ID   SFTPA_SHEEP             Reviewed;         248 AA.
AC   Q9TT06;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=SFTPA;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=10749753; DOI=10.1152/ajplung.2000.278.4.l754;
RA   Braems G.A., Yao L.-J., Inchley K., Brickenden A., Han V.K.M., Grolla A.,
RA   Challis J.R.G., Possmayer F.;
RT   "Ovine surfactant protein cDNAs: use in studies on fetal lung growth and
RT   maturation after prolonged hypoxemia.";
RL   Am. J. Physiol. 278:L754-L764(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   PubMed=10749754; DOI=10.1152/ajplung.2000.278.4.l765;
RA   Pietschmann S.M., Pison U.;
RT   "cDNA cloning of ovine pulmonary SP-A, SP-B, and SP-C: isolation of two
RT   different sequences for SP-B.";
RL   Am. J. Physiol. 278:L765-L778(2000).
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   -!- SIMILARITY: Belongs to the SFTPA family. {ECO:0000305}.
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DR   EMBL; AF211856; AAF18995.1; -; mRNA.
DR   EMBL; AF076633; AAF31148.1; -; mRNA.
DR   RefSeq; NP_001009728.2; NM_001009728.2.
DR   AlphaFoldDB; Q9TT06; -.
DR   SMR; Q9TT06; -.
DR   STRING; 9940.ENSOARP00000010907; -.
DR   GeneID; 443033; -.
DR   KEGG; oas:443033; -.
DR   CTD; 653509; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   OrthoDB; 1172460at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Calcium; Collagen; Disulfide bond; Extracellular matrix; Gaseous exchange;
KW   Glycoprotein; Lectin; Metal-binding; Reference proteome; Secreted; Signal;
KW   Surface film.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..248
FT                   /note="Pulmonary surfactant-associated protein A"
FT                   /id="PRO_0000017463"
FT   DOMAIN          28..100
FT                   /note="Collagen-like"
FT   DOMAIN          127..247
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   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   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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"
SQ   SEQUENCE   248 AA;  26394 MW;  D65E7293BBFF1FD9 CRC64;
     MLLCSLTLML LWMVASGLEC DTKEVCLGSP GIPGTPGSHG LPGRDGRDGI KGDPGPPGPM
     GPPGGMPGLP GRDGMTGAPG LPGERGEKGE PGERGPPGFP AYLDEELQGT LHEIRHQVLQ
     SQGVLILQGS MLEVGEKVFS TNGQSLNFDA IKELCARAGG HIAAPRSPEE NEAITSIVKK
     HNTYAYLGLA EGPTAGDFYY LDGAPVNYTN WYPGEPRGRG KEKCVEIYTD GQWNDKNCLQ
     YRLAICEF