908;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 135.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SIGNAL SEQUENCE CLEAVAGE SITE.
RX PubMed=3863100; DOI=10.1073/pnas.82.19.6379;
RA Benson B., Hawgood S., Schilling J., Clements J., Damm D., Cordell B.,
RA White R.T.;
RT "Structure of canine pulmonary surfactant apoprotein: cDNA and complete
RT amino acid sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:6379-6383(1985).
RN [2]
RP DOMAIN.
RX PubMed=3808053; DOI=10.1038/325490a0;
RA Patthy L.;
RT "Is lung surfactant protein a lectin-collagen hybrid?";
RL Nature 325:490-490(1987).
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; M11769; AAA30887.1; -; mRNA.
DR PIR; A25296; LNDGPS.
DR AlphaFoldDB; P06908; -.
DR SMR; P06908; -.
DR STRING; 9615.ENSCAFP00000023171; -.
DR PaxDb; P06908; -.
DR InParanoid; P06908; -.
DR Proteomes; UP000002254; 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: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 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 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..17
FT /evidence="ECO:0000269|PubMed:3863100"
FT CHAIN 18..248
FT /note="Pulmonary surfactant-associated protein A"
FT /id="PRO_0000017454"
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 29..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Pro residues"
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 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 CARBOHYD 20
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 155..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DISULFID 224..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ SEQUENCE 248 AA; 26269 MW; 340FE95D4E2502C0 CRC64;
MWLRCLALAL TLLMVSGIEN NTKDVCVGNP GIPGTPGSHG LPGRDGRDGV KGDPGPPGPL
GPPGGMPGHP GPNGMTGAPG VAGERGEKGE PGERGPPGLP ASLDEELQTT LHDLRHQILQ
TMGVLSLHES LLVVGRKVFS SNAQSINFND IQELCAGAGG QIAAPMSPEE NEAVASIVKK
YNTYAYLGLV ESPDSGDFQY MDGAPVNYTN WYPGEPRGRG KEQCVEMYTD GQWNNKNCLQ
YRLAICEF