SFTA1_HUMAN
ID SFTA1_HUMAN Reviewed; 248 AA.
AC Q8IWL2; A8K3T8; B7ZW50; E3VLD8; E3VLD9; E3VLE0; E3VLE1; G5E9J3; P07714;
AC Q14DV4; Q5RIR5; Q5RIR7; Q6PIT0; Q8TC19;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Pulmonary surfactant-associated protein A1;
DE Short=PSP-A;
DE Short=PSPA;
DE Short=SP-A;
DE Short=SP-A1;
DE AltName: Full=35 kDa pulmonary surfactant-associated protein;
DE AltName: Full=Alveolar proteinosis protein;
DE AltName: Full=Collectin-4;
DE Flags: Precursor;
GN Name=SFTPA1; Synonyms=COLEC4, PSAP, SFTP1, SFTPA, SFTPA1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2995821; DOI=10.1038/317361a0;
RA White R.T., Damm D., Miller J., Spratt K., Schilling J., Hawgood S.,
RA Benson B., Cordell B.;
RT "Isolation and characterization of the human pulmonary surfactant
RT apoprotein gene.";
RL Nature 317:361-363(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-19, AND ACETYLATION.
RX PubMed=3755136; DOI=10.1016/s0021-9258(19)84483-6;
RA Floros J., Steinbrink R., Jacobs K., Phelps D., Kriz R., Recny M.,
RA Sultzman L., Jones S., Taeusch H.W., Frank H.A., Fritsch E.F.;
RT "Isolation and characterization of cDNA clones for the 35-kDa pulmonary
RT surfactant-associated protein.";
RL J. Biol. Chem. 261:9029-9033(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-19; VAL-50 AND TRP-219.
RX PubMed=20693318; DOI=10.1152/ajplung.00113.2010;
RA Silveyra P., Wang G., Floros J.;
RT "Human SP-A1 (SFTPA1) variant-specific 3' UTRs and poly(A) tail
RT differentially affect the in vitro translation of a reporter gene.";
RL Am. J. Physiol. 299:L523-L534(2010).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-9; ALA-19; VAL-50 AND
RP TRP-219.
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [9]
RP DISULFIDE BONDS, AND SUBUNIT.
RX PubMed=2610270; DOI=10.1152/ajplung.1989.257.6.l421;
RA Haagsman H.P., White R.T., Schilling J., Lau K., Benson B.J., Golden J.,
RA Hawgood S., Clements J.A.;
RT "Studies of the structure of lung surfactant protein SP-A.";
RL Am. J. Physiol. 257:L421-L429(1989).
RN [10]
RP DEFINITION OF SFTPA1 ALLELES.
RX PubMed=9813381; DOI=10.1016/s0925-4439(98)00077-5;
RA Floros J., Hoover R.R.;
RT "Genetics of the hydrophilic surfactant proteins A and D.";
RL Biochim. Biophys. Acta 1408:312-322(1998).
RN [11]
RP INVOLVEMENT IN RDS.
RX PubMed=10762543; DOI=10.1086/302906;
RA Raemet M., Haataja R., Marttila R., Floros J., Hallman M.;
RT "Association between the surfactant protein A (SP-A) gene locus and
RT respiratory-distress syndrome in the Finnish population.";
RL Am. J. Hum. Genet. 66:1569-1579(2000).
RN [12]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH M.BOVIS APA.
RX PubMed=17158455; DOI=10.1074/jbc.m610183200;
RA Ragas A., Roussel L., Puzo G., Riviere M.;
RT "The Mycobacterium tuberculosis cell-surface glycoprotein Apa as a
RT potential adhesin to colonize target cells via the innate immune system
RT pulmonary C-type lectin surfactant protein A.";
RL J. Biol. Chem. 282:5133-5142(2007).
RN [13]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=21203928; DOI=10.1007/s13238-010-0101-3;
RA Carroll M.V., Sim R.B., Bigi F., Jaekel A., Antrobus R., Mitchell D.A.;
RT "Identification of four novel DC-SIGN ligands on Mycobacterium bovis BCG.";
RL Protein Cell 1:859-870(2010).
RN [14]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH S.AUREUS EPA.
RX PubMed=21123169; DOI=10.1074/jbc.m110.125567;
RA Sever-Chroneos Z., Krupa A., Davis J., Hasan M., Yang C.H., Szeliga J.,
RA Herrmann M., Hussain M., Geisbrecht B.V., Kobzik L., Chroneos Z.C.;
RT "Surfactant protein A (SP-A)-mediated clearance of Staphylococcus aureus
RT involves binding of SP-A to the staphylococcal adhesin eap and the
RT macrophage receptors SP-A receptor 210 and scavenger receptor class A.";
RL J. Biol. Chem. 286:4854-4870(2011).
RN [15]
RP VARIANT TRP-219, AND ASSOCIATION WITH IDIOPATHIC PULMONARY FIBROSIS.
RX PubMed=13680361; DOI=10.1007/s00439-003-1015-4;
RA Selman M., Lin H.-M., Montano M., Jenkins A.L., Estrada A., Lin Z.,
RA Wang G., DiAngelo S.L., Guo X., Umstead T.M., Lang C.M., Pardo A.,
RA Phelps D.S., Floros J.;
RT "Surfactant protein A and B genetic variants predispose to idiopathic
RT pulmonary fibrosis.";
RL Hum. Genet. 113:542-550(2003).
RN [16]
RP VARIANTS LEU-5; THR-9; ALA-19; VAL-50 AND TRP-219.
RX PubMed=19100526; DOI=10.1016/j.ajhg.2008.11.010;
RA Wang Y., Kuan P.J., Xing C., Cronkhite J.T., Torres F., Rosenblatt R.L.,
RA DiMaio J.M., Kinch L.N., Grishin N.V., Garcia C.K.;
RT "Genetic defects in surfactant protein A2 are associated with pulmonary
RT fibrosis and lung cancer.";
RL Am. J. Hum. Genet. 84:52-59(2009).
RN [17]
RP VARIANT ILD1 ARG-211, CHARACTERIZATION OF VARIANT ILD1 ARG-211, VARIANT
RP TRP-219, CHARACTERIZATION OF VARIANT TRP-219, INVOLVEMENT IN ILD1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26792177; DOI=10.1093/hmg/ddw014;
RA Nathan N., Giraud V., Picard C., Nunes H., Dastot-Le Moal F., Copin B.,
RA Galeron L., De Ligniville A., Kuziner N., Reynaud-Gaubert M., Valeyre D.,
RA Couderc L.J., Chinet T., Borie R., Crestani B., Simansour M., Nau V.,
RA Tissier S., Duquesnoy P., Mansour-Hendili L., Legendre M.,
RA Kannengiesser C., Coulomb-L'Hermine A., Gouya L., Amselem S., Clement A.;
RT "Germline SFTPA1 mutation in familial idiopathic interstitial pneumonia and
RT lung cancer.";
RL Hum. Mol. Genet. 25:1457-1467(2016).
RN [18]
RP VARIANT ILD1 MET-178, AND INVOLVEMENT IN ILD1.
RX PubMed=30854216; DOI=10.1038/s41439-019-0044-z;
RA Doubkova M., Stano Kozubik K., Radova L., Pesova M., Trizuljak J., Pal K.,
RA Svobodova K., Reblova K., Svozilova H., Vrzalova Z., Pospisilova S.,
RA Doubek M.;
RT "A novel germline mutation of the SFTPA1 gene in familial interstitial
RT pneumonia.";
RL Hum. Genome Var. 6:12-12(2019).
RN [19]
RP VARIANT ILD1 HIS-208.
RX PubMed=31601679; DOI=10.1084/jem.20182351;
RA Takezaki A., Tsukumo S.I., Setoguchi Y., Ledford J.G., Goto H.,
RA Hosomichi K., Uehara H., Nishioka Y., Yasutomo K.;
RT "A homozygous SFTPA1 mutation drives necroptosis of type II alveolar
RT epithelial cells in patients with idiopathic pulmonary fibrosis.";
RL J. Exp. Med. 216:2724-2735(2019).
RN [20]
RP VARIANTS ILD1 MET-178 AND MET-225, CHARACTERIZATION OF VARIANTS ILD1
RP MET-178; ARG-211 AND MET-225, AND SUBCELLULAR LOCATION.
RX PubMed=32855221; DOI=10.1183/13993003.02806-2020;
RA Legendre M., Butt A., Borie R., Debray M.P., Bouvry D., Filhol-Blin E.,
RA Desroziers T., Nau V., Copin B., Dastot-Le Moal F., Hery M., Duquesnoy P.,
RA Allou N., Bergeron A., Bermudez J., Cazes A., Chene A.L., Cottin V.,
RA Crestani B., Dalphin J.C., Dombret C., Doray B., Dupin C., Giraud V.,
RA Gondouin A., Gouya L., Israel-Biet D., Kannengiesser C., Le Borgne A.,
RA Leroy S., Longchampt E., Lorillon G., Nunes H., Picard C.,
RA Reynaud-Gaubert M., Traclet J., de Vuyst P., Coulomb L'Hermine A.,
RA Clement A., Amselem S., Nathan N.;
RT "Functional assessment and phenotypic heterogeneity of SFTPA1 and SFTPA2
RT mutations in interstitial lung diseases and lung cancer.";
RL Eur. Respir. J. 56:0-0(2020).
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 (By similarity). {ECO:0000250|UniProtKB:P35242}.
CC -!- FUNCTION: (Microbial infection) Recognition of M.tuberculosis by
CC dendritic cells may occur partially via this molecule (PubMed:17158455,
CC PubMed:21203928). Can recognize, bind, and opsonize pathogens to
CC enhance their elimination by alveolar macrophages (PubMed:21123169).
CC {ECO:0000269|PubMed:17158455, ECO:0000269|PubMed:21123169,
CC ECO:0000269|PubMed:21203928}.
CC -!- SUBUNIT: Oligomeric complex of 6 set of homotrimers.
CC {ECO:0000269|PubMed:2610270}.
CC -!- SUBUNIT: (Microbial infection) Binds M.bovis cell surface protein Apa
CC via its glycosylated sites; probably also recognizes other bacterial
CC moieties. {ECO:0000269|PubMed:17158455}.
CC -!- SUBUNIT: (Microbial infection) Binds to the S.aureus extracellular
CC adherence protein, Eap, thereby enhancing phagocytosis and killing of
CC S.aureus by alveolar macrophages. {ECO:0000269|PubMed:21123169}.
CC -!- INTERACTION:
CC Q8IWL2; Q9UGM3: DMBT1; NbExp=2; IntAct=EBI-11316418, EBI-1044970;
CC Q8IWL2; P75409: MPN_372; Xeno; NbExp=2; IntAct=EBI-11316418, EBI-2259548;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26792177,
CC ECO:0000269|PubMed:32855221}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000305}. Secreted, extracellular space,
CC surface film {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IWL2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IWL2-2; Sequence=VSP_046802;
CC -!- PTM: N-acetylated. {ECO:0000269|PubMed:3755136}.
CC -!- POLYMORPHISM: At least 5 allelic variants of SFTPA1 are known: 6A,
CC 6A(2), 6A(3), 6A(4) and 6A(5). The sequence shown is that of allele
CC 6A(3).
CC -!- DISEASE: Interstitial lung disease 1 (ILD1) [MIM:619611]: A form of
CC interstitial lung disease, a heterogeneous group of diseases affecting
CC the distal part of the lung and characterized by a progressive
CC remodeling of the alveolar interstitium. The disease spectrum ranges
CC from idiopathic interstitial pneumonia or pneumonitis to idiopathic
CC pulmonary fibrosis, that is associated with an increased risk of
CC developing lung cancer. Clinical features of interstitial lung disease
CC include dyspnea, clubbing of the fingers, and restrictive lung
CC capacity. ILD1 inheritance can be autosomal dominant with incomplete
CC penetrance, and autosomal recessive. {ECO:0000269|PubMed:26792177,
CC ECO:0000269|PubMed:30854216, ECO:0000269|PubMed:31601679,
CC ECO:0000269|PubMed:32855221}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Respiratory distress syndrome in premature infants (RDS)
CC [MIM:267450]: A lung disease affecting usually premature newborn
CC infants. It is characterized by deficient gas exchange, diffuse
CC atelectasis, high-permeability lung edema and fibrin-rich alveolar
CC deposits called 'hyaline membranes'. {ECO:0000269|PubMed:10762543}.
CC Note=Disease susceptibility may be associated with variants affecting
CC the gene represented in this entry. The association between SFTPA1
CC alleles and respiratory distress syndrome in premature infants is
CC dependent on a variation Ile to Thr at position 131 in SFTPB.
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 -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/sftpa1/";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Pulmonary surfactant protein SP-A1;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_232";
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DR EMBL; M30838; AAA36510.1; -; Genomic_DNA.
DR EMBL; M13686; AAA60211.1; -; mRNA.
DR EMBL; HQ021433; ADO27676.1; -; mRNA.
DR EMBL; HQ021434; ADO27677.1; -; mRNA.
DR EMBL; HQ021435; ADO27678.1; -; mRNA.
DR EMBL; HQ021436; ADO27679.1; -; mRNA.
DR EMBL; HQ021437; ADO27680.1; -; mRNA.
DR EMBL; HQ021438; ADO27681.1; -; mRNA.
DR EMBL; HQ021439; ADO27682.1; -; mRNA.
DR EMBL; HQ021440; ADO27683.1; -; mRNA.
DR EMBL; HQ021441; ADO27684.1; -; mRNA.
DR EMBL; HQ021442; ADO27685.1; -; mRNA.
DR EMBL; AK290703; BAF83392.1; -; mRNA.
DR EMBL; AY198391; AAO13486.1; -; Genomic_DNA.
DR EMBL; BX248123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54657.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54651.1; -; Genomic_DNA.
DR EMBL; CH471083; EAW54658.1; -; Genomic_DNA.
DR EMBL; BC029913; AAH29913.1; -; mRNA.
DR EMBL; BC111570; AAI11571.1; -; mRNA.
DR EMBL; BC171875; AAI71875.1; -; mRNA.
DR CCDS; CCDS44444.2; -. [Q8IWL2-2]
DR CCDS; CCDS44445.1; -. [Q8IWL2-1]
DR PIR; A24622; LNHUPS.
DR PIR; A25720; LNHUP6.
DR RefSeq; NP_001087239.2; NM_001093770.2. [Q8IWL2-2]
DR RefSeq; NP_001158116.1; NM_001164644.1. [Q8IWL2-1]
DR RefSeq; NP_001158119.1; NM_001164647.1. [Q8IWL2-1]
DR RefSeq; NP_005402.3; NM_005411.4. [Q8IWL2-1]
DR RefSeq; XP_005270119.1; XM_005270062.4. [Q8IWL2-1]
DR RefSeq; XP_006718016.1; XM_006717953.2. [Q8IWL2-2]
DR AlphaFoldDB; Q8IWL2; -.
DR SMR; Q8IWL2; -.
DR BioGRID; 575839; 4.
DR IntAct; Q8IWL2; 2.
DR STRING; 9606.ENSP00000397082; -.
DR BindingDB; Q8IWL2; -.
DR DrugBank; DB03814; 2-(N-morpholino)ethanesulfonic acid.
DR GlyGen; Q8IWL2; 1 site.
DR iPTMnet; Q8IWL2; -.
DR PhosphoSitePlus; Q8IWL2; -.
DR BioMuta; SFTPA1; -.
DR DMDM; 60416440; -.
DR CPTAC; CPTAC-1214; -.
DR MassIVE; Q8IWL2; -.
DR PaxDb; Q8IWL2; -.
DR PeptideAtlas; Q8IWL2; -.
DR PRIDE; Q8IWL2; -.
DR ProteomicsDB; 33955; -.
DR ProteomicsDB; 70869; -. [Q8IWL2-1]
DR ABCD; Q8IWL2; 8 sequenced antibodies.
DR Antibodypedia; 45521; 402 antibodies from 35 providers.
DR DNASU; 653509; -.
DR Ensembl; ENST00000398636.8; ENSP00000381633.3; ENSG00000122852.15. [Q8IWL2-1]
DR Ensembl; ENST00000419470.6; ENSP00000397082.2; ENSG00000122852.15. [Q8IWL2-2]
DR Ensembl; ENST00000428376.6; ENSP00000411102.2; ENSG00000122852.15. [Q8IWL2-1]
DR GeneID; 653509; -.
DR KEGG; hsa:653509; -.
DR MANE-Select; ENST00000398636.8; ENSP00000381633.3; NM_005411.5; NP_005402.3.
DR UCSC; uc001kap.4; human. [Q8IWL2-1]
DR CTD; 653509; -.
DR DisGeNET; 653509; -.
DR GeneCards; SFTPA1; -.
DR HGNC; HGNC:10798; SFTPA1.
DR HPA; ENSG00000122852; Tissue enriched (lung).
DR MalaCards; SFTPA1; -.
DR MIM; 178630; gene.
DR MIM; 267450; phenotype.
DR MIM; 619611; phenotype.
DR neXtProt; NX_Q8IWL2; -.
DR OpenTargets; ENSG00000122852; -.
DR Orphanet; 2032; Idiopathic pulmonary fibrosis.
DR PharmGKB; PA35710; -.
DR VEuPathDB; HostDB:ENSG00000122852; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000156653; -.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; Q8IWL2; -.
DR OMA; KCNQNRL; -.
DR OrthoDB; 1172460at2759; -.
DR PhylomeDB; Q8IWL2; -.
DR TreeFam; TF330481; -.
DR PathwayCommons; Q8IWL2; -.
DR Reactome; R-HSA-166016; Toll Like Receptor 4 (TLR4) Cascade.
DR Reactome; R-HSA-168179; Toll Like Receptor TLR1:TLR2 Cascade.
DR Reactome; R-HSA-391160; Signal regulatory protein family interactions.
DR Reactome; R-HSA-5683826; Surfactant metabolism.
DR Reactome; R-HSA-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-HSA-5688849; Defective CSF2RB causes SMDP5.
DR Reactome; R-HSA-5688890; Defective CSF2RA causes SMDP4.
DR SignaLink; Q8IWL2; -.
DR BioGRID-ORCS; 653509; 14 hits in 993 CRISPR screens.
DR GeneWiki; Pulmonary_surfactant-associated_protein_A1; -.
DR GenomeRNAi; 653509; -.
DR Pharos; Q8IWL2; Tbio.
DR PRO; PR:Q8IWL2; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q8IWL2; protein.
DR Bgee; ENSG00000122852; Expressed in right lung and 78 other tissues.
DR ExpressionAtlas; Q8IWL2; baseline and differential.
DR Genevisible; Q8IWL2; HS.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; TAS:Reactome.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0042599; C:lamellar body; TAS:Reactome.
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:0005319; F:lipid transporter activity; TAS:ProtInc.
DR GO; GO:0008228; P:opsonization; IMP:UniProtKB.
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 Acetylation; Alternative splicing; Calcium; Collagen; Disease variant;
KW Disulfide bond; Extracellular matrix; Gaseous exchange; Glycoprotein;
KW Hydroxylation; Lectin; Reference proteome; Secreted; Signal; Surface film.
FT SIGNAL 1..20
FT CHAIN 21..248
FT /note="Pulmonary surfactant-associated protein A1"
FT /id="PRO_0000017457"
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 31..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..76
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 26
FT /note="Interchain"
FT /evidence="ECO:0000305|PubMed:2610270"
FT DISULFID 155..246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:2610270"
FT DISULFID 224..238
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040,
FT ECO:0000269|PubMed:2610270"
FT VAR_SEQ 1
FT /note="M -> MRPCQVPGAATGPRAM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_046802"
FT VARIANT 5
FT /note="P -> L (in dbSNP:rs72659389)"
FT /evidence="ECO:0000269|PubMed:19100526"
FT /id="VAR_063517"
FT VARIANT 9
FT /note="N -> T (in dbSNP:rs139899873)"
FT /evidence="ECO:0000269|PubMed:19100526, ECO:0000269|Ref.5"
FT /id="VAR_004184"
FT VARIANT 19
FT /note="V -> A (in allele 6A and allele 6A(5);
FT dbSNP:rs1059047)"
FT /evidence="ECO:0000269|PubMed:19100526,
FT ECO:0000269|PubMed:20693318, ECO:0000269|PubMed:3755136,
FT ECO:0000269|Ref.5"
FT /id="VAR_021292"
FT VARIANT 50
FT /note="L -> V (in allele 6A(2); dbSNP:rs1136450)"
FT /evidence="ECO:0000269|PubMed:19100526,
FT ECO:0000269|PubMed:20693318, ECO:0000269|Ref.5"
FT /id="VAR_012231"
FT VARIANT 178
FT /note="V -> M (in ILD1; impaired secretion)"
FT /evidence="ECO:0000269|PubMed:30854216,
FT ECO:0000269|PubMed:32855221"
FT /id="VAR_086118"
FT VARIANT 208
FT /note="Y -> H (in ILD1)"
FT /evidence="ECO:0000269|PubMed:31601679"
FT /id="VAR_086119"
FT VARIANT 211
FT /note="W -> R (in ILD1; impaired secretion)"
FT /evidence="ECO:0000269|PubMed:26792177,
FT ECO:0000269|PubMed:32855221"
FT /id="VAR_086120"
FT VARIANT 219
FT /note="R -> W (may be associated with susceptibility to
FT idiopathic pulmonary fibrosis in smokers; allele 6A(4) and
FT allele 6A(5); does not affect secretion; dbSNP:rs4253527)"
FT /evidence="ECO:0000269|PubMed:13680361,
FT ECO:0000269|PubMed:19100526, ECO:0000269|PubMed:20693318,
FT ECO:0000269|PubMed:26792177, ECO:0000269|Ref.5"
FT /id="VAR_012232"
FT VARIANT 223
FT /note="Q -> K (in dbSNP:rs1965708)"
FT /id="VAR_012233"
FT VARIANT 225
FT /note="V -> M (in ILD1; unknown pathological significance;
FT impaired secretion)"
FT /evidence="ECO:0000269|PubMed:32855221"
FT /id="VAR_086121"
FT CONFLICT 45
FT /note="D -> H (in Ref. 1; AAA36510)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="P -> L (in Ref. 1; AAA36510)"
FT /evidence="ECO:0000305"
FT CONFLICT 100
FT /note="P -> R (in Ref. 1; AAA36510)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 248 AA; 26242 MW; AFFFCF38B87BE081 CRC64;
MWLCPLALNL ILMAASGAVC EVKDVCVGSP GIPGTPGSHG LPGRDGRDGL KGDPGPPGPM
GPPGEMPCPP GNDGLPGAPG IPGECGEKGE PGERGPPGLP AHLDEELQAT LHDFRHQILQ
TRGALSLQGS IMTVGEKVFS SNGQSITFDA IQEACARAGG RIAVPRNPEE NEAIASFVKK
YNTYAYVGLT EGPSPGDFRY SDGTPVNYTN WYRGEPAGRG KEQCVEMYTD GQWNDRNCLY
SRLTICEF
