SFTPD_HUMAN
ID SFTPD_HUMAN Reviewed; 375 AA.
AC P35247; Q5T0M3; Q6FH08; Q86YK9; Q8TCD8; Q9UCJ2; Q9UCJ3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=Pulmonary surfactant-associated protein D;
DE Short=PSP-D;
DE Short=SP-D;
DE AltName: Full=Collectin-7;
DE AltName: Full=Lung surfactant protein D;
DE Flags: Precursor;
GN Name=SFTPD; Synonyms=COLEC7, PSPD, SFTP4;
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], PROTEIN SEQUENCE OF 214-243, AND VARIANTS
RP THR-31 AND ALA-180.
RC TISSUE=Amniotic fluid, and Lung;
RX PubMed=1339284; DOI=10.1042/bj2840795;
RA Lu J., Willis A.C., Reid K.B.M.;
RT "Purification, characterization and cDNA cloning of human lung surfactant
RT protein D.";
RL Biochem. J. 284:795-802(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8428971; DOI=10.1016/s0021-9258(18)53869-2;
RA Crouch E., Rust K., Veile R., Donis-Keller H., Grosso L.;
RT "Genomic organization of human surfactant protein D (SP-D). SP-D is encoded
RT on chromosome 10q22.2-23.1.";
RL J. Biol. Chem. 268:2976-2983(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS THR-31 AND ALA-180.
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS THR-31; VAL-123; ALA-180;
RP THR-290 AND LYS-309.
RG SeattleSNPs variation discovery resource;
RL Submitted (JAN-2003) 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].
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 46-72 AND 223-260.
RX PubMed=8424457;
RA Crouch E., Persson A., Chang D.;
RT "Accumulation of surfactant protein D in human pulmonary alveolar
RT proteinosis.";
RL Am. J. Pathol. 142:241-248(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-375, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Lung;
RX PubMed=1898081; DOI=10.1016/0003-9861(91)90597-c;
RA Rust K., Grosso L., Zhang V., Chang D., Persson A., Longmore W., Cai G.-Z.,
RA Crouch E.;
RT "Human surfactant protein D: SP-D contains a C-type lectin carbohydrate
RT recognition domain.";
RL Arch. Biochem. Biophys. 290:116-126(1991).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=23478426; DOI=10.1038/ijo.2013.23;
RA Ortega F.J., Pueyo N., Moreno-Navarrete J.M., Sabater M.,
RA Rodriguez-Hermosa J.I., Ricart W., Tinahones F.J., Fernandez-Real J.M.;
RT "The lung innate immune gene surfactant protein-D is expressed in adipose
RT tissue and linked to obesity status.";
RL Int. J. Obes. Relat. Metab. Disord. 37:1532-1538(2013).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10368295; DOI=10.1016/s0969-2126(99)80036-7;
RA Hakansson K., Lim N.K., Hoppe H.-J., Reid K.B.M.;
RT "Crystal structure of the trimeric alpha-helical coiled-coil and the three
RT lectin domains of human lung surfactant protein D.";
RL Structure 7:255-264(1999).
RN [11]
RP VARIANTS THR-31; VAL-123; ALA-180 AND THR-290.
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).
CC -!- FUNCTION: Contributes to the lung's defense against inhaled
CC microorganisms, organic antigens and toxins. Interacts with compounds
CC such as bacterial lipopolysaccharides, oligosaccharides and fatty acids
CC and modulates leukocyte action in immune response. May participate in
CC the extracellular reorganization or turnover of pulmonary surfactant.
CC Binds strongly maltose residues and to a lesser extent other alpha-
CC glucosyl moieties. {ECO:0000269|PubMed:23478426}.
CC -!- SUBUNIT: Oligomeric complex of 4 set of homotrimers.
CC -!- INTERACTION:
CC P35247; Q9BYF1: ACE2; NbExp=2; IntAct=EBI-11316157, EBI-7730807;
CC P35247; O00322: UPK1A; NbExp=3; IntAct=EBI-11316157, EBI-14031976;
CC P35247; P0DTC2: S; Xeno; NbExp=3; IntAct=EBI-11316157, EBI-25474821;
CC PRO_0000017465; P0DTC2: S; Xeno; NbExp=11; IntAct=EBI-27021977, EBI-25474821;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix. Secreted, extracellular space, surface film.
CC -!- TISSUE SPECIFICITY: Expressed in lung, brain, pancreas and adipose
CC tissue (mainly mature adipocytes). {ECO:0000269|PubMed:23478426}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Hydroxylation on proline residues within the sequence motif, GXPG,
CC is most likely to be 4-hydroxy as this fits the requirement for 4-
CC hydroxylation in vertebrates. {ECO:0000250}.
CC -!- PTM: S-nitrosylation at Cys-35 and Cys-40 alters the quaternary
CC structure which results in a pro-inflammatory chemoattractive signaling
CC activity with macrophages. {ECO:0000250}.
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 SFTPD family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/sftpd/";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Pulmonary surfactant protein SP-D;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Ctlect_228";
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DR EMBL; X65018; CAA46152.1; -; mRNA.
DR EMBL; L05485; AAB59450.1; -; Genomic_DNA.
DR EMBL; L05483; AAB59450.1; JOINED; Genomic_DNA.
DR EMBL; L05484; AAB59450.1; JOINED; Genomic_DNA.
DR EMBL; CR541948; CAG46746.1; -; mRNA.
DR EMBL; AY216721; AAO22991.1; -; Genomic_DNA.
DR EMBL; AL512662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022318; AAH22318.1; -; mRNA.
DR CCDS; CCDS7362.1; -.
DR PIR; A45225; A45225.
DR RefSeq; NP_003010.4; NM_003019.4.
DR RefSeq; XP_011538389.1; XM_011540087.1.
DR PDB; 1B08; X-ray; 2.30 A; A/B/C=218-375.
DR PDB; 1M7L; NMR; -; A/B/C=220-257.
DR PDB; 1PW9; X-ray; 1.60 A; A/B/C=199-375.
DR PDB; 1PWB; X-ray; 1.40 A; A/B/C=199-375.
DR PDB; 2GGU; X-ray; 1.90 A; A/B/C=223-375.
DR PDB; 2GGX; X-ray; 1.90 A; A/B/C=223-375.
DR PDB; 2ORJ; X-ray; 1.80 A; A/B/C=223-375.
DR PDB; 2ORK; X-ray; 1.89 A; A/B/C=223-375.
DR PDB; 2OS9; X-ray; 1.70 A; A/B/C=223-375.
DR PDB; 2RIA; X-ray; 1.80 A; A/B/C=223-375.
DR PDB; 2RIB; X-ray; 1.80 A; A/B/C=223-375.
DR PDB; 2RIC; X-ray; 1.80 A; A/B/C=223-375.
DR PDB; 2RID; X-ray; 1.80 A; A/B/C=223-375.
DR PDB; 2RIE; X-ray; 1.60 A; A/B/C=223-375.
DR PDB; 3DBZ; X-ray; 1.80 A; A/B/C=223-375.
DR PDB; 3G81; X-ray; 1.80 A; A/B/C=223-375.
DR PDB; 3G83; X-ray; 1.90 A; A/B/C=223-375.
DR PDB; 3G84; X-ray; 2.30 A; A/B/C=223-375.
DR PDB; 3IKN; X-ray; 1.60 A; A/B/C=199-375.
DR PDB; 3IKP; X-ray; 1.75 A; A/B/C=199-375.
DR PDB; 3IKQ; X-ray; 2.25 A; A/B/C=199-375.
DR PDB; 3IKR; X-ray; 1.65 A; A/B/C=199-375.
DR PDB; 4E52; X-ray; 1.70 A; A/B/C=201-375.
DR PDB; 4M17; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=229-375.
DR PDB; 4M18; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J/K/L=229-375.
DR PDB; 5OXR; X-ray; 1.75 A; A/B/C=201-375.
DR PDB; 5OXS; X-ray; 1.65 A; A/B/C=201-375.
DR PDBsum; 1B08; -.
DR PDBsum; 1M7L; -.
DR PDBsum; 1PW9; -.
DR PDBsum; 1PWB; -.
DR PDBsum; 2GGU; -.
DR PDBsum; 2GGX; -.
DR PDBsum; 2ORJ; -.
DR PDBsum; 2ORK; -.
DR PDBsum; 2OS9; -.
DR PDBsum; 2RIA; -.
DR PDBsum; 2RIB; -.
DR PDBsum; 2RIC; -.
DR PDBsum; 2RID; -.
DR PDBsum; 2RIE; -.
DR PDBsum; 3DBZ; -.
DR PDBsum; 3G81; -.
DR PDBsum; 3G83; -.
DR PDBsum; 3G84; -.
DR PDBsum; 3IKN; -.
DR PDBsum; 3IKP; -.
DR PDBsum; 3IKQ; -.
DR PDBsum; 3IKR; -.
DR PDBsum; 4E52; -.
DR PDBsum; 4M17; -.
DR PDBsum; 4M18; -.
DR PDBsum; 5OXR; -.
DR PDBsum; 5OXS; -.
DR AlphaFoldDB; P35247; -.
DR SMR; P35247; -.
DR BioGRID; 112339; 8.
DR IntAct; P35247; 6.
DR STRING; 9606.ENSP00000361366; -.
DR ChEMBL; CHEMBL2176857; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR UniLectin; P35247; -.
DR GlyGen; P35247; 1 site.
DR iPTMnet; P35247; -.
DR PhosphoSitePlus; P35247; -.
DR BioMuta; SFTPD; -.
DR DMDM; 317373510; -.
DR EPD; P35247; -.
DR MassIVE; P35247; -.
DR PaxDb; P35247; -.
DR PeptideAtlas; P35247; -.
DR PRIDE; P35247; -.
DR ProteomicsDB; 55012; -.
DR Antibodypedia; 3886; 548 antibodies from 38 providers.
DR DNASU; 6441; -.
DR Ensembl; ENST00000372292.8; ENSP00000361366.3; ENSG00000133661.17.
DR GeneID; 6441; -.
DR KEGG; hsa:6441; -.
DR MANE-Select; ENST00000372292.8; ENSP00000361366.3; NM_003019.5; NP_003010.4.
DR UCSC; uc001kbh.4; human.
DR CTD; 6441; -.
DR DisGeNET; 6441; -.
DR GeneCards; SFTPD; -.
DR HGNC; HGNC:10803; SFTPD.
DR HPA; ENSG00000133661; Tissue enriched (lung).
DR MIM; 178635; gene.
DR neXtProt; NX_P35247; -.
DR OpenTargets; ENSG00000133661; -.
DR PharmGKB; PA35715; -.
DR VEuPathDB; HostDB:ENSG00000133661; -.
DR eggNOG; KOG4297; Eukaryota.
DR GeneTree; ENSGT00940000155748; -.
DR HOGENOM; CLU_049894_3_0_1; -.
DR InParanoid; P35247; -.
DR OMA; EMFTNGK; -.
DR OrthoDB; 1341167at2759; -.
DR PhylomeDB; P35247; -.
DR TreeFam; TF330481; -.
DR PathwayCommons; P35247; -.
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-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
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 Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR SignaLink; P35247; -.
DR SIGNOR; P35247; -.
DR BioGRID-ORCS; 6441; 9 hits in 1069 CRISPR screens.
DR EvolutionaryTrace; P35247; -.
DR GeneWiki; Surfactant_protein_D; -.
DR GenomeRNAi; 6441; -.
DR Pharos; P35247; Tbio.
DR PRO; PR:P35247; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P35247; protein.
DR Bgee; ENSG00000133661; Expressed in lower lobe of lung and 113 other tissues.
DR ExpressionAtlas; P35247; baseline and differential.
DR Genevisible; P35247; 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:0030139; C:endocytic vesicle; TAS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; TAS:UniProtKB.
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; TAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0042742; P:defense response to bacterium; TAS:UniProtKB.
DR GO; GO:0043152; P:induction of bacterial agglutination; IMP:AgBase.
DR GO; GO:0045087; P:innate immune response; TAS:UniProtKB.
DR GO; GO:0048286; P:lung alveolus development; IMP:UniProtKB.
DR GO; GO:0048246; P:macrophage chemotaxis; TAS:UniProtKB.
DR GO; GO:0052403; P:negative regulation by host of symbiont catalytic activity; IDA:AgBase.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; TAS:UniProtKB.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; TAS:UniProtKB.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IBA:GO_Central.
DR GO; GO:0072593; P:reactive oxygen species metabolic process; TAS:UniProtKB.
DR GO; GO:0006898; P:receptor-mediated endocytosis; TAS:UniProtKB.
DR GO; GO:1905226; P:regulation of adhesion of symbiont to host epithelial cell; IDA:AgBase.
DR GO; GO:0001817; P:regulation of cytokine production; NAS:UniProtKB.
DR GO; GO:0007585; P:respiratory gaseous exchange by respiratory system; IEA:UniProtKB-KW.
DR GO; GO:0043129; P:surfactant homeostasis; IMP:UniProtKB.
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; IPR008160; Collagen.
DR InterPro; IPR033990; Collectin_CTLD.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR015097; Surfac_D-trimer.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF09006; Surfac_D-trimer; 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 3D-structure; Calcium; Coiled coil; Collagen; Direct protein sequencing;
KW Disulfide bond; Extracellular matrix; Gaseous exchange; Glycoprotein;
KW Hydroxylation; Immunity; Innate immunity; Lectin; Reference proteome;
KW Repeat; S-nitrosylation; Secreted; Signal; Surface film.
FT SIGNAL 1..20
FT /evidence="ECO:0000250"
FT CHAIN 21..375
FT /note="Pulmonary surfactant-associated protein D"
FT /id="PRO_0000017465"
FT DOMAIN 46..222
FT /note="Collagen-like"
FT DOMAIN 260..375
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT REGION 45..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 223..252
FT /evidence="ECO:0000255"
FT COMPBIAS 49..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..117
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 35
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P35248"
FT MOD_RES 40
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P35248"
FT MOD_RES 78
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 87
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 96
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 99
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250"
FT MOD_RES 171
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 177
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 281..373
FT DISULFID 351..365
FT VARIANT 31
FT /note="M -> T (in dbSNP:rs721917)"
FT /evidence="ECO:0000269|PubMed:1339284,
FT ECO:0000269|PubMed:19100526, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4"
FT /id="VAR_020937"
FT VARIANT 123
FT /note="L -> V (in dbSNP:rs17878336)"
FT /evidence="ECO:0000269|PubMed:19100526, ECO:0000269|Ref.4"
FT /id="VAR_020938"
FT VARIANT 180
FT /note="T -> A (in dbSNP:rs2243639)"
FT /evidence="ECO:0000269|PubMed:1339284,
FT ECO:0000269|PubMed:19100526, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4"
FT /id="VAR_020939"
FT VARIANT 290
FT /note="S -> T (in dbSNP:rs3088308)"
FT /evidence="ECO:0000269|PubMed:19100526, ECO:0000269|Ref.4"
FT /id="VAR_020940"
FT VARIANT 309
FT /note="E -> K (in dbSNP:rs4469829)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_020941"
FT CONFLICT 22
FT /note="E -> G (in Ref. 6; AAH22318)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="P -> F (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="P -> A (in Ref. 2; AAB59450)"
FT /evidence="ECO:0000305"
FT CONFLICT 240
FT /note="H -> P (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="E -> K (in Ref. 6; AAH22318)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="R -> S (in Ref. 3; CAG46746)"
FT /evidence="ECO:0000305"
FT HELIX 226..253
FT /evidence="ECO:0007829|PDB:1PWB"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:1PWB"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:1PWB"
FT STRAND 263..273
FT /evidence="ECO:0007829|PDB:1PWB"
FT HELIX 274..283
FT /evidence="ECO:0007829|PDB:1PWB"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1PWB"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:1PWB"
FT STRAND 311..316
FT /evidence="ECO:0007829|PDB:2RIA"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:1PWB"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:2GGX"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:1PWB"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:1PWB"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:1PWB"
FT STRAND 367..375
FT /evidence="ECO:0007829|PDB:1PWB"
SQ SEQUENCE 375 AA; 37728 MW; 298917699FC40F6A CRC64;
MLLFLLSALV LLTQPLGYLE AEMKTYSHRT MPSACTLVMC SSVESGLPGR DGRDGREGPR
GEKGDPGLPG AAGQAGMPGQ AGPVGPKGDN GSVGEPGPKG DTGPSGPPGP PGVPGPAGRE
GPLGKQGNIG PQGKPGPKGE AGPKGEVGAP GMQGSAGARG LAGPKGERGV PGERGVPGNT
GAAGSAGAMG PQGSPGARGP PGLKGDKGIP GDKGAKGESG LPDVASLRQQ VEALQGQVQH
LQAAFSQYKK VELFPNGQSV GEKIFKTAGF VKPFTEAQLL CTQAGGQLAS PRSAAENAAL
QQLVVAKNEA AFLSMTDSKT EGKFTYPTGE SLVYSNWAPG EPNDDGGSED CVEIFTNGKW
NDRACGEKRL VVCEF
