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Pulmonary surfactant-associated protein A (PSAP) (PSP-A) (SP-A)

 SFTPA_CANLF             Reviewed;         248 AA.
P06908;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
22-NOV-2017, entry version 121.
RecName: Full=Pulmonary surfactant-associated protein A;
Short=PSAP;
Short=PSP-A;
Short=SP-A;
Flags: Precursor;
Name=SFTPA1; Synonyms=SFTP1, SFTPA;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SIGNAL SEQUENCE CLEAVAGE SITE.
PubMed=3863100; DOI=10.1073/pnas.82.19.6379;
Benson B., Hawgood S., Schilling J., Clements J., Damm D., Cordell B.,
White R.T.;
"Structure of canine pulmonary surfactant apoprotein: cDNA and
complete amino acid sequence.";
Proc. Natl. Acad. Sci. U.S.A. 82:6379-6383(1985).
[2]
DOMAIN.
PubMed=3808053; DOI=10.1038/325490a0;
Patthy L.;
"Is lung surfactant protein a lectin-collagen hybrid?";
Nature 325:490-490(1987).
-!- FUNCTION: In presence of calcium ions, it binds to surfactant
phospholipids and contributes to lower the surface tension at the
air-liquid interface in the alveoli of the mammalian lung and is
essential for normal respiration. Enhances the expression of
MYO18A/SP-R210 on alveolar macrophages.
{ECO:0000250|UniProtKB:P35242}.
-!- SUBUNIT: Oligomeric complex of 6 set of homotrimers.
{ECO:0000250|UniProtKB:Q8IWL2}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix. Secreted, extracellular space, surface film.
-!- MISCELLANEOUS: Pulmonary surfactant consists of 90% lipid and 10%
protein. There are 4 surfactant-associated proteins: 2
collagenous, carbohydrate-binding glycoproteins (SP-A and SP-D)
and 2 small hydrophobic proteins (SP-B and SP-C).
-!- SIMILARITY: Belongs to the SFTPA family. {ECO:0000305}.
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EMBL; M11769; AAA30887.1; -; mRNA.
PIR; A25296; LNDGPS.
ProteinModelPortal; P06908; -.
SMR; P06908; -.
STRING; 9615.ENSCAFP00000023171; -.
PaxDb; P06908; -.
eggNOG; KOG4297; Eukaryota.
eggNOG; ENOG410XPJ1; LUCA.
HOGENOM; HOG000085660; -.
HOVERGEN; HBG108270; -.
InParanoid; P06908; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0007585; P:respiratory gaseous exchange; IEA:UniProtKB-KW.
CDD; cd03591; CLECT_collectin_like; 1.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR033990; Collectin_CTLD.
InterPro; IPR016187; CTDL_fold.
Pfam; PF00059; Lectin_C; 1.
SMART; SM00034; CLECT; 1.
SUPFAM; SSF56436; SSF56436; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
1: Evidence at protein level;
Calcium; Collagen; Complete proteome; Disulfide bond;
Extracellular matrix; Gaseous exchange; Glycoprotein; Hydroxylation;
Lectin; Metal-binding; Reference proteome; Repeat; Secreted; Signal;
Surface film.
SIGNAL 1 17 {ECO:0000269|PubMed:3863100}.
CHAIN 18 248 Pulmonary surfactant-associated protein
A.
/FTId=PRO_0000017454.
DOMAIN 28 100 Collagen-like.
DOMAIN 132 248 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
METAL 215 215 Calcium. {ECO:0000250}.
METAL 217 217 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 234 234 Calcium. {ECO:0000250}.
MOD_RES 30 30 4-hydroxyproline. {ECO:0000250}.
MOD_RES 33 33 4-hydroxyproline. {ECO:0000250}.
MOD_RES 36 36 4-hydroxyproline. {ECO:0000250}.
MOD_RES 42 42 4-hydroxyproline. {ECO:0000250}.
MOD_RES 54 54 4-hydroxyproline. {ECO:0000250}.
MOD_RES 57 57 4-hydroxyproline. {ECO:0000250}.
MOD_RES 63 63 4-hydroxyproline. {ECO:0000250}.
MOD_RES 67 67 4-hydroxyproline. {ECO:0000250}.
MOD_RES 70 70 4-hydroxyproline. {ECO:0000250}.
CARBOHYD 20 20 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 155 246 {ECO:0000255|PROSITE-ProRule:PRU00040}.
DISULFID 224 238 {ECO:0000255|PROSITE-ProRule:PRU00040}.
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


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