ID   SFPA2_HUMAN             Reviewed;         248 AA.
AC   Q8IWL1; A4QPA7; B2RXI6; B2RXK9; C9J9I7; E3VLC6; E3VLC7; E3VLC8; E3VLC9;
AC   P07714; Q14DV3; Q5RIR8; Q5RIR9;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 2.
DT   24-JAN-2024, entry version 181.
DE   RecName: Full=Pulmonary surfactant-associated protein A2;
DE            Short=PSP-A;
DE            Short=PSPA;
DE            Short=SP-A;
DE            Short=SP-A2;
DE   AltName: Full=35 kDa pulmonary surfactant-associated protein;
DE   AltName: Full=Alveolar proteinosis protein;
DE   AltName: Full=Collectin-5;
DE   Flags: Precursor;
GN   Name=SFTPA2; Synonyms=COLEC5, PSAP, SFTP1, SFTPA, SFTPA2B;
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], ACETYLATION, AND VARIANTS ASN-9 AND PRO-91.
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   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1372511; DOI=10.1165/ajrcmb/6.4.446;
RA   Katyal S.L., Singh G., Locker J.L.;
RT   "Characterization of a second human pulmonary surfactant-associated protein
RT   SP-A gene.";
RL   Am. J. Respir. Cell Mol. Biol. 6:446-452(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ASN-9 AND LYS-223.
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 [GENOMIC DNA], AND VARIANTS ASN-9; LEU-50; PRO-91 AND
RP   LYS-223.
RG   SeattleSNPs variation discovery resource;
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-9 AND LYS-223.
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   [7]
RP   DISULFIDE BONDS.
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   [8]
RP   DEFINITION OF SFTPA2 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   [9]
RP   VARIANTS ASN-9; TRP-12; LEU-50; PRO-91 AND LYS-223, AND VARIANTS ILD2
RP   SER-198 AND VAL-231.
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   [10]
RP   CHARACTERIZATION OF VARIANT ILD2 SER-198, AND 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   [11]
RP   VARIANTS ILD2 ILE-171; MET-178; CYS-181; ARG-233; CYS-233; LEU-233; SER-238
RP   AND GLN-242, CHARACTERIZATION OF VARIANTS ILD2 ILE-171; MET-178; CYS-181;
RP   ARG-233; CYS-233; LEU-233; SER-238 AND GLN-242, 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.
CC   -!- SUBUNIT: Oligomeric complex of 6 set of homotrimers.
CC   -!- INTERACTION:
CC       Q8IWL1; P62166: NCS1; NbExp=3; IntAct=EBI-12350685, EBI-746987;
CC       Q8IWL1; Q9UHD9: UBQLN2; NbExp=6; IntAct=EBI-12350685, EBI-947187;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26792177,
CC       ECO:0000269|PubMed:32855221}. Secreted, extracellular space,
CC       extracellular matrix. Secreted, extracellular space, surface film.
CC   -!- PTM: N-acetylated. {ECO:0000269|PubMed:3755136}.
CC   -!- POLYMORPHISM: At least 6 alleles of SFTPA2 are known: 1A, 1A(0), 1A(1),
CC       1A(2), 1A(3) and 1A(4). The sequence shown is that of allele 1A(2).
CC   -!- DISEASE: Interstitial lung disease 2 (ILD2) [MIM:178500]: 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. ILD2 inheritance is autosomal dominant.
CC       {ECO:0000269|PubMed:19100526, ECO:0000269|PubMed:26792177,
CC       ECO:0000269|PubMed:32855221}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
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/sftpa2/";
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DR   EMBL; K03475; AAA36520.1; -; mRNA.
DR   EMBL; M68519; AAA60319.1; -; Genomic_DNA.
DR   EMBL; HQ021421; ADO27664.1; -; mRNA.
DR   EMBL; HQ021422; ADO27665.1; -; mRNA.
DR   EMBL; HQ021423; ADO27666.1; -; mRNA.
DR   EMBL; HQ021424; ADO27667.1; -; mRNA.
DR   EMBL; HQ021427; ADO27670.1; -; mRNA.
DR   EMBL; HQ021428; ADO27671.1; -; mRNA.
DR   EMBL; HQ021429; ADO27672.1; -; mRNA.
DR   EMBL; HQ021430; ADO27673.1; -; mRNA.
DR   EMBL; AY206682; AAO13490.1; -; Genomic_DNA.
DR   EMBL; BX248123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC111571; AAI11572.1; -; mRNA.
DR   EMBL; BC139727; AAI39728.1; -; mRNA.
DR   EMBL; BC157866; AAI57867.1; -; mRNA.
DR   EMBL; BC157890; AAI57891.1; -; mRNA.
DR   CCDS; CCDS41540.1; -.
DR   PIR; B25720; LNHUP1.
DR   PIR; I51921; I51921.
DR   RefSeq; NP_001092138.1; NM_001098668.3.
DR   RefSeq; NP_001307742.1; NM_001320813.1.
DR   RefSeq; XP_005270189.1; XM_005270132.3.
DR   RefSeq; XP_011538426.1; XM_011540124.1.
DR   RefSeq; XP_011538427.1; XM_011540125.1.
DR   RefSeq; XP_016872097.1; XM_017016608.1.
DR   AlphaFoldDB; Q8IWL1; -.
DR   SMR; Q8IWL1; -.
DR   BioGRID; 609641; 46.
DR   IntAct; Q8IWL1; 2.
DR   GlyCosmos; Q8IWL1; 1 site, No reported glycans.
DR   GlyGen; Q8IWL1; 1 site.
DR   iPTMnet; Q8IWL1; -.
DR   PhosphoSitePlus; Q8IWL1; -.
DR   BioMuta; SFTPA2; -.
DR   DMDM; 60416439; -.
DR   MassIVE; Q8IWL1; -.
DR   PeptideAtlas; Q8IWL1; -.
DR   ProteomicsDB; 15282; -.
DR   ProteomicsDB; 70868; -.
DR   ABCD; Q8IWL1; 8 sequenced antibodies.
DR   Antibodypedia; 57893; 170 antibodies from 22 providers.
DR   DNASU; 729238; -.
DR   Ensembl; ENST00000372325.7; ENSP00000361400.2; ENSG00000185303.17.
DR   Ensembl; ENST00000372327.9; ENSP00000361402.5; ENSG00000185303.17.
DR   GeneID; 729238; -.
DR   KEGG; hsa:729238; -.
DR   MANE-Select; ENST00000372325.7; ENSP00000361400.2; NM_001098668.4; NP_001092138.1.
DR   UCSC; uc001kal.5; human.
DR   AGR; HGNC:10799; -.
DR   CTD; 729238; -.
DR   DisGeNET; 729238; -.
DR   GeneCards; SFTPA2; -.
DR   GeneReviews; SFTPA2; -.
DR   HGNC; HGNC:10799; SFTPA2.
DR   HPA; ENSG00000185303; Tissue enriched (lung).
DR   MalaCards; SFTPA2; -.
DR   MIM; 178500; phenotype.
DR   MIM; 178642; gene.
DR   neXtProt; NX_Q8IWL1; -.
DR   OpenTargets; ENSG00000185303; -.
DR   Orphanet; 2032; Idiopathic pulmonary fibrosis.
DR   PharmGKB; PA35711; -.
DR   VEuPathDB; HostDB:ENSG00000185303; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   GeneTree; ENSGT00940000156653; -.
DR   HOGENOM; CLU_049894_3_0_1; -.
DR   InParanoid; Q8IWL1; -.
DR   OMA; NWHQHEP; -.
DR   OrthoDB; 4641030at2759; -.
DR   PhylomeDB; Q8IWL1; -.
DR   TreeFam; TF330481; -.
DR   PathwayCommons; Q8IWL1; -.
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-5687868; Defective SFTPA2 causes IPF.
DR   Reactome; R-HSA-5688849; Defective CSF2RB causes SMDP5.
DR   Reactome; R-HSA-5688890; Defective CSF2RA causes SMDP4.
DR   SignaLink; Q8IWL1; -.
DR   BioGRID-ORCS; 729238; 16 hits in 1070 CRISPR screens.
DR   ChiTaRS; SFTPA2; human.
DR   GeneWiki; SFTPA2; -.
DR   GenomeRNAi; 729238; -.
DR   Pharos; Q8IWL1; Tbio.
DR   PRO; PR:Q8IWL1; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q8IWL1; Protein.
DR   Bgee; ENSG00000185303; Expressed in lower lobe of lung and 99 other cell types or tissues.
DR   ExpressionAtlas; Q8IWL1; baseline and differential.
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:0030246; F:carbohydrate 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; Mannose-Binding Protein A, subunit A; 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   PANTHER; PTHR22801:SF53; 27 KDA PRIMARY MESENCHYME-SPECIFIC SPICULE PROTEIN; 1.
DR   PANTHER; PTHR22801; LITHOSTATHINE; 1.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; C-type lectin-like; 1.
DR   SUPFAM; SSF57944; Triple coiled coil domain of C-type lectins; 1.
DR   PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR   Genevisible; Q8IWL1; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Calcium; Collagen; Disease variant; Disulfide bond;
KW   Extracellular matrix; Gaseous exchange; Glycoprotein; Hydroxylation;
KW   Lectin; Reference proteome; Secreted; Signal; Surface film.
FT   SIGNAL          1..20
FT   CHAIN           21..248
FT                   /note="Pulmonary surfactant-associated protein A2"
FT                   /id="PRO_0000017458"
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          33..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   VARIANT         9
FT                   /note="T -> N (in allele 1A(0); dbSNP:rs1059046)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:19100526, ECO:0000269|PubMed:20693318,
FT                   ECO:0000269|PubMed:3755136, ECO:0000269|Ref.4"
FT                   /id="VAR_021293"
FT   VARIANT         12
FT                   /note="L -> W (in dbSNP:rs72659394)"
FT                   /evidence="ECO:0000269|PubMed:19100526"
FT                   /id="VAR_063518"
FT   VARIANT         50
FT                   /note="V -> L (in dbSNP:rs192907309)"
FT                   /evidence="ECO:0000269|PubMed:19100526, ECO:0000269|Ref.4"
FT                   /id="VAR_021294"
FT   VARIANT         91
FT                   /note="A -> P (in allele 1A; dbSNP:rs17886395)"
FT                   /evidence="ECO:0000269|PubMed:19100526,
FT                   ECO:0000269|PubMed:3755136, ECO:0000269|Ref.4"
FT                   /id="VAR_021295"
FT   VARIANT         171
FT                   /note="N -> I (in ILD2; uncertain significance; impaired
FT                   secretion)"
FT                   /evidence="ECO:0000269|PubMed:32855221"
FT                   /id="VAR_086122"
FT   VARIANT         178
FT                   /note="V -> M (in ILD2; impaired secretion)"
FT                   /evidence="ECO:0000269|PubMed:32855221"
FT                   /id="VAR_086123"
FT   VARIANT         181
FT                   /note="Y -> C (in ILD2; uncertain significance; impaired
FT                   secretion)"
FT                   /evidence="ECO:0000269|PubMed:32855221"
FT                   /id="VAR_086124"
FT   VARIANT         198
FT                   /note="F -> S (in ILD2; the mutant protein is retained in
FT                   the endoplasmic reticulum and is not secreted;
FT                   dbSNP:rs121917738)"
FT                   /evidence="ECO:0000269|PubMed:19100526,
FT                   ECO:0000269|PubMed:26792177"
FT                   /id="VAR_063519"
FT   VARIANT         223
FT                   /note="Q -> K (in allele 1A(1), allele 1A(3) and allele
FT                   1A(4); dbSNP:rs1965708)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:19100526, ECO:0000269|PubMed:20693318,
FT                   ECO:0000269|Ref.4"
FT                   /id="VAR_021296"
FT   VARIANT         231
FT                   /note="G -> V (in ILD2; the mutant protein is retained in
FT                   the endoplasmic reticulum and is not secreted;
FT                   dbSNP:rs121917737)"
FT                   /evidence="ECO:0000269|PubMed:19100526"
FT                   /id="VAR_063520"
FT   VARIANT         233
FT                   /note="W -> C (in ILD2; impaired secretion)"
FT                   /evidence="ECO:0000269|PubMed:32855221"
FT                   /id="VAR_086125"
FT   VARIANT         233
FT                   /note="W -> L (in ILD2; impaired secretion)"
FT                   /evidence="ECO:0000269|PubMed:32855221"
FT                   /id="VAR_086126"
FT   VARIANT         233
FT                   /note="W -> R (in ILD2; impaired secretion)"
FT                   /evidence="ECO:0000269|PubMed:32855221"
FT                   /id="VAR_086127"
FT   VARIANT         238
FT                   /note="C -> S (in ILD2; impaired secretion)"
FT                   /evidence="ECO:0000269|PubMed:32855221"
FT                   /id="VAR_086128"
FT   VARIANT         242
FT                   /note="R -> Q (in ILD2; uncertain significance; impaired
FT                   secretion)"
FT                   /evidence="ECO:0000269|PubMed:32855221"
FT                   /id="VAR_086129"
FT   CONFLICT        247
FT                   /note="E -> D (in Ref. 2; AAA60319)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   248 AA;  26169 MW;  5E5510F0E9A7B6A4 CRC64;
     MWLCPLALTL ILMAASGAAC EVKDVCVGSP GIPGTPGSHG LPGRDGRDGV KGDPGPPGPM
     GPPGETPCPP GNNGLPGAPG VPGERGEKGE AGERGPPGLP AHLDEELQAT LHDFRHQILQ
     TRGALSLQGS IMTVGEKVFS SNGQSITFDA IQEACARAGG RIAVPRNPEE NEAIASFVKK
     YNTYAYVGLT EGPSPGDFRY SDGTPVNYTN WYRGEPAGRG KEQCVEMYTD GQWNDRNCLY
     SRLTICEF
//