SFPA2_HUMAN
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 03-AUG-2022, entry version 173.
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 BioGRID; 609641; 46.
DR IntAct; Q8IWL1; 2.
DR GlyGen; Q8IWL1; 1 site.
DR iPTMnet; Q8IWL1; -.
DR PhosphoSitePlus; Q8IWL1; -.
DR BioMuta; SFTPA2; -.
DR DMDM; 60416439; -.
DR MassIVE; Q8IWL1; -.
DR PaxDb; Q8IWL1; -.
DR PeptideAtlas; Q8IWL1; -.
DR PRIDE; Q8IWL1; -.
DR ProteomicsDB; 15282; -.
DR ProteomicsDB; 70868; -.
DR ABCD; Q8IWL1; 8 sequenced antibodies.
DR Antibodypedia; 57893; 160 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 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 OrthoDB; 1172460at2759; -.
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; 15 hits in 998 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 98 other tissues.
DR ExpressionAtlas; Q8IWL1; baseline and differential.
DR Genevisible; Q8IWL1; 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: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; 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; unknown pathological significance;
FT impaired 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; unknown pathological significance;
FT impaired 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; unknown pathological significance;
FT impaired 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
