SFTPA_MACMU
ID SFTPA_MACMU Reviewed; 248 AA.
AC Q9TUC5; F6Y0S1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 2.
DT 03-AUG-2022, entry version 113.
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 Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17431167; DOI=10.1126/science.1139247;
RA Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA Kuhn R.M., Smith K.E., Zwieg A.S.;
RT "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL Science 316:222-234(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 49-213.
RX PubMed=10074480; DOI=10.1172/jci5232;
RA Sekhon H.S., Jia Y., Raab R., Kuryatov A., Pankow J.F., Whitsett J.A.,
RA Lindstrom J., Spindel E.R.;
RT "Prenatal nicotine increases pulmonary alpha7 nicotinic receptor expression
RT and alters fetal lung development in monkeys.";
RL J. Clin. Invest. 103:637-647(1999).
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; AF087691; AAF02223.1; -; mRNA.
DR RefSeq; NP_001182305.1; NM_001195376.1.
DR RefSeq; XP_015002613.1; XM_015147127.1.
DR RefSeq; XP_015002614.1; XM_015147128.1.
DR AlphaFoldDB; Q9TUC5; -.
DR SMR; Q9TUC5; -.
DR STRING; 9544.ENSMMUP00000012817; -.
DR GeneID; 574108; -.
DR KEGG; mcc:574108; -.
DR CTD; 653509; -.
DR eggNOG; KOG4297; Eukaryota.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; Q9TUC5; -.
DR OMA; KCNQNRL; -.
DR OrthoDB; 1172460at2759; -.
DR TreeFam; TF330481; -.
DR Proteomes; UP000006718; 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; 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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..248
FT /note="Pulmonary surfactant-associated protein A"
FT /id="PRO_0000046689"
FT DOMAIN 31..100
FT /note="Collagen-like"
FT DOMAIN 134..247
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 33..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 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"
FT CONFLICT 213
FT /note="P -> R (in Ref. 2; AAF02223)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 26086 MW; DCEDB793CCDDC11F CRC64;
MWLCPLALTL TLMAASGAAC EVKDICVGSP GIPGTPGSHG LPGRDGRDGV KGDPGPPGPM
GPPGDMPCFP GNDGLPGAPG IPGECGEKGE PGERGPPGLP AHLDEELQAT LHDFRHQILQ
TRGALSLQES ILAIGGKVFS TNGQSATFDA IQEACARAGG HIAVPRSPEE NEAIASFVKK
YNTYAYVGLT EGPSPGDFRY SDGTPVNYTN WYPGEPAGRG TEQCVEMYTD GRWNDRNCLY
NRLTICEF
